Publications of M. Kainosho: Difference between revisions

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== All publications ==
== All publications ==


[[#2009|2009]]
[[#2008|2008]]  
[[#2008|2008]]  
[[#2007|2007]]  
[[#2007|2007]]  
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==== In press/accepted ====
==== In press/accepted ====


* 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. Protein Sci.
* 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 ====
==== 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. (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 ====
==== 2008 ====
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==== 2005 ====
==== 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. 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. 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. 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. 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. J. Mol. Biol. 336, 1211–1221 (2004)
* Iwai, H., Forrer, P., Plückthun, A. & Güntert, P. Assignments of <sup>1</sup>H and <sup>15</sup>N 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. 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. 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. 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. 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 phero¬mone binding and release. 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)<sup>ox</sup> and Aβ(1– 42)<sup>ox</sup>. 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. 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. 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. J. Mol. Biol. 291, 417–428 (1999)
* Güntert, P. Megahertz and Gigaflops: NMR protein structure determination and high- performance computing. Speedup 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 <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C 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. J. Mol. Biol. 273, 283–298 (1997)
* Ottiger, M., Zerbe, O., Güntert, P. & Wüthrich, K. The NMR solution conformation of unligated human Cyclophilin A. 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. 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. 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''. 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. 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). 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. 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. 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. 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. 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. J. Mol. Biol. 217, 531–540 (1991)
==== 1989 ====
* Güntert, P., Braun, W., Billeter, M. & Wüthrich, K. Automated stereospecific <sup>1</sup>H NMR assignments and their impact on the precision of protein structure determinations in solution. J. Amer. Chem. Soc. 111, 3997–4004 (1989)

Revision as of 18:31, 16 December 2008

Selected publications

  • Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. & Güntert, P. Optimal isotope labeling for NMR protein structure determinations. Nature 440, 52–57 (2006)


All publications

2008 2007 2006 2005 2004 2003 2002 2001 2000 1999 1998 1997 1996 1995 1994 1993 1992 1991 1989

In press/accepted

2009

2008

  • Takeda, M., Sugimori, N., Torizawa, T., Terauchi, T., Ono, A. M., Yagi, H., Yamaguchi, Y., Kato, K., Ikeya, T., 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. 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. J. Mol. Biol. 384, 690–701 (2008)
  • Ohki, S. & Kainosho, M. Stable Isotope Labeling Methods for Protein NMR Spectroscopy. [http:// Prog. NMR Spectrosc. 53, 208-226 (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. J. Mol. Biol. 380, 608–622 (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)

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)
  • Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M. & Güntert, P. Optimal isotope labeling for NMR protein structure determinations. Nature 440, 52–57 (2006)

2005

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