| Year |
Citation |
Score |
| 2020 |
Lamichhane R, Liu JJ, White KL, Katritch V, Stevens RC, Wüthrich K, Millar DP. Biased Signaling of the G-Protein-Coupled Receptor βAR Is Governed by Conformational Exchange Kinetics. Structure (London, England : 1993). PMID 31978323 DOI: 10.1016/J.Str.2020.01.001 |
0.66 |
|
| 2019 |
Chen S, Lu M, Liu D, Yang L, Yi C, Ma L, Zhang H, Liu Q, Frimurer TM, Wang MW, Schwartz TW, Stevens RC, Wu B, Wüthrich K, Zhao Q. Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography. Nature Communications. 10: 638. PMID 30733446 DOI: 10.1038/S41467-019-08568-5 |
0.441 |
|
| 2018 |
Sušac L, Eddy MT, Didenko T, Stevens RC, Wüthrich K. A adenosine receptor functional states characterized by F-NMR. Proceedings of the National Academy of Sciences of the United States of America. PMID 30463958 DOI: 10.1073/Pnas.1813649115 |
0.48 |
|
| 2018 |
Eddy MT, Gao ZG, Mannes P, Patel N, Jacobson KA, Katritch V, Stevens RC, Wüthrich K. Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor. Journal of the American Chemical Society. PMID 29874058 DOI: 10.1021/Jacs.8B03805 |
0.547 |
|
| 2017 |
Eddy MT, Lee MY, Gao ZG, White KL, Didenko T, Horst R, Audet M, Stanczak P, McClary KM, Han GW, Jacobson KA, Stevens RC, Wüthrich K. Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor. Cell. PMID 29290469 DOI: 10.1016/J.Cell.2017.12.004 |
0.472 |
|
| 2016 |
Eddy MT, Didenko T, Stevens RC, Wüthrich K. β2-Adrenergic Receptor Conformational Response to Fusion Protein in the Third Intracellular Loop. Structure (London, England : 1993). 24: 2190-2197. PMID 27839952 DOI: 10.1016/J.Str.2016.09.015 |
0.503 |
|
| 2015 |
Lamichhane R, Liu JJ, Pljevaljcic G, White KL, van der Schans E, Katritch V, Stevens RC, Wüthrich K, Millar DP. Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β2AR. Proceedings of the National Academy of Sciences of the United States of America. 112: 14254-9. PMID 26578769 DOI: 10.1073/Pnas.1519626112 |
0.664 |
|
| 2015 |
Sušac L, O'Connor C, Stevens RC, Wüthrich K. In-Membrane Chemical Modification (IMCM) for Site-Specific Chromophore Labeling of GPCRs. Angewandte Chemie (International Ed. in English). 54: 15246-9. PMID 26545333 DOI: 10.1002/Anie.201508506 |
0.424 |
|
| 2015 |
O'Connor C, White KL, Doncescu N, Didenko T, Roth BL, Czaplicki G, Stevens RC, Wüthrich K, Milon A. NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor. Proceedings of the National Academy of Sciences of the United States of America. 112: 11852-7. PMID 26372966 DOI: 10.1073/Pnas.1510117112 |
0.469 |
|
| 2015 |
Didenko T, Proudfoot A, Dutta SK, Serrano P, Wüthrich K. Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination. Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 12363-9. PMID 26227870 DOI: 10.1002/chem.201502544 |
0.325 |
|
| 2015 |
Jaudzems K, Pedrini B, Geralt M, Serrano P, Wüthrich K. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4. Journal of Biomolecular Nmr. 61: 65-72. PMID 25428766 DOI: 10.1007/s10858-014-9886-3 |
0.331 |
|
| 2015 |
Dutta SK, Serrano P, Proudfoot A, Geralt M, Pedrini B, Herrmann T, Wüthrich K. APSY-NMR for protein backbone assignment in high-throughput structural biology. Journal of Biomolecular Nmr. 61: 47-53. PMID 25428764 DOI: 10.1007/s10858-014-9881-8 |
0.358 |
|
| 2014 |
Sušac L, Horst R, Wüthrich K. Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles. Chembiochem : a European Journal of Chemical Biology. 15: 995-1000. PMID 24692152 DOI: 10.1002/cbic.201300729 |
0.326 |
|
| 2013 |
Damberger FF, Michel E, Ishida Y, Leal WS, Wüthrich K. Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein. Proceedings of the National Academy of Sciences of the United States of America. 110: 18680-5. PMID 24158483 DOI: 10.1073/Pnas.1317706110 |
0.633 |
|
| 2013 |
Horst R, Liu JJ, Stevens RC, Wüthrich K. β₂-adrenergic receptor activation by agonists studied with ¹⁹F NMR spectroscopy. Angewandte Chemie (International Ed. in English). 52: 10762-5. PMID 23956158 DOI: 10.1002/Anie.201305286 |
0.695 |
|
| 2013 |
Didenko T, Liu JJ, Horst R, Stevens RC, Wüthrich K. Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs. Current Opinion in Structural Biology. 23: 740-747. PMID 23932201 DOI: 10.1016/J.Sbi.2013.07.011 |
0.697 |
|
| 2013 |
Pedrini B, Serrano P, Mohanty B, Geralt M, Wüthrich K. NMR-profiles of protein solutions. Biopolymers. 99: 825-31. PMID 23839514 DOI: 10.1002/bip.22348 |
0.373 |
|
| 2013 |
Christen B, Damberger FF, Pérez DR, Hornemann S, Wüthrich K. Structural plasticity of the cellular prion protein and implications in health and disease. Proceedings of the National Academy of Sciences of the United States of America. 110: 8549-54. PMID 23650394 DOI: 10.1073/Pnas.1306178110 |
0.652 |
|
| 2013 |
Stevens RC, Cherezov V, Katritch V, Abagyan R, Kuhn P, Rosen H, Wüthrich K. The GPCR Network: a large-scale collaboration to determine human GPCR structure and function. Nature Reviews. Drug Discovery. 12: 25-34. PMID 23237917 DOI: 10.1038/Nrd3859 |
0.434 |
|
| 2013 |
