__NOTOC__
== Selected publications ==

* 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. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature.

* 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. & Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase. [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]

* López-Méndez, B. & Güntert, P. Automated protein structure determination from NMR spectra. [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]

* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. & Güntert, P. Optimal isotope labeling for NMR protein structure determinations. [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]

* Fernández, C., Hilty, C., Wider, G., Güntert, P. & Wüthrich, K. NMR structure of the integral membrane protein OmpX. [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]

* Herrmann, T., Güntert, P. & Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. [http://dx.doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]

* Güntert, P., Mumenthaler, C. & 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)]

* Bartels, C., Güntert, P., Billeter, M. & Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra. [http://www3.interscience.wiley.com/journal/48372/abstract J. Comp. Chem. 18, 139–149 (1997)]

* Bartels, C., Xia, T., Billeter, M., Güntert, P. & 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)]

* Güntert, P., Braun, W. & 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. [http://dx.doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]

== All publications ==

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==== In press/accepted ====

* 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. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature.

* Peroza, E. A., Schmucki, R., Güntert, P., Freisinger, E. & Zerbe O. The βE-domain of Ec-1 metallothionein: A metal-binding domain with a distinctive structure. J. Mol. Biol.

* 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. & Yokoyama, S. Solution structure of the RNA binding domain in the human muscleblind-like protein 2. Protein Sci.

==== 2009 ====

* Güntert, P. Automated structure determination from NMR Spectra. [http://dx.doi.org/10.1007/s00249-008-0367-z Eur. Biophys. J. 38, 129-143 (2009)]

* He, F., Dang, W., Saito, K., Watanabe, S., Kobayashi, N., Güntert, P., Kigawa, T, Tanaka, A., Muto, Y. & Yokoyama, S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily. [http://www3.interscience.wiley.com/journal/121617285/abstract Protein Sci. (2009)]

* Schmucki, R., Yokoyama, S. & Güntert, P. Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm. [http://dx.doi.org/10.1007/s10858-008-9291-x J. Biomol. NMR. 43, 97-109 (2009)]

* Ohnishi, S. Pääkkönen, K., Koshiba, S., Tochio, N., Sato, M., Kobayashi, N., Harada, T., Watanabe, S., Muto, Y., Güntert, P., Tanaka, A., Kigawa, T. & Yokoyama, S. Solution structure of the GUCT domain from human RNA helicase II/Guβ reveals the RRM fold, but implausible RNA interactions. [http://dx.doi.org/10.1002/prot.22138 Proteins 74, 133–144 (2009)]

==== 2008 ====

* 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. & Kainosho, M. Structure of the putative 32 kDa myrosinase binding protein from Arabidopsis (At3g16450.1) as determined by the SAIL-NMR method. [http://dx.doi.org/10.1111/j.1742-4658.2008.06717.x FEBS J. 275, 5873–5884 (2008)]

* Yoshida, H., Furuya, N., Lin, Y. J., Güntert, P., Komano, T. & Kainosho, M. Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation. [http://dx.doi.org/10.1016/j.jmb.2008.09.067 J. Mol. Biol. 384, 690–701 (2008)]

* 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://dx.doi.org/10.1110/ps.037580.108 Protein Sci. 17, 2174–2179 (2008)]

* 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. & Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase. [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]

* Nagata, T., Suzuki, S., Endo, R., Shirouzu, M., Terada, T., Inoue, M., Kigawa, T, Güntert, P., Hayashizaki, Y., Muto, Y. & Yokoyama, S. The RRM domain of poly(A)-specific ribonuclease (PARN) has a non-canonical binding site for mRNA cap analog recognition. [http://dx.doi.org/10.1093/nar/gkn458 Nucl. Acids Res. 36, 4754–4767 (2008)]

* Takeda, M., Chang, C. K., Ikeya, T., Güntert, P., Chang, Y. H., Hsu, Y. L., Huang, T. H. & Kainosho, M. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein determined by the SAIL-NMR method. [http://dx.doi.org/10.1016/j.jmb.2007.11.093 J. Mol. Biol. 380, 608–622 (2008)]

* Reckel, S., Sobhanifar, S., Schneider, B., Junge, F., Schwarz, D., Durst, F., Löhr, F., Güntert, P., Bernhard, F. & Dötsch, V. Transmembrane segment enhanced labeling as a tool for the backbone assignment of helical membrane proteins. [http://dx.doi.org/10.1073/pnas.0710843105 Proc. Natl. Acad. Sci. USA 105, 8262–8267 (2008)]

