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		<title>Publications of P. Güntert</title>
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Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
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==== Preprints ====&lt;br /&gt;
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* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
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==== Accepted/in press ====&lt;br /&gt;
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==== 2026 ====&lt;br /&gt;
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* Nguyen, C. K. X., Esteban-Hofer, L., Damberger, F. F., Yulikov, M., Güntert, P., Galazzo, L., Cléry, A., Jeschke, G. &amp;amp; Allain, F. H.-T. Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling[https://uni-frankfurt.guentert.science/Reprints/Nguyen26-SRSF1.pdf .] [https://doi.org/10.1093/nar/gkag269 Nucl. Acids Res. 54, gkag269 (2026)]&lt;br /&gt;
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* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80, 1 (2026)]&lt;br /&gt;
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* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
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==== 2025 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
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* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
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==== 2024 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
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* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
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* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
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* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
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==== 2023 ====&lt;br /&gt;
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* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
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* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
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* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
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* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
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* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
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* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
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==== 2022 ====&lt;br /&gt;
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* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
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* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
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* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
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* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
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* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
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* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
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* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
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* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Knehans11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Yamashita11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ikeya10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sobhanifar10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
&lt;br /&gt;
* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
==== 2000 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
&lt;br /&gt;
==== 1999 ====&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
&lt;br /&gt;
==== 1998 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
&lt;br /&gt;
==== 1997 ====&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
&lt;br /&gt;
* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
&lt;br /&gt;
==== 1996 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
&lt;br /&gt;
* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
&lt;br /&gt;
==== 1995 ====&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
==== 1994 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
==== 1993 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
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==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
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== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
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		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59332</id>
		<title>Publications of P. Güntert</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59332"/>
		<updated>2026-04-01T06:32:40Z</updated>

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Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
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==== Accepted/in press ====&lt;br /&gt;
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&lt;br /&gt;
==== 2026 ====&lt;br /&gt;
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* Nguyen, C. K. X., Esteban-Hofer, L., Damberger, F. F., Yulikov, M., Güntert, P., Galazzo, L., Cléry, A., Jeschke, G. &amp;amp; Allain, F. H.-T. Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling[https://uni-frankfurt.guentert.science/Reprints/Nguyen26-SRSF1.pdf.] [https://doi.org/10.1093/nar/gkag269 Nucl. Acids Res. 54, gkag269 (2026)]&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80, 1 (2026)]&lt;br /&gt;
&lt;br /&gt;
* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
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==== 2025 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
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* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
&lt;br /&gt;
==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
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* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
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* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
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==== 2023 ====&lt;br /&gt;
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* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
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* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
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* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
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* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
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* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
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==== 2022 ====&lt;br /&gt;
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* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
&lt;br /&gt;
* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
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==== 1995 ====&lt;br /&gt;
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* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
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* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
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* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
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==== 1994 ====&lt;br /&gt;
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* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
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* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
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==== 1993 ====&lt;br /&gt;
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* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
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* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
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* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
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* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
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* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
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==== 1992 ====&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59331</id>
		<title>ETHermodynamics</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59331"/>
		<updated>2026-03-26T11:43:00Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;The new way to learn thermodynamics&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics is a software for thermodynamic (computer) experiments that are performed by simulating the motion of a large number of gas particles, i.e., their microscopic time evolution governed by the laws of classical mechanics, from which macroscopic thermodynamic quantities can be obtained and compared with theoretical results of statistical thermodynamics or real (laboratory) measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics (Copyright (c) 2021 ETH Zürich) is available for computers with Windows, MacOS and Linux operating system. The current version is 2.0.4.&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-windows-installer-x64-2.0.4.exe|ETHermodynamics for Windows]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-macos-installer-x64-2.0.4.pkg|ETHermodynamics for MacOS]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-linux-x64-2.0.4.zip|ETHermodynamics for Linux]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics (Copyright (c) 2021 ETH Zürich) was developed at ETH Zürich with financial support from an ETH Innovedum grant by Anatol Aicher, Piotr Klukowski and Peter Güntert.&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59330</id>
		<title>ETHermodynamics</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59330"/>
		<updated>2026-03-26T11:41:44Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;The new way to learn thermodynamics&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics (Copyright (c) 2021 ETH Zürich) is available for computers with Windows, MacOS and Linux operating system. The current version is 2.0.4.&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-windows-installer-x64-2.0.4.exe|ETHermodynamics for Windows]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-macos-installer-x64-2.0.4.pkg|ETHermodynamics for MacOS]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-linux-x64-2.0.4.zip|ETHermodynamics for Linux]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics (Copyright (c) 2021 ETH Zürich) was developed at ETH Zürich with financial support from an ETH Innovedum grant by Anatol Aicher, Piotr Klukowski and Peter Güntert.&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59329</id>
		<title>ETHermodynamics</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59329"/>
		<updated>2026-03-26T11:41:14Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;The new way to learn thermodynamics&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
ETHermodynamics (Copyright (c) 2021 ETH Zürich) is available for computers with Windows, MacOS and Linux operating system. The current version is 2.0.4.&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-windows-installer-x64-2.0.4.exe|ETHermodynamics for Windows]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-macos-installer-x64-2.0.4.pkg|ETHermodynamics for MacOS]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-linux-x64-2.0.4.zip|ETHermodynamics for Linux]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* ETHermodynamics was developed at ETH Zürich with financial support from an ETH Innovedum grant by Anatol Aicher, Piotr Klukowski and Peter Güntert.&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59328</id>
		<title>ETHermodynamics</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59328"/>
		<updated>2026-03-26T11:40:56Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;The new way to learn thermodynamics&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ETHermodynamics (Copyright (c) 2021 ETH Zürich) is available for computers with Windows, MacOS and Linux operating system. The current version is 2.0.4.&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-windows-installer-x64-2.0.4.exe|ETHermodynamics for Windows]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-macos-installer-x64-2.0.4.pkg|ETHermodynamics for MacOS]]&lt;br /&gt;
&lt;br /&gt;
* [[Media:ETHermodynamics-linux-x64-2.0.4.zip|ETHermodynamics for Linux]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* ETHermodynamics was developed at ETH Zürich with financial support from an ETH Innovedum grant by Anatol Aicher, Piotr Klukowski and Peter Güntert.&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59327</id>
		<title>ETHermodynamics</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ETHermodynamics&amp;diff=59327"/>
		<updated>2026-03-26T10:38:19Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: Created page with &amp;quot;&amp;#039;&amp;#039;The new way to learn thermodynamics&amp;#039;&amp;#039;   Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.  == Availability ==  * ETHermodynamics (Copyright (c) 2021 ETH Zürich) is av...&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;The new way to learn thermodynamics&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ETHermodynamics (Copyright (c) 2021 ETH Zürich) is available for computers with Windows, MacOS and Linux operating system.&lt;br /&gt;
&lt;br /&gt;
* [[ &lt;br /&gt;
&lt;br /&gt;
within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis and within [https://nmrtist.bruker.com/ NMRtist@Bruker].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* ETHermodynamics was developed at ETH Zürich with financial support from an ETH Innovedum grant by Anatol Aicher, Piotr Klukowski and Peter Güntert.&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59326</id>
		<title>Software</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59326"/>
		<updated>2026-03-26T10:25:08Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Software developed by P. Güntert and collaborators.&lt;br /&gt;
&lt;br /&gt;
== Available software == &lt;br /&gt;
&lt;br /&gt;
* [[ARTINA]]: Artificial intelligence for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[ATNOS]]: Automated NOESY peak picking&lt;br /&gt;
&lt;br /&gt;
* [[AUTOPSY]]: Automated peak picking in NMR spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[CANDID]]: Combined automated NOE assignment and structure determination module&lt;br /&gt;
&lt;br /&gt;
* [[Chess2FLYA]]: Chemical shift statistics to FLYA&lt;br /&gt;
&lt;br /&gt;
* [[COCO]]: Compare covalent geometry&lt;br /&gt;
&lt;br /&gt;
* [[COFIMA]]: Coordinate and constraint file manipulation&lt;br /&gt;
&lt;br /&gt;
* [http://www.cyana.org/wiki CYANA]: Combined assignment and dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[CYLIB]]: CYANA library entry preparation from mmCIF or Mol2 files &lt;br /&gt;
&lt;br /&gt;
* [https://uni-frankfurt.guentert.science/cyrange CYRANGE]: Determination of optimum residue ranges for the superposition of protein structures&lt;br /&gt;
&lt;br /&gt;
* [[ETHermodynamics]]: The new way to learn thermodynamics&lt;br /&gt;
&lt;br /&gt;
* [[GARANT]]: General algorithm for resonance assignment&lt;br /&gt;
&lt;br /&gt;
* [[INFIT]]: Coupling constants from inverse Fourier transformation of in-phase multiplets&lt;br /&gt;
&lt;br /&gt;
* [[KUJIRA]]: Interactive and semi-automatic NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [https://nmrtist.org/ NMRtist]: Online platform for automated biomolecular NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [[MAPPER]]: Sequence-specific NMR assignment of proteins by global sequence mapping&lt;br /&gt;
&lt;br /&gt;
* [[POMA]]: Product operator formalism in Mathematica&lt;br /&gt;
&lt;br /&gt;
* [[PROSA]]: Processing algorithms&lt;br /&gt;
&lt;br /&gt;
* [[UPLABEL]]: Unique pair labeling&lt;br /&gt;
&lt;br /&gt;
== Other software ==&lt;br /&gt;
&lt;br /&gt;
Not separately available, not yet available, or outdated software.&lt;br /&gt;
&lt;br /&gt;
* [[ASNO]]: Semi-automated assignment of NOEs&lt;br /&gt;
&lt;br /&gt;
* [[CALIBA]]: Calibration of NOE distance constraints&lt;br /&gt;
&lt;br /&gt;
* [[DIANA]]: Distance geometry algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[DYANA]]: Dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[EASY]]: ETH automated spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[FLATT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[FLYA]]: Fully automated structure determination of proteins in solution&lt;br /&gt;
&lt;br /&gt;
* [[FOUND]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[GLOMSA]]: Global method for stereo-specific assignments&lt;br /&gt;
&lt;br /&gt;
* [[HABAS]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[IFLAT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[INCLAN]]: Interactive command language&lt;br /&gt;
&lt;br /&gt;
* [[OPAL]]: Energy refinement and MD simulation algorithm for vector supercomputers&lt;br /&gt;
&lt;br /&gt;
* [[OPALp]]: Energy refinement and MD simulation algorithm&lt;br /&gt;
&lt;br /&gt;
* [[XEASY]]: X-windows version of ETH automated Spectroscopy&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59325</id>
		<title>Publications of P. Güntert</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59325"/>
		<updated>2026-03-23T17:25:45Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;__NOTOC__&lt;br /&gt;
Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
--&amp;gt;&lt;br /&gt;
==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Nguyen, C. K. X., Esteban-Hofer, L., Damberger, F. F., Yulikov, M., Güntert, P., Galazzo, L., Cléry, A., Jeschke, G. &amp;amp; Allain, F. H.-T. Characterization of flexible RNA binding by tandem RNA recognition motifs through integrative ensemble modelling. Nucl. Acids Res.&lt;br /&gt;
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==== 2026 ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80, 1 (2026)]&lt;br /&gt;
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* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
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==== 2025 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
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* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
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==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
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* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
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* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
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* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
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==== 2023 ====&lt;br /&gt;
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* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
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* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
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* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
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* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
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* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
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* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
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==== 2022 ====&lt;br /&gt;
&lt;br /&gt;
* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
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* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
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* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
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* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&lt;br /&gt;
* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&lt;br /&gt;
* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&lt;br /&gt;
* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
&lt;br /&gt;
* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
&lt;br /&gt;
* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Handa10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ikeya10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sobhanifar10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
&lt;br /&gt;
* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
&lt;br /&gt;
==== 1998 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
&lt;br /&gt;
==== 1997 ====&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
&lt;br /&gt;
* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
&lt;br /&gt;
==== 1996 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
&lt;br /&gt;
* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
&lt;br /&gt;
==== 1995 ====&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
==== 1994 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
==== 1993 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59324</id>
		<title>Publications of P. Güntert</title>
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Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
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==== Preprints ====&lt;br /&gt;
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* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
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==== Accepted/in press ====&lt;br /&gt;
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* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80, 1 (2026)]&lt;br /&gt;
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==== 2026 ====&lt;br /&gt;
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* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
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==== 2025 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
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* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
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==== 2024 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
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* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
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* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
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* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
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==== 2023 ====&lt;br /&gt;
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* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
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* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
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* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
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* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
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* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
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* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
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==== 2022 ====&lt;br /&gt;
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* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
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* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
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* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
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* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
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* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
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* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
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* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
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* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
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* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Yamashita11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ikeya10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sobhanifar10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
&lt;br /&gt;
* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
==== 2000 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
&lt;br /&gt;
==== 1999 ====&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
&lt;br /&gt;
==== 1998 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
&lt;br /&gt;
==== 1997 ====&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
&lt;br /&gt;
* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
&lt;br /&gt;
==== 1996 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
&lt;br /&gt;
* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
&lt;br /&gt;
==== 1995 ====&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
==== 1994 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
==== 1993 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
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==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
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== All publications ==&lt;br /&gt;
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		<author><name>GuentertWiki</name></author>
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		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59323</id>
		<title>Publications of P. Güntert</title>
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		<updated>2026-02-23T08:36:34Z</updated>

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Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
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==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80 (2026)]&lt;br /&gt;
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==== 2026 ====&lt;br /&gt;
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* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
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==== 2025 ====&lt;br /&gt;
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* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
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* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
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==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
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==== 2023 ====&lt;br /&gt;
&lt;br /&gt;
* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
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* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
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* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
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* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
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* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
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* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
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==== 2022 ====&lt;br /&gt;
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* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
&lt;br /&gt;
* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
&lt;br /&gt;
* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
&lt;br /&gt;
* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Knehans11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Yamashita11&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ikeya10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sobhanifar10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
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==== 1995 ====&lt;br /&gt;
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* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
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* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
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* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
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==== 1994 ====&lt;br /&gt;
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* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
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* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
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==== 1993 ====&lt;br /&gt;
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* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
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* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
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* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
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* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
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* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
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==== 1992 ====&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
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* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
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==== 1991 ====&lt;br /&gt;
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* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
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* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
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* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
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* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
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==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59322</id>
		<title>Publications of P. Güntert</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59322"/>
		<updated>2026-02-23T08:36:15Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
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&lt;div&gt;__NOTOC__&lt;br /&gt;
Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
--&amp;gt;&lt;br /&gt;
==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot25-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80 (2026)]&lt;br /&gt;
&lt;br /&gt;
==== 2026 ====&lt;br /&gt;
&lt;br /&gt;
* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
&lt;br /&gt;
==== 2025 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
&lt;br /&gt;
==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
&lt;br /&gt;
==== 2023 ====&lt;br /&gt;
&lt;br /&gt;
* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
==== 2022 ====&lt;br /&gt;
&lt;br /&gt;
* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
&lt;br /&gt;
==== 2021 ====&lt;br /&gt;
&lt;br /&gt;
* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
&lt;br /&gt;
==== 2020 ====&lt;br /&gt;
&lt;br /&gt;
* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&lt;br /&gt;
* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He10&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Coutandin09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_3&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
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==== 1995 ====&lt;br /&gt;
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* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
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* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
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* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
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==== 1994 ====&lt;br /&gt;
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* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
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* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
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==== 1993 ====&lt;br /&gt;
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* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
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* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
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* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
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* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
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* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
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==== 1992 ====&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
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* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59321</id>
		<title>Publications of P. Güntert</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59321"/>
		<updated>2026-02-23T08:24:54Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
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&lt;div&gt;__NOTOC__&lt;br /&gt;
Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
--&amp;gt;&lt;br /&gt;
==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot26-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80 (2026)]&lt;br /&gt;
&lt;br /&gt;
==== 2026 ====&lt;br /&gt;
&lt;br /&gt;
* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
&lt;br /&gt;
==== 2025 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
&lt;br /&gt;
==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
&lt;br /&gt;
==== 2023 ====&lt;br /&gt;
&lt;br /&gt;
* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
==== 2022 ====&lt;br /&gt;
&lt;br /&gt;
* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
&lt;br /&gt;
==== 2021 ====&lt;br /&gt;
&lt;br /&gt;
* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
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* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Reckel08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
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==== 1995 ====&lt;br /&gt;
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* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
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* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
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* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
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==== 1994 ====&lt;br /&gt;
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* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
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* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
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==== 1993 ====&lt;br /&gt;
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* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
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* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
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* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
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* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
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* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
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		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59320</id>
		<title>Publications of P. Güntert</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59320"/>
		<updated>2026-02-23T08:19:36Z</updated>

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&lt;div&gt;__NOTOC__&lt;br /&gt;
Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&amp;lt;!-- &lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
--&amp;gt;&lt;br /&gt;
==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot25-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80 (2026)]&lt;br /&gt;
&lt;br /&gt;
==== 2026 ====&lt;br /&gt;
&lt;br /&gt;
* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
&lt;br /&gt;
==== 2025 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
&lt;br /&gt;
==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
&lt;br /&gt;
==== 2023 ====&lt;br /&gt;
&lt;br /&gt;
* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
==== 2022 ====&lt;br /&gt;
&lt;br /&gt;
* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
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* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
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* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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==== 2010 ====&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kainosho06_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
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* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
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* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
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==== 1995 ====&lt;br /&gt;
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* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
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* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
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* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
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==== 1994 ====&lt;br /&gt;
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* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
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* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
==== 1993 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
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		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Publications_of_P._G%C3%BCntert&amp;diff=59319</id>
		<title>Publications of P. Güntert</title>
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Publications in [https://europepmc.org/search?query=G%C3%BCntert%20P Europe PMC]&amp;lt;!--[https://pubmed.ncbi.nlm.nih.gov/?sort=date&amp;amp;size=200&amp;amp;term=Guntert%20P&amp;amp;sort_order=desc PubMed]--&amp;gt;, [https://www.webofscience.com/wos/alldb/summary/dd9f7771-0c42-433a-ab04-e7471729e6bd-010d72e6ca/relevance/1 Web of Science] or [https://scholar.google.com/citations?hl=en&amp;amp;user=JBYc4jMAAAAJ&amp;amp;view_op=list_works&amp;amp;sortby=pubdate Google Scholar].&lt;br /&gt;
&lt;br /&gt;
==== Preprints ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://www.biorxiv.org/content/10.1101/2025.10.21.682867v1.full.pdf .] [https://doi.org/10.1101/2025.10.21.682867 bioRxiv 682867 (2025)]&lt;br /&gt;
&amp;lt;!-- --&amp;gt;&lt;br /&gt;
==== Accepted/in press ====&lt;br /&gt;
&lt;br /&gt;
* Henot, F., Vibert, B., Giraud, A., Dbira, S., Imbert, L., Favier, A., Güntert, P., Clavier, S., Crublet, E., Doyen, C., Boisbouvier, J., Frances, O. A fast and efficient strategy for the NMR assignment of Fab methyl groups[https://uni-frankfurt.guentert.science/Reprints/Henot25-FabMethyls.pdf .] [https://doi.org/10.1007/s10858-025-00480-z J. Biomol. NMR 80 (2026)]&lt;br /&gt;
&lt;br /&gt;
==== 2026 ====&lt;br /&gt;
&lt;br /&gt;
* Dang, W., Muto, Y. He, F. Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S., Kuwasako, K. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the CID domain of SR-related- and CTD-associated factor 8 (SCAF8)[https://uni-frankfurt.guentert.science/wiki/images/Reprints/Dang25-SCAF8.pdf .] [https://doi.org/10.1007/s12104-025-10252-3 Biomol. NMR Assignments (2026) 20, 7]&lt;br /&gt;
&lt;br /&gt;
==== 2025 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P., Klukowski, P., Riek, R. Super-resolution triple resonance NMR spectroscopy for the sequential assignment of proteins[https://uni-frankfurt.guentert.science/Reprints/Gampp25-SuperResolutionTripleResonance.pdf .] [https://doi.org/10.1126/sciadv.adv6246 Sci. Adv. 11, eadv6246 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Okada, M., Tateishi, Y., Nojiri, E., Mikawa, T. Rajesh, S., Ogasa, H., Ueda, T., Yagi, H. Kohno, T., Kigawa, T., Shimada, I., Güntert, P., Ito, Y. &amp;amp; Ikeya, T. Multi-state structure determination and dynamics analysis reveals a unique recognition mechanism of ubiquitin C-terminal hydrolase[https://uni-frankfurt.guentert.science/Reprints/Okada25-MultistateYUH1.pdf .] [https://doi.org/10.1021/jacs.5c06502 J. Am. Chem. Soc. 147, 29884-29894 (2025)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Machine learning in NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Klukowski25-MachineLearningInNMRSpectroscopy.pdf .] [http://doi.org/10.1016/j.pnmrs.2025.101575 Prog. NMR Spectrosc. 148–149, 101575 (2025)]&lt;br /&gt;
&lt;br /&gt;
==== 2024 ====&lt;br /&gt;
&lt;br /&gt;
* Gampp, O., Wenchel, L., Güntert, P. &amp;amp; Riek, R. Homonuclear super-resolution NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Gampp24-HomonuclearSuperResolution.pdf .] [http://doi.org/10.1002/anie.202414324 Angew. Chem. Int. Ed. 64, e202414324 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Damberger, F. F., Allain, F. H.-T., Iwai, H., Kadavath, H., Ramelot, T. A., Montelione, G. T., Riek, R. &amp;amp; Güntert, P. The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski24-100ProteinDataset.pdf .] [http://doi.org/10.1038/s41597-023-02879-5 Scientific Data 11, 30 (2024)]&lt;br /&gt;
&lt;br /&gt;
==== 2023 ====&lt;br /&gt;
&lt;br /&gt;
* Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kazemi, S., Lopata, A., Kniss, A., Pluska, L., Güntert, P., Sommer, T., Prisner, T. F., Collauto, A. &amp;amp; Dötsch, V. Efficient determination of the accessible conformational space of multi-domain complexes based on EPR PELDOR data[https://uni-frankfurt.guentert.science/Reprints/Kazemi23-DiUbiquitinEPR.pdf .] [http://doi.org/10.1007/s10858-023-00426-3 J. Biomol. NMR (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Wetton, H., Klukowski, P., Riek, R. &amp;amp; Güntert, P. Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA[https://uni-frankfurt.guentert.science/Reprints/Wetton23-ShiftTransfer.pdf .] [http://doi.org/10.3389/fmolb.2023.1244029 Front. Mol. Biosci. 10, 1244029 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Lipiński, W. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E. &amp;amp; Wiegand, T. Fibrils emerging from droplets: Molecular guiding principles behind phase transitions of a short peptide-based condensate studied by solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Lipinski23-Fibrils.pdf .] [http://doi.org/10.1002/chem.202301159 Chem. Eur. J. 29, e202301159 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Kuschert, S., Stroet, M., Chin, Y. K. Y., Conibear, A. C., Jia, X., Lee, T., Bartling, C. R. O., Strømgaard, K., Güntert, P., Rosengren, K. J., Mark, A. E. &amp;amp; Mobli, M. Facilitating the structural characterisation of non-canonical amino acids in biomolecular NMR[https://uni-frankfurt.guentert.science/Reprints/Kuschert23-ncAAs.pdf .] [https://doi.org/10.5194/mr-4-57-2023 Magn. Reson. 4, 57-72 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
==== 2022 ====&lt;br /&gt;
&lt;br /&gt;
* Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
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* Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
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* He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Kadavath, H., Riek, R. &amp;amp; Güntert, P. Optimization and validation of multi-state NMR protein structures using structural correlations[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor2.pdf .] [http://doi.org/10.1007/s10858-022-00392-2 J. Biomol. NMR 76, 39–47 (2022)]&lt;br /&gt;
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* Ashkinadze, D., Klukowski, P., Kadavath, H., Güntert, P. &amp;amp; Riek, R. PDBcor: An automated correlation network extraction calculator for multi-state protein structures[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDBcor.pdf .] [http://doi.org/10.1016/j.str.2021.12.002 Structure 30, 646–652 (2022)]&lt;br /&gt;
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* Güntert, P. A B-factor for NOEs[https://uni-frankfurt.guentert.science/Reprints/Guntert22-BFactorForNOEs.pdf ?] [http://doi.org/10.1016/j.jmr.2022.107189 J. Magn. Reson. 338, 107189 (2022)]&lt;br /&gt;
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* Klein, A., Rovó, P., Sakhrani, V. V., Wang, Y., Holmes, J. B., Liu, V., Skowronek, P., Kukuk, L., Vasa, S. K., Güntert, P., Mueller, L. J. &amp;amp; Linser, R. Atomic-resolution chemical characterization of (2x)72 kDa tryptophan synthase via 4D and 5D &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H-detected solid-state NMR[https://uni-frankfurt.guentert.science/Reprints/Klein22-TryptophanSynthase.pdf .] [http://doi.org/10.1073/pnas.2114690119 Proc. Nat. Acad. Sci. USA 119, e2114690119 (2022)]&lt;br /&gt;
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==== 2021 ====&lt;br /&gt;
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* Cucuzza, S., Güntert, P., Plückthun, A. &amp;amp; Zerbe, O. An automated iterative approach for protein structure refinement using pseudocontact shifts[https://uni-frankfurt.guentert.science/Reprints/Cucuzza21-PCS.pdf .] [http://doi.org/10.1007/s10858-021-00376-8 J. Biomol. NMR 75, 319-334 (2021)]&lt;br /&gt;
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* Sobol, A., Güntert, P. &amp;amp; Riek, R. On the entropy of a one-dimensional gas with and without mixing using Sinai billiard[https://uni-frankfurt.guentert.science/Reprints/Sobol21-OneDimensionalGas.pdf .] [https://doi.org/10.3390/e23091188 Entropy 23, 1188 (2021)]&lt;br /&gt;
&lt;br /&gt;
* Maden Yılmaz, E., Güntert, P. &amp;amp; Etaner-Uyar, Ş. Evaluation of multi-objective optimization algorithms for NMR chemical shift assignment[https://uni-frankfurt.guentert.science/Reprints/MadenYilmaz21-MultiObjectiveOptimization.pdf .] [http://doi.org/10.3390/molecules26123699 Molecules 26, 3699 (2021)]&lt;br /&gt;
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* Zehnder, J., Cadalbert, R., Terradot, L., Güntert, P., Böckmann, A., Meier, B. H. &amp;amp; Wiegand, T. Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Zehnder21_DnaB.pdf .] [http://doi.org/10.1002/chem.202100462 Chem. Eur. J. 27, 7745-7755 (2021)]&lt;br /&gt;
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* He., F., Endo, R., Kuwasako, K., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the YTH domain of YTHDC2[https://uni-frankfurt.guentert.science/Reprints/He21_YTHDC2Assignment.pdf .] [http://doi.org/10.1007/s12104-020-09974-3 Biomol. NMR Assignments 15, 1-7 (2021)]&lt;br /&gt;
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==== 2020 ====&lt;br /&gt;
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* Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
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* Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
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* Kooijman, L., Schuster, M., Baumann, C., Jurt, S., Ansorge, P., Löhr, F., Fürtig, B., Güntert, P. &amp;amp; Zerbe, O. Dynamics of bacteriorhodopsin in the dark-adapted state from solution NMR[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-Bacteriorhodopsin.pdf .] [http://doi.org/10.1002/anie.202004393 Angew. Chem. Int. Ed. 59, 20965–20972 (2020)]&lt;br /&gt;
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* Pritišanac, I., Alderson, T. R. &amp;amp; Güntert, P. Automated assignment of methyl NMR spectra from large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac20-MethylAssignmentReview.pdf .] [http://doi.org/10.1016/j.pnmrs.2020.04.001 Prog. NMR Spectrosc. 118–119, 54–73 (2020)]&lt;br /&gt;
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* Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B. &amp;amp; Pintacuda, G. Automated backbone NMR resonance assignment of large proteins using redundant linking from a single simultaneous acquisition[https://uni-frankfurt.guentert.science/Reprints/Stanek20-RAVASSA.pdf .] [http://doi.org/10.1021/jacs.0c00251 J. Am. Chem. Soc. 142, 5793−5799 (2020)]&lt;br /&gt;
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* Kooijman, L., Ansorge, P., Schuster, M., Baumann, C., Löhr, F., Jurt, S., Güntert, P., &amp;amp; Zerbe, O. Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs[https://uni-frankfurt.guentert.science/Reprints/Kooijman20-BRFLYA.pdf .] [http://doi.org/10.1007/s10858-019-00289-7 J. Biomol. NMR 74, 45–60 (2020)]&lt;br /&gt;
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* Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
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* Ikeya, T., Güntert, P., Ito, Y. Protein structure determination in living cells from NOE-derived distance restraints[https://uni-frankfurt.guentert.science/Reprints/Ikeya20-InCellChapterRSC.pdf .] In [http://doi.org/10.1039/9781788013079-00063 In-cell NMR (Eds. Ito, Y., Dötsch, V., Shirakawa, M.), Royal Society of Chemistry, pp. 65–89 (2020)]&lt;br /&gt;
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==== 2019 ====&lt;br /&gt;
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* Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M., Alderson, T. R., Güntert, P. Automatic structure-based NMR methyl resonance assignment in large proteins[https://uni-frankfurt.guentert.science/Reprints/Pritisanac19-MethylFLYA.pdf .] [http://doi.org/10.1038/s41467-019-12837-8 Nat. Commun. 10, 4922 (2019)]&lt;br /&gt;
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* Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P., Böckmann, A., Meier, B. H. Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7[https://uni-frankfurt.guentert.science/Reprints/Torosyan19-Rpo47Assignment.pdf .] [http://doi.org/10.3389/fmolb.2019.00100 Front. Mol. Biosci. 6, 100 (2019)]&lt;br /&gt;
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* Güntert, P. CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert19-CYANA.pdf .] In [http://doi.org/10.1007/978-3-642-35943-9_323-1 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2019)]&lt;br /&gt;
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* Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
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* Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells[https://uni-frankfurt.guentert.science/Reprints/Ikeya19-InCellReview.pdf .] [http://doi.org/10.3390/ijms20102442 Int. J. Mol. Sci. 20, 2442 (2019)]&lt;br /&gt;
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* Möbius, K., Kazemi, S., Güntert, P., Jakob, A., Heckel, A., Becker-Baldus, J. &amp;amp; Glaubitz, C. Global response of diacylglycerol kinase towards substrate binding observed by 2D and 3D MAS NMR[https://uni-frankfurt.guentert.science/Reprints/Moebius19-DGK.pdf .] [http://doi.org/10.1038/s41598-019-40264-8 Sci. Rep. 9, 3995 (2019)]&lt;br /&gt;
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==== 2018 ====&lt;br /&gt;
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* Kobayashi, N., Hattori, Y., Nagata, T., Shinya, S., Güntert, P., Kojima, C. &amp;amp; Fujiwara, T. Noise peak filtering in multi-dimensional NMR spectra using convolutional neural networks[https://uni-frankfurt.guentert.science/Reprints/Kobayashi18-FiltRobot.pdf .] [http://doi.org/10.1093/bioinformatics/bty581 Bioinformatics 34, 4300–4301 (2018)]&lt;br /&gt;
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* Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
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* Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
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* Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
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* Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
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* Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, C., Riek, R., Güntert, P. &amp;amp; Vögeli, B. Extending the applicability of exact nuclear Overhauser enhancements to large proteins and RNA[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOEReview.pdf .] [http://doi.org/10.1002/cbic.201800237 ChemBioChem 19, 1695-1701 (2018)]&lt;br /&gt;
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* Pritišanac, I., Würz, J. M. &amp;amp; Güntert, P. Fully automated assignment of methyl resonances of a 36 kDa protein dimer from sparse NOESY data[https://uni-frankfurt.guentert.science/Reprints/Pritisanac18-ATCase.pdf .] [http://doi.org/10.1088/1742-6596/1036/1/012008 J. Phys Conf. Ser. 1036, 012008 (2018)]&lt;br /&gt;
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* Nichols, P. J., Henen, M. A., Born, A., Strotz, D., Güntert, P. &amp;amp; Vögeli, B. High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints[https://uni-frankfurt.guentert.science/Reprints/Nichols18-eNOERNA.pdf .] [http://doi.org/10.1038/s42003-018-0067-x Comm. Biol. 1, 61 (2018)]&lt;br /&gt;
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* Kniss, A., Schuetz, D., Kazemi, S., Pluska, L., Spindler, P. E., Rogov, V. V., Husnjak, K., Dikic, I., Güntert, P., Sommer, T., Prisner, T. F. &amp;amp; Dötsch, V. Chain assembly and disassembly processes differently affect the conformational space of ubiquitin chains[https://uni-frankfurt.guentert.science/Reprints/Kniss18-UbiquitinChains.pdf .] [http://doi.org/10.1016/j.str.2017.12.011 Structure 26, 249–258 (2018)]&lt;br /&gt;
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* Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
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==== 2017 ====&lt;br /&gt;