Horst R, Stanczak P, Stevens RC, Wüthrich K. β2-Adrenergic receptor solutions for structural biology analyzed with microscale NMR diffusion measurements. Angewandte Chemie (International Ed. in English). 52: 331-5. PMID 23097212 DOI: 10.1002/Anie.201205474 |
0.43 |
|
| 2012 |
Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371 |
0.664 |
|
| 2012 |
Rance M, Sørensen OW, Bodenhausen G, Wagner G, Ernst RR, Wüthrich K. Improved spectral resolution in COSY (1)H NMR spectra of proteins via double quantum filtering. 1983. Biochemical and Biophysical Research Communications. 425: 527-33. PMID 22925669 DOI: 10.1016/j.bbrc.2012.08.019 |
0.723 |
|
| 2012 |
Christen B, Hornemann S, Damberger FF, Wüthrich K. Prion protein mPrP[F175A](121-231): structure and stability in solution. Journal of Molecular Biology. 423: 496-502. PMID 22922482 DOI: 10.1016/J.Jmb.2012.08.011 |
0.679 |
|
| 2012 |
Bartels C, Billeter M, Güntert P, Wüthrich K. Automated sequence-specific NMR assignment of homologous proteins using the program GARANT. Journal of Biomolecular Nmr. 7: 207-13. PMID 22911044 DOI: 10.1007/BF00202037 |
0.383 |
|
| 2012 |
Zerbe O, Szyperski T, Ottiger M, Wüthrich K. Three-dimensional (1)H-TOCSY-relayed ct-[(13)C, (1)H]-HMQC for aromatic spin system identification in uniformly (13)C-labeled proteins. Journal of Biomolecular Nmr. 7: 99-106. PMID 22911006 DOI: 10.1007/Bf00203820 |
0.548 |
|
| 2012 |
Stanczak P, Zhang Q, Horst R, Serrano P, Wüthrich K. Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles. Journal of Biomolecular Nmr. 54: 129-33. PMID 22890565 DOI: 10.1007/S10858-012-9658-X |
0.322 |
|
| 2012 |
Serrano P, Pedrini B, Mohanty B, Geralt M, Herrmann T, Wüthrich K. The J-UNIO protocol for automated protein structure determination by NMR in solution. Journal of Biomolecular Nmr. 53: 341-54. PMID 22752932 DOI: 10.1007/s10858-012-9645-2 |
0.365 |
|
| 2012 |
Liu JJ, Horst R, Katritch V, Stevens RC, Wüthrich K. Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR. Science (New York, N.Y.). 335: 1106-10. PMID 22267580 DOI: 10.1126/Science.1215802 |
0.681 |
|
| 2011 |
Damberger FF, Christen B, Pérez DR, Hornemann S, Wüthrich K. Cellular prion protein conformation and function. Proceedings of the National Academy of Sciences of the United States of America. 108: 17308-13. PMID 21987789 DOI: 10.1073/Pnas.1106325108 |
0.686 |
|
| 2011 |
Koculi E, Horst R, Horwich AL, Wüthrich K. Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL. Protein Science : a Publication of the Protein Society. 20: 1380-6. PMID 21633984 DOI: 10.1002/Pro.665 |
0.324 |
|
| 2011 |
Michel E, Damberger FF, Ishida Y, Fiorito F, Lee D, Leal WS, Wüthrich K. Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein. Journal of Molecular Biology. 408: 922-31. PMID 21396939 DOI: 10.1016/J.Jmb.2011.03.008 |
0.682 |
|
| 2011 |
Choutko A, Glättli A, Fernández C, Hilty C, Wüthrich K, van Gunsteren WF. Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle. European Biophysics Journal : Ebj. 40: 39-58. PMID 20922370 DOI: 10.1007/S00249-010-0626-7 |
0.588 |
|
| 2010 |
Vila JA, Serrano P, Wüthrich K, Scheraga HA. Sequential nearest-neighbor effects on computed 13Calpha chemical shifts. Journal of Biomolecular Nmr. 48: 23-30. PMID 20644980 DOI: 10.1007/S10858-010-9435-7 |
0.468 |
|
| 2010 |
Pérez DR, Damberger FF, Wüthrich K. Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. Journal of Molecular Biology. 400: 121-8. PMID 20460128 DOI: 10.1016/J.Jmb.2010.04.066 |
0.684 |
|
| 2010 |
De Groot CO, Jelesarov I, Damberger FF, Bjelić S, Schärer MA, Bhavesh NS, Grigoriev I, Buey RM, Wüthrich K, Capitani G, Akhmanova A, Steinmetz MO. Molecular insights into mammalian end-binding protein heterodimerization. The Journal of Biological Chemistry. 285: 5802-14. PMID 20008324 DOI: 10.1074/Jbc.M109.068130 |
0.666 |
|
| 2009 |
Stanczak P, Horst R, Serrano P, Wüthrich K. NMR characterization of membrane protein-detergent micelle solutions by use of microcoil equipment. Journal of the American Chemical Society. 131: 18450-6. PMID 19950959 DOI: 10.1021/ja907842u |
0.302 |
|
| 2009 |
Serrano P, Johnson MA, Chatterjee A, Neuman BW, Joseph JS, Buchmeier MJ, Kuhn P, Wüthrich K. Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3. Journal of Virology. 83: 12998-3008. PMID 19828617 DOI: 10.1128/Jvi.01253-09 |
0.317 |
|
| 2009 |
Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. An EB1-binding motif acts as a microtubule tip localization signal. Cell. 138: 366-76. PMID 19632184 DOI: 10.1016/J.Cell.2009.04.065 |
0.625 |
|
| 2009 |
Hornemann S, von Schroetter C, Damberger FF, Wüthrich K. Prion protein-detergent micelle interactions studied by NMR in solution. The Journal of Biological Chemistry. 284: 22713-21. PMID 19546219 DOI: 10.1074/Jbc.M109.000430 |
0.676 |
|
| 2009 |
Christen B, Hornemann S, Damberger FF, Wüthrich K. Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects. Journal of Molecular Biology. 389: 833-45. PMID 19393664 DOI: 10.1016/J.Jmb.2009.04.040 |
0.66 |
|
| 2008 |