* 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. & 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://dx.doi.org/10.1021/bi7024723 Biochemistry 47, 6437–6450 (2008)]

* Kuwasako, K., Dohmae, N., Inoue, M., Shirouzu, M., Taguchi, S., Güntert, P., Séraphin, B., Muto, Y. & 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://dx.doi.org/10.1002/prot.21839 Proteins 71, 1617–1636 (2008)]

==== 2007 ====

* Ikeya, T., Güntert, P. & 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, Maruzen, Tokyo, pp. 148–166 (2007) (in Japanese)

* Takeda, M., Ikeya, T., Güntert, P. & Kainosho, M. Automated structure determination of proteins with the SAIL-FLYA NMR method. [http://dx.doi.org/10.1038/nprot.2007.423 Nature Protocols 2, 2896–2902 (2007)]

* Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Güntert, P., Kigawa, T. & Yokoyama, S. KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. [http://10.1007/s10858-007-9175-5 J. Biomol. NMR 39, 31–52 (2007)]

* Hwang, E., Ryu, K. S., Pääkkönen, K., Güntert, P., Cheong, H. K., Lim, D. S., Lee, J. O., Jeon, Y. H. & Cheong, C. Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway. [http://dx.doi.org/10.1073/pnas.0610716104 Proc. Natl. Acad. Sci. USA. 104, 9236–9241 (2007)]

* 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. & Yokoyama, S. Solution structure of an atypical WW domain in a novel β-clam-like dimeric form. [http://dx.doi.org/10.1016/j.febslet.2007.01.008 FEBS Lett. 581, 462–468 (2007)]

==== 2006 ====

* Jurt, S., Aemissegger, A., Güntert, P., Zerbe, O. & Hilvert, D. A photoswitchable miniprotein based on the sequence of avian pancreatic polypeptide. [http://dx.doi.org/10.1002/anie.200602084 Angew. Chem. Int. Ed. 45, 6297-6300 (2006)]

* Kuwasako, K., He, F., Inoue, M., Tanaka, A., Sugano, S., Güntert, P., Muto, Y. & Yokoyama, S. Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP. [http://dx.doi.org/10.1016/j.str.2006.09.009 Structure 14, 1677–1689 (2006)]

* López-Méndez, B. & Güntert, P. Automated protein structure determination from NMR spectra. [http://dx.doi.org/10.1021/ja061136l J. Am. Chem. Soc. 128, 13112–13122 (2006)]

* Pääkkönen, K., Tossavainen, H., Permi, P., Rakkolainen, H., Rauvala, H., Raulo, E., Kilpeläinen, I. & Güntert, P. Solution structures of the first and fourth TSR domains of F-spondin. [http://dx.doi.org/10.1002/prot.21030 Proteins 64, 665–672 (2006)]

* Kainosho, M. & 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)

* Scott, A., López-Méndez, B. & Güntert, P. Fully automated structure determinations of the Fes SH2 domain using different sets of NMR spectra. [http://dx.doi.org/10.1002/mrc.1813 Magn. Reson. Chem. 44, S83–S88 (2006)]

* Ikeya, T., Terauchi, T., Güntert, P., Kainosho, M. Evaluation of stereo-array isotope labeling (SAIL) patterns for automated structural analysis of proteins with CYANA. [http://dx.doi.org/10.1002/mrc.1815 Magn. Reson. Chem. 44, S152–S157 (2006)]

* 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. & Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase. [http://dx.doi.org/10.1110/ps.051700406 Protein Sci. 15, 1010–1016 (2006)]

* Aachmann, F. L., Svanem, B. I. G., Güntert, P., Petersen, S. B., Valla, S. & Wimmer, R. NMR structure of the R-module - A parallel β-roll subunit from an ''Azotobacter vinelandii'' mannuronan C-5 epimerase. [http://dx.doi.org/10.1074/jbc.M510069200 J. Biol. Chem. 281, 7350–7356 (2006)]

* Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. & Güntert, P. Optimal isotope labeling for NMR protein structure determinations. [http://dx.doi.org/10.1038/nature04525 Nature 440, 52–57 (2006)]

* Güntert, P. Symbolic NMR product operator calculations. [http://dx.doi.org/10.1002/qua.20754 Int. J. Quant. Chem. 106, 344–350 (2006)]