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* Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[https://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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* Grytz, C. M., Kazemi, S., Marko, A., Cekan, P., Güntert, P., Sigurdsson, S. Th. &amp;amp; Prisner, T. F. Determination of helix orientations in a flexible DNA by multi-frequency EPR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Grytz17-PeldorDNA.pdf .] [http://doi.org/10.1039/C7CP04997H Phys. Chem. Chem. Phys. 19, 29801-29811 (2017)]&lt;br /&gt;
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* Würz, J. M., Kazemi, S., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. NMR-based automated protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-ReviewArchBiochemBiophys.pdf .] [http://doi.org/10.1016/j.abb.2017.02.011 Arch. Biochem. Biophys. 628, 24-32 (2017)]&lt;br /&gt;
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* Nichols, P., Born, A., Henen, M. A., Strotz, D., Orts, J., Olsson, S., Güntert, P., Riek, R., Chi, C. N. &amp;amp; Vögeli, B. The exact nuclear Overhauser enhancement: recent advances[https://uni-frankfurt.guentert.science/Reprints/Nichols17-eNOEReview.pdf .] [http://doi.org/10.3390/molecules22071176 Molecules 22, 1176 (2017)]&lt;br /&gt;
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* Würz, J. M. &amp;amp; Güntert, P. Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK[https://uni-frankfurt.guentert.science/Reprints/Wuerz17-CYPICK.pdf .] [http://doi.org/10.1007/s10858-016-0084-3 J. Biomol. NMR.  67, 63–76 (2017)]&lt;br /&gt;
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* Kazemi, S., Würz, J. M., Schmidt, E., Bagaria, A. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Kazemi17-ModMagnResonReview.pdf .] In [http://doi.org/10.1007/978-3-319-28275-6_32-1 Modern Magnetic Resonance 2nd Ed. (Ed. G. Webb), Springer (2017)]&lt;br /&gt;
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* Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[https://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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* Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[https://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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==== 2016 ====&lt;br /&gt;
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*Poms, M., Ansorge, P., Martinez-Gill, L., Jurt, S., Gottstein, D., Fracchiolla, K. E., Cohen, L. S., Güntert, P., Mingarro, I., Naider, F. &amp;amp; Zerbe, O. NMR investigation of structures of G-protein coupled receptor folding intermediates[https://uni-frankfurt.guentert.science/Reprints/Poms16-GPCRFragments.pdf .] [http://doi.org/10.1074/jbc.M116.740985 J. Biol. Chem. 291, 27170-27186 (2016)]&lt;br /&gt;
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* Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://doi.org/10.1038/srep38312 Sci. Rep. 6, 38312 (2016)]&lt;br /&gt;
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* Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[https://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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* Ravotti, F., Wälti, M. A., Güntert, P., Meier, B. H., Riek, R. &amp;amp; Böckmann, A. Solid-state NMR sequential assignment of an amyloid-β(1-42) fibril polymorph[https://uni-frankfurt.guentert.science/Reprints/Ravotti16-Abeta42Assignment.pdf .] [http://doi.org/10.1007/s12104-016-9682-y Biomol. NMR Assign. 10, 269-276]&lt;br /&gt;
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* Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril[https://uni-frankfurt.guentert.science/Reprints/Waelti16-Abeta42.pdf .] [http://doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA  113, E4976–E4984 (2016)]&lt;br /&gt;
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* von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[https://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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* Orts, J., Wälti, M. A., Marsh, M., Vera, L., Gossert, A. D., Güntert, P. &amp;amp; Riek, R. NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Orts16-NMR2.pdf .] [http://doi.org/10.1021/jacs.5b12391 J. Am. Chem. Soc. 138, 4393–4400 (2016)]&lt;br /&gt;
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* Ikeya, T., Ikeda, S., Kigawa, T., Ito, Y. &amp;amp; Güntert, P. Protein NMR structure refinement based on Bayesian inference[https://uni-frankfurt.guentert.science/Reprints/Ikeya16-Bayes.pdf .] [http://doi.org/10.1088/1742-6596/699/1/012005 J. Phys. Conf. Ser. 699, 012005 (2016)]&lt;br /&gt;
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* Wiegand, T., Gardiennet, C., Ravotti, F., Bazin, A., Kunert, B., Lacabanne, D., Cadalbert, R., Güntert, P., Terradot, L., Böckmann, A. &amp;amp; Meier, B. H. Solid-state NMR sequential assignments of the N-terminal domain of &#039;&#039;Hp&#039;&#039;DnaB helicase[https://uni-frankfurt.guentert.science/Reprints/Wiegand16-HpDnaBAssignment.pdf .] [http://doi.org/10.1007/s12104-015-9629-8 Biomol. NMR Assign. 10, 13-23 (2016)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Güntert, P. &amp;amp; Riek, R. The exact NOE as an alternative in ensemble structure determination[https://uni-frankfurt.guentert.science/Reprints/Voegeli16-eNOEGB3.pdf .] [http://doi.org/10.1016/j.bpj.2015.11.031 Biophys. J. 110, 113-126 (2016)]&lt;br /&gt;
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==== 2015 ====&lt;br /&gt;
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* Chi, C. N., Vögeli, B., Bibow, S., Strotz, D., Orts, J., Güntert, P. &amp;amp; Riek, R. A structural ensemble of the enzyme cyclophilin in solution reveals an orchestrated mode of action at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Chi15-eNOECyclophilin.pdf .] [http://doi.org/10.1002/anie.201503698 Angew. Chem. Int. Ed. 54, 11657-11661 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEDataInBrief.pdf .] [http://doi.org/10.1016/j.dib.2015.08.020 Data in Brief 5, 99-106 (2015)]&lt;br /&gt;
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* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
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* Güntert, P. &amp;amp; Buchner, L. Combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert15-NoeassignAlgorithm.pdf .] [http://doi.org/10.1007/s10858-015-9924-9 J. Biomol. NMR 62, 453-471 (2015)]&lt;br /&gt;
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* Vögeli, B., Olsson, S., Riek, R. &amp;amp; Güntert, P. Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics[https://uni-frankfurt.guentert.science/Reprints/Voegeli15-eNOEJStructBiol.pdf .] [http://doi.org/10.1016/j.jsb.2015.07.008 J. Struct. Biol. 191, 306-317 (2015)]&lt;br /&gt;
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* Gutmanas, A., Adams, P. D., Bardiaux, B., Berman, H. M., Case, D. A., Fogh, R. H. Güntert, P., Hendrickx, P. M. S., Herrmann, T., Kleywegt, G. J., Kobayashi, N., Lange, O. F., Markley, J. L., Montelione, G. T., Nilges, M., Ragan, T. J., Schwieters, C. D., Tejero, R., Ulrich, E., Velankar, S., Vranken, W. F., Wedell, J., Westbrook, J., Wishart, D. S. &amp;amp; Vuister, G. W. NMR Exchange Format: a unified and open standard for representation of NMR restraint data[https://uni-frankfurt.guentert.science/Reprints/Gutmanas15-NMRExchangeFormat.pdf .] [http://doi.org/10.1038/nsmb.3041 Nat. Struct. Mol. Biol. 22, 433–434 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Systematic evaluation of combined automated NOE assignment and structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Buchner15-NoeassignEvaluation.pdf .] [http://doi.org/10.1007/s10858-015-9921-z J. Biomol. NMR 62, 81–95 (2015)]&lt;br /&gt;
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* Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[https://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173–180 (2015)]&lt;br /&gt;
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* Buchner, L. &amp;amp; Güntert, P. Increased reliability of NMR protein structures by consensus structure bundles[https://uni-frankfurt.guentert.science/Reprints/Buchner15-ConsensusBundles.pdf .] [http://doi.org/10.1016/j.str.2014.11.014 Structure 23, 425–434 (2015)]&lt;br /&gt;
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* Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P. &amp;amp; Ito, Y. Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins[https://uni-frankfurt.guentert.science/Reprints/Shigemitsu15-MaximumEntropy.pdf .] [http://doi.org/10.1016/j.bbrc.2014.12.088 Biochem. Biophys. Res. Comm. 457, 200–205 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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* Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R. &amp;amp; Meier, B. H. Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation[https://uni-frankfurt.guentert.science/Reprints/Schuetz15-AbetaDeutsch.pdf .] [http://doi.org/10.1002/ange.201408598 Angew. Chem. 127, 337–342 (2015)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Automated structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Schmidt15-AutomatedNMR.pdf .] [http://doi.org/10.1007/978-1-4939-2230-7_16 Meth. Mol. Biol. 1261, 303–329 (2015)]&lt;br /&gt;
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==== 2014 ====&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Kirchner, D. K. &amp;amp; Güntert, P. Influence of NMR data completeness on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin14-Homodimer.pdf .] [http://doi.org/10.1002/jccs.201400095 J. Chin. Chem. Soc. 61, 1297-1306 (2014)]&lt;br /&gt;
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* Schmidt, E., Ikeya, T., Takeda, M., Löhr, F., Buchner, L., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Automated resonance assignment of the 21 kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA[https://uni-frankfurt.guentert.science/Reprints/Schmidt14-SAILDsbA.pdf .] [http://doi.org/10.1016/j.jmr.2014.10.005 J. Magn. Reson. 249, 88–93 (2014)]&lt;br /&gt;
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* Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[https://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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* Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[https://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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* Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[https://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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* Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[https://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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* Krähenbühl, B., El Bakkali, I., Schmidt, E., Güntert, P. &amp;amp; Wider, G. Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments[https://uni-frankfurt.guentert.science/Reprints/Kraehenbuehl14-APSYFLYA.pdf .] [http://doi.org/10.1007/s10858-014-9829-z J. Biomol. NMR 59, 87-93 (2014)]&lt;br /&gt;
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* Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[https://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Chi, C., Minges, M., Wälti, M. A., Güntert, P. &amp;amp; Riek, R. Towards a true protein movie: A perspective on the potential impact of the ensemble-based structure determination using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli14-eNOE.pdf .] [http://doi.org/10.1016/j.jmr.2013.11.016 J. Magn. Reson. 241, 53-59 (2014)]&lt;br /&gt;
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* Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[https://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V., Dötsch, V. &amp;amp; Güntert, P. Peak picking NMR spectral data using non-negative matrix factorization[https://uni-frankfurt.guentert.science/Reprints/Tikole14-PeakPickingByNMF.pdf .] [http://doi.org/10.1186/1471-2105-15-46 BMC Bioinformatics 15, 46 (2014)]&lt;br /&gt;
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==== 2013 ====&lt;br /&gt;
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* Orts, J., Vögeli, B., Riek, R. &amp;amp; Güntert, P. Stereospecific assignments in proteins using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Orts13-eNOEStereoassignment.pdf .] [http://doi.org/10.1007/s10858-013-9780-4 J. Biomol. NMR 57, 211-218 (2013)]&lt;br /&gt;
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* Aeschbacher, T., Schmidt, E., Blatter, M., Maris, C., Duss, O., Allain, F. H.-T., Güntert, P. &amp;amp; Schubert, M. Automated and assisted RNA resonance assignment using NMR chemical shift statistics[https://uni-frankfurt.guentert.science/Reprints/Aeschbacher13-RNAFLYA.pdf .] [http://doi.org/10.1093/nar/gkt665 Nucl. Acids Res. 41, e172 (2013)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. Reliability of exclusively NOESY-based automated resonance assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-NOESYFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9779-x J. Biomol. NMR 57, 193-204 (2013)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V. &amp;amp; Güntert, P. Estimating structure quality trends in the Protein Data Bank by equivalent resolution[https://uni-frankfurt.guentert.science/Reprints/Bagaria13-EquivalentResolution.pdf .] [http://doi.org/10.1016/j.compbiolchem.2013.04.004 Comp. Biol. Chem. 46, 8–15 (2013)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Orekhov, V. Yu. &amp;amp; Güntert, P. Effects of NMR spectral resolution on protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Tikole13-NMRResolution.pdf .] [http://doi.org/10.1371/journal.pone.0068567 PLoS ONE 8, e68567 (2013)]&lt;br /&gt;
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* Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[https://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
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* Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
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* Montelione, G. T., Nilges, M., Bax, A., Güntert, P., Herrmann, T., Richardson, J. S., Schwieters, C., Vranken, W. F., Vuister, G. W., Wishart, D. S., Berman, H. M., Kleywegt, G. J. &amp;amp; Markley, J. L. Recommendations of the wwPDB NMR Validation Task Force[https://uni-frankfurt.guentert.science/Reprints/Montelione13-NMRVTFRecommendations.pdf .] [http://doi.org/10.1016/j.str.2013.07.021 Structure 21, 1563–1570 (2013)]&lt;br /&gt;
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* Schmidt, E., Gath, J., Habenstein, B., Ravotti, F., Székely, K., Huber, M., Buchner, L., Böckmann, A., Meier, B. H. &amp;amp; Güntert, P. Automated solid-state NMR resonance assignment of protein microcrystals and amyloids[https://uni-frankfurt.guentert.science/Reprints/Schmidt13-SolidStateFLYA.pdf .] [http://doi.org/10.1007/s10858-013-9742-x J. Biomol. NMR 56, 243–254 (2013)]&lt;br /&gt;
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* Hefke, F. &amp;amp; Güntert, P. Prediction of peak overlap in NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Hefke13-OverlapPrediction.pdf .] [http://doi.org/10.1007/s10858-013-9727-9 J. Biomol. NMR 56, 113–123 (2013)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C, and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignment of the dsRBDs of mouse RNA helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata13-dsRBDAssignment.pdf .] [http://doi.org/10.1007/s12104-012-9380-3 Biomol. NMR Assign. 7, 69–72 (2013)]&lt;br /&gt;
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* Buchner, L., Schmidt, E. &amp;amp; Güntert, P. Peakmatch: a simple and robust method for peak list matching[https://uni-frankfurt.guentert.science/Reprints/Buchner13-Peakmatch.pdf .] [http://doi.org/10.1007/s10858-013-9708-z J. Biomol. NMR. 55, 267–277 (2013)]&lt;br /&gt;
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* Vögeli, B., Güntert, P., &amp;amp; Riek, R. Multiple-state ensemble structure determination from eNOE spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Voegeli13-eNOEMultipleStates.pdf .] [http://doi.org/10.1080/00268976.2012.728257 Mol. Phys. 111, 437–454 (2013)]&lt;br /&gt;
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* Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[https://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
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* Güntert, P. CYANA. In [http://www.springer.com/life+sciences/biochemistry+%26+biophysics/book/978-3-642-16711-9 Encyclopedia of Biophysics (Ed. G. Roberts), Springer, New York (2013)]&lt;br /&gt;
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==== 2012 ====&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Jurkša, S., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar12-WeNMR.pdf .] [http://doi.org/10.1007/s10723-012-9246-z J. Grid. Comput. 10, 743-767 (2012)]&lt;br /&gt;
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* Vögeli, B., Orts, J., Strotz, D., Güntert, P. &amp;amp; Riek, R. Discrete three-dimensional representation of macromolecular motion from eNOE-based ensemble calculation[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsCHIMIA.pdf .] [http://www.ingentaconnect.com/content/scs/chimia/2012/00000066/00000010/art00011 Chimia 66, 787-790 (2012)]&lt;br /&gt;
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* He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[https://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
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* Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
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* Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[https://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://doi.org/10.1038/nsmb.2355 Nat. Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
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* Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[https://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
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* Schmidt, E. &amp;amp; Güntert, P. A new algorithm for reliable and general NMR resonance assignment[https://uni-frankfurt.guentert.science/Reprints/Schmidt12-AssignmentAlgorithm.pdf .] [http://doi.org/10.1021/ja305091n J. Am. Chem. Soc. 134, 12817–12829 (2012)]&lt;br /&gt;
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* Lin, Y. J., Kirchner, D. K. &amp;amp; Güntert, P. Influence of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins[https://uni-frankfurt.guentert.science/Reprints/Lin12-Homodimer.pdf .] [http://doi.org/10.1016/j.jmr.2012.07.001 J. Magn. Reson. 222, 96–104 (2012)]&lt;br /&gt;
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* Gottstein, D., Reckel, S., Dötsch, V. &amp;amp; Güntert, P. Requirements on paramagnetic relaxation enhancement data for α-helical membrane protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-PREs.pdf .] [http://doi.org/10.1016/j.str.2012.03.010 Structure 20, 1019-1027 (2012)]&lt;br /&gt;
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* Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[https://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
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* Tikole, S., Jaravine, V., Rogov, V. V., Rozenknop, A., Schmöe, K., Löhr, F., Dötsch, V. &amp;amp; Güntert, P. Fast automated NMR spectroscopy of short-lived biological samples[https://uni-frankfurt.guentert.science/Reprints/Tikole12-FastNMRofShortLivedSamples.pdf .] [http://doi.org/10.1002/cbic.201200044 ChemBioChem 13, 964–967 (2012)]&lt;br /&gt;
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* Rogov, V. V., Rozenknop, A., Rogova, N. Y., Löhr, F., Tikole, S., Jaravine, V., Güntert, P., Dikic, I. &amp;amp; Dötsch, V. A universal expression tag for structural and functional studies of proteins[https://uni-frankfurt.guentert.science/Reprints/Rogov12-UniversalExpressionTag.pdf .] [http://doi.org/10.1002/cbic.201200045 ChemBioChem 13, 959–963 (2012)]&lt;br /&gt;
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* Gottstein, D., Kirchner, D. K. &amp;amp; Güntert, P. Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space[https://uni-frankfurt.guentert.science/Reprints/Gottstein12-REGMEAN.pdf .] [http://doi.org/10.1007/s10858-012-9615-8 J. Biomol. NMR 52, 351-364 (2012)]&lt;br /&gt;
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* Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[https://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
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* He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[https://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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* Rosato, A., Aramini, J. M., Arrowsmith, C., Bagaria, A., Baker, D., Cavalli, A., Doreleijers, J. F., Eletsky, A., Giachetti, A., Guerry, P., Gutmanas, A., Güntert, P., He. Y. F., Herrmann, T., Huang, Y. J., Jaravine, V., Jonker, H. R. A., Kennedy, M. A., Lange, O. F., Liu, G., Malliavin, T. E., Mani, R., Mao, B., Montelione, G. T., Nilges, M., Rossi, P., van der Schot, G., Schwalbe, H., Szyperski, T., Vendruscolo, M., Vernon, R., Vranken, W. F., de Vries, S., Vuister, G. W., Wu, B., Yang, Y. &amp;amp; Bonvin, A. M. J. J. Blind testing of routine, fully automated determination of protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato12-CASDNMR.pdf .] [http://doi.org/10.1016/j.str.2012.01.002 Structure 20, 227–236 (2012)]&lt;br /&gt;
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* Bagaria, A., Jaravine, V., Huang, Y. J., Montelione, G. T. &amp;amp; Güntert, P. Protein structure validation by generalized linear model RMSD prediction[https://uni-frankfurt.guentert.science/Reprints/Bagaria12-RMSDPrediction.pdf .] [http://doi.org/10.1002/pro.2007 Protein Sci. 21, 229–238 (2012)]&lt;br /&gt;
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==== 2011 ====&lt;br /&gt;
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* Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[https://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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* Wassenaar, T. A., van Dijk, M., Loureiro-Ferreira, N., van der Schot, G., de Vries, S. J., Schmitz, C., van der Zwan, J., Boelens, R., Giachetti, A., Ferella, L., Rosato, A., Bertini, I., Herrmann, T., Jonker, H. R. A., Bagaria, A., Jaravine, V., Güntert, P., Schwalbe, H., Vranken, W. F., Doreleijers, J. F., Vriend, G., Vuister, G. W., Franke, D., Kikhney, A., Svergun, D. I., Fogh, R., Ionides, J., Laue, E. D., Spronk, C., Verlato, M., Badoer, S., Dal Pra, S., Mazzucato, M., Frizziero, E. &amp;amp; Bonvin, A. M. J. J. WeNMR: Structural biology on the Grid[https://uni-frankfurt.guentert.science/Reprints/Wassenaar11-WeNMR-IWSG2011.pdf .] [http://ceur-ws.org/Vol-819 Proceedings of IWSG-Life2011 (2011)]&lt;br /&gt;
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* Cohen, L. S., Arshava, B., Neumoin, A., Becker, J. M., Güntert, P., Zerbe, O. &amp;amp; Naider, F. Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments[https://uni-frankfurt.guentert.science/Reprints/Cohen11-Ste2p.pdf .] [http://doi.org/10.1016/j.bbamem.2011.07.011 Biochim. Biophys. Acta 1808, 2674–2684 (2011)]&lt;br /&gt;
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* Güntert, P. Calculation of structures from NMR restraints[https://uni-frankfurt.guentert.science/Reprints/Guntert11-WileyBookChapter.pdf .] In [http://doi.org/10.1002/9781119972006.ch5 Protein NMR Spectroscopy: Practical Techniques and Applications (Eds. G. Roberts &amp;amp; L.-Y. Lian), Wiley, New York, pp. 159–192 (2011)]&lt;br /&gt;
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* Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[https://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)]&lt;br /&gt;
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* Kirchner, D. K. &amp;amp; Güntert, P. Objective identification of residue ranges for the superposition of protein structures[https://uni-frankfurt.guentert.science/Reprints/Kirchner11-CYRANGE.pdf .] [http://doi.org/10.1186/1471-2105-12-170 BMC Bioinformatics 12, 170 (2011)]&lt;br /&gt;
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* Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[https://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)]&lt;br /&gt;
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* Ikeya, T., Jee. J. G., Shigemitsu, Y., Hamatsu, J., Mishima, M., Ito, Y., Kainosho, M. &amp;amp; Güntert, P. Exclusively NOESY-based automated NMR assignment and structure determination of proteins[https://uni-frankfurt.guentert.science/Reprints/Ikeya11-NOESYonly.pdf .] [http://doi.org/10.1007/s10858-011-9502-8 J. Biomol. NMR 50, 137–146 (2011)]&lt;br /&gt;
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* Knehans, T., Schüller, A., Doan, D. N., Nacro, K., Hill, J., Güntert, P., Madhusudhan, M.S, Weil, T. &amp;amp; Vasudevan, S. G. Structure-guided fragment-based in silico drug design of dengue protease inhibitors[https://uni-frankfurt.guentert.science/Reprints/Knehans11-DengueProtease.pdf .] [http://doi.org/10.1007/s10822-011-9418-0 J. Comput. Aided Mol. Des. 25, 263–274 (2011)]&lt;br /&gt;
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* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert11-AutomatedNMR.pdf .] In [http://doi.org/10.3233/978-1-60750-695-9-338 Advances in Biomedical Spectroscopy. Volume 3: Biomolecular NMR Spectroscopy (Eds. A. Dingley &amp;amp; S. Pascal), IOS Press, Amsterdam, pp. 338–365 (2011)]&lt;br /&gt;
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* Hefke, F., Bagaria, A., Reckel, S., Ullrich, S. J., Dötsch, V., Glaubitz, C. &amp;amp; Güntert, P. Optimization of amino acid type- specific &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm[https://uni-frankfurt.guentert.science/Reprints/Hefke11-UPLABEL.pdf .] [http://doi.org/10.1007/s10858-010-9462-4 J. Biomol. NMR 49, 75-84 (2011)]&lt;br /&gt;
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* Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[https://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)]&lt;br /&gt;
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* Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[https://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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* Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[https://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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* He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[https://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)]&lt;br /&gt;
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* Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[https://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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* Elgán, T.H., Planson, A.G., Beckwith, J., Güntert, P. &amp;amp; Berndt, K.D. Determinants of activity in glutaredoxins: an &#039;&#039;in vitro&#039;&#039; evolved Grx1-like variant of &#039;&#039;Escherichia coli&#039;&#039; Grx3[https://uni-frankfurt.guentert.science/Reprints/Elgan_BiochemJ_2010.pdf .] [http://doi.org/10.1042/BJ20100289 Biochem. J. 430, 487-495 (2010)]&lt;br /&gt;
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* Loureiro-Ferreira, N., Wassenaar, T. A., de Vries, S. J., van Dijk, M., van der Schot, G., van der Zwan, J., Boelens, R., Giachetti, A., Carotenuto, D., Rosato, A., Bertini, I., Herrmann, T., Bagaria, A., Zharavin, V., Jonker, H. R. A., Güntert, P., Schwalbe, H., Vranken, W. F., Dal Pra, S., Mazzucato, M., Frizziero, E., Traldi, S., Verlato, M. &amp;amp; Bonvin, A. M. J. J. e-NMR gLite grid enabled infrastructure[https://uni-frankfurt.guentert.science/Reprints/Loureiro10-Ibergrid-eNMR.pdf .] In [http://www.netbiblo.com/content/j8828w/ IBERGRID 4th Iberian Grid Infrastructure Conference Proceedings] (Eds. A. Proença, A. Pina, J. García Tobío &amp;amp; L. Ribeiro), Netbiblo, La Coruña, Spain, pp. 360–382 (2010)&lt;br /&gt;
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* Ikeya, T., Sasaki, A., Sakakibara, D., Shigemitsu, Y., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Nietlisbach, D., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. NMR protein structure determination in living &#039;&#039;E. coli&#039;&#039; cells using nonlinear sampling[https://uni-frankfurt.guentert.science/Reprints/Ikeya10-InCellProtocol.pdf .] [http://doi.org/10.1038/nprot.2010.69 Nat. Protocols 5, 1051–1060 (2010)]&lt;br /&gt;
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* Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[https://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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==== 2009 ====&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. SAIL – Stereo-array isotope labeling[https://uni-frankfurt.guentert.science/Reprints/Kainosho10-SAILQRB.pdf .] [http://doi.org/10.1017/S0033583510000016 Q. Rev. Biophys. 42, 247-300 (2009)]&lt;br /&gt;
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* Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[https://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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* He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the &#039;&#039;Drosophila&#039;&#039; Neuralized E3 ligase in the Notch signaling pathway[https://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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* Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H. &amp;amp; Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[https://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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* Rosato, A., Bagaria, A., Baker, D., Bardiaux, B., Cavalli, A., Doreleijers, J. F., Giachetti, A., Guerry, P., Güntert, P., Herrmann, T., Huang, Y. J., Jonker, H. R. A., Mao, B., Malliavin, T. E., Montelione, G. T., Nilges, M., Raman, S., van der Schot, G., Vranken, W., Vuister, G. W. &amp;amp; Bonvin, A. M. J. J. CASD-NMR: a rolling experiment for the critical assessment of automated structure determination of proteins from NMR data[https://uni-frankfurt.guentert.science/Reprints/Rosato09-CASDNMR.pdf .] [http://doi.org/10.1038/nmeth0909-625 Nat. Meth. 6, 625–626 (2009)]&lt;br /&gt;
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* Ikeya, T., Takeda, M., Yoshida, H., Terauchi, T., Jee, J., Kainosho, M. &amp;amp; Güntert, P. Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system[https://uni-frankfurt.guentert.science/Reprints/Ikeya09-SAILUbiquitin.pdf .]  [http://doi.org/10.1007/s10858-009-9339-6 J. Biomol. NMR 44, 261-272 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Tsuda09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[https://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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* Ito, Y. &amp;amp; Güntert, P. Seeing proteins in living cells[https://uni-frankfurt.guentert.science/Reprints/Ito09-SeeingProteinsInLivingCells.pdf .] [http://corporate.gitverlag.com/media/blaetterkatalog/bfe/2009-5/ BIOforum Europe 13(5), 25–27 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Sakakibara09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[https://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Peroza09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[https://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;He09_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[https://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated structure determination from NMR Spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert09-AutomatedStructureDeterminationReview.pdf .] [http://doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]&lt;br /&gt;
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* Schmucki, R., Yokoyama, S. &amp;amp; Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm[https://uni-frankfurt.guentert.science/Reprints/Schmucki09-DYNASSIGN.pdf .] [http://doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR 43, 97-109 (2009)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi09&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[https://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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==== 2008 ====&lt;br /&gt;
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* Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR[https://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[https://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[https://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Koglin08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nagata08&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease has a non-canonical binding site for mRNA cap analog recognition[https://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
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* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins[https://uni-frankfurt.guentert.science/Reprints/Reckel08-TransmembraneLabeling.pdf .] [http://doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako08_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[https://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
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==== 2007 ====&lt;br /&gt;
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* Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. NMRによる蛋白質構造決定の自動化. In 計算シミュレーションと分析データ解析[https://uni-frankfurt.guentert.science/Reprints/Ikeya07-MaruzenBookChapter.pdf .] Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Takeda07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Takeda, M., Ikeya, T., Güntert, P. &amp;amp; Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method[https://uni-frankfurt.guentert.science/Reprints/Takeda07-SAILProtocol.pdf .] [http://doi.org/10.1038/nprot.2007.423 Nat. Protocols 2, 2896–2902 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kobayashi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies[https://uni-frankfurt.guentert.science/Reprints/Kobayashi07-Kujira.pdf .] [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]&lt;br /&gt;
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* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[https://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA 104, 9236–9241 (2007)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ohnishi07&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[https://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
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==== 2006 ====&lt;br /&gt;
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* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[https://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Kuwasako06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[https://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
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* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[https://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
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* Kainosho, M. &amp;amp; Güntert, P. 高分子量タンパク質のNMR構造決定-より速く、より正確に: タンパク質NMRの常識を覆す革新技術SAIL法. Stereo-array isotope labeling for faster and more accurate NMR structure determinations of high molecular weight proteins. Biotechnology J. (Tokyo) 6, 467–470 (2006) (in Japanese)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., López-Méndez, B. &amp;amp; Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra[http://www.guentert.com/Intranet/Reprints/Scott06a.pdf .] [http://doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]&lt;br /&gt;
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* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA[https://uni-frankfurt.guentert.science/Reprints/Ikeya06a.pdf .] [http://doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hamada06&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[https://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
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* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[https://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
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* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
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* Güntert, P. Symbolic NMR product operator calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert06a.pdf .] [http://doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]&lt;br /&gt;
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==== 2005 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Li05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[https://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
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* Lin, Y. J. &amp;amp; Güntert, P. 利用核磁共振光譜自動化決定蛋白質在水溶液中的三度空間結構. Automated 3D structure determination of proteins in solution using NMR spectra. [http://www.itrc.org.tw/Publication/Bimonthly/Content/abstract.php?articleid=026060870 Instruments Today 146, 87–93 (2005)] (in Chinese)&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR 31, 351–356 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[https://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR 31, 357–361 (2005)]&lt;br /&gt;
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* Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., Ulrich, E. L., Kaptein, R. &amp;amp; Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank[https://uni-frankfurt.guentert.science/Reprints/Nederveen05a.pdf .] [http://doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[https://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://doi.org/10.1110/ps.04975305 Protein Sci. 14, 756–764 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lysek05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[https://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[https://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda05&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[https://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://doi.org/10.1110/ps.041138705 Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
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==== 2004 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Scott04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES[https://uni-frankfurt.guentert.science/Reprints/Scott04a.pdf .] [http://doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Nameki04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[https://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR structure calculation with CYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert04a.pdf .] [http://doi.org/10.1385/1-59259-809-9:353 Meth. Mol. Biol. 278, 353–378 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;López-Méndez04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* López-Méndez, B., Pantoja-Uceda, D., Tomizawa, T., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Lopez04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019239.44783.66 J. Biomol. NMR 29, 205–206 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pantoja-Uceda04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Kigawa, T., Shirouzu, M., Terada, T., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Hirota, H., Yoshida, M., Tanaka, A., Osanai, T., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from &#039;&#039;Arabidopsis thaliana&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pantoja04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Fernández04&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
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* Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. Assignments of &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonances of the bacteriophage λ capsid stabilizing protein gpD[https://uni-frankfurt.guentert.science/Reprints/Iwai04a.pdf .] [http://doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol NMR 28, 89–90 (2004)]&lt;br /&gt;
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==== 2003 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. Automated NMR protein structure calculation[https://uni-frankfurt.guentert.science/Reprints/Guntert03a.pdf .] [http://doi.org/10.1016/S0079-6565(03)00021-9 Prog. NMR Spectrosc. 43, 105–125 (2003)]&lt;br /&gt;
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* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[https://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Jee03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Jee, J. G. &amp;amp; Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment[https://uni-frankfurt.guentert.science/Reprints/Jee03.pdf .] [http://doi.org/10.1023/A:1026122726574 J. Struct. Funct. Genom. 4, 179–189 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Hilge03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[https://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://doi.org/10.1038/nsb924 Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
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* Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[https://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Zahn03&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[https://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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==== 2002 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS[https://uni-frankfurt.guentert.science/Reprints/Herrmann02b.pdf .] [http://doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Structure calculation using automated techniques[https://uni-frankfurt.guentert.science/Reprints/Guntert02-StructureCalculationUsingAutomatedTechniques.pdf .] Meth. Principles Med. Chem. 16, 39–66 (2002)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Enggist02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[https://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Lee02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[https://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard02&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Herrmann02_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
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* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[https://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
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==== 2001 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Horst01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[https://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Güntert, P., Döbeli, H., Wipf, B. &amp;amp; Wüthrich, K. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1–40)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt; and Aβ(1– 42)&amp;lt;sup&amp;gt;ox&amp;lt;/sup&amp;gt;[https://uni-frankfurt.guentert.science/Reprints/Riek01.pdf .] [http://doi.org/10.1046/j.0014-2956.2001.02537.x Eur. J. Biochem. 268, 5930–5936 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations[https://uni-frankfurt.guentert.science/Reprints/Guntert01.pdf .] [http://doi.org/10.1016/S0010-4655(01)00204-1 Comp. Phys. Comm. 138, 155–169 (2001)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Ellgaard01&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[https://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
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==== 2000 ====&lt;br /&gt;
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* Güntert, P., Salzmann, M., Braun, D. &amp;amp; Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER[https://uni-frankfurt.guentert.science/Reprints/Guntert00.pdf .] [http://doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Calzolai00&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[https://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
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* Koradi, R., Billeter, M. &amp;amp; Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation[https://uni-frankfurt.guentert.science/Reprints/Koradi00.pdf .] [http://doi.org/10.1016/S0010-4655(99)00436-1 Comp. Phys. Comm. 124, 139–147 (2000)]&lt;br /&gt;
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==== 1999 ====&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Riek99&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[https://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
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* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. [http://www.speedup.ch/journal/SpeedupJournal12-2.html Speedup J. 12, 47–52 (1999)]&lt;br /&gt;
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==== 1998 ====&lt;br /&gt;
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* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. &amp;amp; Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND[https://uni-frankfurt.guentert.science/Reprints/Guntert98b.pdf .] [http://doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]&lt;br /&gt;
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* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. &amp;amp; Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics[https://uni-frankfurt.guentert.science/Reprints/Banci98.pdf .] [http://doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]&lt;br /&gt;
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* Koradi, R., Billeter, M., Engeli, M., Güntert, P. &amp;amp; Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY[https://uni-frankfurt.guentert.science/Reprints/Koradi98.pdf .] [http://doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]&lt;br /&gt;
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* Güntert, P. Structure calculation of biological macromolecules from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert98a.pdf .] [http://journals.cambridge.org/action/displayAbstract?aid=26555 Q. Rev. Biophys. 31, 145–237 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://doi.org/10.1038/2325 Nat. Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Pellecchia98_1&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. Sequence-specific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N and &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C assignments of the periplasmic chaperone FimC from &#039;&#039;Escherichia coli&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Pellecchia98a.pdf .] [http://doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]&lt;br /&gt;
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==== 1997 ====&lt;br /&gt;
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* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. &amp;amp; Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Billeter97-MDSimulationsCSCS.pdf .] Crosscuts 6, 19–21 (1997)&lt;br /&gt;
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* Mumenthaler, C., Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Mumenthaler97.pdf .] [http://doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Güntert97_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
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* Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[https://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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* Güntert, P. Calculating protein structures from NMR data[https://uni-frankfurt.guentert.science/Reprints/Guntert97-CalculatingProteinStructuresFromNMRData.pdf .] Meth. Mol. Biol. 60, 157–194 (1997)&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Bartels97&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra[https://uni-frankfurt.guentert.science/Reprints/Bartels97.pdf .] [http://doi.org/10.1002/(SICI)1096-987X(19970115)18:1&amp;amp;#60;139::AID-JCC13&amp;amp;#62;3.0.CO;2-H J. Comp. Chem. 18, 139–149 (1997)]&lt;br /&gt;
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==== 1996 ====&lt;br /&gt;
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* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. &amp;amp; Wider, G. NMR studies of hydration of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Wuthrich96-NMRStudiesOfHydration.pdf .] [http://doi.org/10.1039/FD9960300245 Faraday Discuss. 103, 245–253 (1996)]&lt;br /&gt;
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* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. &amp;amp; von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment[https://uni-frankfurt.guentert.science/Reprints/Arbenz96-OPALSciddlePVM.pdf .] Lecture Notes in Computer Science 1156, 142–149 (1996)&lt;br /&gt;
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* Luginbühl, P., Güntert, P., Billeter, M. &amp;amp; Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Luginbuhl96-OPAL.pdf .] [http://doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]&lt;br /&gt;
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* Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[https://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://doi.org/10.1038/nsb0896-662 Nat. Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&amp;lt;span id=&amp;quot;Billeter96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Bartels96&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Bartels, C., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT[https://uni-frankfurt.guentert.science/Reprints/Bartels96.pdf .] [http://doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water[https://uni-frankfurt.guentert.science/Reprints/Berndt96a.pdf .] [http://doi.org/10.1002/(SICI)1097-0134(199603)24:3&amp;amp;#60;304::AID-PROT3&amp;amp;#62;3.0.CO;2-G Proteins 24, 304–313 (1996)]&lt;br /&gt;
&lt;br /&gt;
==== 1995 ====&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Güntert, P. &amp;amp; Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals[https://uni-frankfurt.guentert.science/Reprints/Bartels95-IFLAT.pdf .] [http://doi.org/10.1006/jmra.1995.0780 J. Magn. Reson. A 117, 330–333 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. &amp;amp; van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations[https://uni-frankfurt.guentert.science/Reprints/Brunne95-BPTILongTermMD.pdf .] [http://doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules[https://uni-frankfurt.guentert.science/Reprints/Bartels95-XEASY.pdf .] [http://doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
==== 1994 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Computer–supported protein structure determination by NMR[https://uni-frankfurt.guentert.science/Reprints/Guntert94-StructureDeterminationChapter.pdf .] In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)&lt;br /&gt;
&lt;br /&gt;
* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
==== 1993 ====&lt;br /&gt;
&lt;br /&gt;
* Wüthrich, K., Güntert, P. &amp;amp; Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors[https://uni-frankfurt.guentert.science/Reprints/Wuthrich93-NMRProteaseInhibitors.pdf .] In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[https://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Berndt, K. D. &amp;amp; Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination[https://uni-frankfurt.guentert.science/Reprints/Guntert93c.pdf .] [http://doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Schaefer, N., Otting, G. &amp;amp; Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism[https://uni-frankfurt.guentert.science/Reprints/Guntert93-POMA.pdf .] [http://doi.org/10.1006/jmra.1993.1016 J. Magn. Reson. A 101, 103–105 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. &amp;amp; Wüthrich, K. Protein dynamics studied by rotating frame &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N spin relaxation times[https://uni-frankfurt.guentert.science/Reprints/Szyperski93.pdf .] [http://doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz[https://uni-frankfurt.guentert.science/Reprints/Guntert93a.pdf .] [http://e-collection.ethbib.ethz.ch/show?type=diss&amp;amp;nr=10135 Ph.D. Thesis ETH 10135 (1993)]&lt;br /&gt;
&lt;br /&gt;
==== 1992 ====&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. &amp;amp; Wüthrich, K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the NMR solution structure of hirudin(1–51)[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinContacts.pdf .] [http://doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;span id=&amp;quot;Güntert92_2&amp;quot;&amp;gt;&amp;lt;/span&amp;gt;&lt;br /&gt;
* Güntert, P., Dötsch, V., Wider, G. &amp;amp; Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA[https://uni-frankfurt.guentert.science/Reprints/Guntert92b.pdf .] [http://doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[https://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Szyperski, T., Güntert, P., Otting, G. &amp;amp; Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets[https://uni-frankfurt.guentert.science/Reprints/Szyperski92-INFIT.pdf .] [http://doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Guntert92-FLATT.pdf .] [http://doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]&lt;br /&gt;
&lt;br /&gt;
==== 1991 ====&lt;br /&gt;
&lt;br /&gt;
* Mertz, J. E., Güntert, P., Wüthrich, K. &amp;amp; Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities[https://uni-frankfurt.guentert.science/Reprints/Mertz91-RelaxationMatrixRefinementDIANA.pdf .] [http://doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Eccles, C., Güntert, P., Billeter, M. &amp;amp; Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY[https://uni-frankfurt.guentert.science/Reprints/Eccles91.pdf .] [http://doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P. &amp;amp; Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints[https://uni-frankfurt.guentert.science/Reprints/Guntert91c.pdf .] [http://doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
==== 1989 ====&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W., Billeter, M. &amp;amp; Wüthrich, K. Automated stereospecific &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H NMR assignments and their impact on the precision of protein structure determinations in solution[https://uni-frankfurt.guentert.science/Reprints/Guntert89.pdf .] [http://doi.org/10.1021/ja00193a036 J. Am. Chem. Soc. 111, 3997–4004 (1989)]&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!--&lt;br /&gt;
== Selected publications ==&lt;br /&gt;
&lt;br /&gt;
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[https://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[https://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[https://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