Serrano P, Johnson MA, Chatterjee A, Pedrini B, Wüthrich K. NMR assignment of the nonstructural protein nsp3(1066-1181) from SARS-CoV. Biomolecular Nmr Assignments. 2: 135-8. PMID 19636888 DOI: 10.1007/s12104-008-9104-x |
0.394 |
|
| 2008 |
Hiller S, Wider G, Wüthrich K. APSY-NMR with proteins: practical aspects and backbone assignment. Journal of Biomolecular Nmr. 42: 179-95. PMID 18841481 DOI: 10.1007/s10858-008-9266-y |
0.311 |
|
| 2008 |
Billeter M, Wagner G, Wüthrich K. Solution NMR structure determination of proteins revisited. Journal of Biomolecular Nmr. 42: 155-8. PMID 18827972 DOI: 10.1007/s10858-008-9277-8 |
0.589 |
|
| 2008 |
Fiorito F, Herrmann T, Damberger FF, Wüthrich K. Automated amino acid side-chain NMR assignment of proteins using (13)C- and (15)N-resolved 3D [ (1)H, (1)H]-NOESY. Journal of Biomolecular Nmr. 42: 23-33. PMID 18709333 DOI: 10.1007/S10858-008-9259-X |
0.722 |
|
| 2008 |
Zhang Q, Horst R, Geralt M, Ma X, Hong WX, Finn MG, Stevens RC, Wüthrich K. Microscale NMR screening of new detergents for membrane protein structural biology. Journal of the American Chemical Society. 130: 7357-63. PMID 18479092 DOI: 10.1021/Ja077863D |
0.507 |
|
| 2008 |
Neuman BW, Joseph JS, Saikatendu KS, Serrano P, Chatterjee A, Johnson MA, Liao L, Klaus JP, Yates JR, Wüthrich K, Stevens RC, Buchmeier MJ, Kuhn P. Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3. Journal of Virology. 82: 5279-94. PMID 18367524 DOI: 10.1128/Jvi.02631-07 |
0.43 |
|
| 2007 |
Chatterjee A, Johnson MA, Serrano P, Pedrini B, Wüthrich K. NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3. Biomolecular Nmr Assignments. 1: 191-4. PMID 19636862 DOI: 10.1007/s12104-007-9052-x |
0.366 |
|
| 2007 |
Johnson MA, Southworth MW, Perler FB, Wüthrich K. NMR assignment of a KlbA intein precursor from Methanococcus jannaschii. Biomolecular Nmr Assignments. 1: 19-21. PMID 19636816 DOI: 10.1007/s12104-007-9009-0 |
0.33 |
|
| 2007 |
Damberger FF, Ishida Y, Leal WS, Wüthrich K. Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5. Journal of Molecular Biology. 373: 811-9. PMID 17884092 DOI: 10.1016/J.Jmb.2007.07.078 |
0.694 |
|
| 2007 |
Serrano P, Johnson MA, Almeida MS, Horst R, Herrmann T, Joseph JS, Neuman BW, Subramanian V, Saikatendu KS, Buchmeier MJ, Stevens RC, Kuhn P, Wüthrich K. Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus. Journal of Virology. 81: 12049-60. PMID 17728234 DOI: 10.1128/Jvi.00969-07 |
0.517 |
|
| 2007 |
Placzek WJ, Etezady-Esfarjani T, Herrmann T, Pedrini B, Peti W, Alimenti C, Luporini P, Wüthrich K. Cold-adapted signal proteins: NMR structures of pheromones from the Antarctic ciliate Euplotes nobilii. Iubmb Life. 59: 578-85. PMID 17701553 DOI: 10.1080/15216540701258165 |
0.601 |
|
| 2007 |
Hiller S, Wasmer C, Wider G, Wüthrich K. Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy. Journal of the American Chemical Society. 129: 10823-8. PMID 17691781 DOI: 10.1021/ja072564+ |
0.371 |
|
| 2006 |
Horst R, Wider G, Fiaux J, Bertelsen EB, Horwich AL, Wüthrich K. Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures. Proceedings of the National Academy of Sciences of the United States of America. 103: 15445-50. PMID 17032756 DOI: 10.1073/Pnas.0607141103 |
0.305 |
|
| 2006 |
Almeida MS, Johnson MA, Wüthrich K. NMR assignment of the SARS-CoV protein nsp1. Journal of Biomolecular Nmr. 36: 46. PMID 16821128 DOI: 10.1007/s10858-006-9018-9 |
0.315 |
|
| 2006 |
Serrano P, Almeida MS, Johnson MA, Wüthrich K. NMR assignment of the protein nsp3a from SARS-CoV. Journal of Biomolecular Nmr. 36: 45. PMID 16799860 DOI: 10.1007/s10858-006-9017-x |
0.318 |
|
| 2006 |
Fiorito F, Hiller S, Wider G, Wüthrich K. Automated resonance assignment of proteins: 6D APSY-NMR. Journal of Biomolecular Nmr. 35: 27-37. PMID 16791738 DOI: 10.1007/s10858-006-0030-x |
0.318 |
|
| 2006 |
Johnson MA, Peti W, Herrmann T, Wilson IA, Wüthrich K. Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence. Protein Science : a Publication of the Protein Society. 15: 1030-41. PMID 16597827 DOI: 10.1110/Ps.051964606 |
0.589 |
|
| 2006 |
Etezady-Esfarjani T, Herrmann T, Horst R, Wüthrich K. Automated protein NMR structure determination in crude cell-extract. Journal of Biomolecular Nmr. 34: 3-11. PMID 16505959 DOI: 10.1007/s10858-005-4519-5 |
0.319 |
|
| 2006 |
Baker KA, Hilty C, Peti W, Prince A, Pfaffinger PJ, Wider G, Wüthrich K, Choe S. NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain. Biochemistry. 45: 1663-72. PMID 16460013 DOI: 10.1021/Bi0516430 |
0.713 |
|
| 2006 |
Lee D, Hilty C, Wider G, Wüthrich K. Effective rotational correlation times of proteins from NMR relaxation interference. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 178: 72-6. PMID 16188473 DOI: 10.1016/J.Jmr.2005.08.014 |
0.658 |
|
| 2005 |
Peti W, Page R, Moy K, O'Neil-Johnson M, Wilson IA, Stevens RC, Wüthrich K. Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR. Journal of Structural and Functional Genomics. 6: 259-67. PMID 16283429 DOI: 10.1007/S10969-005-9000-X |