==== 2005 ====

* 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. & Yokoyama, S. Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold. [http://dx.doi.org/10.1007/s10858-005-7959-z J. Biomol. NMR 32, 329–334 (2005)]

* Lin, Y. J. & 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)

* Iwai, H., Forrer, P., Plückthun, A. & Güntert, P. NMR solution structure of the monomeric form of the bacteriophage λ capsid stabilizing protein gpD. [http://dx.doi.org/10.1007/s10858-005-0945-7 J. Biomol. NMR. 31, 351–356 (2005)]

* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. & Güntert, P. Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes. [http://dx.doi.org/10.1007/s10858-005-0946-6 J. Biomol. NMR. 31, 357–361 (2005)]

* 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. & Bonvin, A. M. J. J. RECOORD: a REcalculated COORdinates Database of 500+ proteins from the PDB using restraints from the BioMagResBank. [http://dx.doi.org/10.1002/prot.20408 Proteins 59, 662–672 (2005)]

* 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. & Yokoyama, S. Solution structure of the PWWP domain of the hepatoma-derived growth factor family. Protein Sci. 14, 756–764 (2005)

* Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. & Wüthrich, K. Prion protein NMR structures of cat, dog, pig and sheep. [http://dx.doi.org/10.1073/pnas.0408937102 Proc. Natl. Acad. Sci. USA 102, 640–645 (2005)]

* Calzolai, L., Lysek, D. A., Pérez, D. R., Güntert, P. & Wüthrich, K. Prion protein NMR structures of chicken, turtle and frog. [http://dx.doi.org/10.1073/pnas.0408939102 Proc. Natl. Acad. Sci. USA 102, 651–655 (2005)]

* Pantoja-Uceda, D., López-Méndez, B., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Seki, M., Shinozaki, K., Yokoyama, S. & Güntert, P. Solution structure of the rhodanese homology domain At4g01050(175–295) from Arabidopsis thaliana. Protein Sci. 14, 224–230 (2005)

==== 2004 ====

* Scott, A., Pantoja-Uceda, D., Koshiba, S., Inoue, M., Kigawa, T., Terada, T., Shirouzu, M., Tanaka, A., Sugano, S., Yokoyama, S. & Güntert, P. NMR assignment of the SH2 domain of the human feline sarcoma oncogene FES. [http://dx.doi.org/10.1007/s10858-004-5432-z J. Biomol. NMR 30, 463–464 (2004)]

* 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. & Yokoyama, S. Solution structure of the RWD domain of the mouse GCN2 protein. Protein Sci. 13, 2089–2100 (2004)

* Güntert, P. Automated NMR structure calculation with CYANA. Meth. Mol. Biol. 278, 353–378 (2004)

* 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. & Güntert, P. NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from ''Arabidopsis thaliana''. J. Biomol. NMR 29, 205–206 (2004)

* 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. & Güntert, P. NMR assignment of the hypothetical rhodanese domain At4g01050 from ''Arabidopsis thaliana.'' [http://dx.doi.org/10.1023/B:JNMR.0000019241.66789.c3 J. Biomol. NMR 29, 207–208 (2004)]

* Fernández, C., Hilty, C., Wider, G., Güntert, P. & Wüthrich, K. NMR structure of the integral membrane protein OmpX. [http://dx.doi.org/10.1016/j.jmb.2003.09.014 J. Mol. Biol. 336, 1211–1221 (2004)]

* Iwai, H., Forrer, P., Plückthun, A. & Güntert, P. Assignments of 1H and 15N resonances of the bacteriophage λ capsid stabilizing protein gpD. [http://dx.doi.org/10.1023/B:JNMR.0000012844.21707.8c J. Biomol. NMR 28, 89–90 (2004)]

==== 2003 ====

* Güntert, P. Automated NMR protein structure calculation. Prog. NMR Spectrosc. 43, 105–125 (2003)

* Vanwetswinkel, S., Kriek, J., Andersen, G. R., Güntert, P., Dijk, P., Canters, G. W. & Siegal, G. Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bγ. J. Biol. Chem. 278, 43443–43451 (2003)

* Jee, J. G. & Güntert, P. Influence of the completeness of chemical shift assignments on NMR structures obtained with automated NOE assignment. J. Struct. Funct. Genom. 4, 179–189 (2003)