* López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[https://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
* Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[https://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
* Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA[https://uni-frankfurt.guentert.science/Reprints/Herrmann02a.pdf .] [http://doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[https://uni-frankfurt.guentert.science/Reprints/Guntert97b.pdf .] [http://doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;br /&gt;
&lt;br /&gt;
* Billeter, M., Güntert, P., Luginbühl, P. &amp;amp; Wüthrich, K. Hydration and DNA recognition by homeodomains[https://uni-frankfurt.guentert.science/Reprints/Billeter96.pdf .] [http://doi.org/10.1016/S0092-8674(00)81306-9 Cell 85, 1057–1065 (1996)]&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Braun, W. &amp;amp; Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA[https://uni-frankfurt.guentert.science/Reprints/Guntert91a.pdf .] [http://doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== All publications ==&lt;br /&gt;
--&amp;gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59318</id>
		<title>XEASY</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59318"/>
		<updated>2026-01-25T11:33:21Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;  X windows version of ETH automated spectroscopy   &#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
XEASY is a program for interactive, computer-supported NMR spectrum analysis. It is the successor of [[EASY]], the first program package for the interactive analysis of multidimensional NMR spectra that was developed in the group of Prof. K. Wüthrich at ETH Zürich.    &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
XEASY is currently not available.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [[Media:XeasyManual.pdf|Manual (PDF)]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. [http://dx.doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with XEASY must cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59317</id>
		<title>XEASY</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59317"/>
		<updated>2026-01-25T11:32:51Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;  X windows version of ETH automated spectroscopy   &#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
XEASY is a program for interactive, computer-supported NMR spectrum analysis. It is the successor of [[EASY]], the first program package for the interactive analysis of multidimensional NMR spectra that was developed within the group of Prof. K. Wüthrich at ETH Zürich.    &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
XEASY is currently not available.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [[Media:XeasyManual.pdf|Manual (PDF)]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. [http://dx.doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with XEASY must cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59316</id>
		<title>Software</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59316"/>
		<updated>2026-01-25T11:32:01Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Software developed by P. Güntert and collaborators.&lt;br /&gt;
&lt;br /&gt;
== Available software == &lt;br /&gt;
&lt;br /&gt;
* [[ARTINA]]: Artificial intelligence for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[ATNOS]]: Automated NOESY peak picking&lt;br /&gt;
&lt;br /&gt;
* [[AUTOPSY]]: Automated peak picking in NMR spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[CANDID]]: Combined automated NOE assignment and structure determination module&lt;br /&gt;
&lt;br /&gt;
* [[Chess2FLYA]]: Chemical shift statistics to FLYA&lt;br /&gt;
&lt;br /&gt;
* [[COCO]]: Compare covalent geometry&lt;br /&gt;
&lt;br /&gt;
* [[COFIMA]]: Coordinate and constraint file manipulation&lt;br /&gt;
&lt;br /&gt;
* [http://www.cyana.org/wiki CYANA]: Combined assignment and dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[CYLIB]]: CYANA library entry preparation from mmCIF or Mol2 files &lt;br /&gt;
&lt;br /&gt;
* [https://uni-frankfurt.guentert.science/cyrange CYRANGE]: Determination of optimum residue ranges for the superposition of protein structures&lt;br /&gt;
&lt;br /&gt;
* [[GARANT]]: General algorithm for resonance assignment&lt;br /&gt;
&lt;br /&gt;
* [[INFIT]]: Coupling constants from inverse Fourier transformation of in-phase multiplets&lt;br /&gt;
&lt;br /&gt;
* [[KUJIRA]]: Interactive and semi-automatic NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [https://nmrtist.org/ NMRtist]: Online platform for automated biomolecular NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [[MAPPER]]: Sequence-specific NMR assignment of proteins by global sequence mapping&lt;br /&gt;
&lt;br /&gt;
* [[POMA]]: Product operator formalism in Mathematica&lt;br /&gt;
&lt;br /&gt;
* [[PROSA]]: Processing algorithms&lt;br /&gt;
&lt;br /&gt;
* [[UPLABEL]]: Unique pair labeling&lt;br /&gt;
&lt;br /&gt;
== Other software ==&lt;br /&gt;
&lt;br /&gt;
Not separately available, not yet available, or outdated software.&lt;br /&gt;
&lt;br /&gt;
* [[ASNO]]: Semi-automated assignment of NOEs&lt;br /&gt;
&lt;br /&gt;
* [[CALIBA]]: Calibration of NOE distance constraints&lt;br /&gt;
&lt;br /&gt;
* [[DIANA]]: Distance geometry algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[DYANA]]: Dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[EASY]]: ETH automated spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[FLATT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[FLYA]]: Fully automated structure determination of proteins in solution&lt;br /&gt;
&lt;br /&gt;
* [[FOUND]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[GLOMSA]]: Global method for stereo-specific assignments&lt;br /&gt;
&lt;br /&gt;
* [[HABAS]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[IFLAT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[INCLAN]]: Interactive command language&lt;br /&gt;
&lt;br /&gt;
* [[OPAL]]: Energy refinement and MD simulation algorithm for vector supercomputers&lt;br /&gt;
&lt;br /&gt;
* [[OPALp]]: Energy refinement and MD simulation algorithm&lt;br /&gt;
&lt;br /&gt;
* [[XEASY]]: X-windows version of ETH automated Spectroscopy&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59315</id>
		<title>Software</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59315"/>
		<updated>2026-01-25T11:19:35Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Software developed by P. Güntert and collaborators.&lt;br /&gt;
&lt;br /&gt;
== Available software == &lt;br /&gt;
&lt;br /&gt;
* [[ARTINA]]: Artificial intelligence for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[ATNOS]]: Automated NOESY peak picking&lt;br /&gt;
&lt;br /&gt;
* [[AUTOPSY]]: Automated peak picking in NMR spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[CANDID]]: Combined automated NOE assignment and structure determination module&lt;br /&gt;
&lt;br /&gt;
* [[Chess2FLYA]]: Chemical shift statistics to FLYA&lt;br /&gt;
&lt;br /&gt;
* [[COCO]]: Compare covalent geometry&lt;br /&gt;
&lt;br /&gt;
* [[COFIMA]]: Coordinate and constraint file manipulation&lt;br /&gt;
&lt;br /&gt;
* [http://www.cyana.org/wiki CYANA]: Combined assignment and dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[CYLIB]]: CYANA library entry preparation from mmCIF or Mol2 files &lt;br /&gt;
&lt;br /&gt;
* [https://uni-frankfurt.guentert.science/cyrange CYRANGE]: Determination of optimum residue ranges for the superposition of protein structures&lt;br /&gt;
&lt;br /&gt;
* [[GARANT]]: General algorithm for resonance assignment&lt;br /&gt;
&lt;br /&gt;
* [[INFIT]]: Coupling constants from inverse Fourier transformation of in-phase multiplets&lt;br /&gt;
&lt;br /&gt;
* [[KUJIRA]]: Interactive and semi-automatic NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [https://nmrtist.org/ NMRtist]: Online platform for automated biomolecular NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [[MAPPER]]: Sequence-specific NMR assignment of proteins by global sequence mapping&lt;br /&gt;
&lt;br /&gt;
* [[POMA]]: Product operator formalism in Mathematica&lt;br /&gt;
&lt;br /&gt;
* [[PROSA]]: Processing algorithms&lt;br /&gt;
&lt;br /&gt;
* [[UPLABEL]]: Unique pair labeling&lt;br /&gt;
&lt;br /&gt;
* [[XEASY]]: X-windows version of ETH automated Spectroscopy&lt;br /&gt;
&lt;br /&gt;
== Other software ==&lt;br /&gt;
&lt;br /&gt;
Not separately available, not yet available, or outdated software.&lt;br /&gt;
&lt;br /&gt;
* [[ASNO]]: Semi-automated assignment of NOEs&lt;br /&gt;
&lt;br /&gt;
* [[CALIBA]]: Calibration of NOE distance constraints&lt;br /&gt;
&lt;br /&gt;
* [[DIANA]]: Distance geometry algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[DYANA]]: Dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[EASY]]: ETH automated spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[FLATT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[FLYA]]: Fully automated structure determination of proteins in solution&lt;br /&gt;
&lt;br /&gt;
* [[FOUND]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[GLOMSA]]: Global method for stereo-specific assignments&lt;br /&gt;
&lt;br /&gt;
* [[HABAS]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[IFLAT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[INCLAN]]: Interactive command language&lt;br /&gt;
&lt;br /&gt;
* [[OPAL]]: Energy refinement and MD simulation algorithm for vector supercomputers&lt;br /&gt;
&lt;br /&gt;
* [[OPALp]]: Energy refinement and MD simulation algorithm&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59314</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59314"/>
		<updated>2026-01-25T11:18:55Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis and within [https://nmrtist.bruker.com/ NMRtist@Bruker].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59313</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59313"/>
		<updated>2026-01-25T11:16:38Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
[https://nmrtist.org/static/public/NMRtist_video_tutorial.mp4 Video tutorial]&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis and within [https://nmrtist.bruker.com/ NMRtist@Bruker].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59312</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59312"/>
		<updated>2026-01-25T11:14:11Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. Tested on a 100-protein benchmark comprising 1329 multidimensional NMR spectra, ARTINA demonstrated its ability to solve structures with 1.44 Å median RMSD to the PDB reference and to identify 91.36% correct NMR resonance assign-&lt;br /&gt;
ments. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis and within [https://nmrtist.bruker.com/ NMRtist@Bruker].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59311</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59311"/>
		<updated>2026-01-25T11:13:23Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. Tested on a 100-protein benchmark comprising 1329 multidimensional NMR spectra, ARTINA demonstrated its ability to solve structures with 1.44 Å median RMSD to the PDB reference and to identify 91.36% correct NMR resonance assign-&lt;br /&gt;
ments. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis. It is also available within [https://nmrtist.bruker.com/ NMRtist @ Bruker].&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59310</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59310"/>
		<updated>2026-01-25T11:09:57Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
Using only NMR spectra and the protein sequence as input, ARTINA delivers signal positions, resonance assignments, and structures strictly without human intervention. Tested on a 100-protein benchmark comprising 1329 multidimensional NMR spectra, ARTINA demonstrated its ability to solve structures with 1.44 Å median RMSD to the PDB reference and to identify 91.36% correct NMR resonance assign-&lt;br /&gt;
ments. ARTINA can be used by non-experts, reducing the effort for a protein assignment or structure determination by NMR essentially to the preparation of the sample and the spectra measurements.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59309</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59309"/>
		<updated>2026-01-25T11:08:20Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
ATNOS is a software for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H,&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H]-NOESY spectra during de novo protein structure determination by NMR. By incorporating the analysis of the raw NMR data into the process of automated de novo protein structure determination, ATNOS enables direct feedback between the protein structure, the NOE assignments and the experimental NOESY spectra.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available within the [https://nmrtist.org/ NMRtist] online platform for automated biomolecular NMR spectra analysis.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59308</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59308"/>
		<updated>2026-01-25T11:07:09Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
ATNOS is a software for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H,&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H]-NOESY spectra during de novo protein structure determination by NMR. By incorporating the analysis of the raw NMR data into the process of automated de novo protein structure determination, ATNOS enables direct feedback between the protein structure, the NOE assignments and the experimental NOESY spectra.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available in the [[NMRtist]] web platform.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. NMRtist: an online platform for automated biomolecular NMR spectra analysis[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-NMRtist.pdf .] [http://doi.org/10.1093/bioinformatics/btad066 Bioinformatics 39, btad066 (2023)]&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Time-optimized protein NMR assignment with an integrative deep learning approach using AlphaFold and chemical shift prediction[https://uni-frankfurt.guentert.science/Reprints/Klukowski23-ARTINAAlphaFold.pdf .] [http://doi.org/10.1126/sciadv.adi9323 Sci. Adv. 9, eadi9323 (2023)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59307</id>
		<title>ARTINA</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=ARTINA&amp;diff=59307"/>
		<updated>2026-01-25T11:06:21Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: Created page with &amp;quot;&amp;#039;&amp;#039;Artificial intelligence for NMR applications&amp;#039;&amp;#039;   ATNOS is a software for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H,&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H]-NOESY spectra during de novo protein structure determination by NMR. By incorporating the analysis of the raw NMR data into the process of automated de novo protein structure determination, ATNOS enables direct feedback between the protein structure, the NOE assi...&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;Artificial intelligence for NMR applications&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
ATNOS is a software for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H,&amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H]-NOESY spectra during de novo protein structure determination by NMR. By incorporating the analysis of the raw NMR data into the process of automated de novo protein structure determination, ATNOS enables direct feedback between the protein structure, the NOE assignments and the experimental NOESY spectra.&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* ARTINA is available in the [[NMRtist]] web platform.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Klukowski, P., Riek, R. &amp;amp; Güntert, P. Rapid protein assignments and structures from raw NMR spectra with the deep learning technique ARTINA[https://uni-frankfurt.guentert.science/Reprints/Klukowski22-ARTINA.pdf .] [http://doi.org/10.1038/s41467-022-33879-5 Nat. Commun. 13, 6151 (2022)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59306</id>
		<title>XEASY</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=XEASY&amp;diff=59306"/>
		<updated>2026-01-24T18:41:23Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;  X windows version of ETH automated spectroscopy   &#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
XEASY is a program for interactive, computer-supported NMR spectrum analysis. It is the successor of [[EASY]], the first program package for the interactive analysis of multidimensional NMR spectra that was developed within the group of Prof. K. Wüthrich at ETH Zürich.    &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
XEASY is [http://www.mol.biol.ethz.ch/groups/wuthrich_group/software available] from the group of Prof. K. Wüthrich at ETH Zürich.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [[Media:XeasyManual.pdf|Manual (PDF)]]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Bartels, C., Xia, T., Billeter, M., Güntert, P. &amp;amp; Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. [http://dx.doi.org/10.1007/BF00417486 J. Biomol. NMR 6, 1–10 (1995)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with XEASY must cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59305</id>
		<title>Software</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59305"/>
		<updated>2026-01-24T17:55:59Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Software developed by P. Güntert and collaborators.&lt;br /&gt;
&lt;br /&gt;
== Available software == &lt;br /&gt;
&lt;br /&gt;
* [[ARTINA]]: Artificial intelligence for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[ATNOS]]: Automated NOESY peak picking&lt;br /&gt;
&lt;br /&gt;
* [[AUTOPSY]]: Automated peak picking in NMR spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[CANDID]]: Combined automated NOE assignment and structure determination module&lt;br /&gt;
&lt;br /&gt;
* [[Chess2FLYA]]: Chemical shift statistics to FLYA&lt;br /&gt;
&lt;br /&gt;
* [[COCO]]: Compare covalent geometry&lt;br /&gt;
&lt;br /&gt;
* [[COFIMA]]: Coordinate and constraint file manipulation&lt;br /&gt;
&lt;br /&gt;
* [http://www.cyana.org/wiki CYANA]: Combined assignment and dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[CYLIB]]: CYANA library entry preparation from mmCIF or MOL2 files &lt;br /&gt;
&lt;br /&gt;
* [https://uni-frankfurt.guentert.science/cyrange CYRANGE]: Determination of optimum residue ranges for the superposition of protein structures&lt;br /&gt;
&lt;br /&gt;
* [[GARANT]]: General algorithm for resonance assignment&lt;br /&gt;
&lt;br /&gt;
* [[INFIT]]: Coupling constants from inverse Fourier transformation of in-phase multiplets&lt;br /&gt;
&lt;br /&gt;
* [[KUJIRA]]: Interactive and semi-automatic NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [https://nmrtist.org/ NMRtist]: Online platform for automated biomolecular NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [[MAPPER]]: Sequence-specific NMR assignment of proteins by global sequence mapping&lt;br /&gt;
&lt;br /&gt;
* [[POMA]]: Product operator formalism in Mathematica&lt;br /&gt;
&lt;br /&gt;
* [[PROSA]]: Processing algorithms&lt;br /&gt;
&lt;br /&gt;
* [[UPLABEL]]: Unique pair labeling&lt;br /&gt;
&lt;br /&gt;
* [[XEASY]]: X-windows version of ETH automated Spectroscopy&lt;br /&gt;
&lt;br /&gt;
== Other software ==&lt;br /&gt;
&lt;br /&gt;
Not separately available, not yet available, or outdated software.&lt;br /&gt;
&lt;br /&gt;
* [[ASNO]]: Semi-automated assignment of NOEs&lt;br /&gt;
&lt;br /&gt;
* [[CALIBA]]: Calibration of NOE distance constraints&lt;br /&gt;
&lt;br /&gt;
* [[DIANA]]: Distance geometry algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[DYANA]]: Dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[EASY]]: ETH automated spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[FLATT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[FLYA]]: Fully automated structure determination of proteins in solution&lt;br /&gt;
&lt;br /&gt;
* [[FOUND]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[GLOMSA]]: Global method for stereo-specific assignments&lt;br /&gt;
&lt;br /&gt;
* [[HABAS]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[IFLAT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[INCLAN]]: Interactive command language&lt;br /&gt;
&lt;br /&gt;
* [[OPAL]]: Energy refinement and MD simulation algorithm for vector supercomputers&lt;br /&gt;
&lt;br /&gt;
* [[OPALp]]: Energy refinement and MD simulation algorithm&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59304</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59304"/>
		<updated>2026-01-24T17:52:09Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from molecular topology descriptions given as [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] or [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] mmCIF files. &lt;br /&gt;
&lt;br /&gt;
Setting up CYANA residue library entries therefore involves, besides straightforward format conversion, the non-trivial step of defining a suitable tree structure of torsion angles, and to re-order the atoms in a way that is compatible with this tree structure. This can be done manually for small numbers of molecules but is time-consuming and error-prone. CYLIB automates this process.&lt;br /&gt;
&lt;br /&gt;
The tree structure of torsion angles is needed by the CYANA structure calculation algorithm because it uses torsion angle molecular dynamics for the efficient computation of three-dimensional structures from NMR-derived restraints. For this, the molecules have to be represented in torsion angle space with rotations around covalent single bonds as the only degrees of freedom. The molecule must be given a tree structure of torsion angles connecting rigid units composed of one or several atsoms with fixed relative positions. &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== Reference ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=File:Cylib-2.2.tgz&amp;diff=59303</id>
		<title>File:Cylib-2.2.tgz</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=File:Cylib-2.2.tgz&amp;diff=59303"/>
		<updated>2026-01-24T17:51:27Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59302</id>
		<title>CYLIB 2.2 Software License</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59302"/>
		<updated>2026-01-24T17:45:58Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;To use CYANA you must accept the following software license (also available in [[Media:CylibLicense.pdf|PDF format]]) :&lt;br /&gt;
&lt;br /&gt;
=== CYLIB 2.2 Software License===&lt;br /&gt;
&lt;br /&gt;
The CYLIB 2.2 Software License is a legal agreement, governed by the laws of&lt;br /&gt;
Switzerland, between an end user (the &amp;quot;Licensee&amp;quot;), either an individual or an entity,&lt;br /&gt;
and Dr. Peter Güntert (the &amp;quot;Licensor&amp;quot;). The program package CYLIB 2.2 (copyright (c)&lt;br /&gt;
2015 by Peter Güntert), comprising all computer programs, source code, license keys,&lt;br /&gt;
documentation, example data and other files delivered to the Licensee, as well as any&lt;br /&gt;
copies, modifications or derivative works made by the Licensee, are hereinafter referred&lt;br /&gt;
to collectively as the &amp;quot;Software&amp;quot;. A derivative work is any software that contains one&lt;br /&gt;
or several parts of the Software in original or modified form. If the Licensor provides&lt;br /&gt;
the Licensee with updates of the Software, these will become part of the Software and&lt;br /&gt;
will be controlled by this license.&lt;br /&gt;
&lt;br /&gt;
1. The Licensor grants to the Licensee a non-exclusive, non-transferable, permanent&lt;br /&gt;
license to install and use the Software on computer systems located at the site of&lt;br /&gt;
the Licensee&#039;s organization. However, a violation of any of the clauses of this&lt;br /&gt;
license agreement by the Licensee shall terminate automatically and with immediate&lt;br /&gt;
effect the Licensee&#039;s right to install, use or store the Software in any form. Use&lt;br /&gt;
of the Software is restricted to the Licensee and to direct collaborators who are&lt;br /&gt;
members of the organization of the Licensee at the site of the Licensee and who&lt;br /&gt;
accept the terms of this license. The Licensee shall neither use the Software to&lt;br /&gt;
produce other software that duplicates functionality of the Software nor translate&lt;br /&gt;
source code of the Software into another programming language.&lt;br /&gt;
&lt;br /&gt;
2. The Licensor retains at all times ownership of the Software delivered to the&lt;br /&gt;
Licensee. Any modifications or derivative works based on the Software are considered&lt;br /&gt;
part of the Software, and ownership thereof is retained by the Licensor. All parts&lt;br /&gt;
of the Software must carry the copyright notice, will be controlled by this license,&lt;br /&gt;
and will be promptly destroyed by the Licensee upon termination of this license.&lt;br /&gt;
&lt;br /&gt;
3. The Licensee shall not disclose in any form the Software or any modifications or&lt;br /&gt;
derivative works based on the Software to third parties without prior written&lt;br /&gt;
authorization from the Licensor.&lt;br /&gt;
&lt;br /&gt;
4. The Licensee agrees that the Software has been developed in connection with academic&lt;br /&gt;
research projects and is provided &amp;quot;as is&amp;quot;. The Licensor disclaims all warranties&lt;br /&gt;
with regard to the Software or any of its results, including any implied warranties&lt;br /&gt;
of merchantability or fitness for a particular purpose. In no event shall the&lt;br /&gt;
Licensor be liable for any damages, however caused, including, without limitation,&lt;br /&gt;
any damages arising out of the use of the Software, loss of use of the Software, or&lt;br /&gt;
damage of any sort to the Licensee.&lt;br /&gt;
&lt;br /&gt;
5. The Licensee agrees that any reports or publications of results obtained with the&lt;br /&gt;
Software will acknowledge its use by the literature citation: Maden Yilmaz, E. &amp;amp;&lt;br /&gt;
Güntert, P. NMR structure calculation for all small molecule ligands and&lt;br /&gt;
non-standard residues from the PDB Chemical Component Dictionary. J. Biomol. NMR&lt;br /&gt;
63, 21-37 (2015).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Media:cylib-2.2.tgz|ACCEPT]]      or      [[Software|Decline]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59301</id>
		<title>CYLIB 2.2 Software License</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59301"/>
		<updated>2026-01-24T17:38:40Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;To use CYANA you must accept the following software license (also available in [[Media:CylibLicense.pdf|PDF format]]) :&lt;br /&gt;
&lt;br /&gt;
=== CYLIB 2.2 Software License===&lt;br /&gt;
&lt;br /&gt;
The CYLIB 2.0 Software License is a legal agreement, governed by the laws of&lt;br /&gt;
Switzerland, between an end user (the &amp;quot;Licensee&amp;quot;), either an individual or an entity,&lt;br /&gt;
and Dr. Peter Guentert (the &amp;quot;Licensor&amp;quot;). The program package CYLIB 2.0 (copyright (c)&lt;br /&gt;
2015-16 by Peter Guentert), comprising all computer programs, source code, license keys,&lt;br /&gt;
documentation, example data and other files delivered to the Licensee, as well as any&lt;br /&gt;
copies, modifications or derivative works made by the Licensee, are hereinafter referred&lt;br /&gt;
to collectively as the &amp;quot;Software&amp;quot;. A derivative work is any software that contains one&lt;br /&gt;
or several parts of the Software in original or modified form. If the Licensor provides&lt;br /&gt;
the Licensee with updates of the Software, these will become part of the Software and&lt;br /&gt;
will be controlled by this license.&lt;br /&gt;
&lt;br /&gt;
1. The Licensor grants to the Licensee a non-exclusive, non-transferable, permanent&lt;br /&gt;
license to install and use the Software on computer systems located at the site of&lt;br /&gt;
the Licensee&#039;s organization. However, a violation of any of the clauses of this&lt;br /&gt;
license agreement by the Licensee shall terminate automatically and with immediate&lt;br /&gt;
effect the Licensee&#039;s right to install, use or store the Software in any form. Use&lt;br /&gt;
of the Software is restricted to the Licensee and to direct collaborators who are&lt;br /&gt;
members of the organization of the Licensee at the site of the Licensee and who&lt;br /&gt;
accept the terms of this license. The Licensee shall neither use the Software to&lt;br /&gt;
produce other software that duplicates functionality of the Software nor translate&lt;br /&gt;
source code of the Software into another programming language.&lt;br /&gt;
&lt;br /&gt;
2. The Licensor retains at all times ownership of the Software delivered to the&lt;br /&gt;
Licensee. Any modifications or derivative works based on the Software are considered&lt;br /&gt;
part of the Software, and ownership thereof is retained by the Licensor. All parts&lt;br /&gt;
of the Software must carry the copyright notice, will be controlled by this license,&lt;br /&gt;
and will be promptly destroyed by the Licensee upon termination of this license.&lt;br /&gt;
&lt;br /&gt;
3. The Licensee shall not disclose in any form the Software or any modifications or&lt;br /&gt;
derivative works based on the Software to third parties without prior written&lt;br /&gt;
authorization from the Licensor.&lt;br /&gt;
&lt;br /&gt;
4. The Licensee agrees that the Software has been developed in connection with academic&lt;br /&gt;
research projects and is provided &amp;quot;as is&amp;quot;. The Licensor disclaims all warranties&lt;br /&gt;
with regard to the Software or any of its results, including any implied warranties&lt;br /&gt;
of merchantability or fitness for a particular purpose. In no event shall the&lt;br /&gt;
Licensor be liable for any damages, however caused, including, without limitation,&lt;br /&gt;
any damages arising out of the use of the Software, loss of use of the Software, or&lt;br /&gt;
damage of any sort to the Licensee.&lt;br /&gt;
&lt;br /&gt;
5. The Licensee agrees that any reports or publications of results obtained with the&lt;br /&gt;
Software will acknowledge its use by the literature citation: Maden Yilmaz, E. &amp;amp;&lt;br /&gt;
Güntert, P. NMR structure calculation for all small molecule ligands and&lt;br /&gt;
non-standard residues from the PDB Chemical Component Dictionary. J. Biomol. NMR&lt;br /&gt;
63, 21-37 (2015).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Media:cylib-2.2.tgz|ACCEPT]]      or      [[Software|Decline]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59300</id>
		<title>CYLIB 2.2 Software License</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59300"/>
		<updated>2026-01-24T17:37:28Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;To use COFIMA you must accept the following software license (also available in [[Media:CofimaLicense.pdf|PDF format]]) :&lt;br /&gt;
&lt;br /&gt;
=== CYLIB 2.2 Software License===&lt;br /&gt;
&lt;br /&gt;
The CYLIB 2.0 Software License is a legal agreement, governed by the laws of&lt;br /&gt;
Switzerland, between an end user (the &amp;quot;Licensee&amp;quot;), either an individual or an entity,&lt;br /&gt;
and Dr. Peter Guentert (the &amp;quot;Licensor&amp;quot;). The program package CYLIB 2.0 (copyright (c)&lt;br /&gt;
2015-16 by Peter Guentert), comprising all computer programs, source code, license keys,&lt;br /&gt;
documentation, example data and other files delivered to the Licensee, as well as any&lt;br /&gt;
copies, modifications or derivative works made by the Licensee, are hereinafter referred&lt;br /&gt;
to collectively as the &amp;quot;Software&amp;quot;. A derivative work is any software that contains one&lt;br /&gt;
or several parts of the Software in original or modified form. If the Licensor provides&lt;br /&gt;
the Licensee with updates of the Software, these will become part of the Software and&lt;br /&gt;
will be controlled by this license.&lt;br /&gt;
&lt;br /&gt;
1. The Licensor grants to the Licensee a non-exclusive, non-transferable, permanent&lt;br /&gt;
license to install and use the Software on computer systems located at the site of&lt;br /&gt;
the Licensee&#039;s organization. However, a violation of any of the clauses of this&lt;br /&gt;
license agreement by the Licensee shall terminate automatically and with immediate&lt;br /&gt;
effect the Licensee&#039;s right to install, use or store the Software in any form. Use&lt;br /&gt;
of the Software is restricted to the Licensee and to direct collaborators who are&lt;br /&gt;
members of the organization of the Licensee at the site of the Licensee and who&lt;br /&gt;
accept the terms of this license. The Licensee shall neither use the Software to&lt;br /&gt;
produce other software that duplicates functionality of the Software nor translate&lt;br /&gt;
source code of the Software into another programming language.&lt;br /&gt;
&lt;br /&gt;
2. The Licensor retains at all times ownership of the Software delivered to the&lt;br /&gt;
Licensee. Any modifications or derivative works based on the Software are considered&lt;br /&gt;
part of the Software, and ownership thereof is retained by the Licensor. All parts&lt;br /&gt;
of the Software must carry the copyright notice, will be controlled by this license,&lt;br /&gt;
and will be promptly destroyed by the Licensee upon termination of this license.&lt;br /&gt;
&lt;br /&gt;
3. The Licensee shall not disclose in any form the Software or any modifications or&lt;br /&gt;
derivative works based on the Software to third parties without prior written&lt;br /&gt;
authorization from the Licensor.&lt;br /&gt;
&lt;br /&gt;
4. The Licensee agrees that the Software has been developed in connection with academic&lt;br /&gt;
research projects and is provided &amp;quot;as is&amp;quot;. The Licensor disclaims all warranties&lt;br /&gt;
with regard to the Software or any of its results, including any implied warranties&lt;br /&gt;
of merchantability or fitness for a particular purpose. In no event shall the&lt;br /&gt;
Licensor be liable for any damages, however caused, including, without limitation,&lt;br /&gt;
any damages arising out of the use of the Software, loss of use of the Software, or&lt;br /&gt;
damage of any sort to the Licensee.&lt;br /&gt;
&lt;br /&gt;
5. The Licensee agrees that any reports or publications of results obtained with the&lt;br /&gt;
Software will acknowledge its use by the literature citation: Maden Yilmaz, E. &amp;amp;&lt;br /&gt;
Güntert, P. NMR structure calculation for all small molecule ligands and&lt;br /&gt;
non-standard residues from the PDB Chemical Component Dictionary. J. Biomol. NMR&lt;br /&gt;
63, 21-37 (2015).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Media:cylib-2.2.tgz|ACCEPT]]      or      [[Software|Decline]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59299</id>
		<title>CYLIB 2.2 Software License</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB_2.2_Software_License&amp;diff=59299"/>
		<updated>2026-01-24T17:33:42Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: Created page with &amp;quot;To use COFIMA you must accept the following software license (also available in PDF format) :  === CYLIB 2.2 Software License===  The CYLIB 2.0 Software License is a legal agreement, governed by the laws of Switzerland, between an end user (the &amp;quot;Licensee&amp;quot;), either an individual or an entity, and Dr. Peter Guentert (the &amp;quot;Licensor&amp;quot;). The program package CYLIB 2.0 (copyright (c) 2015-16 by Peter Guentert), comprising all computer programs, source...&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;To use COFIMA you must accept the following software license (also available in [[Media:CofimaLicense.pdf|PDF format]]) :&lt;br /&gt;
&lt;br /&gt;
=== CYLIB 2.2 Software License===&lt;br /&gt;
&lt;br /&gt;
The CYLIB 2.0 Software License is a legal agreement, governed by the laws of&lt;br /&gt;
Switzerland, between an end user (the &amp;quot;Licensee&amp;quot;), either an individual or an entity,&lt;br /&gt;
and Dr. Peter Guentert (the &amp;quot;Licensor&amp;quot;). The program package CYLIB 2.0 (copyright (c)&lt;br /&gt;
2015-16 by Peter Guentert), comprising all computer programs, source code, license keys,&lt;br /&gt;
documentation, example data and other files delivered to the Licensee, as well as any&lt;br /&gt;
copies, modifications or derivative works made by the Licensee, are hereinafter referred&lt;br /&gt;
to collectively as the &amp;quot;Software&amp;quot;. A derivative work is any software that contains one&lt;br /&gt;
or several parts of the Software in original or modified form. If the Licensor provides&lt;br /&gt;
the Licensee with updates of the Software, these will become part of the Software and&lt;br /&gt;
will be controlled by this license.&lt;br /&gt;
&lt;br /&gt;
1. The Licensor grants to the Licensee a non-exclusive, non-transferable, permanent&lt;br /&gt;
  license to install and use the Software on computer systems located at the site of&lt;br /&gt;
  the Licensee&#039;s organization. However, a violation of any of the clauses of this&lt;br /&gt;
  license agreement by the Licensee shall terminate automatically and with immediate&lt;br /&gt;
  effect the Licensee&#039;s right to install, use or store the Software in any form. Use&lt;br /&gt;
  of the Software is restricted to the Licensee and to direct collaborators who are&lt;br /&gt;
  members of the organization of the Licensee at the site of the Licensee and who&lt;br /&gt;
  accept the terms of this license. The Licensee shall neither use the Software to&lt;br /&gt;
  produce other software that duplicates functionality of the Software nor translate&lt;br /&gt;
  source code of the Software into another programming language.&lt;br /&gt;
&lt;br /&gt;
2. The Licensor retains at all times ownership of the Software delivered to the&lt;br /&gt;
  Licensee. Any modifications or derivative works based on the Software are considered&lt;br /&gt;
  part of the Software, and ownership thereof is retained by the Licensor. All parts&lt;br /&gt;
  of the Software must carry the copyright notice, will be controlled by this license,&lt;br /&gt;
  and will be promptly destroyed by the Licensee upon termination of this license.&lt;br /&gt;
&lt;br /&gt;
3. The Licensee shall not use the Software for any purpose (research or otherwise) that&lt;br /&gt;
  is supported by a &amp;quot;for profit&amp;quot; organization without prior written authorization from&lt;br /&gt;
  the Licensor.&lt;br /&gt;
  [This Article does not apply to Licensees who have obtained a Commercial License.]&lt;br /&gt;
&lt;br /&gt;
4. The Licensee shall not disclose in any form the Software or any modifications or&lt;br /&gt;
  derivative works based on the Software to third parties without prior written&lt;br /&gt;
  authorization from the Licensor.&lt;br /&gt;
&lt;br /&gt;
5. The Licensee agrees that the Software has been developed in connection with academic&lt;br /&gt;
  research projects and is provided &amp;quot;as is&amp;quot;. The Licensor disclaims all warranties&lt;br /&gt;
  with regard to the Software or any of its results, including any implied warranties&lt;br /&gt;
  of merchantability or fitness for a particular purpose. In no event shall the&lt;br /&gt;
  Licensor be liable for any damages, however caused, including, without limitation,&lt;br /&gt;
  any damages arising out of the use of the Software, loss of use of the Software, or&lt;br /&gt;
  damage of any sort to the Licensee.&lt;br /&gt;
&lt;br /&gt;
6. The Licensee agrees that any reports or publications of results obtained with the&lt;br /&gt;
  Software will acknowledge its use by the literature citation: Maden Yilmaz, E. &amp;amp;&lt;br /&gt;
  G�ntert, P. NMR structure calculation for all small molecule ligands and&lt;br /&gt;
  non-standard residues from the PDB Chemical Component Dictionary.  J. Biomol. NMR&lt;br /&gt;
  63, 21-37 (2015).&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Media:cylib-2.2.tgz|ACCEPT]]      or      [[Software|Decline]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59298</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59298"/>
		<updated>2026-01-24T17:31:58Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from molecular topology descriptions given as [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] or [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] mmCIF files. &lt;br /&gt;
&lt;br /&gt;
Setting up CYANA residue library entries therefore involves, besides straightforward format conversion, the non-trivial step of defining a suitable tree structure of torsion angles, and to re-order the atoms in a way that is compatible with this tree structure. This can be done manually for small numbers of molecules but is time-consuming and error-prone. CYLIB automates this process.&lt;br /&gt;
&lt;br /&gt;
The tree structure of torsion angles is needed by the CYANA structure calculation algorithm because it uses torsion angle molecular dynamics for the efficient computation of three-dimensional structures from NMR-derived restraints. For this, the molecules have to be represented in torsion angle space with rotations around covalent single bonds as the only degrees of freedom. The molecule must be given a tree structure of torsion angles connecting rigid units composed of one or several atsoms with fixed relative positions. &lt;br /&gt;
&lt;br /&gt;
The input topology-file must be either in MOL2 format (with extension .mol2) or in the mmCIF format of the PDB Chemical Component Dictionary (with extension .cif).&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== Reference ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59297</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59297"/>
		<updated>2026-01-24T17:29:28Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from molecular topology descriptions given as [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] or [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] mmCIF files. &lt;br /&gt;
&lt;br /&gt;
Setting up CYANA residue library entries therefore involves, besides straightforward format conversion, the non-trivial step of defining a suitable tree structure of torsion angles, and to re-order the atoms in a way that is compatible with this tree structure. This can be done manually for small numbers of molecules but the process is time-consuming and error-prone. CYLIB automates this process.&lt;br /&gt;
&lt;br /&gt;
The tree structure of torsion angles is needed by the CYANA structure calculation algorithm because it uses torsion angle molecular dynamics for the efficient computation of three-dimensional structures from NMR-derived restraints. For this, the molecules have to be represented in torsion angle space with rotations around covalent single bonds as the only degrees of freedom. The molecule must be given a tree structure of torsion angles connecting rigid units composed of one or several atsoms with fixed relative positions. &lt;br /&gt;
&lt;br /&gt;
The input topology-file must be either in MOL2 format (with extension .mol2) or in the mmCIF format of the PDB Chemical Component Dictionary (with extension .cif).&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59296</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59296"/>
		<updated>2026-01-24T17:24:28Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from molecular topology descriptions given as [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] or [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] mmCIF files. &lt;br /&gt;
&lt;br /&gt;
CYLIB is an algorithm for converting molecular topology descriptions in MOL2 format or from the PDB&lt;br /&gt;
    Chemical Component Dictionary into CYANA residue library entries.&lt;br /&gt;
&lt;br /&gt;
Setting up CYANA residue library entries therefore involves, besides straightforward format conversion, the non-trivial step of defining a suitable tree structure of torsion angles, and to re-order the atoms in a way that is compatible with this tree structure. This can be done manually for small numbers of ligands but the&lt;br /&gt;
    process is time-consuming and error-prone. An automated method is necessary in order to handle the&lt;br /&gt;
    large number of different potential ligand molecules to be studied in drug design projects. CyLib is&lt;br /&gt;
    an algorithm for this purpose.&lt;br /&gt;
    The CYANA structure calculation algorithm uses torsion angle molecular dynamics for the efficient&lt;br /&gt;
    computation of three-dimensional structures from NMR-derived restraints. For this, the molecules have&lt;br /&gt;
    to be represented in torsion angle space with rotations around covalent single bonds as the only&lt;br /&gt;
    degrees of freedom. The molecule must be given a tree structure of torsion angles connecting rigid&lt;br /&gt;
    units composed of one or several atsoms with fixed relative positions. Setting up CYANA residue&lt;br /&gt;
    library entries therefore involves, besides straightforward format conversion, the non-trivial step&lt;br /&gt;
    of defining a suitable tree structure of torsion angles, and to re-order the atoms in a way that is&lt;br /&gt;
    compatible with this tree structure. This can be done manually for small numbers of ligands but the&lt;br /&gt;
    process is time-consuming and error-prone. An automated method is necessary in order to handle the&lt;br /&gt;
    large number of different potential ligand molecules to be studied in drug design projects. CyLib is&lt;br /&gt;
    an algorithm for this purpose.&lt;br /&gt;
&lt;br /&gt;
    The input topology-file must be either in MOL2 format (with extension .mol2) or in the mmCIF format&lt;br /&gt;
    of the PDB Chemical Component Dictionary (with extension .cif).&lt;br /&gt;
  &lt;br /&gt;
&lt;br /&gt;
With CYLIB you can easily: &lt;br /&gt;
&lt;br /&gt;
* Convert between different data file formats&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59295</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59295"/>
		<updated>2026-01-24T17:19:42Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from mmCIF files of the [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] or [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] files.   &lt;br /&gt;
&lt;br /&gt;
With CYLIB you can easily: &lt;br /&gt;
&lt;br /&gt;
* Convert between different data file formats&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59294</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59294"/>
		<updated>2026-01-24T17:19:02Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library residue entry preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from mmCIF files of the [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] or [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] files.   &lt;br /&gt;
&lt;br /&gt;
With CYLIB you can easily: &lt;br /&gt;
&lt;br /&gt;
* Convert between different data file formats&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Maden Yilmaz, E. &amp;amp; Güntert, P. NMR structure calculation for all small molecule ligands and non-standard residues from the PDB Chemical Component Dictionary[https://uni-frankfurt.guentert.science/Reprints/Maden15-Cylib.pdf .]  [http://doi.org/10.1007/s10858-015-9959-y J. Biomol. NMR 63, 21-37 (2015)]&lt;br /&gt;
&lt;br /&gt;
:&#039;&#039;Reports or publications of results obtained with CYLIB should cite this paper.&#039;&#039;&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59293</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59293"/>
		<updated>2026-01-24T17:17:00Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library residue entry preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the [https://cyana.org/wiki/Residue_library_file CYANA residue library] starting from mmCIF files of the [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] or [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] files.   &lt;br /&gt;
&lt;br /&gt;
With CYLIB you can easily: &lt;br /&gt;
&lt;br /&gt;
* Convert between different data file formats&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [[Media:CofimaManual.pdf|Manual (PDF)]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59292</id>
		<title>CYLIB</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=CYLIB&amp;diff=59292"/>
		<updated>2026-01-24T17:15:22Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: Created page with &amp;quot;&amp;#039;&amp;#039;CYANA library residue entry preparation&amp;#039;&amp;#039;   CYLIB (© by Peter Güntert) can be used to prepare new entries for the CYANA residue library starting from mmCIF files from the [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] or [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] files.     With COFIMA you can easily:   * Convert between different data file formats   == Availability == * CYLIB is available free-of-charge....&amp;quot;&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039;CYANA library residue entry preparation&#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
CYLIB (© by Peter Güntert) can be used to prepare new entries for the CYANA residue library starting from mmCIF files from the [https://www.wwpdb.org/data/ccd PDB Chemical Component Dictionary] or [https://aideepmed.com/DockRMSD/mol2.pdf Tripos Mol2] files.   &lt;br /&gt;
&lt;br /&gt;
With COFIMA you can easily: &lt;br /&gt;
&lt;br /&gt;
* Convert between different data file formats&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
* CYLIB is [[CYLIB 2.2 Software License|available]] free-of-charge. The current version is CYLIB 2.2.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [[Media:CofimaManual.pdf|Manual (PDF)]]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59291</id>
		<title>Software</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Software&amp;diff=59291"/>
		<updated>2026-01-24T16:58:51Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Software developed by P. Güntert and collaborators.&lt;br /&gt;
&lt;br /&gt;
== Available software == &lt;br /&gt;
&lt;br /&gt;
* [[ATNOS]]: Automated NOESY peak picking&lt;br /&gt;
&lt;br /&gt;
* [[AUTOPSY]]: Automated peak picking in NMR spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[CANDID]]: Combined automated NOE assignment and structure determination module&lt;br /&gt;
&lt;br /&gt;
* [[Chess2FLYA]]: Chemical shift statistics to FLYA&lt;br /&gt;
&lt;br /&gt;
* [[COCO]]: Compare covalent geometry&lt;br /&gt;
&lt;br /&gt;
* [[COFIMA]]: Coordinate and constraint file manipulation&lt;br /&gt;
&lt;br /&gt;
* [http://www.cyana.org/wiki CYANA]: Combined assignment and dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[CYLIB]]: CYANA library entry preparation from mmCIF or MOL2 files &lt;br /&gt;
&lt;br /&gt;
* [https://uni-frankfurt.guentert.science/cyrange CYRANGE]: Determination of optimum residue ranges for the superposition of protein structures&lt;br /&gt;
&lt;br /&gt;
* [[GARANT]]: General algorithm for resonance assignment&lt;br /&gt;
&lt;br /&gt;
* [[INFIT]]: Coupling constants from inverse Fourier transformation of in-phase multiplets&lt;br /&gt;
&lt;br /&gt;
* [[KUJIRA]]: Interactive and semi-automatic NMR spectra analysis&lt;br /&gt;
&lt;br /&gt;
* [[MAPPER]]: Sequence-specific NMR assignment of proteins by global sequence mapping&lt;br /&gt;
&lt;br /&gt;
* [[POMA]]: Product operator formalism in Mathematica&lt;br /&gt;
&lt;br /&gt;
* [[PROSA]]: Processing algorithms&lt;br /&gt;
&lt;br /&gt;
* [[UPLABEL]]: Unique pair labeling&lt;br /&gt;
&lt;br /&gt;
* [[XEASY]]: X-windows version of ETH automated Spectroscopy&lt;br /&gt;
&lt;br /&gt;
== Other software ==&lt;br /&gt;
&lt;br /&gt;
Not separately available, not yet available, or outdated software.&lt;br /&gt;
&lt;br /&gt;
* [[ASNO]]: Semi-automated assignment of NOEs&lt;br /&gt;
&lt;br /&gt;
* [[CALIBA]]: Calibration of NOE distance constraints&lt;br /&gt;
&lt;br /&gt;
* [[DIANA]]: Distance geometry algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[DYANA]]: Dynamics algorithm for NMR applications&lt;br /&gt;
&lt;br /&gt;
* [[EASY]]: ETH automated spectroscopy&lt;br /&gt;
&lt;br /&gt;
* [[FLATT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[FLYA]]: Fully automated structure determination of proteins in solution&lt;br /&gt;
&lt;br /&gt;
* [[FOUND]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[GLOMSA]]: Global method for stereo-specific assignments&lt;br /&gt;
&lt;br /&gt;
* [[HABAS]]: Grid search and stereospecific assignment algorithm&lt;br /&gt;
&lt;br /&gt;
* [[IFLAT]]: Baseline correction for multidimensional NMR spectra&lt;br /&gt;
&lt;br /&gt;
* [[INCLAN]]: Interactive command language&lt;br /&gt;
&lt;br /&gt;
* [[OPAL]]: Energy refinement and MD simulation algorithm for vector supercomputers&lt;br /&gt;
&lt;br /&gt;
* [[OPALp]]: Energy refinement and MD simulation algorithm&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=INCLAN&amp;diff=59290</id>
		<title>INCLAN</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=INCLAN&amp;diff=59290"/>
		<updated>2026-01-14T08:17:31Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: /* Documentation */&lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039; Interactive command language &#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
INCLAN is a general command interface language for seamless integration into Fortran or C/C++-based programs that allows the programmer to separate the user interface from the core part of the program and thus to provide a sophisticated, command-driven user interface with minimal programming effort. Similarly, INCLAN can be used as a general driver for coarse-grained parallel applications, in which parallelization occurs at the level of loops in INCLAN scripts rather than within the core algorithms of the underlying application.  &lt;br /&gt;
&lt;br /&gt;
Features of INCLAN include: &lt;br /&gt;
&lt;br /&gt;
* A versatile, easy-to-learn, interpreted scripting language&lt;br /&gt;
* Shell-like variables combined with Fortran-style arithmetic, character or logical expressions &lt;br /&gt;
* Flow control: loops, conditional statements etc.&lt;br /&gt;
* Parallelization of loops on shared-memory and distributed-memory parallel computers&lt;br /&gt;
* Production of plots and other graphics&lt;br /&gt;