0.696 |
|
| 2005 |
Almeida MS, Herrmann T, Peti W, Wilson IA, Wüthrich K. NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins. Protein Science : a Publication of the Protein Society. 14: 2880-6. PMID 16199668 DOI: 10.1110/Ps.051755805 |
0.561 |
|
| 2005 |
Peti W, Johnson MA, Herrmann T, Neuman BW, Buchmeier MJ, Nelson M, Joseph J, Page R, Stevens RC, Kuhn P, Wüthrich K. Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7. Journal of Virology. 79: 12905-13. PMID 16188992 DOI: 10.1128/Jvi.79.20.12905-12913.2005 |
0.63 |
|
| 2005 |
Fadel V, Bettendorff P, Herrmann T, de Azevedo WF, Oliveira EB, Yamane T, Wüthrich K. Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus. Toxicon : Official Journal of the International Society On Toxinology. 46: 759-67. PMID 16185738 DOI: 10.1016/j.toxicon.2005.07.018 |
0.332 |
|
| 2005 |
Columbus L, Peti W, Etezady-Esfarjani T, Herrmann T, Wüthrich K. NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima. Proteins. 60: 552-7. PMID 15937903 DOI: 10.1002/Prot.20465 |
0.73 |
|
| 2005 |
Pérez DR, Wüthrich K. NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226) [3] Journal of Biomolecular Nmr. 31: 260. PMID 15803401 DOI: 10.1007/s10858-004-7914-4 |
0.325 |
|
| 2005 |
Peti W, Herrmann T, Zagnitko O, Grzechnik SK, Wüthrich K. NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima Proteins: Structure, Function and Genetics. 59: 387-390. PMID 15723348 DOI: 10.1002/Prot.20352 |
0.623 |
|
| 2005 |
Michel E, Damberger FF, Chen AM, Ishida Y, Leal WS, Wüthrich K. Assignments for the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5 [1] Journal of Biomolecular Nmr. 31: 65. PMID 15692741 DOI: 10.1007/S10858-004-5981-1 |
0.635 |
|
| 2005 |
Page R, Peti W, Wilson IA, Stevens RC, Wüthrich K. NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline. Proceedings of the National Academy of Sciences of the United States of America. 102: 1901-5. PMID 15677718 DOI: 10.1073/Pnas.0408490102 |
0.67 |
|
| 2005 |
Gossert AD, Bonjour S, Lysek DA, Fiorito F, Wüthrich K. Prion protein NMR structures of elk and of mouse/elk hybrids. Proceedings of the National Academy of Sciences of the United States of America. 102: 646-50. PMID 15647363 DOI: 10.1073/pnas.0409008102 |
0.303 |
|
| 2005 |
Wüthrich K. NMR - this other method for protein and nucleic acid structure determination. Acta Crystallographica. Section D, Biological Crystallography. 51: 249-70. PMID 15299291 DOI: 10.1107/S0907444994010188 |
0.335 |
|
| 2004 |
Calzolai L, Lysek DA, Wüthrich K. NMR assignment of the turtle prion protein fragment tPrP(121-225) Journal of Biomolecular Nmr. 30: 97. PMID 15543686 |
0.325 |
|
| 2004 |
Lysek DA, Calzolai L, Wüthrich K. NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242) Journal of Biomolecular Nmr. 30: 97. PMID 15459548 DOI: 10.1023/b:jnmr.0000043504.61065.f4 |
0.325 |
|
| 2004 |
Kelker MS, Foss TR, Peti W, Teyton L, Kelly JW, Wüthrich K, Wilson IA. Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 A. Journal of Molecular Biology. 342: 1237-48. PMID 15351648 DOI: 10.1016/j.jmb.2004.07.089 |
0.513 |
|
| 2004 |
Peti W, Etezady-Esfarjani T, Herrmann T, Klock HE, Lesley SA, Wüthrich K. NMR for structural proteomics of Thermotoga maritima: Screening and structure determination Journal of Structural and Functional Genomics. 5: 205-215. PMID 15263836 DOI: 10.1023/B:Jsfg.0000029055.84242.9F |
0.617 |
|
| 2004 |
Almeida MS, Peti W, Wüthrich K. Letter to the editor: 1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima [29] Journal of Biomolecular Nmr. 29: 453-454. PMID 15213465 DOI: 10.1023/B:Jnmr.0000032522.43753.F1 |
0.604 |
|
| 2004 |
Etezady-Esfarjani T, Herrmann T, Peti W, Klock HE, Lesley SA, Wüthrich K. Letter to the editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis [5] Journal of Biomolecular Nmr. 29: 403-406. PMID 15213441 DOI: 10.1023/B:Jnmr.0000032615.51536.1A |
0.562 |
|
| 2004 |
Hilty C, Wider G, Fernández C, Wüthrich K. Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents. Chembiochem : a European Journal of Chemical Biology. 5: 467-73. PMID 15185370 DOI: 10.1002/Cbic.200300815 |
0.64 |
|
| 2004 |
Fernández C, Hilty C, Wider G, Güntert P, Wüthrich K. NMR structure of the integral membrane protein OmpX. Journal of Molecular Biology. 336: 1211-21. PMID 15037080 DOI: 10.1016/J.Jmb.2003.09.014 |
0.619 |
|
| 2004 |
Tafer H, Hiller S, Hilty C, Fernández C, Wüthrich K. Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX). Biochemistry. 43: 860-9. PMID 14744128 DOI: 10.1021/Bi0356606 |
0.682 |
|
| 2003 |
Braun D, Wüthrich K, Wider G. Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 165: 89-94. PMID 14568519 DOI: 10.1016/S1090-7807(03)00273-8 |
0.371 |
|
| 2003 |
Hilty C, Wider G, Fernández C, Wüthrich K. Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles. Journal of Biomolecular Nmr. 27: 377-82. PMID 14512734 DOI: 10.1023/A:1025877326533 |
0.638 |
|
| 2003 |