* Hilge, M., Siegal, G., Vuister, G. W., Güntert, P., Gloor, S. M. & Abrahams, J. P. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nat. Struct. Biol. 10, 468–474 (2003)

* Lührs, T., Riek, R., Güntert, P. & Wüthrich, K. NMR structure of the human doppel protein. [http://dx.doi.org/10.1016/S0022-2836(02)01471-7 J. Mol. Biol. 326, 1549–1557 (2003)]

* Zahn, R., Güntert, P. & Wüthrich, K. NMR structure of a variant human prion protein with two disulfide bonds. [http://dx.doi.org/10.1016/S0022-2836(02)01332-3 J. Mol. Biol. 326, 225–234 (2003)]

==== 2002 ====

* Herrmann, T., Güntert, P. & Wüthrich, K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. [http://dx.doi.org/10.1023/A:1021614115432 J. Biomol. NMR 24, 171–189 (2002)]

* Güntert, P. Structure calculation using automated techniques. Meth. Principles Med. Chem. 16, 39–66 (2002)

* Enggist, E., Thöny-Meyer, L., Güntert, P. & Pervushin, K. NMR structure of the heme chaperone CcmE reveals a new functional motif. Structure 10, 1551–1557 (2002)

* Lee, D., Damberger, F. D., Peng, G., Horst, R., Güntert, P., Nikonova, L., Leal, W. S. & Wüthrich, K. NMR structure of the unliganded ''Bombyx mori'' pheromone-binding protein at physiological pH. FEBS Lett. 531, 314–318 (2002)

* Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. & Wüthrich, K. NMR Structures of 36 and 73-residue fragments of the calreticulin P-domain. [http://dx.doi.org/10.1016/S0022-2836(02)00812-4 J. Mol. Biol. 322, 773–784 (2002)]

* Herrmann, T., Güntert, P. & Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. [http://dx.doi.org/10.1016/S0022-2836(02)00241-3 J. Mol. Biol. 319, 209–227 (2002)]

* Miura, T., Klaus, W., Ross, A., Güntert, P., Senn, H. The NMR structure of the class I human ubiquitin-conjugating enzyme 2b. [http://dx.doi.org/10.1023/A:1013807519703 J. Biomol. NMR 22, 89–92 (2002)]

==== 2001 ====

* Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. & Wüthrich, K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. [http://dx.doi.org/10.1073/pnas.251532998 Proc. Natl. Acad. Sci. USA 98, 14374–14379 (2001)]

* Riek, R., Güntert, P., Döbeli, H., Wipf, B. & 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)ox and Aβ(1– 42)ox. Eur. J. Biochem. 268, 5930–5936 (2001)

* Güntert, P. & Wüthrich, K. Sampling of conformation space in torsion angle dynamics calculations. Comp. Phys. Commun. 138, 155–169 (2001)

* Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. & Wüthrich, K. NMR structure of the calreticulin P-domain. [http://dx.doi.org/10.1073/pnas.051630098 Proc. Natl. Acad. Sci. USA 98, 3133–3138 (2001)]

==== 2000 ====

* Güntert, P., Salzmann, M., Braun, D. & Wüthrich, K. Sequence-specific NMR assignments of proteins by global fragment mapping with the program MAPPER. [http://dx.doi.org/10.1023/A:1008318805889 J. Biomol. NMR 18, 129–137 (2000)]

* Calzolai, L., Lysek, D. A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. & Wüthrich, K. NMR structures of three single-residue variants of the human prion protein. [http://www.pnas.org/content/97/15/8340.abstract Proc. Natl. Acad. Sci. USA 97, 8340–8345 (2000)]

* Koradi, R., Billeter, M. & Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation. Comp. Phys. Commun. 124, 139–147 (2000)

==== 1999 ====

* Riek, R., Prêcheur, B., Wang, Y., Wider, G., Güntert, P., Liu, A., Kägi, J. H. R. & Wüthrich, K. NMR structure of the sea urchin (''Strongylocentrotus purpuratus'') metallothionein MTA. [http://dx.doi.org/10.1006/jmbi.1999.2967 J. Mol. Biol. 291, 417–428 (1999)]

* 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)]

==== 1998 ====

* Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L. & Wüthrich, K. Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND. [http://dx.doi.org/10.1023/A:1008391403193 J. Biomol. NMR 12, 543–548 (1998)]