* User access to variables of the underlying program&lt;br /&gt;
* Straightforward and uniform syntax checking for parameter lists of commands of the underlying program and for user-written INCLAN scripts&lt;br /&gt;
* Output control based on importance level; output redirection&lt;br /&gt;
* Error handling&lt;br /&gt;
* Interface to operating system functions&lt;br /&gt;
* CPU time measurements&lt;br /&gt;
* Recursive procedures&lt;br /&gt;
* Implemented on the major Unix systems, Linux, and on Microsoft Windows with Cygwin &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
	&lt;br /&gt;
* INCLAN provides the command line interface and scripting language of the programs [http://www.cyana.org/wiki CYANA], [[DYANA]], [[PROSA]], [[GARANT]], [[OPALp]] and [[OPAL]]. INCLAN is not available as a stand-alone program.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [https://cyana.org/wiki/INCLAN_Reference_Manual Reference Manual]&lt;br /&gt;
* [[Media:InclanManual.pdf|Manual (PDF)]]&lt;br /&gt;
Tutorials:&lt;br /&gt;
* [http://www.cyana.org/wiki/Writing_and_using_INCLAN_macros Writing and using INCLAN macros]&lt;br /&gt;
* [http://www.cyana.org/wiki/Using_INCLAN_variables Using INCLAN variables]&lt;br /&gt;
* [http://www.cyana.org/wiki/Using_INCLAN_control_statements Using INCLAN control statements]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. [http://dx.doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=INCLAN&amp;diff=59289</id>
		<title>INCLAN</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=INCLAN&amp;diff=59289"/>
		<updated>2026-01-14T08:16:59Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&#039;&#039; Interactive command language &#039;&#039;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
INCLAN is a general command interface language for seamless integration into Fortran or C/C++-based programs that allows the programmer to separate the user interface from the core part of the program and thus to provide a sophisticated, command-driven user interface with minimal programming effort. Similarly, INCLAN can be used as a general driver for coarse-grained parallel applications, in which parallelization occurs at the level of loops in INCLAN scripts rather than within the core algorithms of the underlying application.  &lt;br /&gt;
&lt;br /&gt;
Features of INCLAN include: &lt;br /&gt;
&lt;br /&gt;
* A versatile, easy-to-learn, interpreted scripting language&lt;br /&gt;
* Shell-like variables combined with Fortran-style arithmetic, character or logical expressions &lt;br /&gt;
* Flow control: loops, conditional statements etc.&lt;br /&gt;
* Parallelization of loops on shared-memory and distributed-memory parallel computers&lt;br /&gt;
* Production of plots and other graphics&lt;br /&gt;
* User access to variables of the underlying program&lt;br /&gt;
* Straightforward and uniform syntax checking for parameter lists of commands of the underlying program and for user-written INCLAN scripts&lt;br /&gt;
* Output control based on importance level; output redirection&lt;br /&gt;
* Error handling&lt;br /&gt;
* Interface to operating system functions&lt;br /&gt;
* CPU time measurements&lt;br /&gt;
* Recursive procedures&lt;br /&gt;
* Implemented on the major Unix systems, Linux, and on Microsoft Windows with Cygwin &lt;br /&gt;
&lt;br /&gt;
== Availability ==&lt;br /&gt;
	&lt;br /&gt;
* INCLAN provides the command line interface and scripting language of the programs [http://www.cyana.org/wiki CYANA], [[DYANA]], [[PROSA]], [[GARANT]], [[OPALp]] and [[OPAL]]. INCLAN is not available as a stand-alone program.&lt;br /&gt;
&lt;br /&gt;
== Documentation ==&lt;br /&gt;
&lt;br /&gt;
* [https://cyana.org/wiki/INCLAN_Reference_Manual Reference Manual]&lt;br /&gt;
* [[Media:InclanManual.pdf|Manual (PDF)]]&lt;br /&gt;
Tutorials:&lt;br /&gt;
* [http://www.cyana.org/wiki/index.php/Writing_and_using_INCLAN_macros Writing and using INCLAN macros]&lt;br /&gt;
* [http://www.cyana.org/wiki/index.php/Using_INCLAN_variables Using INCLAN variables]&lt;br /&gt;
* [http://www.cyana.org/wiki/index.php/Using_INCLAN_control_statements Using INCLAN control statements]&lt;br /&gt;
&lt;br /&gt;
== References ==&lt;br /&gt;
&lt;br /&gt;
* Güntert, P., Mumenthaler, C. &amp;amp; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. [http://dx.doi.org/10.1006/jmbi.1997.1284 J. Mol. Biol. 273, 283–298 (1997)]&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59288</id>
		<title>Protein structures</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59288"/>
		<updated>2026-01-13T22:05:17Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;NMR protein structures co-authored by P. Güntert.&lt;br /&gt;
&lt;br /&gt;
{|&lt;br /&gt;
&lt;br /&gt;
|[[image:8ox2.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8OX2]]&lt;br /&gt;
|Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OVI 8OVI]&#039;&#039;&#039; [http://files.rcsb.org/download/8ovi_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34811 34811]&#039;&#039;&#039; (monomer)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OX2 8OX2]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34813 34813]&#039;&#039;&#039; (trimer)&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8kcq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8KCQ]]&lt;br /&gt;
|Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8KCQ 8KCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=36589 36589]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8qbp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8QBP]]&lt;br /&gt;
|Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QBP 8QBP]&#039;&#039;&#039; [http://files.rcsb.org/download/8qbp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34850 34850]&#039;&#039;&#039; (OmphA “indole-In)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8Q7J 8Q7J]&#039;&#039;&#039; [http://files.rcsb.org/download/8q7j_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34846 34846]&#039;&#039;&#039; (CsA)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAQ 8QAQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8qaq_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34848 34848]&#039;&#039;&#039; (OmphA&lt;br /&gt;
conformation 1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAS 8QAS]&#039;&#039;&#039; [http://files.rcsb.org/download/8qas_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34849 34849]&#039;&#039;&#039; (OmphA “indole-Out”)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:8pxs.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8PXS]]&lt;br /&gt;
|Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8PXS 8PXS]&#039;&#039;&#039; [http://files.rcsb.org/download/8pxs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34838 34838]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7x9u.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7X9U]]&lt;br /&gt;
|Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7X9U 7X9U]&#039;&#039;&#039; [http://files.rcsb.org/download/7x9u_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36478 36478]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qtr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QTR]]&lt;br /&gt;
|Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTR 7QTR]&#039;&#039;&#039; [http://files.rcsb.org/download/7qtr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34700 34700]&#039;&#039;&#039; (GB1 in cells at a protein concentration of 50 μM)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTS 7QTS]&#039;&#039;&#039; [http://files.rcsb.org/download/7qts_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34701 34701]&#039;&#039;&#039;  (GB1 in cells at a protein concentration of 10 μM)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qcx.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QCX]]&lt;br /&gt;
|Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCX 7QCX]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcx_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34688 34688]&#039;&#039;&#039; (two-state structure of apo PDZ2)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCY 7QCY]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcy_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34689 34689]&#039;&#039;&#039; (two-state structure of PDZ2 complexed with RA-GEF2 peptide)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7fbr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7FBR]]&lt;br /&gt;
|He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBR 7FBR]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36430 36430]&#039;&#039;&#039; (first RRM domain of Matrin-3)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBV 7FBV]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbv_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36431 36431]&#039;&#039;&#039; (second RRM domain of Matrin-3)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6tub.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6TUB]]&lt;br /&gt;
|Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6TUB 6TUB]&#039;&#039;&#039; [http://files.rcsb.org/download/6tub_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=26715 26715]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6svc.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6SVE]]&lt;br /&gt;
| Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVC 6SVC]&#039;&#039;&#039; [http://files.rcsb.org/download/6svc_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34432 34432]&#039;&#039;&#039;&lt;br /&gt;
(WW domain apo structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVE 6SVE]&#039;&#039;&#039; [http://files.rcsb.org/download/6sve_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34433 34433]&#039;&#039;&#039; (WW domain with pCdc25C bound)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVH 6SVH]&#039;&#039;&#039; [http://files.rcsb.org/download/6svh_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34434 34434]&#039;&#039;&#039; (WW domain with FFpSPR bound)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6qk6.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6QK6]]&lt;br /&gt;
|Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK5 6QK5]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34355 34355]&#039;&#039;&#039; (Zn-loaded form)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK6 6QK6]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34356 34356]&#039;&#039;&#039; (Cd-loaded form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5zcz.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5ZCZ]]&lt;br /&gt;
|Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZCZ 5ZCZ]&#039;&#039;&#039; [http://files.rcsb.org/download/5zcz_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27354 27354]&#039;&#039;&#039; (&#039;&#039;T. thermophilus&#039;&#039; HB8 TTHA1718 protein in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZD0 5ZD0]&#039;&#039;&#039; [http://files.rcsb.org/download/5zd0_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27356 27356]&#039;&#039;&#039; (ubiquitin with three alanine mutations in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5Z4B 5Z4B]&#039;&#039;&#039; [http://files.rcsb.org/download/5z4b_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36153 36153]&#039;&#039;&#039; (GB1 in living eukaryotic cells)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6h8c.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6H8C]]&lt;br /&gt;
|Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6H8C 6H8C]&#039;&#039;&#039; [http://files.rcsb.org/download/6h8c_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34307 34307]&#039;&#039;&#039; (GABARAPL2 in complex with UBA5 LIR motif)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6HB9 6HB9]&#039;&#039;&#039; [http://files.rcsb.org/download/6hb9_nmr-data.nef.gz NMR data] (crystal structure of GABARAP in complex with UBA5 LIR motif)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f98.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F98]]&lt;br /&gt;
|Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F98 6F98]&#039;&#039;&#039; [http://files.rcsb.org/download/6f98_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34217 34217]&#039;&#039;&#039; (RING domain of E3 ubiquitin ligase HRD1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F99 6F99]&#039;&#039;&#039; [http://files.rcsb.org/download/6f99_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34218 34218]&#039;&#039;&#039; (MRH domain of Yos9)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F9A 6F9A]&#039;&#039;&#039; [http://files.rcsb.org/download/6f9a_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34219 34219]&#039;&#039;&#039; (MRH domain of Yos9 complexed with alpha3,alpha6-Man5)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6es5.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ES5]]&lt;br /&gt;
|Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES5 6ES5]&#039;&#039;&#039; [http://files.rcsb.org/download/6es5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34187 34187]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES6 6ES6]&#039;&#039;&#039; [http://files.rcsb.org/download/6es6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34188 34188]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES7 6ES7]&#039;&#039;&#039; [http://files.rcsb.org/download/6es7_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34189 34189]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6esp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ESP]]&lt;br /&gt;
|Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ESP 6ESP]&#039;&#039;&#039; [http://files.rcsb.org/download/6esp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34190 34190]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6by4.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6BY4]]&lt;br /&gt;
|Nichols, P.J., Henen, M.A., Born, A., Strotz, D., Guntert, P., Vogeli, B. &amp;lt;br&amp;gt; High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints. [https://doi.org/10.1038/s42003-018-0067-x .] [Commun Biol 2018]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY4 6BY4]&#039;&#039;&#039; [http://files.rcsb.org/download/6by4_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY5 6BY5]&#039;&#039;&#039; [http://files.rcsb.org/download/6by5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6fgn.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6FGN]]&lt;br /&gt;
|Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGN 6FGN]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgn_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34231 34231]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGS 6FGS]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34233 34233]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f3k.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F3K]]&lt;br /&gt;
|Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F3K 6F3K]&#039;&#039;&#039; [http://files.rcsb.org/download/6f3k_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6R8N 6R8N]&#039;&#039;&#039; [http://files.rcsb.org/download/6r8n_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure after Phenix refinement)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n2o.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N2O]]&lt;br /&gt;
|Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N2O 5N2O]&#039;&#039;&#039; [http://files.rcsb.org/download/5n2o_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34095 34095]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n6r.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N6R]]&lt;br /&gt;
|Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[http://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N6R 5N6R]&#039;&#039;&#039; [http://files.rcsb.org/download/5N6R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=34101 34101]&#039;&#039;&#039; (DH NMR structure)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N7E 5N7E]&#039;&#039;&#039; (DH/Mb(Bcr-DH_4))&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5OC7 5OC7]&#039;&#039;&#039; (PH/Mb(Bcr-PH_4))&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N5E_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N5E]]&lt;br /&gt;
|Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[http://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://dx.doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N5E 2N5E]&#039;&#039;&#039; [http://files.rcsb.org/download/2N5E.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25710 25710]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:5gvq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5GVQ]]&lt;br /&gt;
|Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[http://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://dx.doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5GVQ 5GVQ]&#039;&#039;&#039; [http://files.rcsb.org/download/5GVQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=36018 36018]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N9L_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N9L]]&lt;br /&gt;
|Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[http://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://dx.doi.org/10.1038/srep38312 Sci Rep. 6, 38312 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N9L 2N9L]&#039;&#039;&#039; [http://files.rcsb.org/download/2N9L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25910 25910]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2NB1_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NB1]]&lt;br /&gt;
|Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[http://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://dx.doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NB1 2NB1]&#039;&#039;&#039; [http://files.rcsb.org/download/2NB1.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25958 25958]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
|[[image:2NAO_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NAO]]&lt;br /&gt;
|Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. [http://dx.doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NAO 2NAO]&#039;&#039;&#039; [http://files.rcsb.org/download/2NAO.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=26692 26692]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MYX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MYX]]&lt;br /&gt;
|von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[http://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://dx.doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MYX 2MYX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MYX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25461 25461]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MWX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MWX]]&lt;br /&gt;
|Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[http://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://dx.doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173-180 (2015)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MWX 2MWX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MWX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25376 25376]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MVX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MVX]]&lt;br /&gt;
|Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., and Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[http://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://dx.doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MVX 2MVX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MVX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25289 25289]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RUG_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RUG]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[http://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://dx.doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RUG 2RUG]&#039;&#039;&#039; [http://files.rcsb.org/download/2RUG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11563 11563]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RU3_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[http://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://dx.doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU3 2RU3]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU3.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11517 11517]&#039;&#039;&#039; (SUP-12–RNA&amp;lt;sub&amp;gt;6&amp;lt;/sub&amp;gt; complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MGZ 2MGZ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MGZ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11518 11518]&#039;&#039;&#039; (ASD-1–SUP-12–RNA&amp;lt;sub&amp;gt;12&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MMJ_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[http://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://dx.doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MMJ 2MMJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MMJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19856 19856]&#039;&#039;&#039; (M-Nleu11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN9 2MN9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19883 19883]&#039;&#039;&#039; (M-Nleu13 trans)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN8 2MN8]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19882 19882]&#039;&#039;&#039; (M-Nleu13 cis)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RU5_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU5]]&lt;br /&gt;
|Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[http://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://dx.doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU5 2RU5]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU5.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11548 11548]&#039;&#039;&#039; (uncomplexed MA)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU4 2RU4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11544 11544]&#039;&#039;&#039; (MA-YM&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MD9_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MD9]]&lt;br /&gt;
|Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[http://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://dx.doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MD9 2MD9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MD9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19479 19479]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RTX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RTX]]&lt;br /&gt;
|Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[http://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://dx.doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RTX 2RTX]&#039;&#039;&#039; [http://files.rcsb.org/download/2RTX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11534 11534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M8I_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M8I]]&lt;br /&gt;
|Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[http://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://dx.doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8I 2M8I]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8I.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19258 19258]&#039;&#039;&#039; (wildtype&lt;br /&gt;
WW domain)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8J 2M8J]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19259 19259]&#039;&#039;&#039; (WW(S16E) mutant)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUE_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUE]]&lt;br /&gt;
|Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://dx.doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LUE 2LUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2LUE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18518 18518]&#039;&#039;&#039; (NMR structure of LC3B OPTN-LIR Ptot complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTU]&#039;&#039;&#039; (crystal structure of human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTV]&#039;&#039;&#039; (crystal structure of Optineurin LIR-fused human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTW]&#039;&#039;&#039; (crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M99_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99]]&lt;br /&gt;
|Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[http://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://dx.doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99 2M99]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2M99.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19287 19287]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK6]]&lt;br /&gt;
|He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[http://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://dx.doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DK6 2DK6]&#039;&#039;&#039; [http://files.rcsb.org/download/2DK6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11500 11500]&#039;&#039;&#039; (WWE domain from PARP11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X4R 1X4R]&#039;&#039;&#039; [http://files.rcsb.org/download/1X4R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11501 11501]&#039;&#039;&#039; (WWE domain&lt;br /&gt;
from PARP14)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LVL_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL]]&lt;br /&gt;
|Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://dx.doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL 2LVL]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LVL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17534 17534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM]]&lt;br /&gt;
|Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[http://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://dx.doi.org/10.1038/nsmb.2355 Nature Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM 2LUM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LUM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18531 18531]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RSM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM]]&lt;br /&gt;
|Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[http://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM 2RSM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RSM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11491 11491]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RS6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RS6]]&lt;br /&gt;
|Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[http://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://dx.doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS6 2RS6]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11456 11456]&#039;&#039;&#039; (dsRBD1)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS7 2RS7]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS7.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11457 11457]&#039;&#039;&#039; (dsRBD2)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LIW_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LIW]]&lt;br /&gt;
|Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[http://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://dx.doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIU 2LIU]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17906 17906]&#039;&#039;&#039; (holo-ACPI)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIW 2LIW]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIW.mr NMR restraints] [http://www.rcsb.org/pdb/files/2LIW_cs.str.gz chemical shifts] (HMG-ACPI)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2DK4_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4]]&lt;br /&gt;
|He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[http://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://dx.doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4 2DK4]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2DK4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11355 11355]&#039;&#039;&#039;&lt;br /&gt;
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|[[image:2L6X_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X]]&lt;br /&gt;
|Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[http://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://dx.doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X 2L6X]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L6X.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17327 17327]&#039;&#039;&#039;&lt;br /&gt;
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|[[image:2L8J_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J]]&lt;br /&gt;
|Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[http://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J 2L8J]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17412 17412]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2KX7_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7]]&lt;br /&gt;
|Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[http://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://dx.doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7 2KX7]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KX7.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2RRB_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB]]&lt;br /&gt;
|Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[http://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://dx.doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB 2RRB]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RRB.mr NMR restraints] &lt;br /&gt;
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|[[image:3llh_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH 3LLH]&#039;&#039;&#039;&lt;br /&gt;
[http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=STRUCTFACT&amp;amp;compression=NO&amp;amp;structureId=3LLH Structure factors]&lt;br /&gt;
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|[[image:2cpn_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN 2CPN]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2CPN.mr NMR restraints] &lt;br /&gt;
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|[[image:1j26_asym_r_500_2.jpg|120px|link=http://www.pdb.org/pdb/explore/explore.do?structureId=1J26]]&lt;br /&gt;
|Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[http://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://dx.doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/images.do?structureId=1J26 1J26]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rqo_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO]]&lt;br /&gt;
|Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[http://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://dx.doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO 2RQO]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RQO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e61_bio_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2E61]]&lt;br /&gt;
|He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[http://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2E61 2E61]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2E61.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kr6_asym_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2KR6]]&lt;br /&gt;
|Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[http://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://dx.doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2KR6 2KR6]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KR6.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kby_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KBY]]&lt;br /&gt;
|Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[http://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://dx.doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KBY 2KBY]&#039;&#039;&#039; [http://files.rcsb.org/download/2KBY.mr NMR restraints]&lt;br /&gt;
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|[[image:2yue_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2YUE]]&lt;br /&gt;
|He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the Drosophila Neuralized E3 ligase in the Notch signaling pathway[http://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2YUE 2YUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2YUE.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E63 2E63]&#039;&#039;&#039; [http://files.rcsb.org/download/2E63.mr NMR restraints]&lt;br /&gt;
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|[[image:2klo_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KLO]]&lt;br /&gt;
|Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H., Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[http://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://dx.doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KLO 2KLO]&#039;&#039;&#039; [http://files.rcsb.org/download/2KLO.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3A4C 3A4C]&#039;&#039;&#039;&lt;br /&gt;
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|[[image:2rqc_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RQC]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[http://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://dx.doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQC 2RQC]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQC.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQ4 2RQ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQ4.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rpj_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RPJ]]&lt;br /&gt;
|He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[http://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RPJ 2RPJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2RPJ.mr NMR restraints]&lt;br /&gt;
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|[[image:2kak_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KAK]]&lt;br /&gt;
|Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[http://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KAK 2KAK]&#039;&#039;&#039; [http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=NMR&amp;amp;structureId=2KAK NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=16025 16025]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rog_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2ROG]]&lt;br /&gt;
|Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[http://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROG 2ROG]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11037 11037]&#039;&#039;&#039; (in-cell)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROE 2ROE]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11035 11035]&#039;&#039;&#039; (in solution)&lt;br /&gt;
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|[[image:2e5s_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E5S]]&lt;br /&gt;
|He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[http://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E5S 2E5S]&#039;&#039;&#039;　[http://files.rcsb.org/download/2E5S.mr NMR restraints]&lt;br /&gt;
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|[[image:2e29_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E29]]&lt;br /&gt;
|Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[http://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E29 2E29]&#039;&#039;&#039;&lt;br /&gt;
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|[[image:2jz4_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JZ4]]&lt;br /&gt;
|Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JZ4 2JZ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2JZ4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15607 15607]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2ba3_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2BA3]]&lt;br /&gt;
|Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[http://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2BA3 2BA3]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15784 15784]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jns_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JNS]]&lt;br /&gt;
|Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[http://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JNS 2JNS]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15125 15125]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2ron_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RON]]&lt;br /&gt;
|Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[http://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RON 2RON]&#039;&#039;&#039; [http://files.rcsb.org/download/2RON.mr NMR restraints] (SrfTEII)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2K2Q 2K2Q]&#039;&#039;&#039; [http://files.rcsb.org/download/2K2Q.mr NMR restraints] (complex of SrfTEII and H state TycC3–PCP)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1whv_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition[http://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WHV 1WHV]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROK 2ROK]&#039;&#039;&#039; (cap-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jw8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JW8 2JW8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15511 15511]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rne_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RNE 2RNE]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2fho asym r 250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2FHO]]&lt;br /&gt;
|Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2FHO 2FHO]&#039;&#039;&#039;  [http://files.rcsb.org/download/2FHO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jo8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[http://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JO8 2JO8]&#039;&#039;&#039;  [http://files.rcsb.org/download/2JO8.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dwv asym r 250.jpg|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2DWV]]&lt;br /&gt;
|Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[http://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DWV 2DWV]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dt6 asym r 250.jpg|120px]]&lt;br /&gt;
|Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[http://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT6 2DT6]&#039;&#039;&#039; (SURP1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT7 2DT7]&#039;&#039;&#039; (SURP2-SF3a60)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcp asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270(9-135) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCP 2DCP]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCP.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with [[FLYA]]. Structure does not supersede the original deposition 1VDY.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcq asym r 250.jpg|120px]]&lt;br /&gt;
|Rhodanese homology domain At3g16270(175-295) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCQ 2DCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCQ.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1VEE.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcr asym r 250.jpg|120px]]&lt;br /&gt;
|Src homology domain 2 from the human feline sarcoma oncogene Fes.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCR 2DCR]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCR.mr NMR restraints]br&amp;gt;Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1WQU.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2h3s asym r 250.jpg|120px]]&lt;br /&gt;
|Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[http://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H4B 2H4B]&#039;&#039;&#039; [http://files.rcsb.org/download/2H4B.mr NMR restraints] (cis-1-PP)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3S 2H3S]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3S.mr NMR restraints] (cis-1-PP bound to DPC micelles)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3T 2H3T]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3T.mr NMR restraints] (trans-1-PP bound to DPC micelles)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wvo asym r 250.jpg|120px]]&lt;br /&gt;
|Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[http://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WVO 1WVO]&#039;&#039;&#039; [http://files.rcsb.org/download/1WVO.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2agm asym r 250.jpg|120px]]&lt;br /&gt;
|Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[http://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2AGM 2AGM]&#039;&#039;&#039; [http://files.rcsb.org/download/2AGM.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2d21 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) maltodextrin-binding protein MBP.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2D21 2D21]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6807 6807]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1x02 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) calmodulin.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X02 1X02]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6541 6541]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wwq asym r 250.jpg|120px]]&lt;br /&gt;
|Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WWQ 1WWQ]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wqu asym r 250.jpg|120px]]&lt;br /&gt;
|Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[http://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WQU 1WQU]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6331 6331]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1n27 asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[http://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://www3.interscience.wiley.com/journal/121602709/abstract Protein Sci. 14, 756–764 (2005)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1N27 1N27]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1u3m asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[http://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U3M 1U3M]&#039;&#039;&#039; [http://files.rcsb.org/download/1U3M.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6269 6269]&#039;&#039;&#039; (chicken PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U5L 1U5L]&#039;&#039;&#039; [http://files.rcsb.org/download/1U5L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6270 6270]&#039;&#039;&#039; (turtle PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XU0 1XU0]&#039;&#039;&#039; [http://files.rcsb.org/download/1XU0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6282 6282]&#039;&#039;&#039; (frog PrP(90-222))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1xyj asym r 250.jpg|120px]]&lt;br /&gt;
|Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[http://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYJ 1XYJ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6377 6377]&#039;&#039;&#039; (cat PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYK 1XYK]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYK.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6378 6378]&#039;&#039;&#039; (dog PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYQ 1XYQ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6380 6380]&#039;&#039;&#039; (pig PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYU 1XYU]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6381 6381]&#039;&#039;&#039; (sheep PrP[R168](121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Y2S 1Y2S]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6403 6403]&#039;&#039;&#039; (sheep PrP[H168](121-231))&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1vex asym r 250.jpg|120px]]&lt;br /&gt;
|Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[http://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SZL 1SZL]&#039;&#039;&#039;　[http://files.rcsb.org/download/1SZL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6175 6175]&#039;&#039;&#039; (TSR1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEX 1VEX]&#039;&#039;&#039; (TSR4)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1vdy asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VDY 1VDY]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5928 5928]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1vd0 asym r 250.jpg|120px]]&lt;br /&gt;
|Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[http://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VD0 1VD0]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1vee asym r 250.jpg|120px]]&lt;br /&gt;
|Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[http://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://www3.interscience.wiley.com/journal/121602579/abstract Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEE 1VEE]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5929 5929]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1ukx asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[http://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://dx.doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1UKX 1UKX]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6297 6297]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1q9g asym r 250.jpg|120px]]&lt;br /&gt;
|Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[http://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Q9G 1Q9G]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1wln asym r 250.jpg|120px]]&lt;br /&gt;
|FHA domain of mouse afadin 6.&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WLN 1WLN]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1pbu asym r 250.jpg|120px]]&lt;br /&gt;
|Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[http://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PBU 1PBU]&#039;&#039;&#039; [http://files.rcsb.org/download/1PBU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5628 5628]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1mo8 asym r 250.jpg|120px]]&lt;br /&gt;
|Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[http://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://www.nature.com/nsmb/journal/v10/n6/abs/nsb924.html Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO7 1MO7]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5577 5577]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO8 1MO8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5576 5576]&#039;&#039;&#039; (ATP-bound form)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1lg4 asym r 250.jpg|120px]]&lt;br /&gt;
|Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[http://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LG4 1LG4]&#039;&#039;&#039; [http://files.rcsb.org/download/1LG4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5145 5145]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1h0l asym r 250.jpg|120px]]&lt;br /&gt;
|Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[http://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1H0L 1H0L]&#039;&#039;&#039; [http://files.rcsb.org/download/1H0L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5378 5378]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1sr3 asym r 250.jpg|120px]]&lt;br /&gt;
|Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[http://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://dx.doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SR3 1SR3]&#039;&#039;&#039; [http://files.rcsb.org/download/1SR3.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ls8 asym r 250.jpg|120px]]&lt;br /&gt;
|Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[http://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://dx.doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LS8 1LS8]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1k9c asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K9C 1K9C]&#039;&#039;&#039; [http://files.rcsb.org/download/1K9C.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5204 5204]&#039;&#039;&#039; (residues 189-261)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K91 1K91]&#039;&#039;&#039; [http://files.rcsb.org/download/1K91.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5205 5205]&#039;&#039;&#039; (residues 221-256)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1jas asym r 250.jpg|120px]]&lt;br /&gt;
|Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[http://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1JAS 1JAS]&#039;&#039;&#039; [http://files.rcsb.org/download/1JAS.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5038 5038]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1gm0 asym r 250.jpg|120px]]&lt;br /&gt;
|Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[http://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1GM0 1GM0]&#039;&#039;&#039; [http://files.rcsb.org/download/1GM0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4849 4849]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hhn asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HHN 1HHN]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4878 4878]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1e1g asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[http://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1G 1E1G]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1G.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4736 4736]&#039;&#039;&#039; (variant M166V)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1P 1E1P]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1P.mr NMR restraints] (variant S170N)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1U 1E1U]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1U.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4620 4620]&#039;&#039;&#039; (variant R220K)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1qjk asym r 250.jpg|120px]]&lt;br /&gt;
|Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[http://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJK 1QJK]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJK.mr NMR restraints] (&amp;amp;alpha; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJL 1QJL]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJL.mr NMR restraints] (&amp;amp;beta; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4363 4363]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1bf8 asym r 250.jpg|120px]]&lt;br /&gt;
|Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[http://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://dx.doi.org/10.1038/2325 Nature Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1BF8 1BF8]&#039;&#039;&#039; [http://files.rcsb.org/download/1BF8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4070 4070]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1oca asym r 250.jpg|120px]]&lt;br /&gt;
|Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[http://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1OCA 1OCA]&#039;&#039;&#039; [http://files.rcsb.org/download/1OCA.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wkt asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[http://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://dx.doi.org/10.1038/nsb0896-662 Nature Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WKT 1WKT]&#039;&#039;&#039; [http://files.rcsb.org/download/1WKT.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5255 5255]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1tap asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://dx.doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1TAP 1TAP]&#039;&#039;&#039; [http://files.rcsb.org/download/1TAP.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1dtk asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1DTK 1DTK]&#039;&#039;&#039; [http://files.rcsb.org/download/1DTK.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hic asym r 250.jpg|120px]]&lt;br /&gt;
|Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[http://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HIC 1HIC]&#039;&#039;&#039; [http://files.rcsb.org/download/1HIC.mr NMR restraints]&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=1128 1128]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pit asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[http://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PIT 1PIT]&#039;&#039;&#039; [http://files.rcsb.org/download/1PIT.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2hoa asym r 250.jpg|120px]]&lt;br /&gt;
|Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[http://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2HOA 2HOA]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
|}&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59287</id>
		<title>Protein structures</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59287"/>
		<updated>2026-01-13T22:03:11Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;NMR protein structures co-authored by P. Güntert.&lt;br /&gt;
&lt;br /&gt;
{|&lt;br /&gt;
&lt;br /&gt;
|[[image:8ox2.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8OX2]]&lt;br /&gt;
|Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OVI 8OVI]&#039;&#039;&#039; [http://files.rcsb.org/download/8ovi_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34811 34811]&#039;&#039;&#039; (monomer)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OX2 8OX2]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34813 34813]&#039;&#039;&#039; (trimer)&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8kcq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8KCQ]]&lt;br /&gt;
|Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8KCQ 8KCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=36589 36589]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8qbp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8QBP]]&lt;br /&gt;
|Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QBP 8QBP]&#039;&#039;&#039; [http://files.rcsb.org/download/8qbp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34850 34850]&#039;&#039;&#039; (OmphA “indole-In)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8Q7J 8Q7J]&#039;&#039;&#039; [http://files.rcsb.org/download/8q7j_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34846 34846]&#039;&#039;&#039; (CsA)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAQ 8QAQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8qaq_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34848 34848]&#039;&#039;&#039; (OmphA&lt;br /&gt;