Etezady-Esfarjani T, Peti W, Wüthrich K. NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima [6] Journal of Biomolecular Nmr. 25: 167-168. PMID 12652129 DOI: 10.1023/A:1022215901456 |
0.625 |
|
| 2003 |
Lührs T, Riek R, Güntert P, Wüthrich K. NMR structure of the human doppel protein. Journal of Molecular Biology. 326: 1549-57. PMID 12595265 DOI: 10.1016/S0022-2836(02)01471-7 |
0.516 |
|
| 2003 |
Fiaux J, Cakar ZP, Sonderegger M, Wüthrich K, Szyperski T, Sauer U. Metabolic-flux profiling of the yeasts Saccharomyces cerevisiae and Pichia stipitis. Eukaryotic Cell. 2: 170-80. PMID 12582134 DOI: 10.1128/Ec.2.1.170-180.2003 |
0.43 |
|
| 2003 |
Zahn R, Güntert P, von Schroetter C, Wüthrich K. NMR structure of a variant human prion protein with two disulfide bridges. Journal of Molecular Biology. 326: 225-34. PMID 12547204 DOI: 10.1016/S0022-2836(02)01332-3 |
0.303 |
|
| 2002 |
Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. Journal of Biomolecular Nmr. 24: 171-89. PMID 12522306 DOI: 10.1023/A:1021614115432 |
0.358 |
|
| 2002 |
Lee D, Damberger FF, Peng G, Horst R, Güntert P, Nikonova L, Leal WS, Wüthrich K. NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. Febs Letters. 531: 314-8. PMID 12417333 DOI: 10.1016/S0014-5793(02)03548-2 |
0.683 |
|
| 2002 |
Hilty C, Fernández C, Wider G, Wüthrich K. Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles. Journal of Biomolecular Nmr. 23: 289-301. PMID 12398349 DOI: 10.1023/A:1020218419190 |
0.657 |
|
| 2002 |
Riek R, Fiaux J, Bertelsen EB, Horwich AL, Wuthrich K. Solution NMR techniques for large molecular and supramolecular structures. Journal of the American Chemical Society. 124: 12144-53. PMID 12371854 DOI: 10.1021/Ja026763Z |
0.55 |
|
| 2002 |
Fernández C, Hilty C, Wider G, Wüthrich K. Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 99: 13533-7. PMID 12370417 DOI: 10.1073/Pnas.212515099 |
0.64 |
|
| 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. Journal of Molecular Biology. 319: 209-27. PMID 12051947 DOI: 10.1016/S0022-2836(02)00241-3 |
0.321 |
|
| 2002 |
Dauner M, Sonderegger M, Hochuli M, Szyperski T, Wüthrich K, Hohmann HP, Sauer U, Bailey JE. Intracellular carbon fluxes in riboflavin-producing Bacillus subtilis during growth on two-carbon substrate mixtures. Applied and Environmental Microbiology. 68: 1760-71. PMID 11916694 DOI: 10.1128/Aem.68.4.1760-1771.2002 |
0.469 |
|
| 2002 |
Di Giuseppe G, Miceli C, Zahn R, Damberger F, Wüthrich K, Luporini P. A structurally deviant member of the Euplotes raikovi pheromone family: Er-23 Journal of Eukaryotic Microbiology. 49: 86-92. PMID 11908903 DOI: 10.1111/J.1550-7408.2002.Tb00347.X |
0.649 |
|
| 2002 |
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proceedings of the National Academy of Sciences of the United States of America. 99: 1954-9. PMID 11842220 DOI: 10.1073/Pnas.042699099 |
0.546 |
|
| 2002 |
Emmerling M, Dauner M, Ponti A, Fiaux J, Hochuli M, Szyperski T, Wüthrich K, Bailey JE, Sauer U. Metabolic flux responses to pyruvate kinase knockout in Escherichia coli. Journal of Bacteriology. 184: 152-64. PMID 11741855 DOI: 10.1128/Jb.184.1.152-164.2002 |
0.466 |
|
| 2002 |
Etezady-Esfarjani T, Hilty C, Wüthrich K, Rueping M, Schreiber J, Seebach D. NMR-structural investigations of a β3-dodecapeptide with proteinogenic side chains in methanol and in aqueous solutions Helvetica Chimica Acta. 85: 1197-1209. DOI: 10.1002/1522-2675(200205)85:5<1197::Aid-Hlca1197>3.0.Co;2-E |
0.569 |
|
| 2001 |
Horst R, Damberger F, Luginbühl P, Güntert P, Peng G, Nikonova L, Leal WS, Wüthrich K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proceedings of the National Academy of Sciences of the United States of America. 98: 14374-9. PMID 11724947 DOI: 10.1073/Pnas.251532998 |
0.657 |
|
| 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, A beta(1-40)(ox) and A beta(1-42)(ox). European Journal of Biochemistry / Febs. 268: 5930-6. PMID 11722581 DOI: 10.1046/J.0014-2956.2001.02537.X |
0.469 |
|
| 2001 |
Zahn R, Damberger F, Ortenzi C, Luporini P, Wüthrich K. NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds. Journal of Molecular Biology. 313: 923-31. PMID 11700049 DOI: 10.1006/Jmbi.2001.5099 |
0.685 |
|
| 2001 |
Wüthrich K. The way to NMR structures of proteins. Nature Structural Biology. 8: 923-5. PMID 11685234 DOI: 10.1038/nsb1101-923 |
0.325 |
|
| 2001 |
Fernández C, Hilty C, Bonjour S, Adeishvili K, Pervushin K, Wüthrich K. Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli. Febs Letters. 504: 173-8. PMID 11532450 DOI: 10.1016/S0014-5793(01)02742-9 |
0.651 |
|
| 2001 |
Riek R, Pervushin K, Fernández C, Kainosho M, Wüthrich K. [(13)C,(13)C]- and [(13)C,(1)H]-TROSY in a triple resonance experiment for ribose-base and intrabase correlations in nucleic acids. Journal of the American Chemical Society. 123: 658-64. PMID 11456577 DOI: 10.1021/Ja9938276 |
0.533 |
|
| 2001 |
Wüthrich K, Riek R. Three-dimensional structures of prion proteins. Advances in Protein Chemistry. 57: 55-82. PMID 11447697 DOI: 10.1016/S0065-3233(01)57018-7 |
0.533 |
|
| 2001 |