* Banci, L., Bertini, I., Cremonini, M. A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. & Güntert, P. PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics. [http://dx.doi.org/10.1023/A:1008388614638 J. Biomol. NMR 12, 553–557 (1998)]

* Koradi, R., Billeter, M., Engeli, M., Güntert, P. & Wüthrich, K. Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY. [http://dx.doi.org/10.1006/jmre.1998.1570 J. Magn. Reson.135, 288-297 (1998)]

* Güntert, P. Structure calculation of biological macromolecules from NMR data. Q. Rev. Biophys. 31, 145–237 (1998)

* Pellecchia, M., Güntert, P., Glockshuber, R. & Wüthrich, K. The NMR solution structure of the periplasmic chaperone FimC. Nature Struct. Biol. 5, 885–890 (1998)

* Pellecchia, M., Güntert, P., Glockshuber, R. & Wüthrich, K. Sequence-specific 1H, 15N and 13C assignments of the periplasmic chaperone FimC from ''Escherichia coli''. [http://dx.doi.org/10.1023/A:1008207111214 J. Biomol. NMR 11, 229–230 (1998)]

==== 1997 ====

* Billeter, M., Güntert, P., Luginbühl, P., Koradi, R. & Wüthrich, K. Biological macromolecules studied by molecular dynamics simulations. Crosscuts 6, 19–21 (1997)

* Mumenthaler, C., Güntert, P., Braun, W. & Wüthrich, K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination. [http://dx.doi.org/10.1023/A:1018383106236 J. Biomol. NMR 10, 351–362 (1997)]

* Güntert, P., Mumenthaler, C. & 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)]

* Ottiger, M., Zerbe, O., Güntert, P. & Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A. [http://dx.doi.org/10.1006/jmbi.1997.1220 J. Mol. Biol. 272, 64–81 (1997)]

* Güntert, P. Calculating protein structures from NMR data. Meth. Mol. Biol. 60, 157–194 (1997)

* Bartels, C., Güntert, P., Billeter, M. & Wüthrich, K. GARANT—A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra. J. Comp. Chem. 18, 139–149 (1997)

==== 1996 ====

* Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. & Wider, G. NMR studies of hydration of biological macromolecules. Faraday Discuss. 103, 245–253 (1996)

* Arbenz, P., Billeter, M., Güntert, P., Luginbühl, P., Taufer, M. & von Matt, U. Molecular dynamics simulations on Cray clusters using the SCIDDLE-PVM environment. Lecture Notes in Computer Science 1156, 142–149 (1996)

* Luginbühl, P., Güntert, P., Billeter, M. & Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. [http://dx.doi.org/10.1007/BF00211160 J. Biomol. NMR 8, 136–146 (1996)]

* Antuch, W., Güntert, P. & Wüthrich, K. Ancestral βγ-crystallin precursor structure in a yeast killer toxin. Nature Struct. Biol. 3, 662–665 (1996)

* Billeter, M., Güntert, P., Luginbühl, P. & Wüthrich, K. Hydration and DNA recognition by homeodomains. Cell 85, 1057–1065 (1996)

* Bartels, C., Billeter, M., Güntert, P. & Wüthrich, K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT. [http://dx.doi.org/10.1007/BF00202037 J. Biomol. NMR 7, 207–213 (1996)]

* Berndt, K. D., Güntert, P. & 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. [http://www3.interscience.wiley.com/journal/69577/abstract Proteins 24, 304–313 (1996)]

==== 1995 ====

* Bartels, C., Güntert, P. & Wüthrich, K. IFLAT—A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals. J. Magn. Reson. A 117, 330–333 (1995)

* Brunne, R. M., Berndt, K. D., Güntert, P., Wüthrich, K. & van Gunsteren, W. F. Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations. [http://dx.doi.org/10.1002/prot.340230107 Proteins 23, 49–62 (1995)]

* Bartels, C., Xia, T., Billeter, M., Güntert, P. & 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)]

==== 1994 ====

* Güntert, P. Computer–supported protein structure determination by NMR. In Statistical mechanics, protein structure and protein–substrate interactions (Ed. S. Doniach), Plenum Press, New York, pp. 197–207 (1994)

* Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. & Wüthrich, K. NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick ''Ornithodoros moubata''. FEBS Lett. 352, 251–257 (1994)