conformation 1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAS 8QAS]&#039;&#039;&#039; [http://files.rcsb.org/download/8qas_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34849 34849]&#039;&#039;&#039; (OmphA “indole-Out”)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:8pxs.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8PXS]]&lt;br /&gt;
|Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8PXS 8PXS]&#039;&#039;&#039; [http://files.rcsb.org/download/8pxs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34838 34838]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7x9u.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7X9U]]&lt;br /&gt;
|Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7X9U 7X9U]&#039;&#039;&#039; [http://files.rcsb.org/download/7x9u_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36478 36478]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qtr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QTR]]&lt;br /&gt;
|Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTR 7QTR]&#039;&#039;&#039; [http://files.rcsb.org/download/7qtr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34700 34700]&#039;&#039;&#039; (GB1 in cells at a protein concentration of 50 μM)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTS 7QTS]&#039;&#039;&#039; [http://files.rcsb.org/download/7qts_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34701 34701]&#039;&#039;&#039;  (GB1 in cells at a protein concentration of 10 μM)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qcx.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QCX]]&lt;br /&gt;
|Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCX 7QCX]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcx_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34688 34688]&#039;&#039;&#039; (two-state structure of apo PDZ2)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCY 7QCY]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcy_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34689 34689]&#039;&#039;&#039; (two-state structure of PDZ2 complexed with RA-GEF2 peptide)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7fbr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7FBR]]&lt;br /&gt;
|He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBR 7FBR]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36430 36430]&#039;&#039;&#039; (first RRM domain of Matrin-3)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBV 7FBV]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbv_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36431 36431]&#039;&#039;&#039; (second RRM domain of Matrin-3)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6tub.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6TUB]]&lt;br /&gt;
|Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6TUB 6TUB]&#039;&#039;&#039; [http://files.rcsb.org/download/6tub_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=26715 26715]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6svc.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6SVE]]&lt;br /&gt;
| Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVC 6SVC]&#039;&#039;&#039; [http://files.rcsb.org/download/6svc_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34432 34432]&#039;&#039;&#039;&lt;br /&gt;
(WW domain apo structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVE 6SVE]&#039;&#039;&#039; [http://files.rcsb.org/download/6sve_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34433 34433]&#039;&#039;&#039; (WW domain with pCdc25C bound)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVH 6SVH]&#039;&#039;&#039; [http://files.rcsb.org/download/6svh_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34434 34434]&#039;&#039;&#039; (WW domain with FFpSPR bound)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6qk6.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6QK6]]&lt;br /&gt;
|Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK5 6QK5]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34355 34355]&#039;&#039;&#039; (Zn-loaded form)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK6 6QK6]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34356 34356]&#039;&#039;&#039; (Cd-loaded form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5zcz.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5ZCZ]]&lt;br /&gt;
|Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZCZ 5ZCZ]&#039;&#039;&#039; [http://files.rcsb.org/download/5zcz_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27354 27354]&#039;&#039;&#039; (&#039;&#039;T. thermophilus&#039;&#039; HB8 TTHA1718 protein in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZD0 5ZD0]&#039;&#039;&#039; [http://files.rcsb.org/download/5zd0_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27356 27356]&#039;&#039;&#039; (ubiquitin with three alanine mutations in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5Z4B 5Z4B]&#039;&#039;&#039; [http://files.rcsb.org/download/5z4b_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36153 36153]&#039;&#039;&#039; (GB1 in living eukaryotic cells)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6h8c.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6H8C]]&lt;br /&gt;
|Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6H8C 6H8C]&#039;&#039;&#039; [http://files.rcsb.org/download/6h8c_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34307 34307]&#039;&#039;&#039; (GABARAPL2 in complex with the UBA5 LIR motif)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6HB9 6HB9]&#039;&#039;&#039; [http://files.rcsb.org/download/6hb9_nmr-data.nef.gz NMR data] (crystal structure of GABARAP in complex with UBA5 LIR motif)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f98.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F98]]&lt;br /&gt;
|Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F98 6F98]&#039;&#039;&#039; [http://files.rcsb.org/download/6f98_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34217 34217]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F99 6F99]&#039;&#039;&#039; [http://files.rcsb.org/download/6f99_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34218 34218]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F9A 6F9A]&#039;&#039;&#039; [http://files.rcsb.org/download/6f9a_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34219 34219]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6es5.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ES5]]&lt;br /&gt;
|Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES5 6ES5]&#039;&#039;&#039; [http://files.rcsb.org/download/6es5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34187 34187]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES6 6ES6]&#039;&#039;&#039; [http://files.rcsb.org/download/6es6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34188 34188]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES7 6ES7]&#039;&#039;&#039; [http://files.rcsb.org/download/6es7_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34189 34189]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6esp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ESP]]&lt;br /&gt;
|Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ESP 6ESP]&#039;&#039;&#039; [http://files.rcsb.org/download/6esp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34190 34190]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6by4.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6BY4]]&lt;br /&gt;
|Nichols, P.J., Henen, M.A., Born, A., Strotz, D., Guntert, P., Vogeli, B. &amp;lt;br&amp;gt; High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints. [https://doi.org/10.1038/s42003-018-0067-x .] [Commun Biol 2018]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY4 6BY4]&#039;&#039;&#039; [http://files.rcsb.org/download/6by4_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY5 6BY5]&#039;&#039;&#039; [http://files.rcsb.org/download/6by5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6fgn.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6FGN]]&lt;br /&gt;
|Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGN 6FGN]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgn_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34231 34231]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGS 6FGS]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34233 34233]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f3k.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F3K]]&lt;br /&gt;
|Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F3K 6F3K]&#039;&#039;&#039; [http://files.rcsb.org/download/6f3k_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6R8N 6R8N]&#039;&#039;&#039; [http://files.rcsb.org/download/6r8n_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure after Phenix refinement)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n2o.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N2O]]&lt;br /&gt;
|Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N2O 5N2O]&#039;&#039;&#039; [http://files.rcsb.org/download/5n2o_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34095 34095]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n6r.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N6R]]&lt;br /&gt;
|Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[http://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N6R 5N6R]&#039;&#039;&#039; [http://files.rcsb.org/download/5N6R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=34101 34101]&#039;&#039;&#039; (DH NMR structure)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N7E 5N7E]&#039;&#039;&#039; (DH/Mb(Bcr-DH_4))&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5OC7 5OC7]&#039;&#039;&#039; (PH/Mb(Bcr-PH_4))&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N5E_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N5E]]&lt;br /&gt;
|Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[http://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://dx.doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N5E 2N5E]&#039;&#039;&#039; [http://files.rcsb.org/download/2N5E.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25710 25710]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:5gvq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5GVQ]]&lt;br /&gt;
|Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[http://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://dx.doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5GVQ 5GVQ]&#039;&#039;&#039; [http://files.rcsb.org/download/5GVQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=36018 36018]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N9L_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N9L]]&lt;br /&gt;
|Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[http://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://dx.doi.org/10.1038/srep38312 Sci Rep. 6, 38312 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N9L 2N9L]&#039;&#039;&#039; [http://files.rcsb.org/download/2N9L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25910 25910]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2NB1_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NB1]]&lt;br /&gt;
|Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[http://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://dx.doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NB1 2NB1]&#039;&#039;&#039; [http://files.rcsb.org/download/2NB1.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25958 25958]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
|[[image:2NAO_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NAO]]&lt;br /&gt;
|Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. [http://dx.doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NAO 2NAO]&#039;&#039;&#039; [http://files.rcsb.org/download/2NAO.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=26692 26692]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MYX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MYX]]&lt;br /&gt;
|von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[http://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://dx.doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MYX 2MYX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MYX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25461 25461]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MWX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MWX]]&lt;br /&gt;
|Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[http://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://dx.doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173-180 (2015)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MWX 2MWX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MWX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25376 25376]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MVX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MVX]]&lt;br /&gt;
|Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., and Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[http://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://dx.doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MVX 2MVX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MVX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25289 25289]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RUG_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RUG]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[http://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://dx.doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RUG 2RUG]&#039;&#039;&#039; [http://files.rcsb.org/download/2RUG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11563 11563]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RU3_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[http://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://dx.doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU3 2RU3]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU3.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11517 11517]&#039;&#039;&#039; (SUP-12–RNA&amp;lt;sub&amp;gt;6&amp;lt;/sub&amp;gt; complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MGZ 2MGZ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MGZ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11518 11518]&#039;&#039;&#039; (ASD-1–SUP-12–RNA&amp;lt;sub&amp;gt;12&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MMJ_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[http://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://dx.doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MMJ 2MMJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MMJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19856 19856]&#039;&#039;&#039; (M-Nleu11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN9 2MN9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19883 19883]&#039;&#039;&#039; (M-Nleu13 trans)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN8 2MN8]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19882 19882]&#039;&#039;&#039; (M-Nleu13 cis)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RU5_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU5]]&lt;br /&gt;
|Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[http://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://dx.doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU5 2RU5]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU5.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11548 11548]&#039;&#039;&#039; (uncomplexed MA)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU4 2RU4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11544 11544]&#039;&#039;&#039; (MA-YM&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MD9_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MD9]]&lt;br /&gt;
|Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[http://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://dx.doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MD9 2MD9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MD9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19479 19479]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RTX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RTX]]&lt;br /&gt;
|Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[http://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://dx.doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RTX 2RTX]&#039;&#039;&#039; [http://files.rcsb.org/download/2RTX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11534 11534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M8I_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M8I]]&lt;br /&gt;
|Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[http://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://dx.doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8I 2M8I]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8I.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19258 19258]&#039;&#039;&#039; (wildtype&lt;br /&gt;
WW domain)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8J 2M8J]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19259 19259]&#039;&#039;&#039; (WW(S16E) mutant)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUE_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUE]]&lt;br /&gt;
|Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://dx.doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LUE 2LUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2LUE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18518 18518]&#039;&#039;&#039; (NMR structure of LC3B OPTN-LIR Ptot complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTU]&#039;&#039;&#039; (crystal structure of human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTV]&#039;&#039;&#039; (crystal structure of Optineurin LIR-fused human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTW]&#039;&#039;&#039; (crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M99_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99]]&lt;br /&gt;
|Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[http://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://dx.doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99 2M99]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2M99.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19287 19287]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK6]]&lt;br /&gt;
|He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[http://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://dx.doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DK6 2DK6]&#039;&#039;&#039; [http://files.rcsb.org/download/2DK6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11500 11500]&#039;&#039;&#039; (WWE domain from PARP11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X4R 1X4R]&#039;&#039;&#039; [http://files.rcsb.org/download/1X4R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11501 11501]&#039;&#039;&#039; (WWE domain&lt;br /&gt;
from PARP14)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LVL_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL]]&lt;br /&gt;
|Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://dx.doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL 2LVL]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LVL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17534 17534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM]]&lt;br /&gt;
|Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[http://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://dx.doi.org/10.1038/nsmb.2355 Nature Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM 2LUM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LUM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18531 18531]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RSM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM]]&lt;br /&gt;
|Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[http://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM 2RSM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RSM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11491 11491]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RS6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RS6]]&lt;br /&gt;
|Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[http://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://dx.doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS6 2RS6]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11456 11456]&#039;&#039;&#039; (dsRBD1)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS7 2RS7]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS7.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11457 11457]&#039;&#039;&#039; (dsRBD2)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LIW_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LIW]]&lt;br /&gt;
|Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[http://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://dx.doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIU 2LIU]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17906 17906]&#039;&#039;&#039; (holo-ACPI)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIW 2LIW]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIW.mr NMR restraints] [http://www.rcsb.org/pdb/files/2LIW_cs.str.gz chemical shifts] (HMG-ACPI)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK4_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4]]&lt;br /&gt;
|He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[http://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://dx.doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4 2DK4]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2DK4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11355 11355]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L6X_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X]]&lt;br /&gt;
|Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[http://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://dx.doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X 2L6X]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L6X.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17327 17327]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L8J_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J]]&lt;br /&gt;
|Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[http://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J 2L8J]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17412 17412]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2KX7_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7]]&lt;br /&gt;
|Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[http://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://dx.doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7 2KX7]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KX7.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2RRB_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB]]&lt;br /&gt;
|Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[http://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://dx.doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB 2RRB]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RRB.mr NMR restraints] &lt;br /&gt;
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|[[image:3llh_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH 3LLH]&#039;&#039;&#039;&lt;br /&gt;
[http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=STRUCTFACT&amp;amp;compression=NO&amp;amp;structureId=3LLH Structure factors]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2cpn_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN 2CPN]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2CPN.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1j26_asym_r_500_2.jpg|120px|link=http://www.pdb.org/pdb/explore/explore.do?structureId=1J26]]&lt;br /&gt;
|Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[http://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://dx.doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/images.do?structureId=1J26 1J26]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rqo_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO]]&lt;br /&gt;
|Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[http://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://dx.doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO 2RQO]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RQO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e61_bio_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2E61]]&lt;br /&gt;
|He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[http://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2E61 2E61]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2E61.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kr6_asym_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2KR6]]&lt;br /&gt;
|Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[http://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://dx.doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2KR6 2KR6]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KR6.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kby_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KBY]]&lt;br /&gt;
|Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[http://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://dx.doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KBY 2KBY]&#039;&#039;&#039; [http://files.rcsb.org/download/2KBY.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2yue_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2YUE]]&lt;br /&gt;
|He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the Drosophila Neuralized E3 ligase in the Notch signaling pathway[http://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2YUE 2YUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2YUE.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E63 2E63]&#039;&#039;&#039; [http://files.rcsb.org/download/2E63.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2klo_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KLO]]&lt;br /&gt;
|Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H., Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[http://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://dx.doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KLO 2KLO]&#039;&#039;&#039; [http://files.rcsb.org/download/2KLO.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3A4C 3A4C]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rqc_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RQC]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[http://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://dx.doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQC 2RQC]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQC.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQ4 2RQ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQ4.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rpj_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RPJ]]&lt;br /&gt;
|He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[http://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RPJ 2RPJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2RPJ.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kak_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KAK]]&lt;br /&gt;
|Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[http://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KAK 2KAK]&#039;&#039;&#039; [http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=NMR&amp;amp;structureId=2KAK NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=16025 16025]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rog_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2ROG]]&lt;br /&gt;
|Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[http://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROG 2ROG]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11037 11037]&#039;&#039;&#039; (in-cell)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROE 2ROE]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11035 11035]&#039;&#039;&#039; (in solution)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e5s_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E5S]]&lt;br /&gt;
|He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[http://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E5S 2E5S]&#039;&#039;&#039;　[http://files.rcsb.org/download/2E5S.mr NMR restraints]&lt;br /&gt;
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|[[image:2e29_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E29]]&lt;br /&gt;
|Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[http://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E29 2E29]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2jz4_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JZ4]]&lt;br /&gt;
|Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JZ4 2JZ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2JZ4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15607 15607]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2ba3_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2BA3]]&lt;br /&gt;
|Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[http://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2BA3 2BA3]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15784 15784]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2jns_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JNS]]&lt;br /&gt;
|Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[http://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JNS 2JNS]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15125 15125]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2ron_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RON]]&lt;br /&gt;
|Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[http://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RON 2RON]&#039;&#039;&#039; [http://files.rcsb.org/download/2RON.mr NMR restraints] (SrfTEII)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2K2Q 2K2Q]&#039;&#039;&#039; [http://files.rcsb.org/download/2K2Q.mr NMR restraints] (complex of SrfTEII and H state TycC3–PCP)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1whv_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition[http://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WHV 1WHV]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROK 2ROK]&#039;&#039;&#039; (cap-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jw8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JW8 2JW8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15511 15511]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rne_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RNE 2RNE]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2fho asym r 250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2FHO]]&lt;br /&gt;
|Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2FHO 2FHO]&#039;&#039;&#039;  [http://files.rcsb.org/download/2FHO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jo8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[http://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JO8 2JO8]&#039;&#039;&#039;  [http://files.rcsb.org/download/2JO8.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dwv asym r 250.jpg|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2DWV]]&lt;br /&gt;
|Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[http://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DWV 2DWV]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dt6 asym r 250.jpg|120px]]&lt;br /&gt;
|Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[http://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT6 2DT6]&#039;&#039;&#039; (SURP1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT7 2DT7]&#039;&#039;&#039; (SURP2-SF3a60)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcp asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270(9-135) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCP 2DCP]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCP.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with [[FLYA]]. Structure does not supersede the original deposition 1VDY.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcq asym r 250.jpg|120px]]&lt;br /&gt;
|Rhodanese homology domain At3g16270(175-295) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCQ 2DCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCQ.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1VEE.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcr asym r 250.jpg|120px]]&lt;br /&gt;
|Src homology domain 2 from the human feline sarcoma oncogene Fes.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCR 2DCR]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCR.mr NMR restraints]br&amp;gt;Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1WQU.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2h3s asym r 250.jpg|120px]]&lt;br /&gt;
|Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[http://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H4B 2H4B]&#039;&#039;&#039; [http://files.rcsb.org/download/2H4B.mr NMR restraints] (cis-1-PP)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3S 2H3S]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3S.mr NMR restraints] (cis-1-PP bound to DPC micelles)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3T 2H3T]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3T.mr NMR restraints] (trans-1-PP bound to DPC micelles)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wvo asym r 250.jpg|120px]]&lt;br /&gt;
|Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[http://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WVO 1WVO]&#039;&#039;&#039; [http://files.rcsb.org/download/1WVO.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2agm asym r 250.jpg|120px]]&lt;br /&gt;
|Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[http://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2AGM 2AGM]&#039;&#039;&#039; [http://files.rcsb.org/download/2AGM.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2d21 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) maltodextrin-binding protein MBP.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2D21 2D21]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6807 6807]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1x02 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) calmodulin.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X02 1X02]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6541 6541]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wwq asym r 250.jpg|120px]]&lt;br /&gt;
|Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WWQ 1WWQ]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wqu asym r 250.jpg|120px]]&lt;br /&gt;
|Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[http://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WQU 1WQU]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6331 6331]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1n27 asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[http://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://www3.interscience.wiley.com/journal/121602709/abstract Protein Sci. 14, 756–764 (2005)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1N27 1N27]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1u3m asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[http://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U3M 1U3M]&#039;&#039;&#039; [http://files.rcsb.org/download/1U3M.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6269 6269]&#039;&#039;&#039; (chicken PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U5L 1U5L]&#039;&#039;&#039; [http://files.rcsb.org/download/1U5L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6270 6270]&#039;&#039;&#039; (turtle PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XU0 1XU0]&#039;&#039;&#039; [http://files.rcsb.org/download/1XU0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6282 6282]&#039;&#039;&#039; (frog PrP(90-222))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1xyj asym r 250.jpg|120px]]&lt;br /&gt;
|Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[http://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYJ 1XYJ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6377 6377]&#039;&#039;&#039; (cat PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYK 1XYK]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYK.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6378 6378]&#039;&#039;&#039; (dog PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYQ 1XYQ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6380 6380]&#039;&#039;&#039; (pig PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYU 1XYU]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6381 6381]&#039;&#039;&#039; (sheep PrP[R168](121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Y2S 1Y2S]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6403 6403]&#039;&#039;&#039; (sheep PrP[H168](121-231))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vex asym r 250.jpg|120px]]&lt;br /&gt;
|Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[http://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SZL 1SZL]&#039;&#039;&#039;　[http://files.rcsb.org/download/1SZL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6175 6175]&#039;&#039;&#039; (TSR1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEX 1VEX]&#039;&#039;&#039; (TSR4)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vdy asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VDY 1VDY]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5928 5928]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vd0 asym r 250.jpg|120px]]&lt;br /&gt;
|Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[http://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VD0 1VD0]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1vee asym r 250.jpg|120px]]&lt;br /&gt;
|Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[http://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://www3.interscience.wiley.com/journal/121602579/abstract Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEE 1VEE]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5929 5929]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ukx asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[http://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://dx.doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1UKX 1UKX]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6297 6297]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1q9g asym r 250.jpg|120px]]&lt;br /&gt;
|Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[http://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Q9G 1Q9G]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1wln asym r 250.jpg|120px]]&lt;br /&gt;
|FHA domain of mouse afadin 6.&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WLN 1WLN]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pbu asym r 250.jpg|120px]]&lt;br /&gt;
|Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[http://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PBU 1PBU]&#039;&#039;&#039; [http://files.rcsb.org/download/1PBU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5628 5628]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1mo8 asym r 250.jpg|120px]]&lt;br /&gt;
|Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[http://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://www.nature.com/nsmb/journal/v10/n6/abs/nsb924.html Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO7 1MO7]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5577 5577]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO8 1MO8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5576 5576]&#039;&#039;&#039; (ATP-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1lg4 asym r 250.jpg|120px]]&lt;br /&gt;
|Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[http://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LG4 1LG4]&#039;&#039;&#039; [http://files.rcsb.org/download/1LG4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5145 5145]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1h0l asym r 250.jpg|120px]]&lt;br /&gt;
|Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[http://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1H0L 1H0L]&#039;&#039;&#039; [http://files.rcsb.org/download/1H0L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5378 5378]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1sr3 asym r 250.jpg|120px]]&lt;br /&gt;
|Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[http://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://dx.doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SR3 1SR3]&#039;&#039;&#039; [http://files.rcsb.org/download/1SR3.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ls8 asym r 250.jpg|120px]]&lt;br /&gt;
|Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[http://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://dx.doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LS8 1LS8]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1k9c asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K9C 1K9C]&#039;&#039;&#039; [http://files.rcsb.org/download/1K9C.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5204 5204]&#039;&#039;&#039; (residues 189-261)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K91 1K91]&#039;&#039;&#039; [http://files.rcsb.org/download/1K91.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5205 5205]&#039;&#039;&#039; (residues 221-256)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1jas asym r 250.jpg|120px]]&lt;br /&gt;
|Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[http://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1JAS 1JAS]&#039;&#039;&#039; [http://files.rcsb.org/download/1JAS.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5038 5038]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1gm0 asym r 250.jpg|120px]]&lt;br /&gt;
|Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[http://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1GM0 1GM0]&#039;&#039;&#039; [http://files.rcsb.org/download/1GM0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4849 4849]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hhn asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HHN 1HHN]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4878 4878]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1e1g asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[http://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1G 1E1G]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1G.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4736 4736]&#039;&#039;&#039; (variant M166V)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1P 1E1P]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1P.mr NMR restraints] (variant S170N)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1U 1E1U]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1U.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4620 4620]&#039;&#039;&#039; (variant R220K)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1qjk asym r 250.jpg|120px]]&lt;br /&gt;
|Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[http://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJK 1QJK]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJK.mr NMR restraints] (&amp;amp;alpha; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJL 1QJL]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJL.mr NMR restraints] (&amp;amp;beta; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4363 4363]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1bf8 asym r 250.jpg|120px]]&lt;br /&gt;
|Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[http://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://dx.doi.org/10.1038/2325 Nature Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1BF8 1BF8]&#039;&#039;&#039; [http://files.rcsb.org/download/1BF8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4070 4070]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1oca asym r 250.jpg|120px]]&lt;br /&gt;
|Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[http://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1OCA 1OCA]&#039;&#039;&#039; [http://files.rcsb.org/download/1OCA.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wkt asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[http://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://dx.doi.org/10.1038/nsb0896-662 Nature Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WKT 1WKT]&#039;&#039;&#039; [http://files.rcsb.org/download/1WKT.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5255 5255]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1tap asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://dx.doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1TAP 1TAP]&#039;&#039;&#039; [http://files.rcsb.org/download/1TAP.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1dtk asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1DTK 1DTK]&#039;&#039;&#039; [http://files.rcsb.org/download/1DTK.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hic asym r 250.jpg|120px]]&lt;br /&gt;
|Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[http://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HIC 1HIC]&#039;&#039;&#039; [http://files.rcsb.org/download/1HIC.mr NMR restraints]&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=1128 1128]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pit asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[http://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PIT 1PIT]&#039;&#039;&#039; [http://files.rcsb.org/download/1PIT.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2hoa asym r 250.jpg|120px]]&lt;br /&gt;
|Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[http://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2HOA 2HOA]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
|}&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59286</id>
		<title>Protein structures</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59286"/>
		<updated>2026-01-13T21:59:44Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;NMR protein structures co-authored by P. Güntert.&lt;br /&gt;
&lt;br /&gt;
{|&lt;br /&gt;
&lt;br /&gt;
|[[image:8ox2.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8OX2]]&lt;br /&gt;
|Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OVI 8OVI]&#039;&#039;&#039; [http://files.rcsb.org/download/8ovi_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34811 34811]&#039;&#039;&#039; (monomer)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OX2 8OX2]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34813 34813]&#039;&#039;&#039; (trimer)&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8kcq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8KCQ]]&lt;br /&gt;
|Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8KCQ 8KCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=36589 36589]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8qbp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8QBP]]&lt;br /&gt;
|Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QBP 8QBP]&#039;&#039;&#039; [http://files.rcsb.org/download/8qbp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34850 34850]&#039;&#039;&#039; (OmphA “indole-In)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8Q7J 8Q7J]&#039;&#039;&#039; [http://files.rcsb.org/download/8q7j_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34846 34846]&#039;&#039;&#039; (CsA)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAQ 8QAQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8qaq_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34848 34848]&#039;&#039;&#039; (OmphA&lt;br /&gt;
conformation 1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAS 8QAS]&#039;&#039;&#039; [http://files.rcsb.org/download/8qas_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34849 34849]&#039;&#039;&#039; (OmphA “indole-Out”)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:8pxs.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8PXS]]&lt;br /&gt;
|Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8PXS 8PXS]&#039;&#039;&#039; [http://files.rcsb.org/download/8pxs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34838 34838]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7x9u.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7X9U]]&lt;br /&gt;
|Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7X9U 7X9U]&#039;&#039;&#039; [http://files.rcsb.org/download/7x9u_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36478 36478]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qtr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QTR]]&lt;br /&gt;
|Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTR 7QTR]&#039;&#039;&#039; [http://files.rcsb.org/download/7qtr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34700 34700]&#039;&#039;&#039; (GB1 in cells at a protein concentration of 50 μM)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTS 7QTS]&#039;&#039;&#039; [http://files.rcsb.org/download/7qts_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34701 34701]&#039;&#039;&#039;  (GB1 in cells at a protein concentration of 10 μM)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qcx.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QCX]]&lt;br /&gt;
|Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCX 7QCX]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcx_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34688 34688]&#039;&#039;&#039; (two-state structure of apo PDZ2)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCY 7QCY]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcy_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34689 34689]&#039;&#039;&#039; (two-state structure of PDZ2 complexed with RA-GEF2 peptide)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7fbr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7FBR]]&lt;br /&gt;
|He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBR 7FBR]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36430 36430]&#039;&#039;&#039; (first RRM domain of Matrin-3)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBV 7FBV]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbv_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36431 36431]&#039;&#039;&#039; (second RRM domain of Matrin-3)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6tub.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6TUB]]&lt;br /&gt;
|Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6TUB 6TUB]&#039;&#039;&#039; [http://files.rcsb.org/download/6tub_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=26715 26715]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6svc.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6SVE]]&lt;br /&gt;
| Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVC 6SVC]&#039;&#039;&#039; [http://files.rcsb.org/download/6svc_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34432 34432]&#039;&#039;&#039;&lt;br /&gt;
(WW domain apo structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVE 6SVE]&#039;&#039;&#039; [http://files.rcsb.org/download/6sve_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34433 34433]&#039;&#039;&#039; (WW domain with pCdc25C bound)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVH 6SVH]&#039;&#039;&#039; [http://files.rcsb.org/download/6svh_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34434 34434]&#039;&#039;&#039; (WW domain with FFpSPR bound)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6qk6.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6QK6]]&lt;br /&gt;
|Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK5 6QK5]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34355 34355]&#039;&#039;&#039; (Zn-loaded form)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK6 6QK6]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34356 34356]&#039;&#039;&#039; (Cd-loaded form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5zcz.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5ZCZ]]&lt;br /&gt;
|Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZCZ 5ZCZ]&#039;&#039;&#039; [http://files.rcsb.org/download/5zcz_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27354 27354]&#039;&#039;&#039; (&#039;&#039;T. Thermophilus&#039;&#039; HB8 TTHA1718 protein in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZD0 5ZD0]&#039;&#039;&#039; [http://files.rcsb.org/download/5zd0_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27356 27356]&#039;&#039;&#039; (ubiquitin with three alanine mutations in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5Z4B 5Z4B]&#039;&#039;&#039; [http://files.rcsb.org/download/5z4b_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36153 36153]&#039;&#039;&#039; (GB1 in living eukaryotic cells)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6h8c.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6H8C]]&lt;br /&gt;
|Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6H8C 6H8C]&#039;&#039;&#039; [http://files.rcsb.org/download/6h8c_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34307 34307]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6HB9 6HB9]&#039;&#039;&#039; [http://files.rcsb.org/download/6hb9_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB N/A&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f98.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F98]]&lt;br /&gt;
|Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F98 6F98]&#039;&#039;&#039; [http://files.rcsb.org/download/6f98_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34217 34217]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F99 6F99]&#039;&#039;&#039; [http://files.rcsb.org/download/6f99_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34218 34218]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F9A 6F9A]&#039;&#039;&#039; [http://files.rcsb.org/download/6f9a_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34219 34219]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6es5.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ES5]]&lt;br /&gt;
|Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES5 6ES5]&#039;&#039;&#039; [http://files.rcsb.org/download/6es5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34187 34187]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES6 6ES6]&#039;&#039;&#039; [http://files.rcsb.org/download/6es6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34188 34188]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES7 6ES7]&#039;&#039;&#039; [http://files.rcsb.org/download/6es7_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34189 34189]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:6esp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ESP]]&lt;br /&gt;
|Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ESP 6ESP]&#039;&#039;&#039; [http://files.rcsb.org/download/6esp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34190 34190]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:6by4.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6BY4]]&lt;br /&gt;
|Nichols, P.J., Henen, M.A., Born, A., Strotz, D., Guntert, P., Vogeli, B. &amp;lt;br&amp;gt; High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints. [https://doi.org/10.1038/s42003-018-0067-x .] [Commun Biol 2018]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY4 6BY4]&#039;&#039;&#039; [http://files.rcsb.org/download/6by4_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY5 6BY5]&#039;&#039;&#039; [http://files.rcsb.org/download/6by5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:6fgn.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6FGN]]&lt;br /&gt;
|Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGN 6FGN]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgn_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34231 34231]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGS 6FGS]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34233 34233]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:6f3k.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F3K]]&lt;br /&gt;
|Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F3K 6F3K]&#039;&#039;&#039; [http://files.rcsb.org/download/6f3k_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6R8N 6R8N]&#039;&#039;&#039; [http://files.rcsb.org/download/6r8n_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure after Phenix refinement)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:5n2o.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N2O]]&lt;br /&gt;
|Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N2O 5N2O]&#039;&#039;&#039; [http://files.rcsb.org/download/5n2o_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34095 34095]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:5n6r.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N6R]]&lt;br /&gt;
|Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[http://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N6R 5N6R]&#039;&#039;&#039; [http://files.rcsb.org/download/5N6R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=34101 34101]&#039;&#039;&#039; (DH NMR structure)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N7E 5N7E]&#039;&#039;&#039; (DH/Mb(Bcr-DH_4))&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5OC7 5OC7]&#039;&#039;&#039; (PH/Mb(Bcr-PH_4))&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2N5E_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N5E]]&lt;br /&gt;
|Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[http://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://dx.doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N5E 2N5E]&#039;&#039;&#039; [http://files.rcsb.org/download/2N5E.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25710 25710]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:5gvq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5GVQ]]&lt;br /&gt;
|Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[http://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://dx.doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5GVQ 5GVQ]&#039;&#039;&#039; [http://files.rcsb.org/download/5GVQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=36018 36018]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2N9L_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N9L]]&lt;br /&gt;
|Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[http://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://dx.doi.org/10.1038/srep38312 Sci Rep. 6, 38312 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N9L 2N9L]&#039;&#039;&#039; [http://files.rcsb.org/download/2N9L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25910 25910]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2NB1_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NB1]]&lt;br /&gt;
|Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[http://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://dx.doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NB1 2NB1]&#039;&#039;&#039; [http://files.rcsb.org/download/2NB1.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25958 25958]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2NAO_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NAO]]&lt;br /&gt;
|Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. [http://dx.doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NAO 2NAO]&#039;&#039;&#039; [http://files.rcsb.org/download/2NAO.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=26692 26692]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MYX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MYX]]&lt;br /&gt;
|von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[http://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://dx.doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MYX 2MYX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MYX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25461 25461]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MWX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MWX]]&lt;br /&gt;
|Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[http://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://dx.doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173-180 (2015)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MWX 2MWX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MWX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25376 25376]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MVX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MVX]]&lt;br /&gt;
|Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., and Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[http://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://dx.doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MVX 2MVX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MVX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25289 25289]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2RUG_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RUG]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[http://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://dx.doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RUG 2RUG]&#039;&#039;&#039; [http://files.rcsb.org/download/2RUG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11563 11563]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2RU3_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[http://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://dx.doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU3 2RU3]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU3.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11517 11517]&#039;&#039;&#039; (SUP-12–RNA&amp;lt;sub&amp;gt;6&amp;lt;/sub&amp;gt; complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MGZ 2MGZ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MGZ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11518 11518]&#039;&#039;&#039; (ASD-1–SUP-12–RNA&amp;lt;sub&amp;gt;12&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2MMJ_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[http://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://dx.doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MMJ 2MMJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MMJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19856 19856]&#039;&#039;&#039; (M-Nleu11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN9 2MN9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19883 19883]&#039;&#039;&#039; (M-Nleu13 trans)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN8 2MN8]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19882 19882]&#039;&#039;&#039; (M-Nleu13 cis)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RU5_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU5]]&lt;br /&gt;
|Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[http://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://dx.doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU5 2RU5]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU5.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11548 11548]&#039;&#039;&#039; (uncomplexed MA)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU4 2RU4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11544 11544]&#039;&#039;&#039; (MA-YM&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MD9_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MD9]]&lt;br /&gt;
|Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[http://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://dx.doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MD9 2MD9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MD9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19479 19479]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RTX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RTX]]&lt;br /&gt;
|Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[http://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://dx.doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RTX 2RTX]&#039;&#039;&#039; [http://files.rcsb.org/download/2RTX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11534 11534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M8I_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M8I]]&lt;br /&gt;
|Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[http://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://dx.doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8I 2M8I]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8I.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19258 19258]&#039;&#039;&#039; (wildtype&lt;br /&gt;
WW domain)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8J 2M8J]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19259 19259]&#039;&#039;&#039; (WW(S16E) mutant)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUE_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUE]]&lt;br /&gt;
|Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://dx.doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LUE 2LUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2LUE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18518 18518]&#039;&#039;&#039; (NMR structure of LC3B OPTN-LIR Ptot complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTU]&#039;&#039;&#039; (crystal structure of human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTV]&#039;&#039;&#039; (crystal structure of Optineurin LIR-fused human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTW]&#039;&#039;&#039; (crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M99_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99]]&lt;br /&gt;
|Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[http://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://dx.doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99 2M99]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2M99.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19287 19287]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK6]]&lt;br /&gt;
|He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[http://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://dx.doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DK6 2DK6]&#039;&#039;&#039; [http://files.rcsb.org/download/2DK6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11500 11500]&#039;&#039;&#039; (WWE domain from PARP11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X4R 1X4R]&#039;&#039;&#039; [http://files.rcsb.org/download/1X4R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11501 11501]&#039;&#039;&#039; (WWE domain&lt;br /&gt;
from PARP14)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LVL_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL]]&lt;br /&gt;
|Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://dx.doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL 2LVL]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LVL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17534 17534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM]]&lt;br /&gt;
|Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[http://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://dx.doi.org/10.1038/nsmb.2355 Nature Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM 2LUM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LUM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18531 18531]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RSM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM]]&lt;br /&gt;
|Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[http://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM 2RSM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RSM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11491 11491]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RS6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RS6]]&lt;br /&gt;
|Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[http://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://dx.doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS6 2RS6]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11456 11456]&#039;&#039;&#039; (dsRBD1)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS7 2RS7]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS7.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11457 11457]&#039;&#039;&#039; (dsRBD2)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LIW_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LIW]]&lt;br /&gt;
|Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[http://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://dx.doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIU 2LIU]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17906 17906]&#039;&#039;&#039; (holo-ACPI)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIW 2LIW]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIW.mr NMR restraints] [http://www.rcsb.org/pdb/files/2LIW_cs.str.gz chemical shifts] (HMG-ACPI)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK4_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4]]&lt;br /&gt;
|He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[http://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://dx.doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4 2DK4]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2DK4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11355 11355]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L6X_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X]]&lt;br /&gt;
|Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[http://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://dx.doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X 2L6X]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L6X.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17327 17327]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L8J_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J]]&lt;br /&gt;
|Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[http://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J 2L8J]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17412 17412]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2KX7_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7]]&lt;br /&gt;
|Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[http://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://dx.doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7 2KX7]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KX7.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RRB_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB]]&lt;br /&gt;
|Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[http://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://dx.doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB 2RRB]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RRB.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:3llh_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH 3LLH]&#039;&#039;&#039;&lt;br /&gt;
[http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=STRUCTFACT&amp;amp;compression=NO&amp;amp;structureId=3LLH Structure factors]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2cpn_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN 2CPN]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2CPN.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1j26_asym_r_500_2.jpg|120px|link=http://www.pdb.org/pdb/explore/explore.do?structureId=1J26]]&lt;br /&gt;
|Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[http://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://dx.doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/images.do?structureId=1J26 1J26]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rqo_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO]]&lt;br /&gt;
|Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[http://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://dx.doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO 2RQO]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RQO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e61_bio_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2E61]]&lt;br /&gt;
|He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[http://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)] &lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2E61 2E61]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2E61.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kr6_asym_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2KR6]]&lt;br /&gt;
|Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[http://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://dx.doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2KR6 2KR6]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KR6.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kby_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KBY]]&lt;br /&gt;
|Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[http://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://dx.doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KBY 2KBY]&#039;&#039;&#039; [http://files.rcsb.org/download/2KBY.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2yue_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2YUE]]&lt;br /&gt;
|He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the Drosophila Neuralized E3 ligase in the Notch signaling pathway[http://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2YUE 2YUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2YUE.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E63 2E63]&#039;&#039;&#039; [http://files.rcsb.org/download/2E63.mr NMR restraints]&lt;br /&gt;
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|[[image:2klo_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KLO]]&lt;br /&gt;
|Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H., Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[http://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://dx.doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KLO 2KLO]&#039;&#039;&#039; [http://files.rcsb.org/download/2KLO.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3A4C 3A4C]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rqc_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RQC]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[http://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://dx.doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQC 2RQC]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQC.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQ4 2RQ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQ4.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rpj_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RPJ]]&lt;br /&gt;
|He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[http://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RPJ 2RPJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2RPJ.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2kak_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KAK]]&lt;br /&gt;
|Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[http://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KAK 2KAK]&#039;&#039;&#039; [http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=NMR&amp;amp;structureId=2KAK NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=16025 16025]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rog_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2ROG]]&lt;br /&gt;
|Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[http://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROG 2ROG]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11037 11037]&#039;&#039;&#039; (in-cell)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROE 2ROE]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11035 11035]&#039;&#039;&#039; (in solution)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e5s_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E5S]]&lt;br /&gt;
|He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[http://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E5S 2E5S]&#039;&#039;&#039;　[http://files.rcsb.org/download/2E5S.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2e29_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E29]]&lt;br /&gt;
|Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[http://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E29 2E29]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jz4_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JZ4]]&lt;br /&gt;
|Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JZ4 2JZ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2JZ4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15607 15607]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2ba3_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2BA3]]&lt;br /&gt;
|Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[http://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2BA3 2BA3]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15784 15784]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2jns_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JNS]]&lt;br /&gt;
|Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[http://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JNS 2JNS]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15125 15125]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2ron_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RON]]&lt;br /&gt;
|Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[http://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RON 2RON]&#039;&#039;&#039; [http://files.rcsb.org/download/2RON.mr NMR restraints] (SrfTEII)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2K2Q 2K2Q]&#039;&#039;&#039; [http://files.rcsb.org/download/2K2Q.mr NMR restraints] (complex of SrfTEII and H state TycC3–PCP)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1whv_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition[http://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WHV 1WHV]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROK 2ROK]&#039;&#039;&#039; (cap-bound form)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2jw8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JW8 2JW8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15511 15511]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2rne_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RNE 2RNE]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2fho asym r 250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2FHO]]&lt;br /&gt;
|Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2FHO 2FHO]&#039;&#039;&#039;  [http://files.rcsb.org/download/2FHO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2jo8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[http://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JO8 2JO8]&#039;&#039;&#039;  [http://files.rcsb.org/download/2JO8.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dwv asym r 250.jpg|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2DWV]]&lt;br /&gt;
|Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[http://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DWV 2DWV]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dt6 asym r 250.jpg|120px]]&lt;br /&gt;
|Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[http://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT6 2DT6]&#039;&#039;&#039; (SURP1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT7 2DT7]&#039;&#039;&#039; (SURP2-SF3a60)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcp asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270(9-135) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCP 2DCP]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCP.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with [[FLYA]]. Structure does not supersede the original deposition 1VDY.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcq asym r 250.jpg|120px]]&lt;br /&gt;
|Rhodanese homology domain At3g16270(175-295) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCQ 2DCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCQ.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1VEE.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcr asym r 250.jpg|120px]]&lt;br /&gt;
|Src homology domain 2 from the human feline sarcoma oncogene Fes.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCR 2DCR]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCR.mr NMR restraints]br&amp;gt;Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1WQU.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2h3s asym r 250.jpg|120px]]&lt;br /&gt;
|Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[http://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H4B 2H4B]&#039;&#039;&#039; [http://files.rcsb.org/download/2H4B.mr NMR restraints] (cis-1-PP)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3S 2H3S]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3S.mr NMR restraints] (cis-1-PP bound to DPC micelles)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3T 2H3T]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3T.mr NMR restraints] (trans-1-PP bound to DPC micelles)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wvo asym r 250.jpg|120px]]&lt;br /&gt;
|Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[http://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WVO 1WVO]&#039;&#039;&#039; [http://files.rcsb.org/download/1WVO.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2agm asym r 250.jpg|120px]]&lt;br /&gt;
|Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[http://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2AGM 2AGM]&#039;&#039;&#039; [http://files.rcsb.org/download/2AGM.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2d21 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) maltodextrin-binding protein MBP.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2D21 2D21]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6807 6807]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1x02 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) calmodulin.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X02 1X02]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6541 6541]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wwq asym r 250.jpg|120px]]&lt;br /&gt;
|Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WWQ 1WWQ]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wqu asym r 250.jpg|120px]]&lt;br /&gt;
|Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[http://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WQU 1WQU]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6331 6331]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1n27 asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[http://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://www3.interscience.wiley.com/journal/121602709/abstract Protein Sci. 14, 756–764 (2005)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1N27 1N27]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1u3m asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[http://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U3M 1U3M]&#039;&#039;&#039; [http://files.rcsb.org/download/1U3M.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6269 6269]&#039;&#039;&#039; (chicken PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U5L 1U5L]&#039;&#039;&#039; [http://files.rcsb.org/download/1U5L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6270 6270]&#039;&#039;&#039; (turtle PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XU0 1XU0]&#039;&#039;&#039; [http://files.rcsb.org/download/1XU0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6282 6282]&#039;&#039;&#039; (frog PrP(90-222))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1xyj asym r 250.jpg|120px]]&lt;br /&gt;
|Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[http://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYJ 1XYJ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6377 6377]&#039;&#039;&#039; (cat PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYK 1XYK]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYK.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6378 6378]&#039;&#039;&#039; (dog PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYQ 1XYQ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6380 6380]&#039;&#039;&#039; (pig PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYU 1XYU]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6381 6381]&#039;&#039;&#039; (sheep PrP[R168](121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Y2S 1Y2S]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6403 6403]&#039;&#039;&#039; (sheep PrP[H168](121-231))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vex asym r 250.jpg|120px]]&lt;br /&gt;
|Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[http://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SZL 1SZL]&#039;&#039;&#039;　[http://files.rcsb.org/download/1SZL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6175 6175]&#039;&#039;&#039; (TSR1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEX 1VEX]&#039;&#039;&#039; (TSR4)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vdy asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VDY 1VDY]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5928 5928]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vd0 asym r 250.jpg|120px]]&lt;br /&gt;
|Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[http://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VD0 1VD0]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vee asym r 250.jpg|120px]]&lt;br /&gt;
|Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[http://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://www3.interscience.wiley.com/journal/121602579/abstract Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEE 1VEE]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5929 5929]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ukx asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[http://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://dx.doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1UKX 1UKX]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6297 6297]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1q9g asym r 250.jpg|120px]]&lt;br /&gt;
|Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[http://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Q9G 1Q9G]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wln asym r 250.jpg|120px]]&lt;br /&gt;
|FHA domain of mouse afadin 6.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WLN 1WLN]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pbu asym r 250.jpg|120px]]&lt;br /&gt;
|Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[http://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PBU 1PBU]&#039;&#039;&#039; [http://files.rcsb.org/download/1PBU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5628 5628]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1mo8 asym r 250.jpg|120px]]&lt;br /&gt;
|Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[http://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://www.nature.com/nsmb/journal/v10/n6/abs/nsb924.html Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO7 1MO7]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5577 5577]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO8 1MO8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5576 5576]&#039;&#039;&#039; (ATP-bound form)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1lg4 asym r 250.jpg|120px]]&lt;br /&gt;
|Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[http://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LG4 1LG4]&#039;&#039;&#039; [http://files.rcsb.org/download/1LG4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5145 5145]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1h0l asym r 250.jpg|120px]]&lt;br /&gt;
|Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[http://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1H0L 1H0L]&#039;&#039;&#039; [http://files.rcsb.org/download/1H0L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5378 5378]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1sr3 asym r 250.jpg|120px]]&lt;br /&gt;
|Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[http://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://dx.doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SR3 1SR3]&#039;&#039;&#039; [http://files.rcsb.org/download/1SR3.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1ls8 asym r 250.jpg|120px]]&lt;br /&gt;
|Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[http://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://dx.doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LS8 1LS8]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1k9c asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K9C 1K9C]&#039;&#039;&#039; [http://files.rcsb.org/download/1K9C.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5204 5204]&#039;&#039;&#039; (residues 189-261)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K91 1K91]&#039;&#039;&#039; [http://files.rcsb.org/download/1K91.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5205 5205]&#039;&#039;&#039; (residues 221-256)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1jas asym r 250.jpg|120px]]&lt;br /&gt;
|Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[http://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1JAS 1JAS]&#039;&#039;&#039; [http://files.rcsb.org/download/1JAS.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5038 5038]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1gm0 asym r 250.jpg|120px]]&lt;br /&gt;
|Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[http://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1GM0 1GM0]&#039;&#039;&#039; [http://files.rcsb.org/download/1GM0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4849 4849]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hhn asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HHN 1HHN]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4878 4878]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1e1g asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[http://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1G 1E1G]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1G.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4736 4736]&#039;&#039;&#039; (variant M166V)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1P 1E1P]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1P.mr NMR restraints] (variant S170N)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1U 1E1U]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1U.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4620 4620]&#039;&#039;&#039; (variant R220K)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1qjk asym r 250.jpg|120px]]&lt;br /&gt;
|Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[http://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJK 1QJK]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJK.mr NMR restraints] (&amp;amp;alpha; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJL 1QJL]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJL.mr NMR restraints] (&amp;amp;beta; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4363 4363]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1bf8 asym r 250.jpg|120px]]&lt;br /&gt;
|Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[http://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://dx.doi.org/10.1038/2325 Nature Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1BF8 1BF8]&#039;&#039;&#039; [http://files.rcsb.org/download/1BF8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4070 4070]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1oca asym r 250.jpg|120px]]&lt;br /&gt;
|Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[http://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1OCA 1OCA]&#039;&#039;&#039; [http://files.rcsb.org/download/1OCA.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wkt asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[http://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://dx.doi.org/10.1038/nsb0896-662 Nature Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WKT 1WKT]&#039;&#039;&#039; [http://files.rcsb.org/download/1WKT.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5255 5255]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1tap asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://dx.doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1TAP 1TAP]&#039;&#039;&#039; [http://files.rcsb.org/download/1TAP.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1dtk asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1DTK 1DTK]&#039;&#039;&#039; [http://files.rcsb.org/download/1DTK.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hic asym r 250.jpg|120px]]&lt;br /&gt;
|Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[http://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HIC 1HIC]&#039;&#039;&#039; [http://files.rcsb.org/download/1HIC.mr NMR restraints]&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=1128 1128]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pit asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[http://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PIT 1PIT]&#039;&#039;&#039; [http://files.rcsb.org/download/1PIT.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2hoa asym r 250.jpg|120px]]&lt;br /&gt;
|Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[http://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2HOA 2HOA]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
|}&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59285</id>
		<title>Protein structures</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59285"/>
		<updated>2026-01-13T21:58:14Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;NMR protein structures co-authored by P. Güntert.&lt;br /&gt;
&lt;br /&gt;
{|&lt;br /&gt;
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|[[image:8ox2.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8OX2]]&lt;br /&gt;
|Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OVI 8OVI]&#039;&#039;&#039; [http://files.rcsb.org/download/8ovi_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34811 34811]&#039;&#039;&#039; (monomer)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OX2 8OX2]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34813 34813]&#039;&#039;&#039; (trimer)&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8kcq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8KCQ]]&lt;br /&gt;
|Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8KCQ 8KCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=36589 36589]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8qbp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8QBP]]&lt;br /&gt;
|Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QBP 8QBP]&#039;&#039;&#039; [http://files.rcsb.org/download/8qbp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34850 34850]&#039;&#039;&#039; (OmphA “indole-In)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8Q7J 8Q7J]&#039;&#039;&#039; [http://files.rcsb.org/download/8q7j_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34846 34846]&#039;&#039;&#039; (CsA)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAQ 8QAQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8qaq_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34848 34848]&#039;&#039;&#039; (OmphA&lt;br /&gt;
conformation 1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAS 8QAS]&#039;&#039;&#039; [http://files.rcsb.org/download/8qas_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34849 34849]&#039;&#039;&#039; (OmphA “indole-Out”)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:8pxs.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8PXS]]&lt;br /&gt;
|Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8PXS 8PXS]&#039;&#039;&#039; [http://files.rcsb.org/download/8pxs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34838 34838]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7x9u.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7X9U]]&lt;br /&gt;
|Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7X9U 7X9U]&#039;&#039;&#039; [http://files.rcsb.org/download/7x9u_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36478 36478]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qtr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QTR]]&lt;br /&gt;
|Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTR 7QTR]&#039;&#039;&#039; [http://files.rcsb.org/download/7qtr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34700 34700]&#039;&#039;&#039; (GB1 in cells at a protein concentration of 50 μM)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTS 7QTS]&#039;&#039;&#039; [http://files.rcsb.org/download/7qts_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34701 34701]&#039;&#039;&#039;  (GB1 in cells at a protein concentration of 10 μM)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qcx.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QCX]]&lt;br /&gt;
|Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCX 7QCX]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcx_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34688 34688]&#039;&#039;&#039; (two-state structure of apo PDZ2)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCY 7QCY]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcy_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34689 34689]&#039;&#039;&#039; (two-state structure of PDZ2 complexed with RA-GEF2 peptide)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7fbr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7FBR]]&lt;br /&gt;
|He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBR 7FBR]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36430 36430]&#039;&#039;&#039; (first RRM domain of Matrin-3)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBV 7FBV]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbv_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36431 36431]&#039;&#039;&#039; (second RRM domain of Matrin-3)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6tub.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6TUB]]&lt;br /&gt;
|Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6TUB 6TUB]&#039;&#039;&#039; [http://files.rcsb.org/download/6tub_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=26715 26715]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6svc.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6SVE]]&lt;br /&gt;
| Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVC 6SVC]&#039;&#039;&#039; [http://files.rcsb.org/download/6svc_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34432 34432]&#039;&#039;&#039;&lt;br /&gt;
(WW domain apo structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVE 6SVE]&#039;&#039;&#039; [http://files.rcsb.org/download/6sve_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34433 34433]&#039;&#039;&#039; (WW domain with pCdc25C bound)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVH 6SVH]&#039;&#039;&#039; [http://files.rcsb.org/download/6svh_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34434 34434]&#039;&#039;&#039; (WW domain with FFpSPR bound)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6qk6.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6QK6]]&lt;br /&gt;
|Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK5 6QK5]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34355 34355]&#039;&#039;&#039; (Zn-loaded form)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK6 6QK6]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34356 34356]&#039;&#039;&#039; (Cd-loaded form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5zcz.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5ZCZ]]&lt;br /&gt;
|Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZCZ 5ZCZ]&#039;&#039;&#039; [http://files.rcsb.org/download/5zcz_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27354 27354]&#039;&#039;&#039; (T. Thermophilus HB8 TTHA1718 protein in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZD0 5ZD0]&#039;&#039;&#039; [http://files.rcsb.org/download/5zd0_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27356 27356]&#039;&#039;&#039; (ubiquitin with three alanine mutations in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5Z4B 5Z4B]&#039;&#039;&#039; [http://files.rcsb.org/download/5z4b_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36153 36153]&#039;&#039;&#039; (GB1 in living eukaryotic cells)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6h8c.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6H8C]]&lt;br /&gt;
|Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6H8C 6H8C]&#039;&#039;&#039; [http://files.rcsb.org/download/6h8c_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34307 34307]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6HB9 6HB9]&#039;&#039;&#039; [http://files.rcsb.org/download/6hb9_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB N/A&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f98.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F98]]&lt;br /&gt;
|Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F98 6F98]&#039;&#039;&#039; [http://files.rcsb.org/download/6f98_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34217 34217]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F99 6F99]&#039;&#039;&#039; [http://files.rcsb.org/download/6f99_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34218 34218]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F9A 6F9A]&#039;&#039;&#039; [http://files.rcsb.org/download/6f9a_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34219 34219]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6es5.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ES5]]&lt;br /&gt;
|Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES5 6ES5]&#039;&#039;&#039; [http://files.rcsb.org/download/6es5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34187 34187]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES6 6ES6]&#039;&#039;&#039; [http://files.rcsb.org/download/6es6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34188 34188]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES7 6ES7]&#039;&#039;&#039; [http://files.rcsb.org/download/6es7_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34189 34189]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6esp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ESP]]&lt;br /&gt;
|Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ESP 6ESP]&#039;&#039;&#039; [http://files.rcsb.org/download/6esp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34190 34190]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6by4.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6BY4]]&lt;br /&gt;
|Nichols, P.J., Henen, M.A., Born, A., Strotz, D., Guntert, P., Vogeli, B. &amp;lt;br&amp;gt; High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints. [https://doi.org/10.1038/s42003-018-0067-x .] [Commun Biol 2018]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY4 6BY4]&#039;&#039;&#039; [http://files.rcsb.org/download/6by4_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY5 6BY5]&#039;&#039;&#039; [http://files.rcsb.org/download/6by5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6fgn.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6FGN]]&lt;br /&gt;
|Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGN 6FGN]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgn_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34231 34231]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGS 6FGS]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34233 34233]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:6f3k.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F3K]]&lt;br /&gt;
|Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F3K 6F3K]&#039;&#039;&#039; [http://files.rcsb.org/download/6f3k_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6R8N 6R8N]&#039;&#039;&#039; [http://files.rcsb.org/download/6r8n_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (NMR + EM structure after Phenix refinement)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:5n2o.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N2O]]&lt;br /&gt;
|Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N2O 5N2O]&#039;&#039;&#039; [http://files.rcsb.org/download/5n2o_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34095 34095]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:5n6r.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N6R]]&lt;br /&gt;
|Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[http://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N6R 5N6R]&#039;&#039;&#039; [http://files.rcsb.org/download/5N6R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=34101 34101]&#039;&#039;&#039; (DH NMR structure)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N7E 5N7E]&#039;&#039;&#039; (DH/Mb(Bcr-DH_4))&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5OC7 5OC7]&#039;&#039;&#039; (PH/Mb(Bcr-PH_4))&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2N5E_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N5E]]&lt;br /&gt;
|Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[http://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://dx.doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N5E 2N5E]&#039;&#039;&#039; [http://files.rcsb.org/download/2N5E.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25710 25710]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:5gvq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5GVQ]]&lt;br /&gt;
|Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[http://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://dx.doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5GVQ 5GVQ]&#039;&#039;&#039; [http://files.rcsb.org/download/5GVQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=36018 36018]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2N9L_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N9L]]&lt;br /&gt;
|Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[http://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://dx.doi.org/10.1038/srep38312 Sci Rep. 6, 38312 (2016)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N9L 2N9L]&#039;&#039;&#039; [http://files.rcsb.org/download/2N9L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25910 25910]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2NB1_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NB1]]&lt;br /&gt;
|Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[http://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://dx.doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NB1 2NB1]&#039;&#039;&#039; [http://files.rcsb.org/download/2NB1.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25958 25958]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2NAO_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NAO]]&lt;br /&gt;
|Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. [http://dx.doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NAO 2NAO]&#039;&#039;&#039; [http://files.rcsb.org/download/2NAO.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=26692 26692]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MYX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MYX]]&lt;br /&gt;
|von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[http://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://dx.doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MYX 2MYX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MYX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25461 25461]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MWX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MWX]]&lt;br /&gt;
|Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[http://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://dx.doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173-180 (2015)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MWX 2MWX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MWX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25376 25376]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2MVX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MVX]]&lt;br /&gt;
|Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., and Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[http://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://dx.doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MVX 2MVX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MVX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25289 25289]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2RUG_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RUG]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[http://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://dx.doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RUG 2RUG]&#039;&#039;&#039; [http://files.rcsb.org/download/2RUG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11563 11563]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
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|[[image:2RU3_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[http://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://dx.doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU3 2RU3]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU3.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11517 11517]&#039;&#039;&#039; (SUP-12–RNA&amp;lt;sub&amp;gt;6&amp;lt;/sub&amp;gt; complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MGZ 2MGZ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MGZ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11518 11518]&#039;&#039;&#039; (ASD-1–SUP-12–RNA&amp;lt;sub&amp;gt;12&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2MMJ_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[http://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://dx.doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MMJ 2MMJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MMJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19856 19856]&#039;&#039;&#039; (M-Nleu11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN9 2MN9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19883 19883]&#039;&#039;&#039; (M-Nleu13 trans)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN8 2MN8]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19882 19882]&#039;&#039;&#039; (M-Nleu13 cis)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2RU5_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU5]]&lt;br /&gt;
|Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[http://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://dx.doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU5 2RU5]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU5.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11548 11548]&#039;&#039;&#039; (uncomplexed MA)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU4 2RU4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11544 11544]&#039;&#039;&#039; (MA-YM&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2MD9_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MD9]]&lt;br /&gt;
|Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[http://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://dx.doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MD9 2MD9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MD9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19479 19479]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:2RTX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RTX]]&lt;br /&gt;
|Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[http://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://dx.doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RTX 2RTX]&#039;&#039;&#039; [http://files.rcsb.org/download/2RTX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11534 11534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M8I_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M8I]]&lt;br /&gt;
|Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[http://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://dx.doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8I 2M8I]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8I.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19258 19258]&#039;&#039;&#039; (wildtype&lt;br /&gt;
WW domain)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8J 2M8J]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19259 19259]&#039;&#039;&#039; (WW(S16E) mutant)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUE_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUE]]&lt;br /&gt;
|Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://dx.doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LUE 2LUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2LUE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18518 18518]&#039;&#039;&#039; (NMR structure of LC3B OPTN-LIR Ptot complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTU]&#039;&#039;&#039; (crystal structure of human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTV]&#039;&#039;&#039; (crystal structure of Optineurin LIR-fused human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTW]&#039;&#039;&#039; (crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M99_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99]]&lt;br /&gt;
|Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[http://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://dx.doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99 2M99]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2M99.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19287 19287]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK6]]&lt;br /&gt;
|He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[http://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://dx.doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DK6 2DK6]&#039;&#039;&#039; [http://files.rcsb.org/download/2DK6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11500 11500]&#039;&#039;&#039; (WWE domain from PARP11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X4R 1X4R]&#039;&#039;&#039; [http://files.rcsb.org/download/1X4R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11501 11501]&#039;&#039;&#039; (WWE domain&lt;br /&gt;
from PARP14)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LVL_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL]]&lt;br /&gt;
|Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://dx.doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL 2LVL]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LVL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17534 17534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM]]&lt;br /&gt;
|Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[http://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://dx.doi.org/10.1038/nsmb.2355 Nature Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM 2LUM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LUM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18531 18531]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RSM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM]]&lt;br /&gt;
|Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[http://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM 2RSM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RSM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11491 11491]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RS6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RS6]]&lt;br /&gt;
|Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[http://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://dx.doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS6 2RS6]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11456 11456]&#039;&#039;&#039; (dsRBD1)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS7 2RS7]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS7.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11457 11457]&#039;&#039;&#039; (dsRBD2)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LIW_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LIW]]&lt;br /&gt;
|Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[http://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://dx.doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIU 2LIU]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17906 17906]&#039;&#039;&#039; (holo-ACPI)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIW 2LIW]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIW.mr NMR restraints] [http://www.rcsb.org/pdb/files/2LIW_cs.str.gz chemical shifts] (HMG-ACPI)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK4_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4]]&lt;br /&gt;
|He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[http://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://dx.doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4 2DK4]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2DK4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11355 11355]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L6X_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X]]&lt;br /&gt;
|Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[http://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://dx.doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X 2L6X]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L6X.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17327 17327]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L8J_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J]]&lt;br /&gt;
|Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[http://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J 2L8J]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17412 17412]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2KX7_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7]]&lt;br /&gt;
|Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[http://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://dx.doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7 2KX7]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KX7.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RRB_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB]]&lt;br /&gt;
|Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[http://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://dx.doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB 2RRB]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RRB.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:3llh_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH 3LLH]&#039;&#039;&#039;&lt;br /&gt;
[http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=STRUCTFACT&amp;amp;compression=NO&amp;amp;structureId=3LLH Structure factors]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2cpn_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN 2CPN]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2CPN.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1j26_asym_r_500_2.jpg|120px|link=http://www.pdb.org/pdb/explore/explore.do?structureId=1J26]]&lt;br /&gt;
|Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[http://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://dx.doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/images.do?structureId=1J26 1J26]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rqo_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO]]&lt;br /&gt;
|Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[http://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://dx.doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO 2RQO]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RQO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e61_bio_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2E61]]&lt;br /&gt;
|He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[http://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2E61 2E61]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2E61.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kr6_asym_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2KR6]]&lt;br /&gt;
|Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[http://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://dx.doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2KR6 2KR6]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KR6.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kby_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KBY]]&lt;br /&gt;
|Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[http://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://dx.doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KBY 2KBY]&#039;&#039;&#039; [http://files.rcsb.org/download/2KBY.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2yue_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2YUE]]&lt;br /&gt;
|He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the Drosophila Neuralized E3 ligase in the Notch signaling pathway[http://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2YUE 2YUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2YUE.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E63 2E63]&#039;&#039;&#039; [http://files.rcsb.org/download/2E63.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2klo_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KLO]]&lt;br /&gt;
|Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H., Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[http://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://dx.doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KLO 2KLO]&#039;&#039;&#039; [http://files.rcsb.org/download/2KLO.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3A4C 3A4C]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rqc_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RQC]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[http://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://dx.doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQC 2RQC]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQC.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQ4 2RQ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQ4.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rpj_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RPJ]]&lt;br /&gt;
|He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[http://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RPJ 2RPJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2RPJ.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kak_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KAK]]&lt;br /&gt;
|Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[http://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KAK 2KAK]&#039;&#039;&#039; [http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=NMR&amp;amp;structureId=2KAK NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=16025 16025]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rog_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2ROG]]&lt;br /&gt;
|Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[http://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROG 2ROG]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11037 11037]&#039;&#039;&#039; (in-cell)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROE 2ROE]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11035 11035]&#039;&#039;&#039; (in solution)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e5s_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E5S]]&lt;br /&gt;
|He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[http://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E5S 2E5S]&#039;&#039;&#039;　[http://files.rcsb.org/download/2E5S.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e29_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E29]]&lt;br /&gt;
|Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[http://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E29 2E29]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jz4_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JZ4]]&lt;br /&gt;
|Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JZ4 2JZ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2JZ4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15607 15607]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2ba3_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2BA3]]&lt;br /&gt;
|Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[http://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2BA3 2BA3]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15784 15784]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jns_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JNS]]&lt;br /&gt;
|Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[http://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JNS 2JNS]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15125 15125]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2ron_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RON]]&lt;br /&gt;
|Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[http://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RON 2RON]&#039;&#039;&#039; [http://files.rcsb.org/download/2RON.mr NMR restraints] (SrfTEII)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2K2Q 2K2Q]&#039;&#039;&#039; [http://files.rcsb.org/download/2K2Q.mr NMR restraints] (complex of SrfTEII and H state TycC3–PCP)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1whv_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition[http://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WHV 1WHV]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROK 2ROK]&#039;&#039;&#039; (cap-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jw8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JW8 2JW8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15511 15511]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rne_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RNE 2RNE]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2fho asym r 250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2FHO]]&lt;br /&gt;
|Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2FHO 2FHO]&#039;&#039;&#039;  [http://files.rcsb.org/download/2FHO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jo8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[http://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JO8 2JO8]&#039;&#039;&#039;  [http://files.rcsb.org/download/2JO8.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dwv asym r 250.jpg|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2DWV]]&lt;br /&gt;
|Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[http://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DWV 2DWV]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dt6 asym r 250.jpg|120px]]&lt;br /&gt;
|Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[http://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT6 2DT6]&#039;&#039;&#039; (SURP1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT7 2DT7]&#039;&#039;&#039; (SURP2-SF3a60)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcp asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270(9-135) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCP 2DCP]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCP.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with [[FLYA]]. Structure does not supersede the original deposition 1VDY.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcq asym r 250.jpg|120px]]&lt;br /&gt;
|Rhodanese homology domain At3g16270(175-295) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCQ 2DCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCQ.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1VEE.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcr asym r 250.jpg|120px]]&lt;br /&gt;
|Src homology domain 2 from the human feline sarcoma oncogene Fes.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCR 2DCR]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCR.mr NMR restraints]br&amp;gt;Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1WQU.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2h3s asym r 250.jpg|120px]]&lt;br /&gt;
|Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[http://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H4B 2H4B]&#039;&#039;&#039; [http://files.rcsb.org/download/2H4B.mr NMR restraints] (cis-1-PP)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3S 2H3S]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3S.mr NMR restraints] (cis-1-PP bound to DPC micelles)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3T 2H3T]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3T.mr NMR restraints] (trans-1-PP bound to DPC micelles)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wvo asym r 250.jpg|120px]]&lt;br /&gt;
|Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[http://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WVO 1WVO]&#039;&#039;&#039; [http://files.rcsb.org/download/1WVO.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2agm asym r 250.jpg|120px]]&lt;br /&gt;
|Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[http://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2AGM 2AGM]&#039;&#039;&#039; [http://files.rcsb.org/download/2AGM.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2d21 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) maltodextrin-binding protein MBP.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2D21 2D21]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6807 6807]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1x02 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) calmodulin.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X02 1X02]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6541 6541]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wwq asym r 250.jpg|120px]]&lt;br /&gt;
|Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WWQ 1WWQ]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wqu asym r 250.jpg|120px]]&lt;br /&gt;
|Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[http://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WQU 1WQU]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6331 6331]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1n27 asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[http://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://www3.interscience.wiley.com/journal/121602709/abstract Protein Sci. 14, 756–764 (2005)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1N27 1N27]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1u3m asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[http://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U3M 1U3M]&#039;&#039;&#039; [http://files.rcsb.org/download/1U3M.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6269 6269]&#039;&#039;&#039; (chicken PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U5L 1U5L]&#039;&#039;&#039; [http://files.rcsb.org/download/1U5L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6270 6270]&#039;&#039;&#039; (turtle PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XU0 1XU0]&#039;&#039;&#039; [http://files.rcsb.org/download/1XU0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6282 6282]&#039;&#039;&#039; (frog PrP(90-222))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1xyj asym r 250.jpg|120px]]&lt;br /&gt;
|Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[http://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYJ 1XYJ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6377 6377]&#039;&#039;&#039; (cat PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYK 1XYK]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYK.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6378 6378]&#039;&#039;&#039; (dog PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYQ 1XYQ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6380 6380]&#039;&#039;&#039; (pig PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYU 1XYU]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6381 6381]&#039;&#039;&#039; (sheep PrP[R168](121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Y2S 1Y2S]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6403 6403]&#039;&#039;&#039; (sheep PrP[H168](121-231))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vex asym r 250.jpg|120px]]&lt;br /&gt;
|Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[http://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SZL 1SZL]&#039;&#039;&#039;　[http://files.rcsb.org/download/1SZL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6175 6175]&#039;&#039;&#039; (TSR1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEX 1VEX]&#039;&#039;&#039; (TSR4)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vdy asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VDY 1VDY]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5928 5928]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vd0 asym r 250.jpg|120px]]&lt;br /&gt;
|Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[http://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VD0 1VD0]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vee asym r 250.jpg|120px]]&lt;br /&gt;
|Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[http://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://www3.interscience.wiley.com/journal/121602579/abstract Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEE 1VEE]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5929 5929]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ukx asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[http://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://dx.doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1UKX 1UKX]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6297 6297]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1q9g asym r 250.jpg|120px]]&lt;br /&gt;
|Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[http://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Q9G 1Q9G]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wln asym r 250.jpg|120px]]&lt;br /&gt;
|FHA domain of mouse afadin 6.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WLN 1WLN]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pbu asym r 250.jpg|120px]]&lt;br /&gt;
|Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[http://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PBU 1PBU]&#039;&#039;&#039; [http://files.rcsb.org/download/1PBU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5628 5628]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1mo8 asym r 250.jpg|120px]]&lt;br /&gt;
|Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[http://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://www.nature.com/nsmb/journal/v10/n6/abs/nsb924.html Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO7 1MO7]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5577 5577]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO8 1MO8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5576 5576]&#039;&#039;&#039; (ATP-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1lg4 asym r 250.jpg|120px]]&lt;br /&gt;
|Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[http://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LG4 1LG4]&#039;&#039;&#039; [http://files.rcsb.org/download/1LG4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5145 5145]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1h0l asym r 250.jpg|120px]]&lt;br /&gt;
|Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[http://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1H0L 1H0L]&#039;&#039;&#039; [http://files.rcsb.org/download/1H0L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5378 5378]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1sr3 asym r 250.jpg|120px]]&lt;br /&gt;
|Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[http://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://dx.doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SR3 1SR3]&#039;&#039;&#039; [http://files.rcsb.org/download/1SR3.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ls8 asym r 250.jpg|120px]]&lt;br /&gt;
|Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[http://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://dx.doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LS8 1LS8]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1k9c asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K9C 1K9C]&#039;&#039;&#039; [http://files.rcsb.org/download/1K9C.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5204 5204]&#039;&#039;&#039; (residues 189-261)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K91 1K91]&#039;&#039;&#039; [http://files.rcsb.org/download/1K91.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5205 5205]&#039;&#039;&#039; (residues 221-256)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1jas asym r 250.jpg|120px]]&lt;br /&gt;
|Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[http://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1JAS 1JAS]&#039;&#039;&#039; [http://files.rcsb.org/download/1JAS.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5038 5038]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1gm0 asym r 250.jpg|120px]]&lt;br /&gt;
|Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[http://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1GM0 1GM0]&#039;&#039;&#039; [http://files.rcsb.org/download/1GM0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4849 4849]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hhn asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HHN 1HHN]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4878 4878]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1e1g asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[http://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1G 1E1G]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1G.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4736 4736]&#039;&#039;&#039; (variant M166V)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1P 1E1P]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1P.mr NMR restraints] (variant S170N)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1U 1E1U]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1U.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4620 4620]&#039;&#039;&#039; (variant R220K)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1qjk asym r 250.jpg|120px]]&lt;br /&gt;
|Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[http://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJK 1QJK]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJK.mr NMR restraints] (&amp;amp;alpha; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJL 1QJL]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJL.mr NMR restraints] (&amp;amp;beta; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4363 4363]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1bf8 asym r 250.jpg|120px]]&lt;br /&gt;
|Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[http://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://dx.doi.org/10.1038/2325 Nature Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1BF8 1BF8]&#039;&#039;&#039; [http://files.rcsb.org/download/1BF8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4070 4070]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1oca asym r 250.jpg|120px]]&lt;br /&gt;
|Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[http://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1OCA 1OCA]&#039;&#039;&#039; [http://files.rcsb.org/download/1OCA.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wkt asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[http://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://dx.doi.org/10.1038/nsb0896-662 Nature Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WKT 1WKT]&#039;&#039;&#039; [http://files.rcsb.org/download/1WKT.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5255 5255]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1tap asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://dx.doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1TAP 1TAP]&#039;&#039;&#039; [http://files.rcsb.org/download/1TAP.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1dtk asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1DTK 1DTK]&#039;&#039;&#039; [http://files.rcsb.org/download/1DTK.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hic asym r 250.jpg|120px]]&lt;br /&gt;
|Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[http://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HIC 1HIC]&#039;&#039;&#039; [http://files.rcsb.org/download/1HIC.mr NMR restraints]&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=1128 1128]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pit asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[http://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PIT 1PIT]&#039;&#039;&#039; [http://files.rcsb.org/download/1PIT.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2hoa asym r 250.jpg|120px]]&lt;br /&gt;
|Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[http://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2HOA 2HOA]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
|}&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
	<entry>
		<id>https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59284</id>
		<title>Protein structures</title>
		<link rel="alternate" type="text/html" href="https://uni-frankfurt.guentert.science/wiki/index.php?title=Protein_structures&amp;diff=59284"/>
		<updated>2026-01-13T21:54:46Z</updated>

		<summary type="html">&lt;p&gt;GuentertWiki: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;NMR protein structures co-authored by P. Güntert.&lt;br /&gt;
&lt;br /&gt;
{|&lt;br /&gt;
&lt;br /&gt;
|[[image:8ox2.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8OX2]]&lt;br /&gt;
|Ghosh, D., Torres, F., Schneider, M. M., Ashkinadze, D., Kadavath, H., Fleischmann, Y., Mergenthal, S., Güntert, P. , Krainer, G., Andrzejewska, E. A., Lin, L., Wei, J., Klotzsch, E., Knowles, T. &amp;amp; Riek, R. The inhibitory action of the chaperone BRICHOS against α-Synuclein secondary nucleation pathway at near-atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Ghosh24-BRICHOS.pdf .] [https://doi.org/10.1038/s41467-024-54212-2 Nat. Commun. 15, 10038 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OVI 8OVI]&#039;&#039;&#039; [http://files.rcsb.org/download/8ovi_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34811 34811]&#039;&#039;&#039; (monomer)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8OX2 8OX2]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=34813 34813]&#039;&#039;&#039; (trimer)&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8kcq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8KCQ]]&lt;br /&gt;
|Kuwasako, K., Dang, W., Fahu, H., Takahashi, M., Tsuda, K., Nagata, T., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structure of the N-terminal divergent caplonin homology (NN-CH) domain of human intraflagellar transport protein 54[https://uni-frankfurt.guentert.science/Reprints/Kuwasako24-Protein54Assignment.pdf .] [http://doi.org/10.1007/s12104-024-10170-w Biomol. NMR Assignments 18, 71–78 (2024)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8KCQ 8KCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8ox2_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [http://bmrb.io/data_library/generate_summary.php?bmrbId=36589 36589]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:8qbp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8QBP]]&lt;br /&gt;
|Rüdisser, S. H., Matabaro, E., Sonderegger, L., Güntert, P., Künzler, M., Gossert, A. D. Conformations of macrocyclic peptides sampled by exact NOEs: Models for cell-permeability[https://uni-frankfurt.guentert.science/Reprints/Ruedisser23-eNOEPeptides.pdf .] [http://doi.org/10.1021/jacs.3c09367 J. Am. Chem. Soc. 145, 27601–27615 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QBP 8QBP]&#039;&#039;&#039; [http://files.rcsb.org/download/8qbp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34850 34850]&#039;&#039;&#039; (OmphA “indole-In)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8Q7J 8Q7J]&#039;&#039;&#039; [http://files.rcsb.org/download/8q7j_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34846 34846]&#039;&#039;&#039; (CsA)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAQ 8QAQ]&#039;&#039;&#039; [http://files.rcsb.org/download/8qaq_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34848 34848]&#039;&#039;&#039; (OmphA&lt;br /&gt;
conformation 1)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8QAS 8QAS]&#039;&#039;&#039; [http://files.rcsb.org/download/8qas_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34849 34849]&#039;&#039;&#039; (OmphA “indole-Out”)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:8pxs.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=8PXS]]&lt;br /&gt;
|Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P. , Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J. &amp;amp; Riek, R. An analysis of nucleotide-amyloid interactions reveals selective binding to codon-sized RNA[https://uni-frankfurt.guentert.science/Reprints/Rout23-RNAmyloid.pdf .] [https://doi.org/10.1021/jacs.3c06287 J. Am. Chem. Soc. 145, 21915−21924 (2023)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=8PXS 8PXS]&#039;&#039;&#039; [http://files.rcsb.org/download/8pxs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34838 34838]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7x9u.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7X9U]]&lt;br /&gt;
|Kuwasako, K., Suzuki, S., Nameki, N., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the KH domain of ribosome binding factor A, mtRbfA, from humans, that is involved in mitochondrial ribosome biogenesis[https://uni-frankfurt.guentert.science/Reprints/Kuwasako22-mtRbfA.pdf .] [http://doi.org/10.1007/s12104-022-10094-3 Biomol. NMR Assignments 16, 297–303 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7X9U 7X9U]&#039;&#039;&#039; [http://files.rcsb.org/download/7x9u_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36478 36478]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qtr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QTR]]&lt;br /&gt;
|Gerez, J. A., Prymaczok, N. C., Kadavath, H., Ghosh, D., Bütikofer, M., Güntert, P. &amp;amp; Riek, R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression[https://uni-frankfurt.guentert.science/Reprints/Gerez22-HumanInCellNMR.pdf .] [http://doi.org/10.1038/s42003-022-04251-6 Comm. Biol. 5, 1322 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTR 7QTR]&#039;&#039;&#039; [http://files.rcsb.org/download/7qtr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34700 34700]&#039;&#039;&#039; (GB1 in cells at a protein concentration of 50 μM)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QTS 7QTS]&#039;&#039;&#039; [http://files.rcsb.org/download/7qts_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34701 34701]&#039;&#039;&#039;  (GB1 in cells at a protein concentration of 10 μM)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7qcx.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7QCX]]&lt;br /&gt;
|Ashkinadze, D., Kadavath, H., Chi, C., Friedmann, M., Strotz, D., Kumari, P., Minges, M., Cadalbert, C., Königl, S., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Atomic resolution protein allostery from the multi-state structure of a PDZ Domain[https://uni-frankfurt.guentert.science/Reprints/Ashkinadze22-PDZ.pdf .] [http://doi.org/10.1038/s41467-022-33687-x Nat. Commun. 13, 6232 (2022)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCX 7QCX]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcx_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34688 34688]&#039;&#039;&#039; (two-state structure of apo PDZ2)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7QCY 7QCY]&#039;&#039;&#039; [http://files.rcsb.org/download/7qcy_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34689 34689]&#039;&#039;&#039; (two-state structure of PDZ2 complexed with RA-GEF2 peptide)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:7fbr.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=7FBR]]&lt;br /&gt;
|He., F., Kuwasako, K., Takizawa, M., Takahashi, M., Tsuda, K., Nagata, T., Watanabe, S., Tanaka, A., Kobayashi, N., Kigawa, T., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. &amp;lt;sup&amp;gt;1&amp;lt;/sup&amp;gt;H, &amp;lt;sup&amp;gt;13&amp;lt;/sup&amp;gt;C and &amp;lt;sup&amp;gt;15&amp;lt;/sup&amp;gt;N resonance assignments and solution structures of the two RRM domains of Matrin-3[https://uni-frankfurt.guentert.science/Reprints/He22-Matrin3.pdf .] [http://doi.org/10.1007/s12104-021-10057-0 Biomol. NMR Assignments 16, 41–49 (2022)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBR 7FBR]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbr_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36430 36430]&#039;&#039;&#039; (first RRM domain of Matrin-3)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=7FBV 7FBV]&#039;&#039;&#039; [http://files.rcsb.org/download/7fbv_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36431 36431]&#039;&#039;&#039; (second RRM domain of Matrin-3)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6tub.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6TUB]]&lt;br /&gt;
|Seuring, C., Verasdonck, J., Gath, J., Ghosh, D., Nespovitaya, N., Wälti, M. A., Maji, S., Cadalbert, R., Güntert, P., Meier, B. H. &amp;amp; Riek, R. The three-dimensional structure of human β-endorphin amyloid fibrils[https://uni-frankfurt.guentert.science/Reprints/Seuring20-Endorphin.pdf .] [http://doi.org/10.1038/s41594-020-00515-z Nat. Struct. Mol. Biol. 27, 1178–1184 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6TUB 6TUB]&#039;&#039;&#039; [http://files.rcsb.org/download/6tub_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=26715 26715]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6svc.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6SVE]]&lt;br /&gt;
| Strotz, D., Orts, J., Kadavath, H., Friedmann, M., Ghosh, D., Olsson, S., Chi, C. N., Pokharna, A., Güntert, P., Vögeli, B. &amp;amp; Riek, R. Protein allostery at atomic resolution[https://uni-frankfurt.guentert.science/Reprints/Strotz20-WWAllostery.pdf .] [http://doi.org/10.1002/anie.202008734 Angew. Chem. Int. Ed. 59, 22132-22139 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVC 6SVC]&#039;&#039;&#039; [http://files.rcsb.org/download/6svc_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34432 34432]&#039;&#039;&#039;&lt;br /&gt;
(WW domain apo structure)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVE 6SVE]&#039;&#039;&#039; [http://files.rcsb.org/download/6sve_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34433 34433]&#039;&#039;&#039; (WW domain with pCdc25C bound)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6SVH 6SVH]&#039;&#039;&#039; [http://files.rcsb.org/download/6svh_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34434 34434]&#039;&#039;&#039; (WW domain with FFpSPR bound)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6qk6.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6QK6]]&lt;br /&gt;
|Beil, A., Jurt, S., Walser, R., Schäfer, T., Güntert, P., Capdeville, M., Atrian, S., Dallinger, R. &amp;amp; Zerbe, O. The solution structure and dynamics of Cd-metallothionein from &#039;&#039;Helix pomatia&#039;&#039; reveal optimization for binding Cd over Zn. Biochemistry[https://uni-frankfurt.guentert.science/Reprints/Beil19-HpMT.pdf .] [http://doi.org/10.1021/acs.biochem.9b00830 Biochemistry 58, 4570-4581 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK5 6QK5]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34355 34355]&#039;&#039;&#039; (Zn-loaded form)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6QK6 6QK6]&#039;&#039;&#039; [http://files.rcsb.org/download/6qk6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34356 34356]&#039;&#039;&#039; (Cd-loaded form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5zcz.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5ZCZ]]&lt;br /&gt;
|Tanaka, T., Ikeya, T., Kamoshida, H., Suemoto, Y., Mishima, M., Shirakawa, M., Güntert, P., Ito, Y. High resolution protein 3D structure determination in living eukaryotic cells[https://uni-frankfurt.guentert.science/Reprints/Tanaka19-EukaryoticInCellNMR.pdf .] [http://doi.org/10.1002/anie.201900840 Angew. Chem. Int. Ed. 58, 7284–7288 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZCZ 5ZCZ]&#039;&#039;&#039; [http://files.rcsb.org/download/5zcz_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27354 27354]&#039;&#039;&#039; (T. Thermophilus HB8 TTHA1718 protein in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5ZD0 5ZD0]&#039;&#039;&#039; [http://files.rcsb.org/download/5zd0_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27356 27356]&#039;&#039;&#039; (ubiquitin with three alanine mutations in living eukaryotic cells)&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5Z4B 5Z4B]&#039;&#039;&#039; [http://files.rcsb.org/download/5z4b_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=36153 36153]&#039;&#039;&#039; (GB1 in living eukaryotic cells)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6h8c.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6H8C]]&lt;br /&gt;
|Huber, J., Obata, M., Gruber, J., Akutsu, M., Löhr, F., Rogova, N., Güntert, P., Dikic, I., Krikin, V., Komatsu, M., Dötsch, V. &amp;amp; Rogov, V. V. An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5[https://uni-frankfurt.guentert.science/Reprints/Huber20-UBA5.pdf .] [http://doi.org/10.1080/15548627.2019.1606637 Autophagy 16, 256-270 (2020)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6H8C 6H8C]&#039;&#039;&#039; [http://files.rcsb.org/download/6h8c_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34307 34307]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6HB9 6HB9]&#039;&#039;&#039; [http://files.rcsb.org/download/6hb9_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB N/A&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f98.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F98]]&lt;br /&gt;
|Kniss, A., Kazemi, S., Löhr, F., Berger, M., Rogov, V. V., Güntert, P., Sommer, T., Jarosch, E. &amp;amp; Dötsch, V. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9[https://uni-frankfurt.guentert.science/Reprints/Kniss18-Yos9.pdf .] [http://doi.org/10.1007/s10858-018-0201-6 J. Biomol. NMR 72, 1-10 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F98 6F98]&#039;&#039;&#039; [http://files.rcsb.org/download/6f98_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34217 34217]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F99 6F99]&#039;&#039;&#039; [http://files.rcsb.org/download/6f99_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34218 34218]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F9A 6F9A]&#039;&#039;&#039; [http://files.rcsb.org/download/6f9a_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34219 34219]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6es5.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ES5]]&lt;br /&gt;
|Jemth, P., Andersson, E., Vögeli, B., Hultqvist, G., Dogan, J., Güntert, P. &amp;amp; Riek, R. &amp;amp; Chi, C. N., Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins[https://uni-frankfurt.guentert.science/Reprints/Jemth18-IDPEvolution.pdf .] [http://doi.org/10.1126/sciadv.aau4130 Science Adv. 4, eaau4130 (2018)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES5 6ES5]&#039;&#039;&#039; [http://files.rcsb.org/download/6es5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34187 34187]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES6 6ES6]&#039;&#039;&#039; [http://files.rcsb.org/download/6es6_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34188 34188]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ES7 6ES7]&#039;&#039;&#039; [http://files.rcsb.org/download/6es7_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34189 34189]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6esp.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6ESP]]&lt;br /&gt;
|Sundell, G. N., Arnold, R., Ali, M., Naksukpaiboon, P., Orts, J., Güntert, P., Chi, C. N., Ivarsson, Y. Proteome-wide analysis of phospho-regulated PDZ domain interactions[https://uni-frankfurt.guentert.science/Reprints/Sundell18-PDZ.pdf .] [http://doi.org/10.15252/msb.20178129 Mol. Sys. Biol. 14, e8129 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6ESP 6ESP]&#039;&#039;&#039; [http://files.rcsb.org/download/6esp_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34190 34190]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6by4.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6BY4]]&lt;br /&gt;
|Nichols, P.J., Henen, M.A., Born, A., Strotz, D., Guntert, P., Vogeli, B. &amp;lt;br&amp;gt; High-resolution small RNA structures from exact nuclear Overhauser enhancement measurements without additional restraints. [https://doi.org/10.1038/s42003-018-0067-x .] [Commun Biol 2018]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY4 6BY4]&#039;&#039;&#039; [http://files.rcsb.org/download/6by4_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6BY5 6BY5]&#039;&#039;&#039; [http://files.rcsb.org/download/6by5_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=30386 30386]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6fgn.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6FGN]]&lt;br /&gt;
|Krauskopf, K., Gebel, J., Kazemi, S., Löhr, F., Tuppi, M., Löhr, F., Schäfer, B., Koch, J., Güntert, P., Dötsch, V. &amp;amp; Kehrloesser, S. Regulation of the activity in the p53 family depends on the organization of the transactivation domain[https://uni-frankfurt.guentert.science/Reprints/Krauskopf18-p53TAD.pdf .] [http://doi.org/10.1016/j.str.2018.05.013 Structure 26, 1091–1100 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGN 6FGN]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgn_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34231 34231]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6FGS 6FGS]&#039;&#039;&#039; [http://files.rcsb.org/download/6fgs_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34233 34233]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:6f3k.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=6F3K]]&lt;br /&gt;
|Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E., Kerfah, R., Mas, G., Colletier, J.-P., Güntert, P., Favier, A., Schoehn, G., Schanda, P. &amp;amp; Boisbouvier, J. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex[https://uni-frankfurt.guentert.science/Reprints/Gauto19-TET2.pdf .] [http://doi.org/10.1038/s41467-019-10490-9 Nat. Commun. 10, 2697 (2019)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6F3K 6F3K]&#039;&#039;&#039; [http://files.rcsb.org/download/6f3k_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039;&lt;br /&gt;
&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=6R8N 6R8N]&#039;&#039;&#039; [http://files.rcsb.org/download/6r8n_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=27211 27211]&#039;&#039;&#039; (after PheniX refinement)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n2o.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N2O]]&lt;br /&gt;
|Russo, C., Osterburg, C., Sirico, A., Antonini, D., Ambrosio, R., Würz, J. M., Rinnental J., Schäfer, B., Güntert, P., Sinha, S., Dötsch, V. &amp;amp; Missero, C. Protein aggregation of the p63 transcription factor underlies severe skin fragility in AEC syndrome[https://uni-frankfurt.guentert.science/Reprints/Russo18-p63Aggregation.pdf .] [http://doi.org/10.1073/pnas.1713773115 Proc. Natl. Acad. Sci. USA  115, E906-E915 (2018)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N2O 5N2O]&#039;&#039;&#039; [http://files.rcsb.org/download/5n2o_nmr-data.nef.gz NMR data] &#039;&#039;&#039;BMRB [https://bmrb.io/data_library/generate_summary.php?bmrbId=34095 34095]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:5n6r.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5N6R]]&lt;br /&gt;
|Reckel, S., Gehin, C., Tardivon, D., Harduin, D., Georgeon, S., Kükenshöner, T., Löhr, F., Koide, A., Buchner, L., Panjkovich, A., Reynaud, A., Pinho, S., Gerig, B., Svergun, D., Pojer, F., Güntert, P., Dötsch, V., Koide, S., Gavin, A.-C. &amp;amp; Hantschel, O. Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase[http://uni-frankfurt.guentert.science/Reprints/Reckel17-Bcr-Abl.pdf .] [http://doi.org/10.1038/s41467-017-02313-6 Nat. Commun. 8, 2101 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N6R 5N6R]&#039;&#039;&#039; [http://files.rcsb.org/download/5N6R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=34101 34101]&#039;&#039;&#039; (DH NMR structure)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5N7E 5N7E]&#039;&#039;&#039; (DH/Mb(Bcr-DH_4))&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5OC7 5OC7]&#039;&#039;&#039; (PH/Mb(Bcr-PH_4))&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N5E_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N5E]]&lt;br /&gt;
|Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., McLeod, R. A., Stahlberg, H., Jeschke, G., Güntert, P. &amp;amp; Riek, R. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I[http://uni-frankfurt.guentert.science/Reprints/Bibow17-Nanodisc.pdf .] [http://dx.doi.org/10.1038/nsmb.3345 Nat. Struct. Mol. Biol. 24, 187-193 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N5E 2N5E]&#039;&#039;&#039; [http://files.rcsb.org/download/2N5E.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25710 25710]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:5gvq.pdb-500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=5GVQ]]&lt;br /&gt;
|Kuwasako, K., Nameki, N., Tsuda, K., Takahashi, M., Sato, A., Tochio, N., Inoue, M., Terada, T., Kigawa, T., Kobayashi, N., Shirouzu, M., Ito, T., Sakamoto, T., Wakamatsu, K., Güntert, P., Takahashi, S., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment[http://uni-frankfurt.guentert.science/Reprints/Kuwasako17-SF3b49-SF3b145.pdf .] [http://dx.doi.org/10.1002/pro.3080 Protein Sci. 26, 280-291 (2017)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=5GVQ 5GVQ]&#039;&#039;&#039; [http://files.rcsb.org/download/5GVQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=36018 36018]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2N9L_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2N9L]]&lt;br /&gt;