Ellgaard L, Riek R, Herrmann T, Güntert P, Braun D, Helenius A, Wüthrich K. NMR structure of the calreticulin P-domain. Proceedings of the National Academy of Sciences of the United States of America. 98: 3133-8. PMID 11248044 DOI: 10.1073/Pnas.051630098 |
0.519 |
|
| 2001 |
Horst R, Damberger F, Peng G, Nikonova L, Leal WS, Wüthrich K. NMR assignment of the A form of the pheromone-binding protein of Bombyx mori [2] Journal of Biomolecular Nmr. 19: 79-80. PMID 11246858 DOI: 10.1023/A:1008394615895 |
0.682 |
|
| 2001 |
Fernández C, Adeishvili K, Wüthrich K. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proceedings of the National Academy of Sciences of the United States of America. 98: 2358-63. PMID 11226244 DOI: 10.1073/pnas.051629298 |
0.396 |
|
| 2001 |
Ellgaard L, Riek R, Braun D, Herrmann T, Helenius A, Wüthrich K. Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. Febs Letters. 488: 69-73. PMID 11163798 DOI: 10.1016/S0014-5793(00)02382-6 |
0.544 |
|
| 2001 |
Frey AD, Fiaux J, Szyperski T, Wüthrich K, Bailey JE, Kallio PT. Dissection of central carbon metabolism of hemoglobin-expressing Escherichia coli by 13C nuclear magnetic resonance flux distribution analysis in microaerobic bioprocesses. Applied and Environmental Microbiology. 67: 680-7. PMID 11157231 DOI: 10.1128/Aem.67.2.680-687.2001 |
0.516 |
|
| 2001 |
Wüthrich K, Bax A, Billeter M, Kaptein R, Palmer AG, Sykes BD, Wagner G. Letter from the Editor-in-Chief Journal of Biomolecular Nmr. 19: 1. DOI: 10.1023/A:1008382926453 |
0.322 |
|
| 2000 |
Riek R, Pervushin K, Wüthrich K. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends in Biochemical Sciences. 25: 462-8. PMID 11050425 DOI: 10.1016/S0968-0004(00)01665-0 |
0.575 |
|
| 2000 |
Hochuli M, Szyperski T, Wüthrich K. Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D2O-containing minimal medium. Journal of Biomolecular Nmr. 17: 33-42. PMID 10909864 DOI: 10.1023/A:1008329124672 |
0.493 |
|
| 2000 |
Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K. NMR structures of three single-residue variants of the human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 8340-5. PMID 10900000 DOI: 10.1073/Pnas.97.15.8340 |
0.578 |
|
| 2000 |
López Garcia F, Zahn R, Riek R, Wüthrich K. NMR structure of the bovine prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 8334-9. PMID 10899999 DOI: 10.1073/Pnas.97.15.8334 |
0.563 |
|
| 2000 |
Damberger F, Nikonova L, Horst R, Peng G, Leal WS, Wüthrich K. NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori. Protein Science : a Publication of the Protein Society. 9: 1038-41. PMID 10850815 DOI: 10.1110/Ps.9.5.1038 |
0.666 |
|
| 2000 |
Liu A, Riek R, Wider G, von Schroetter C, Zahn R, Wüthrich K. NMR experiments for resonance assignments of 13C, 15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230). Journal of Biomolecular Nmr. 16: 127-38. PMID 10723992 DOI: 10.1023/A:1008305022907 |
0.575 |
|
| 2000 |
Pervushin K, Fernández C, Riek R, Ono A, Kainosho M, Wüthrich K. Determination of h2J(NN) and h1J(HN) coupling constants across Watson-Crick base pairs in the Antennapedia homeodomain-DNA complex using TROSY. Journal of Biomolecular Nmr. 16: 39-46. PMID 10718611 DOI: 10.1023/A:1008367405025 |
0.51 |
|
| 2000 |
García FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wüthrich K. NMR structure of the sterol carrier protein-2: implications for the biological role. Journal of Molecular Biology. 295: 595-603. PMID 10623549 DOI: 10.1006/Jmbi.1999.3355 |
0.573 |
|
| 2000 |
Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. NMR solution structure of the human prion protein. Proceedings of the National Academy of Sciences of the United States of America. 97: 145-50. PMID 10618385 DOI: 10.1073/Pnas.97.1.145 |
0.565 |
|
| 2000 |
Salzmann M, Pervushin K, Wider G, Senn H, Wüthrich K. NMR assignment and secondary structure determination of an octameric 110 kDA protein using TROSY in triple resonance experiments Journal of the American Chemical Society. 122: 7543-7548. DOI: 10.1021/ja0003268 |
0.36 |
|
| 1999 |
Szyperski T, Glaser RW, Hochuli M, Fiaux J, Sauer U, Bailey JE, Wüthrich K. Bioreaction network topology and metabolic flux ratio analysis by biosynthetic fractional 13C labeling and two-dimensional NMR spectroscopy. Metabolic Engineering. 1: 189-97. PMID 10937933 DOI: 10.1006/Mben.1999.0116 |
0.499 |
|
| 1999 |
Sauer U, Lasko DR, Fiaux J, Hochuli M, Glaser R, Szyperski T, Wüthrich K, Bailey JE. Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism. Journal of Bacteriology. 181: 6679-88. PMID 10542169 DOI: 10.1128/Jb.181.21.6679-6688.1999 |
0.45 |
|
| 1999 |
Szyperski T, Fernández C, Ono A, Wüthrich K, Kainosho M. The 2D [31P] spin-echo-difference constant-time [13C, 1H]-HMQC experiment for simultaneous determination of 3J(H3'P) and 3J(C4'P) in 13C-labeled nucleic acids and their protein complexes. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 140: 491-4. PMID 10497056 DOI: 10.1006/Jmre.1999.1870 |
0.537 |
|
| 1999 |