==== 1993 ====

* Wüthrich, K., Güntert, P. & Berndt, K. D. Computer–supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors. In Proceedings of the workshop on innovations on proteases and their inhibitors: fundamental and applied aspects (Ed. F. X. Avilés), de Gruyter, Berlin (1993)

* Berndt, K. D., Güntert, P. & Wüthrich, K. The NMR solution structure of dendrotoxin K from the venom of ''Dendroaspis polylepis polylepis''. [http://dx.doi.org/10.1006/jmbi.1993.1623 J. Mol. Biol. 234, 735–750 (1993)]

* Güntert, P., Berndt, K. D. & Wüthrich, K. The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination. [http://dx.doi.org/10.1007/BF00174613 J. Biomol. NMR 3, 601–606 (1993)]

* Güntert, P., Schaefer, N., Otting, G. & Wüthrich K. POMA, a complete Mathematica implementation of the NMR product operator formalism. J. Magn. Reson. A 101, 103–105 (1993)

* Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. & Wüthrich, K. Protein dynamics studied by rotating frame 15N spin relaxation times. [http://dx.doi.org/10.1007/BF00178259 J. Biomol. NMR 3, 151–164 (1993)]

* Güntert, P. Neue Rechenverfahren für die Proteinstrukturbestimmung mit Hilfe der magnetischen Kernspinresonanz. [http://e-collection.ethbib.ethz.ch/show?type=diss&nr=10135 Ph.D. Thesis ETH 10135 (1993)]

==== 1992 ====

* Szyperski, T., Güntert, P., Stone, S. R. & 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://dx.doi.org/10.1016/0022-2836(92)90325-E J. Mol. Biol. 228, 1193–1205 (1992)]

* Szyperski, T., Güntert, P., Stone, S. R., Tulinsky, A., Bode, W., Huber, R. & 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). [http://dx.doi.org/10.1016/0022-2836(92)90326-F J. Mol. Biol. 228, 1206–1211 (1992)]

* Güntert, P., Dötsch, V., Wider, G. & Wüthrich K. Processing of multi-dimensional NMR data with the new software PROSA. [http://dx.doi.org/10.1007/BF02192850 J. Biomol. NMR 2, 619–629 (1992)]

* Berndt, K. D., Güntert, P., Orbons, L. P. M. & Wüthrich, K. Determination of a high-quality NMR solution structure of the bovine pancreatic trypsin inhibitor (BPTI) and comparison with three crystal structures. [http://dx.doi.org/10.1016/0022-2836(92)90222-6 J. Mol. Biol. 227, 757–775 (1992)]

* Szyperski, T., Güntert, P., Otting, G. & Wüthrich, K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. [http://dx.doi.org/10.1016/0022-2364(92)90209-P J. Magn. Reson. 99, 552– 560 (1992)]

* Güntert, P. & Wüthrich, K. FLATT—A new procedure for high-quality baseline correction of two- and higher-dimensional NMR spectra. [http://dx.doi.org/10.1016/0022-2364(92)90095-O J. Magn. Reson. 96, 403–407 (1992)]

==== 1991 ====

* Mertz, J. E., Güntert, P., Wüthrich, K. & Braun, W. Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities. [http://dx.doi.org/10.1007/BF01875519 J. Biomol. NMR 1, 257–269 (1991)]

* Eccles, C., Güntert, P., Billeter, M. & Wüthrich, K. Efficient analysis of protein 2D NMR spectra using the software package EASY. [http://dx.doi.org/10.1007/BF01877224 J. Biomol. NMR 1, 111–130 (1991)]

* Güntert, P. & Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. [http://dx.doi.org/10.1007/BF02192866 J. Biomol. NMR 1, 447–456 (1991)]

* Güntert, P., Braun, W. & 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. [http://dx.doi.org/10.1016/0022-2836(91)90754-T J. Mol. Biol. 217, 517–530 (1991)]

* Güntert, P., Qian, Y. Q., Otting, G., Müller, M., Gehring, W. J. & 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://dx.doi.org/10.1016/0022-2836(91)90755-U J. Mol. Biol. 217, 531–540 (1991)]

==== 1989 ====

* Güntert, P., Braun, W., Billeter, M. & Wüthrich, K. Automated stereospecific 1H NMR assignments and their impact on the precision of protein structure determinations in solution. [http://dx.doi.org/10.1021/ja00193a036 J. Amer. Chem. Soc. 111, 3997–4004 (1989)]