|Ikeya, T., Hanashima, T., Hosoya, S., Shimazaki, M., Ikeda, S., Mishima, M., Güntert, P. &amp;amp; Ito, Y. Improved in-cell structure determination of proteins at near-physiological concentration[http://uni-frankfurt.guentert.science/Reprints/Ikeya16-ImprovedInCellStructure.pdf .] [http://dx.doi.org/10.1038/srep38312 Sci Rep. 6, 38312 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2N9L 2N9L]&#039;&#039;&#039; [http://files.rcsb.org/download/2N9L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25910 25910]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2NB1_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NB1]]&lt;br /&gt;
|Gebel, J., Luh, L. M., Coutandin, D., Osterburg, C., Löhr, F., Schäfer, B., Frombach, A., Sumyk, M., Buchner, L., Krojer, T., Salah, E., Mathea, S., Güntert, P., Knapp, S. &amp;amp; Dötsch, V. Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization[http://uni-frankfurt.guentert.science/Reprints/Gebel16-TAp73.pdf .] [http://dx.doi.org/10.1038/cdd.2016.83 Cell Death Diff. 23, 1930-1940 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NB1 2NB1]&#039;&#039;&#039; [http://files.rcsb.org/download/2NB1.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25958 25958]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
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|[[image:2NAO_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2NAO]]&lt;br /&gt;
|Wälti, M. A., Ravotti, F., Arai, H., Glabe, C., Wall, J., Böckmann, A., Güntert, P., Meier, B. H. &amp;amp; Riek, R. Atomic resolution structure of a disease-relevant Aβ(1–42) amyloid fibril. [http://dx.doi.org/10.1073/pnas.1600749113 Proc. Natl. Acad. Sci. USA]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2NAO 2NAO]&#039;&#039;&#039; [http://files.rcsb.org/download/2NAO.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=26692 26692]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MYX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MYX]]&lt;br /&gt;
|von Delbrück, M., Kniss, A., Rogov, V. V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. &amp;amp; Dötsch, V. The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation[http://uni-frankfurt.guentert.science/Reprints/vonDelbrueck16-CUE.pdf .] [http://dx.doi.org/10.1016/j.molcel.2016.04.031 Mol. Cell 62, 918-928 (2016)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MYX 2MYX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MYX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25461 25461]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MWX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MWX]]&lt;br /&gt;
|Huang, S. Y., Chang, C. F., Fan, P. J., Naik, M. T., Güntert, P., Shih, H. M. &amp;amp; Huang, T. H. The RING domain of human promyelocytic leukemia protein (PML)[http://uni-frankfurt.guentert.science/Reprints/Huang15-RINGdomainPML.pdf .] [http://dx.doi.org/10.1007/s10858-015-9901-3 J. Biomol. NMR 61, 173-180 (2015)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MWX 2MWX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MWX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25376 25376]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2MVX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MVX]]&lt;br /&gt;
|Schütz, A. K., Vagt, T., Huber, M., Ovchinnikova, O. Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., and Meier, B. H. Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation[http://uni-frankfurt.guentert.science/Reprints/Schuetz15-Abeta.pdf .] [http://dx.doi.org/10.1002/anie.201408598 Angew. Chem. Int. Ed. 54, 331–335 (2015)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MVX 2MVX]&#039;&#039;&#039; [http://files.rcsb.org/download/2MVX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=25289 25289]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RUG_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RUG]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Nagata, T., Takahashi, M., Kigawa, T., Kobayashi, N., Güntert, P., Shirouzu, M., Yokoyama, S. &amp;amp; Muto, Y. Novel RNA recognition motif domain in cytoplasmic polyadenylation element binding protein 3[http://uni-frankfurt.guentert.science/Reprints/Tsuda14-CPEB3RRM1.pdf .] [http://dx.doi.org/10.1002/prot.24651 Proteins 82, 2879–2886 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RUG 2RUG]&#039;&#039;&#039; [http://files.rcsb.org/download/2RUG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11563 11563]&#039;&#039;&#039;&lt;br /&gt;
|- &lt;br /&gt;
&lt;br /&gt;
|[[image:2RU3_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Unzai, S., Tsuda, K., Yoshikawa, S., He, F., Kobayashi, N., Güntert, P., Shirouzu, M., Ito, T., Tanaka, A., Yokoyama, S., Hagiwara, M., Kuroyanagi, H. &amp;amp; Muto, Y. RBFOX and SUP-12 sandwich a guanine base to cooperatively regulate tissue-specific splicing[http://uni-frankfurt.guentert.science/Reprints/Kuwasako14-RBFOXandSUP-12.pdf .] [http://dx.doi.org/10.1038/nsmb.2870 Nat. Struct. Mol. Biol. 21, 778–786 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU3 2RU3]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU3.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11517 11517]&#039;&#039;&#039; (SUP-12–RNA&amp;lt;sub&amp;gt;6&amp;lt;/sub&amp;gt; complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MGZ 2MGZ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MGZ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11518 11518]&#039;&#039;&#039; (ASD-1–SUP-12–RNA&amp;lt;sub&amp;gt;12&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MMJ_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU3]]&lt;br /&gt;
|Uggerhøj, L. E., Munk, J. K., Hansen, P. R., Güntert, P. &amp;amp; Wimmer, R. Structural features of peptoid-peptide hybrids in lipid-water interfaces[http://uni-frankfurt.guentert.science/Reprints/Uggerhoj14-Peptoid.pdf .] [http://dx.doi.org/10.1016/j.febslet.2014.07.016 FEBS Lett. 588, 3291–3297 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MMJ 2MMJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2MMJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19856 19856]&#039;&#039;&#039; (M-Nleu11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN9 2MN9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19883 19883]&#039;&#039;&#039; (M-Nleu13 trans)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MN8 2MN8]&#039;&#039;&#039; [http://files.rcsb.org/download/2MN8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19882 19882]&#039;&#039;&#039; (M-Nleu13 cis)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RU5_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RU5]]&lt;br /&gt;
|Watson, R. P., Christen, M. T., Bumbak, F., Ewald, C., Reichen, C. Mihajlovic, M., Schmidt, E., Güntert, P., Caflisch, A., Plückthun, A., Zerbe, O. Spontaneous self assembly of fragments of engineered Armadillo repeat proteins into a folded structure[http://uni-frankfurt.guentert.science/Reprints/Watson14-Armadillo.pdf .] [http://dx.doi.org/10.1016/j.str.2014.05.002 Structure 22, 985–995 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU5 2RU5]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU5.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11548 11548]&#039;&#039;&#039; (uncomplexed MA)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RU4 2RU4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RU4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11544 11544]&#039;&#039;&#039; (MA-YM&amp;lt;sub&amp;gt;2&amp;lt;/sub&amp;gt; complex)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2MD9_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2MD9]]&lt;br /&gt;
|Tufar, P., Rahighi, S., Kraas, F. I., Kirchner, D. K., Löhr, F., Henrich, E., Köpke, J., Dikic, I., Güntert, P., Marahiel, M. A. &amp;amp; Dötsch, V. Crystal structure of a PCP/Sfp complex reveals the structural basis for carrier protein posttranslational modification[http://uni-frankfurt.guentert.science/Reprints/Tufar14-PCPSfp.pdf .] [http://dx.doi.org/10.1016/j.chembiol.2014.02.014 Chem. Biol. 21, 552–562 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2MD9 2MD9]&#039;&#039;&#039; [http://files.rcsb.org/download/2MD9.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19479 19479]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RTX_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RTX]]&lt;br /&gt;
|Kogure, H., Handa, Y., Nagata, M., Kanai, N., Güntert, P., Kubota, K. &amp;amp; Nameki, N. Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ[http://uni-frankfurt.guentert.science/Reprints/Kogure14-YaeJ.pdf .] [http://dx.doi.org/10.1093/nar/gkt1280 Nucl. Acids Res. 42, 3152-3163 (2014)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RTX 2RTX]&#039;&#039;&#039; [http://files.rcsb.org/download/2RTX.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11534 11534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M8I_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M8I]]&lt;br /&gt;
|Luh, L. M., Hänsel, R., Löhr, F., Kirchner, D. K., Krauskopf, K., Pitzius, S., Schäfer, B., Tufar, P., Corbeski, I., Güntert, P. &amp;amp; Dötsch, V. Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition[http://uni-frankfurt.guentert.science/Reprints/Luh13-Pin1.pdf .] [http://dx.doi.org/10.1021/ja405244v J. Am. Chem. Soc. 135, 13796−13803 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8I 2M8I]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8I.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19258 19258]&#039;&#039;&#039; (wildtype&lt;br /&gt;
WW domain)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2M8J 2M8J]&#039;&#039;&#039; [http://files.rcsb.org/download/2M8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19259 19259]&#039;&#039;&#039; (WW(S16E) mutant)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUE_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUE]]&lt;br /&gt;
|Rogov, V. V., Suzuki, H., Fiskin, E., Wild, P., Kniss, A., Rozenknop, A., Kato, R., Kawasaki, M., McEwan, D. G., Löhr, F., Güntert, P., Dikic, I., Wakatsuki, S. &amp;amp; Dötsch, V. Structural basis for phosphorylation-triggered autophagic clearance of &#039;&#039;Salmonella&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Rogov13-AutophagicClearance.pdf .] [http://dx.doi.org/10.1042/BJ20121907 Biochem. J. 454, 459–466 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LUE 2LUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2LUE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18518 18518]&#039;&#039;&#039; (NMR structure of LC3B OPTN-LIR Ptot complex)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTU]&#039;&#039;&#039; (crystal structure of human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTV]&#039;&#039;&#039; (crystal structure of Optineurin LIR-fused human LC3B_2-119)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3VTU 3VTW]&#039;&#039;&#039; (crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2M99_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99]]&lt;br /&gt;
|Lin, Y. J., Ikeya, T., Güntert, P. &amp;amp; Chang, L. S. NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra[http://uni-frankfurt.guentert.science/Reprints/Lin13-NACI.pdf .] [http://dx.doi.org/10.3390/molecules18088906 Molecules 18, 8906-8918 (2013)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2M99 2M99]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2M99.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=19287 19287]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK6]]&lt;br /&gt;
|He, F., Tsuda, K., Takahashi, M., Kuwasako, K., Terada, T., Shirouzu, M., Watanabe, S., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the interaction of ADP-ribose with the PARP WWE domains[http://uni-frankfurt.guentert.science/Reprints/He12-PARPWWE.pdf .] [http://dx.doi.org/10.1016/j.febslet.2012.09.009 FEBS Lett. 586, 3858–3864 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DK6 2DK6]&#039;&#039;&#039; [http://files.rcsb.org/download/2DK6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11500 11500]&#039;&#039;&#039; (WWE domain from PARP11)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X4R 1X4R]&#039;&#039;&#039; [http://files.rcsb.org/download/1X4R.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11501 11501]&#039;&#039;&#039; (WWE domain&lt;br /&gt;
from PARP14)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LVL_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL]]&lt;br /&gt;
|Christ, N. A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U. A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.-D. &amp;amp; Wöhnert, J. The first structure of a lantibiotic immunity protein, SpaI from &#039;&#039;Bacillus subtilis&#039;&#039;, reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Christ12-SpaI.pdf .] [http://dx.doi.org/10.1074/jbc.M112.401620 J. Biol. Chem. 287, 35286-35298 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LVL 2LVL]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LVL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17534 17534]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LUM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM]]&lt;br /&gt;
|Vögeli, B., Kazemi, S., Güntert, P. &amp;amp; Riek, R. Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs[http://uni-frankfurt.guentert.science/Reprints/Voegeli12-eNOEsMotion.pdf .] [http://dx.doi.org/10.1038/nsmb.2355 Nature Struct. Mol. Biol. 19, 1053–1057 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2LUM 2LUM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2LUM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=18531 18531]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RSM_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM]]&lt;br /&gt;
|Kogure, H., Hikawa, Y., Hagihara, M., Tochio, N., Koshiba, S., Inoue, Y., Güntert, P., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure and siRNA-mediated knockdown analysis of the mitochondrial disease-related protein C12orf65[http://uni-frankfurt.guentert.science/Reprints/Kogure12-C12orf65.pdf .] [http://onlinelibrary.wiley.com/doi/10.1002/prot.24152/abstract Proteins 80, 2629–2642 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RSM 2RSM]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RSM.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11491 11491]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RS6_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RS6]]&lt;br /&gt;
|Nagata, T., Tsuda, K., Shirouzu, M., Kigawa, T., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structures of the double-stranded RNA-binding domains from RNA-helicase A[http://uni-frankfurt.guentert.science/Reprints/Nagata12-RNAhelicaseA.pdf .] [http://dx.doi.org/10.1002/prot.24059 Proteins 80, 1699–1706 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS6 2RS6]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS6.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11456 11456]&#039;&#039;&#039; (dsRBD1)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RS7 2RS7]&#039;&#039;&#039; [http://files.rcsb.org/download/2RS7.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11457 11457]&#039;&#039;&#039; (dsRBD2)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2LIW_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2LIW]]&lt;br /&gt;
|Busche, A., Gottstein, D., Hein, C., Ripin, N., Pader, I., Tufar, P., Eisman, E. B., Gu, L. Walsh, C. T., Sherman, D. H., Löhr, F., Güntert, P. &amp;amp; Dötsch, V. Characterization of the interaction between an ACP domain and a halogenase in the curacin A polyketide synthetase[http://uni-frankfurt.guentert.science/Reprints/Busche12-ACP.pdf .] [http://dx.doi.org/10.1021/cb200352q ACS Chem. Biol. 7, 378–386 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIU 2LIU]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17906 17906]&#039;&#039;&#039; (holo-ACPI)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2LIW 2LIW]&#039;&#039;&#039; [http://files.rcsb.org/download/2LIW.mr NMR restraints] [http://www.rcsb.org/pdb/files/2LIW_cs.str.gz chemical shifts] (HMG-ACPI)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2DK4_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4]]&lt;br /&gt;
|He, F., Inoue, M., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Kobayashi, N., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Solution structure of the Splicing Factor Motif (SFM) of the human Prp18 protein[http://uni-frankfurt.guentert.science/Reprints/He12-Prp18Structure.pdf .] [http://dx.doi.org/10.1002/prot.24003 Proteins 80, 968–974 (2012)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2DK4 2DK4]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2DK4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11355 11355]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L6X_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X]]&lt;br /&gt;
|Reckel, S., Gottstein, D., Stehle, J., Löhr, F., Verhoefen, M. K., Takeda, M., Silvers, R., Kainosho, M., Glaubitz, C., Wachtveitl, J., Bernhard, F., Schwalbe, H., Güntert, P. &amp;amp; Dötsch, V. Solution NMR structure of proteorhodopsin[http://uni-frankfurt.guentert.science/Reprints/Reckel11-Proteorhodopsin.pdf .] [http://dx.doi.org/10.1002/anie.201105648 Angew. Chem. Int. Ed. 50, 11942–11946 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L6X 2L6X]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L6X.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17327 17327]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2L8J_bio_r_250b.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J]]&lt;br /&gt;
|Rozenknop, A., Rogov, V. V., Löhr, F., Güntert, P., Dikic, I., &amp;amp; Dötsch, V. Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1[http://uni-frankfurt.guentert.science/Reprints/Rozenknop11-GABARAPL-NBR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2011.05.003 J. Mol. Biol. 410, 477–487 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2L8J 2L8J]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2L8J.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=17412 17412]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2KX7_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7]]&lt;br /&gt;
|Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB[http://uni-frankfurt.guentert.science/Reprints/Schmoee11-RcsD-ABL.pdf .] [http://dx.doi.org/10.1016/j.str.2011.01.012 Structure 19, 577–587 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2KX7 2KX7]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KX7.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2RRB_bio_r_250.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB]]&lt;br /&gt;
|Tsuda, K., Someya, T., Kuwasako, K., Takahashi, M., Fahu, H., Inoue, M., Harada, T., Watanabe, S., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural basis for the dual RNA-recognition modes of human Tra2-β RRM[http://uni-frankfurt.guentert.science/Reprints/Tsuda11-Tra2betaRRM.pdf .] [http://dx.doi.org/10.1093/nar/gkq854 Nucl. Acids Res. 39, 1538-1553 (2011)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RRB 2RRB]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RRB.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:3llh_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=3LLH 3LLH]&#039;&#039;&#039;&lt;br /&gt;
[http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=STRUCTFACT&amp;amp;compression=NO&amp;amp;structureId=3LLH Structure factors]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2cpn_asym_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN]]&lt;br /&gt;
|Yamashita, S., Nagata, T., Kawazoe, M., Takemoto, C., Kigawa, T, Güntert, P., Kobayashi, N., Terada, T., Shirouzu, M., Wakiyama, M., Muto, Y. &amp;amp; Yokoyama, S. Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein[http://uni-frankfurt.guentert.science/Reprints/Yamashita_ProSci_2011.pdf .] [http://dx.doi.org/10.1002/pro.543 Protein Sci. 20, 118-130 (2011)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2CPN 2CPN]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2CPN.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1j26_asym_r_500_2.jpg|120px|link=http://www.pdb.org/pdb/explore/explore.do?structureId=1J26]]&lt;br /&gt;
|Handa, Y., Hikawa, Y., Tochio, N., Kogure, H., Inoue, M., Koshiba, S., Güntert, P., Inoue, Y., Kigawa, T., Yokoyama, S. &amp;amp; Nameki, N. Solution structure of the mitochondrial protein ICT1 that is essential for cell vitality[http://uni-frankfurt.guentert.science/Reprints/Handa_JMolBiol_2010.pdf .] [http://dx.doi.org/10.1016/j.jmb.2010.09.033 J. Mol. Biol. 404, 260-273 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/images.do?structureId=1J26 1J26]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rqo_bio_r_500.jpg|120px|link=http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO]]&lt;br /&gt;
|Hamada, T., Matsunaga, S.,Fujiwara, M., Fujita, K., Hirota, H., Schmucki, R., Güntert, P. &amp;amp; Fusetani, N. Solution structure of polytheonamide B, a highly cytotoxic nonribosomal polypeptide from marine sponge[http://uni-frankfurt.guentert.science/Reprints/HamadaJACS2010.pdf .] [http://dx.doi.org/10.1021/ja104616z J. Am. Chem. Soc. 132, 12941–12945 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore/explore.do?structureId=2RQO 2RQO]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2RQO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e61_bio_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2E61]]&lt;br /&gt;
|He, F., Umehara, T., Saito, K., Harada, T., Watanabe, S., Yobuki, T., Kigawa, T., Takahashi, M., Kuwasako, K., Tsuda, K., Matsuda, T., Aoki, M., Seki, E., Kobayashi, N., Güntert, P., Yokoyama, S. &amp;amp; Muto, Y. Structural insight into the zinc finger CW domain as a histone modification reader[http://uni-frankfurt.guentert.science/Reprints/He10-ZincFingerCWDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2010.06.012 Structure 18, 1127–1139 (2010)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2E61 2E61]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2E61.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kr6_asym_r_500.jpg|120px|link=http://www.pdb.org/pdb/explore/images.do?structureId=2KR6]]&lt;br /&gt;
|Sobhanifar, S., Schneider, B., Löhr, F., Gottstein, D., Ikeya, T., Filipek, S., Güntert, P., Bernhard, F. &amp;amp; Dötsch, V. Structural investigation of the C-terminal catalytic fragment of presenilin-1[http://uni-frankfurt.guentert.science/Reprints/Sobhanifar10-Presenilin1.pdf .] [http://dx.doi.org/10.1073/pnas.1000778107 Proc. Natl. Acad. Sci. USA 107, 9644–9649 (2010)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=2KR6 2KR6]&#039;&#039;&#039;&lt;br /&gt;
[http://files.rcsb.org/download/2KR6.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kby_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KBY]]&lt;br /&gt;
|Coutandin, D., Löhr, F., Niesen, F. H., Ikeya, T., Weber, T. A., Schäfer, B., Bullock, A. N., Yang, A., Güntert, P. , Knapp, S., McKeon, F., Der Ou, H. &amp;amp; Dötsch, V. Conformational stability and activity of p73 require a second helix in the tetramerization domain[http://uni-frankfurt.guentert.science/Reprints/Coutandin09-p73Tetramer.pdf .] [http://dx.doi.org/10.1038/cdd.2009.139 Cell Death Diff. 16, 1582–1589 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KBY 2KBY]&#039;&#039;&#039; [http://files.rcsb.org/download/2KBY.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2yue_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2YUE]]&lt;br /&gt;
|He, F., Saito, K., Kobayashi, N., Harada, T., Watanabe, S., Kigawa, T, Güntert, P., Unzai, S., Muto, Y. &amp;amp; Yokoyama, S. Structural and functional characterization of the NHR1 domain of the Drosophila Neuralized E3 ligase in the Notch signaling pathway[http://uni-frankfurt.guentert.science/Reprints/He09-NeuralizedNHR1.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.08.020 J. Mol. Biol. 393, 478-495 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2YUE 2YUE]&#039;&#039;&#039; [http://files.rcsb.org/download/2YUE.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E63 2E63]&#039;&#039;&#039; [http://files.rcsb.org/download/2E63.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2klo_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KLO]]&lt;br /&gt;
|Khayrutdinov, B. I., Bae, W. J., Yun, Y. M., Lee, J. H., Tsuyama, T., Kim, J. J., Hwang, E., Ryu, K. S., Cheong, H. K., Cheong, C., Ko, J. S., Enomoto, T., Karplus, P. A., Güntert, P., Tada, S., Jeon, Y. H., Cho, Y. Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors[http://uni-frankfurt.guentert.science/Reprints/Kharyrutdinov09-Cdt1.pdf .] [http://dx.doi.org/10.1002/pro.236 Protein Sci. 18, 2252-2264 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KLO 2KLO]&#039;&#039;&#039; [http://files.rcsb.org/download/2KLO.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=3A4C 3A4C]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rqc_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RQC]]&lt;br /&gt;
|Tsuda, K., Kuwasako, K., Takahashi, M., Someya, T., Inoue, M., Terada, T., Kobayashi, N., Shirouzu, M., Kigawa, T., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Structural basis for the sequence specific RNA-recognition mechanism of human CUG-BP1 RRM3[http://uni-frankfurt.guentert.science/Reprints/Tsuda09-CUG-BP1RRM3.pdf .] [http://dx.doi.org/10.1093/nar/gkp546 Nucl. Acids Res. 37, 5151–5166 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQC 2RQC]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQC.mr NMR restraints]&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RQ4 2RQ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2RQ4.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rpj_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RPJ]]&lt;br /&gt;
|He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily[http://uni-frankfurt.guentert.science/Reprints/He09-Fn14.pdf .] [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. 18, 650–656 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RPJ 2RPJ]&#039;&#039;&#039; [http://files.rcsb.org/download/2RPJ.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2kak_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2KAK]]&lt;br /&gt;
|Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. &amp;amp; Zerbe O. The β&amp;lt;sub&amp;gt;E&amp;lt;/sub&amp;gt;-domain of Wheat E&amp;lt;sub&amp;gt;c&amp;lt;/sub&amp;gt;-1 metallothionein: A metal-binding domain with a distinctive structure[http://uni-frankfurt.guentert.science/Reprints/Peroza09-WheatMetallothionein.pdf .] [http://dx.doi.org/10.1016/j.jmb.2009.01.035 J. Mol. Biol. 387, 207–218 (2009)]&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2KAK 2KAK]&#039;&#039;&#039; [http://www.rcsb.org/pdb/download/downloadFile.do?fileFormat=NMR&amp;amp;structureId=2KAK NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=16025 16025]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rog_asym_r_500.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2ROG]]&lt;br /&gt;
|Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. &amp;amp; Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy[http://uni-frankfurt.guentert.science/Reprints/Sakakibara09-InCellStructure.pdf .] [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROG 2ROG]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROG.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11037 11037]&#039;&#039;&#039; (in-cell)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROE 2ROE]&#039;&#039;&#039; [http://files.rcsb.org/download/2ROE.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=11035 11035]&#039;&#039;&#039; (in solution)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e5s_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E5S]]&lt;br /&gt;
|He, F., Dang, W., Abe, C., Tsuda, K., Inoue, M., Watanabe, S., Kobayashi, N., Kigawa, T, Matsuda, T., Yabuki, T., Aoki, M., Seki, E., Harada, T., Tomabechi, Y., Terada, T., Shirouzu, M., Tanaka, A., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2[http://uni-frankfurt.guentert.science/Reprints/He09-MuscleblindLikeProtein2.pdf .] [http://www3.interscience.wiley.com/journal/121517649/abstract Protein Sci. 18, 80-91 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E5S 2E5S]&#039;&#039;&#039;　[http://files.rcsb.org/download/2E5S.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2e29_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2E29]]&lt;br /&gt;
|Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions[http://uni-frankfurt.guentert.science/Reprints/Ohnishi09-GUCTDomainStructure.pdf .] [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2E29 2E29]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jz4_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JZ4]]&lt;br /&gt;
|Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., Jee, J., Güntert, P., Aceti, D. J., Markley, J. L. &amp;amp; Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-At3g16450SAIL.pdf .] [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JZ4 2JZ4]&#039;&#039;&#039; [http://files.rcsb.org/download/2JZ4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15607 15607]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2ba3_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2BA3]]&lt;br /&gt;
|Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. &amp;amp; Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation[http://uni-frankfurt.guentert.science/Reprints/Yoshida08-NikADimerStructure.pdf .] [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2BA3 2BA3]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15784 15784]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jns_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JNS]]&lt;br /&gt;
|Lin, Y. J., Umehara, T., Inoue, M., Saito, K., Kigawa, T., Jang, M. K., Ozato, K., Yokoyama, S., Padmanabhan, B., Güntert, P. Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4[http://uni-frankfurt.guentert.science/Reprints/Lin08-Brd4ET.pdf .] [http://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JNS 2JNS]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15125 15125]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2ron_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RON]]&lt;br /&gt;
|Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. &amp;amp; Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase[http://uni-frankfurt.guentert.science/Reprints/Koglin08-SurfactinSynthetase.pdf .] [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RON 2RON]&#039;&#039;&#039; [http://files.rcsb.org/download/2RON.mr NMR restraints] (SrfTEII)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2K2Q 2K2Q]&#039;&#039;&#039; [http://files.rcsb.org/download/2K2Q.mr NMR restraints] (complex of SrfTEII and H state TycC3–PCP)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1whv_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. &amp;amp; Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition[http://uni-frankfurt.guentert.science/Reprints/Nagata08-RRM.pdf .] [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WHV 1WHV]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2ROK 2ROK]&#039;&#039;&#039; (cap-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jw8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. &amp;amp; Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method[http://uni-frankfurt.guentert.science/Reprints/Takeda08-SARS.pdf .] [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JW8 2JW8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=15511 15511]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2rne_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2RNE]]&lt;br /&gt;
|Kuwasako, K., Takahashi, M., Tochio, N., Abe, C., Tsuda, K., Inoue, M., Terada, T., Shirouzu, M., Kobayashi, N., Kigawa, T., Taguchi, S., Tanaka, A., Hayashizaki, Y., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-TIA1RRMDomain.pdf .] [http://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2RNE 2RNE]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2fho asym r 250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2FHO]]&lt;br /&gt;
|Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. &amp;amp; Yokoyama, S. Complex assembly mechanism and an RNA-binding mode of the human p14-SF3b155 spliceosomal protein complex identified by NMR solution structure and functional analyses[http://uni-frankfurt.guentert.science/Reprints/Kuwasako08-p14SF3b155Structure.pdf .] [http://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2FHO 2FHO]&#039;&#039;&#039;  [http://files.rcsb.org/download/2FHO.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2jo8_asym_r_250.jpg‎|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2JO8]]&lt;br /&gt;
|Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. &amp;amp; Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway[http://uni-frankfurt.guentert.science/Reprints/Hwang07-DimericSARAHDomains.pdf .] [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2JO8 2JO8]&#039;&#039;&#039;  [http://files.rcsb.org/download/2JO8.mr NMR restraints] &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dwv asym r 250.jpg|120px|link=http://www.rcsb.org/pdb/explore.do?structureId=2DWV]]&lt;br /&gt;
|Ohnishi, S. Güntert, P., Koshiba, S., Tomizawa, T., Akasaka, R., Tochio, N., Sato, M., Inoue, M., Harada, T., Watanabe, S., Tanaka, T., Shirouzu, M., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form[http://uni-frankfurt.guentert.science/Reprints/Ohnishi07-WWDimer.pdf .] [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DWV 2DWV]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dt6 asym r 250.jpg|120px]]&lt;br /&gt;
|Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. &amp;amp; Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP[http://uni-frankfurt.guentert.science/Reprints/Kuwasako06-SURPDomain.pdf .] [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT6 2DT6]&#039;&#039;&#039; (SURP1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DT7 2DT7]&#039;&#039;&#039; (SURP2-SF3a60)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcp asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270(9-135) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCP 2DCP]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCP.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with [[FLYA]]. Structure does not supersede the original deposition 1VDY.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcq asym r 250.jpg|120px]]&lt;br /&gt;
|Rhodanese homology domain At3g16270(175-295) from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCQ 2DCQ]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCQ.mr NMR restraints]&lt;br /&gt;
&lt;br /&gt;
Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1VEE.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2dcr asym r 250.jpg|120px]]&lt;br /&gt;
|Src homology domain 2 from the human feline sarcoma oncogene Fes.&lt;br /&gt;
López-Méndez, B. &amp;amp; Güntert, P. Automated protein structure determination from NMR spectra[http://uni-frankfurt.guentert.science/Reprints/Lopez06a.pdf .] [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2DCR 2DCR]&#039;&#039;&#039; [http://files.rcsb.org/download/2DCR.mr NMR restraints]br&amp;gt;Note: Automated structure determination with FLYA. Structure does not supersede the original deposition 1WQU.&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2h3s asym r 250.jpg|120px]]&lt;br /&gt;
|Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. &amp;amp; Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide[http://uni-frankfurt.guentert.science/Reprints/Jurt06a.pdf .] [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H4B 2H4B]&#039;&#039;&#039; [http://files.rcsb.org/download/2H4B.mr NMR restraints] (cis-1-PP)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3S 2H3S]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3S.mr NMR restraints] (cis-1-PP bound to DPC micelles)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2H3T 2H3T]&#039;&#039;&#039; [http://files.rcsb.org/download/2H3T.mr NMR restraints] (trans-1-PP bound to DPC micelles)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wvo asym r 250.jpg|120px]]&lt;br /&gt;
|Hamada, T., Ito, Y., Abe, T., Hayashi, F., Güntert, P., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Yoshida, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase[http://uni-frankfurt.guentert.science/Reprints/Hamada06a.pdf .] [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WVO 1WVO]&#039;&#039;&#039; [http://files.rcsb.org/download/1WVO.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2agm asym r 250.jpg|120px]]&lt;br /&gt;
|Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. &amp;amp; Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an &#039;&#039;Azotobacter vinelandii&#039;&#039; mannuronan C-5 epimerase[http://uni-frankfurt.guentert.science/Reprints/Aachmann06a.pdf .] [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2AGM 2AGM]&#039;&#039;&#039; [http://files.rcsb.org/download/2AGM.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2d21 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) maltodextrin-binding protein MBP.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2D21 2D21]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6807 6807]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1x02 asym r 250.jpg|120px]]&lt;br /&gt;
|Stereo-array isotope labeled (SAIL) calmodulin.&lt;br /&gt;
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. &amp;amp; Güntert, P. Optimal isotope labeling for NMR protein structure determinations[http://uni-frankfurt.guentert.science/Reprints/Kainosho06a.pdf .] [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1X02 1X02]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6541 6541]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wwq asym r 250.jpg|120px]]&lt;br /&gt;
|Li, H., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., Motoda, Y., Kobayashi, A., Terada, T., Shirouzu, M., Koshiba, S., Lin, Y. J., Güntert, P., Suzuki, H., Hayashizaki, Y., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold[http://uni-frankfurt.guentert.science/Reprints/Li05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WWQ 1WWQ]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wqu asym r 250.jpg|120px]]&lt;br /&gt;
|Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes[http://uni-frankfurt.guentert.science/Reprints/Scott05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WQU 1WQU]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6331 6331]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1n27 asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Tochio, N., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Fujikura, Y., Saito, M., Ikari, M., Watanabe, M., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Tanaka, A., Hayashizaki, Y., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family[http://uni-frankfurt.guentert.science/Reprints/Nameki05a.pdf .] [http://www3.interscience.wiley.com/journal/121602709/abstract Protein Sci. 14, 756–764 (2005)] &lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1N27 1N27]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1u3m asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog[http://uni-frankfurt.guentert.science/Reprints/Calzolai05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U3M 1U3M]&#039;&#039;&#039; [http://files.rcsb.org/download/1U3M.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6269 6269]&#039;&#039;&#039; (chicken PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1U5L 1U5L]&#039;&#039;&#039; [http://files.rcsb.org/download/1U5L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6270 6270]&#039;&#039;&#039; (turtle PrP(121-225))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XU0 1XU0]&#039;&#039;&#039; [http://files.rcsb.org/download/1XU0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6282 6282]&#039;&#039;&#039; (frog PrP(90-222))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1xyj asym r 250.jpg|120px]]&lt;br /&gt;
|Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. &amp;amp; Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep[http://uni-frankfurt.guentert.science/Reprints/Lysek05a.pdf .] [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYJ 1XYJ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYJ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6377 6377]&#039;&#039;&#039; (cat PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYK 1XYK]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYK.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6378 6378]&#039;&#039;&#039; (dog PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYQ 1XYQ]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYQ.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6380 6380]&#039;&#039;&#039; (pig PrP(121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1XYU 1XYU]&#039;&#039;&#039; [http://files.rcsb.org/download/1XYU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6381 6381]&#039;&#039;&#039; (sheep PrP[R168](121-231))&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Y2S 1Y2S]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6403 6403]&#039;&#039;&#039; (sheep PrP[H168](121-231))&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vex asym r 250.jpg|120px]]&lt;br /&gt;
|Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. &amp;amp; Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin[http://uni-frankfurt.guentert.science/Reprints/Paakkonen06a.pdf .] [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SZL 1SZL]&#039;&#039;&#039;　[http://files.rcsb.org/download/1SZL.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6175 6175]&#039;&#039;&#039; (TSR1)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEX 1VEX]&#039;&#039;&#039; (TSR4)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vdy asym r 250.jpg|120px]]&lt;br /&gt;
|ENTH-VHS domain At3g16270 from &#039;&#039;Arabidopsis thaliana&#039;&#039;.&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VDY 1VDY]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5928 5928]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vd0 asym r 250.jpg|120px]]&lt;br /&gt;
|Iwai, H., Forrer, P., Plückthun, A. &amp;amp; Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD[http://uni-frankfurt.guentert.science/Reprints/Iwai05a.pdf .] [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VD0 1VD0]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1vee asym r 250.jpg|120px]]&lt;br /&gt;
|Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. &amp;amp; Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana[http://uni-frankfurt.guentert.science/Reprints/Pantoja05a.pdf .] [http://www3.interscience.wiley.com/journal/121602579/abstract Protein Sci. 14, 224–230 (2005)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1VEE 1VEE]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5929 5929]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ukx asym r 250.jpg|120px]]&lt;br /&gt;
|Nameki, N., Yoneyama, M., Koshiba, S., Tochio, N., Inoue, M., Seki, E., Matsuda, T., Tomo, Y., Harada, T., Saito, K., Kobayashi, N., Yabuki, T., Aoki, M., Nunokawa, E., Matsuda, N., Sakagami, N., Terada, T., Shirouzu, M., Yoshida, M., Hirota, H., Osanai, T., Tanaka, A., Arakawa, T., Carninci, P., Kawai, J., Hayashizaki, Y., Kinoshita, K., Güntert, P., Kigawa, T. &amp;amp; Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein[http://uni-frankfurt.guentert.science/Reprints/Nameki04a.pdf .] [http://dx.doi.org/10.1110/ps.04751804 Protein Sci. 13, 2089–2100 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1UKX 1UKX]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=6297 6297]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1q9g asym r 250.jpg|120px]]&lt;br /&gt;
|Fernández, C., Hilty, C., Wider, G., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the integral membrane protein OmpX[http://uni-frankfurt.guentert.science/Reprints/Fernandez04.pdf .] [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1Q9G 1Q9G]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4936 4936]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1wln asym r 250.jpg|120px]]&lt;br /&gt;
|FHA domain of mouse afadin 6.&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WLN 1WLN]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pbu asym r 250.jpg|120px]]&lt;br /&gt;
|Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. &amp;amp; Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ[http://uni-frankfurt.guentert.science/Reprints/Vanwetswinkel03.pdf .] [http://www.jbc.org/cgi/content/short/278/44/43443 J. Biol. Chem. 278, 43443–43451 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PBU 1PBU]&#039;&#039;&#039; [http://files.rcsb.org/download/1PBU.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5628 5628]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1mo8 asym r 250.jpg|120px]]&lt;br /&gt;
|Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. &amp;amp; Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase[http://uni-frankfurt.guentert.science/Reprints/Hilge03.pdf .] [http://www.nature.com/nsmb/journal/v10/n6/abs/nsb924.html Nat. Struct. Biol. 10, 468–474 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO7 1MO7]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5577 5577]&#039;&#039;&#039; (free form)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1MO8 1MO8]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5576 5576]&#039;&#039;&#039; (ATP-bound form)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1lg4 asym r 250.jpg|120px]]&lt;br /&gt;
|Lührs, T., Riek, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of the human doppel protein[http://uni-frankfurt.guentert.science/Reprints/Luhrs03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LG4 1LG4]&#039;&#039;&#039; [http://files.rcsb.org/download/1LG4.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5145 5145]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1h0l asym r 250.jpg|120px]]&lt;br /&gt;
|Zahn, R., Güntert, P. &amp;amp; Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds[http://uni-frankfurt.guentert.science/Reprints/Zahn03.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1H0L 1H0L]&#039;&#039;&#039; [http://files.rcsb.org/download/1H0L.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5378 5378]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1sr3 asym r 250.jpg|120px]]&lt;br /&gt;
|Enggist, E., Thöny-Meyer, L., Güntert, P. &amp;amp; Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif[http://uni-frankfurt.guentert.science/Reprints/Enggist02.pdf .] [http://dx.doi.org/10.1016/S0969-2126(02)00885-7 Structure 10, 1551–1557 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1SR3 1SR3]&#039;&#039;&#039; [http://files.rcsb.org/download/1SR3.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1ls8 asym r 250.jpg|120px]]&lt;br /&gt;
|Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure of the unliganded &#039;&#039;Bombyx mori&#039;&#039; pheromone-binding protein at physiological pH[http://uni-frankfurt.guentert.science/Reprints/Lee02.pdf .] [http://dx.doi.org/10.1016/S0014-5793(02)03548-2 FEBS Lett. 531, 314–318 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1LS8 1LS8]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1k9c asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. &amp;amp; Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard02.pdf .] [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K9C 1K9C]&#039;&#039;&#039; [http://files.rcsb.org/download/1K9C.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5204 5204]&#039;&#039;&#039; (residues 189-261)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1K91 1K91]&#039;&#039;&#039; [http://files.rcsb.org/download/1K91.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5205 5205]&#039;&#039;&#039; (residues 221-256)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1jas asym r 250.jpg|120px]]&lt;br /&gt;
|Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b[http://uni-frankfurt.guentert.science/Reprints/Miura02.pdf .] [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1JAS 1JAS]&#039;&#039;&#039; [http://files.rcsb.org/download/1JAS.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5038 5038]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1gm0 asym r 250.jpg|120px]]&lt;br /&gt;
|Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. &amp;amp; Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release[http://uni-frankfurt.guentert.science/Reprints/Horst01.pdf .] [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1GM0 1GM0]&#039;&#039;&#039; [http://files.rcsb.org/download/1GM0.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4849 4849]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hhn asym r 250.jpg|120px]]&lt;br /&gt;
|Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. &amp;amp; Wüthrich, K. NMR structure of the calreticulin P-domain[http://uni-frankfurt.guentert.science/Reprints/Ellgaard01.pdf .] [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HHN 1HHN]&#039;&#039;&#039; &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4878 4878]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1e1g asym r 250.jpg|120px]]&lt;br /&gt;
|Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. &amp;amp; Wüthrich, K. NMR structures of three single-residue variants of the human prion protein[http://uni-frankfurt.guentert.science/Reprints/Calzolai00.pdf .] [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1G 1E1G]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1G.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4736 4736]&#039;&#039;&#039; (variant M166V)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1P 1E1P]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1P.mr NMR restraints] (variant S170N)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1E1U 1E1U]&#039;&#039;&#039; [http://files.rcsb.org/download/1E1U.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4620 4620]&#039;&#039;&#039; (variant R220K)&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1qjk asym r 250.jpg|120px]]&lt;br /&gt;
|Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. &amp;amp; Wüthrich, K. NMR structure of the sea urchin (&#039;&#039;Strongylocentrotus purpuratus&#039;&#039;) metallothionein MTA[http://uni-frankfurt.guentert.science/Reprints/Riek99.pdf .] [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJK 1QJK]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJK.mr NMR restraints] (&amp;amp;alpha; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1QJL 1QJL]&#039;&#039;&#039; [http://files.rcsb.org/download/1QJL.mr NMR restraints] (&amp;amp;beta; domain)&amp;lt;br&amp;gt;&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4363 4363]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
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|[[image:1bf8 asym r 250.jpg|120px]]&lt;br /&gt;
|Pellecchia, M., Güntert, P., Glockshuber, R. &amp;amp; Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC[http://uni-frankfurt.guentert.science/Reprints/Pellecchia98b.pdf .] [http://dx.doi.org/10.1038/2325 Nature Struct. Biol. 5, 885–890 (1998)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1BF8 1BF8]&#039;&#039;&#039; [http://files.rcsb.org/download/1BF8.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=4070 4070]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1oca asym r 250.jpg|120px]]&lt;br /&gt;
|Ottiger, M., Zerbe, O., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A[http://uni-frankfurt.guentert.science/Reprints/Ottiger97.pdf .] [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1OCA 1OCA]&#039;&#039;&#039; [http://files.rcsb.org/download/1OCA.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1wkt asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P. &amp;amp; Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin[http://uni-frankfurt.guentert.science/Reprints/Antuch96.pdf .] [http://dx.doi.org/10.1038/nsb0896-662 Nature Struct. Biol. 3, 662–665 (1996)]&lt;br /&gt;
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&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1WKT 1WKT]&#039;&#039;&#039; [http://files.rcsb.org/download/1WKT.mr NMR restraints] &#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=5255 5255]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1tap asym r 250.jpg|120px]]&lt;br /&gt;
|Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. &amp;amp; Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick &#039;&#039;Ornithodoros moubata&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Antuch94a.pdf .] [http://dx.doi.org/10.1016/0014-5793(94)00941-4 FEBS Lett. 352, 251–257 (1994)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1TAP 1TAP]&#039;&#039;&#039; [http://files.rcsb.org/download/1TAP.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1dtk asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P. &amp;amp; Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of &#039;&#039;Dendroaspis polylepis polylepis&#039;&#039;[http://uni-frankfurt.guentert.science/Reprints/Berndt93-DendrotoxinK.pdf .] [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1DTK 1DTK]&#039;&#039;&#039; [http://files.rcsb.org/download/1DTK.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1hic asym r 250.jpg|120px]]&lt;br /&gt;
|Szyperski, T., Güntert, P., Stone, S. R. &amp;amp; Wüthrich, K. NMR solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain[http://uni-frankfurt.guentert.science/Reprints/Szyperski92-HirudinStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1HIC 1HIC]&#039;&#039;&#039; [http://files.rcsb.org/download/1HIC.mr NMR restraints]&#039;&#039;&#039;BMRB [http://www.bmrb.wisc.edu./data_library/generate_summary.php?bmrbId=1128 1128]&#039;&#039;&#039;&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:1pit asym r 250.jpg|120px]]&lt;br /&gt;
|Berndt, K. D., Güntert, P., Orbons, L. P. M. &amp;amp; Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures[http://uni-frankfurt.guentert.science/Reprints/Berndt92-BPTIStructure.pdf .] [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=1PIT 1PIT]&#039;&#039;&#039; [http://files.rcsb.org/download/1PIT.mr NMR restraints]&lt;br /&gt;
|-&lt;br /&gt;
&lt;br /&gt;
|[[image:2hoa asym r 250.jpg|120px]]&lt;br /&gt;
|Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. &amp;amp; Wüthrich K. Structure determination of the Antp(C39S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA[http://uni-frankfurt.guentert.science/Reprints/Guntert91-AntpC39S.pdf .] [http://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;PDB [http://www.rcsb.org/pdb/explore.do?structureId=2HOA 2HOA]&#039;&#039;&#039; &lt;br /&gt;
|-&lt;br /&gt;
|}&lt;/div&gt;</summary>
		<author><name>GuentertWiki</name></author>
	</entry>
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