Fernández C, Szyperski T, Billeter M, Ono A, Iwai H, Kainosho M, Wüthrich K. Conformational changes of the BS2 operator DNA upon complex formation with the Antennapedia homeodomain studied by NMR with 13C/15N-labeled DNA. Journal of Molecular Biology. 292: 609-17. PMID 10497025 DOI: 10.1006/Jmbi.1999.2987 |
0.535 |
|
| 1999 |
Pervushin KV, Wider G, Riek R, Wüthrich K. The 3D NOESY-[(1)H,(15)N,(1)H]-ZQ-TROSY NMR experiment with diagonal peak suppression. Proceedings of the National Academy of Sciences of the United States of America. 96: 9607-12. PMID 10449740 DOI: 10.1073/Pnas.96.17.9607 |
0.538 |
|
| 1999 |
Riek R, Prêcheur B, Wang Y, Mackay EA, Wider G, Güntert P, Liu A, Kägi JH, Wüthrich K. NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA. Journal of Molecular Biology. 291: 417-28. PMID 10438629 DOI: 10.1006/Jmbi.1999.2967 |
0.524 |
|
| 1999 |
Wimmer R, Herrmann T, Solioz M, Wüthrich K. NMR structure and metal interactions of the CopZ copper chaperone. The Journal of Biological Chemistry. 274: 22597-603. PMID 10428839 DOI: 10.1074/Jbc.274.32.22597 |
0.666 |
|
| 1999 |
Liu A, Riek R, Zahn R, Hornemann S, Glockshuber R, Wüthrich K. Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy. Biopolymers. 51: 145-52. PMID 10397798 DOI: 10.1002/(Sici)1097-0282(1999)51:2<145::Aid-Bip4>3.0.Co;2-4 |
0.573 |
|
| 1999 |
Szyperski T, Götte M, Billeter M, Perola E, Cellai L, Heumann H, Wüthrich K. NMR structure of the chimeric hybrid duplex r(gcaguggc).r(gcca)d(CTGC) comprising the tRNA-DNA junction formed during initiation of HIV-1 reverse transcription. Journal of Biomolecular Nmr. 13: 343-55. PMID 10353196 DOI: 10.1023/A:1008350604637 |
0.502 |
|
| 1999 |
Hochuli M, Patzelt H, Oesterhelt D, Wüthrich K, Szyperski T. Amino acid biosynthesis in the halophilic archaeon haloarcula hispanica Journal of Bacteriology. 181: 3226-3237. PMID 10322026 DOI: 10.1128/Jb.181.10.3226-3237.1999 |
0.483 |
|
| 1999 |
Riek R, Wider G, Pervushin K, Wüthrich K. Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proceedings of the National Academy of Sciences of the United States of America. 96: 4918-23. PMID 10220394 DOI: 10.1073/pnas.96.9.4918 |
0.556 |
|
| 1999 |
Fiaux J, Andersson CIJ, Holmberg N, Bülow L, Kallio PT, Szyperski T, Bailey JE, Wüthrich K. 13C NMR flux ratio analysis of Escherichia coli central carbon metabolism in microaerobic bioprocesses [15] Journal of the American Chemical Society. 121: 1407-1408. DOI: 10.1021/Ja983786Y |
0.473 |
|
| 1999 |
Salzmann M, Wider G, Pervushin K, Senn H, Wüthrich K. TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large Proteins Journal of the American Chemical Society. 121: 844-848. DOI: 10.1021/JA9834226 |
0.32 |
|
| 1998 |
Fernández C, Szyperski T, Ono A, Iwai H, Tate S, Kainosho M, Wüthrich K. NMR with (13)C, (15)N-doubly-labeled DNA: The shape Antennapedia homeodomain complex with a 14-mer DNA duplex. Journal of Biomolecular Nmr. 12: 25-37. PMID 20700689 DOI: 10.1023/A:1008280117211 |
0.561 |
|
| 1998 |
Pervushin K, Ono A, Fernández C, Szyperski T, Kainosho M, Wüthrich K. NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 95: 14147-51. PMID 9826668 DOI: 10.1073/Pnas.95.24.14147 |
0.516 |
|
| 1998 |
Salzmann M, Pervushin K, Wider G, Senn H, Wüthrich K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proceedings of the National Academy of Sciences of the United States of America. 95: 13585-90. PMID 9811843 DOI: 10.1073/PNAS.95.23.13585 |
0.32 |
|
| 1998 |
Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wüthrich K. Prion protein NMR structure and familial human spongiform encephalopathies. Proceedings of the National Academy of Sciences of the United States of America. 95: 11667-72. PMID 9751723 DOI: 10.1073/Pnas.95.20.11667 |
0.557 |
|
| 1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. European Journal of Biochemistry / Febs. 256: 1-15. PMID 9746340 DOI: 10.1046/J.1432-1327.1998.2560001.X |
0.656 |
|
| 1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. Journal of Biomolecular Nmr. 12: 1-23. PMID 9729785 DOI: 10.1023/A:1008290618449 |
0.656 |
|
| 1998 |
Weber FE, Dyer JH, López García F, Werder M, Szyperski T, Wüthrich K, Hauser H. In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1-20 is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2. Cellular and Molecular Life Sciences : Cmls. 54: 751-9. PMID 9711242 DOI: 10.1007/S000180050203 |
0.594 |
|
| 1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Journal of Molecular Biology. 280: 933-52. PMID 9671561 DOI: 10.1006/Jmbi.1998.1852 |
0.648 |
|
| 1998 |
Glockshuber R, Hornemann S, Billeter M, Riek R, Wider G, Wüthrich K. Prion protein structural features indicate possible relations to signal peptidases. Febs Letters. 426: 291-6. PMID 9600253 DOI: 10.1016/S0014-5793(98)00372-X |
0.528 |
|
| 1998 |
Szyperski T, Fernández C, Mumenthaler C, Wüthrich K. Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system. Proceedings of the National Academy of Sciences of the United States of America. 95: 2262-6. PMID 9482873 DOI: 10.1073/Pnas.95.5.2262 |
0.512 |
|
| 1998 |
Mumenthaler C, Güntert P, Braun W, Wüthrich K. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination. Journal of Biomolecular Nmr. 10: 351-62. PMID 9460241 DOI: 10.1023/A:1018383106236 |
0.339 |
|
| 1998 |
Klimasauskas S, Szyperski T, Serva S, Wüthrich K. Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution. The Embo Journal. 17: 317-24. PMID 9427765 DOI: 10.1093/Emboj/17.1.317 |
0.463 |
|
| 1998 |
Pellecchia M, Iwai H, Szyperski T, Wüthrich K. The 2D NMR experiments H(C)CO2 and HCCO2 for assignment and pH titration of carboxylate groups in uniformly 15N/13C-labeled proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 124: 274-8. PMID 9424317 DOI: 10.1006/Jmre.1996.1058 |
0.577 |
|
| 1998 |
Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wüthrich K. Recommendations for the presentation of NMR structures of proteins and nucleic acids (IUPAC Recommendations 1998) Pure and Applied Chemistry. 70: 117-142. DOI: 10.1351/Pac199870010117 |
0.662 |
|
| 1998 |
Pervushin K, Riek R, Wider G, Wüthrich K. Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in13C-Labeled Proteins Journal of the American Chemical Society. 120: 6394-6400. DOI: 10.1021/Ja980742G |
0.563 |
|
| 1998 |
Szyperski T, Fernández C, Ono A, Kainosho M, Wüthrich K. Measurement of Deoxyribose3JHHScalar Couplings Reveals Protein Binding-Induced Changes in the Sugar Puckers of the DNA Journal of the American Chemical Society. 120: 821-822. DOI: 10.1021/Ja973055I |
0.479 |
|
| 1997 |
Pervushin K, Riek R, Wider G, Wüthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proceedings of the National Academy of Sciences of the United States of America. 94: 12366-71. PMID 9356455 DOI: 10.1073/Pnas.94.23.12366 |
0.582 |
|
| 1997 |
Szyperski T, Fernández C, Wüthrich K. Two-Dimensional ct-HC(C)H-COSY for Resonance Assignments of Smaller 13C-Labeled Biomolecules Journal of Magnetic Resonance. 128: 228-232. PMID 9356277 DOI: 10.1006/Jmre.1997.1235 |
0.502 |
|
| 1997 |
Ottiger M, Zerbe O, Güntert P, Wüthrich K. The NMR solution conformation of unligated human cyclophilin A. Journal of Molecular Biology. 272: 64-81. PMID 9299338 DOI: 10.1006/JMBI.1997.1220 |
0.346 |
|
| 1997 |
Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). Febs Letters. 413: 282-8. PMID 9280298 DOI: 10.1016/S0014-5793(97)00920-4 |
0.612 |
|
| 1997 |
Hornemann S, Korth C, Oesch B, Riek R, Wider G, Wüthrich K, Glockshuber R. Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. Febs Letters. 413: 277-81. PMID 9280297 DOI: 10.1016/S0014-5793(97)00921-6 |
0.572 |
|
| 1997 |
Glockshuber R, Hornemann S, Riek R, Wider G, Billeter M, Wüthrich K. Three-dimensional NMR structure of a self-folding domain of the prion protein PrP(121-231) Trends in Biochemical Sciences. 22: 241-2. PMID 9255063 DOI: 10.1016/S0968-0004(97)01070-0 |
0.531 |
|
| 1997 |
Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, Wüthrich K. Prion protein NMR structure and species barrier for prion diseases. Proceedings of the National Academy of Sciences of the United States of America. 94: 7281-5. PMID 9207082 DOI: 10.1073/Pnas.94.14.7281 |
0.553 |
|
| 1997 |
Sauer U, Hatzimanikatis V, Bailey JE, Hochuli M, Szyperski T, Wüthrich K. Metabolic fluxes in riboflavin-producing Bacillus subtilis Nature Biotechnology. 15: 448-452. PMID 9131624 DOI: 10.1038/Nbt0597-448 |
0.453 |
|
| 1997 |
Schott O, Billeter M, Leiting B, Wider G, Wüthrich K. The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor. Journal of Molecular Biology. 267: 673-83. PMID 9126845 DOI: 10.1006/JMBI.1997.0905 |
0.344 |
|
| 1997 |
Fernández C, Szyperski T, Bruyère T, Ramage P, Mösinger E, Wüthrich K. NMR solution structure of the pathogenesis-related protein P14a. Journal of Molecular Biology. 266: 576-93. PMID 9067611 DOI: 10.1006/Jmbi.1996.0772 |
0.534 |
|
| 1997 |
Pervushin K, Billeter M, Siegal G, Wüthrich K. Structural role of a buried salt bridge in the 434 repressor DNA-binding domain. Journal of Molecular Biology. 264: 1002-12. PMID 9000626 DOI: 10.1006/JMBI.1996.0692 |
0.301 |
|
| 1997 |
Szyperski T, Ono A, Fernández C, Iwai H, Tate S, Wüthrich K, Kainosho M. Measurement of3JC2‘PScalar Couplings in a 17 kDa Protein Complex with13C,15N-Labeled DNA Distinguishes the BIand BIIPhosphate Conformations of the DNA Journal of the American Chemical Society. 119: 9901-9902. DOI: 10.1021/Ja972290Y |
0.49 |
|
| 1996 |
Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. Journal of Molecular Biology. 260: 236-50. PMID 8764403 DOI: 10.1006/Jmbi.1996.0395 |
0.576 |
|
| 1996 |
Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K. NMR structure of the mouse prion protein domain PrP(121-231). Nature. 382: 180-2. PMID 8700211 DOI: 10.1038/382180A0 |
0.565 |
|
| 1996 |
Wüthrich K, Billeter M, Güntert P, Luginbühl P, Riek R, Wider G. NMR studies of the hydration of biological macromolecules Faraday Discuss.. 103: 245-253. DOI: 10.1039/Fd9960300245 |
0.57 |
|
| 1996 |
Szyperski T, Braun D, Banecki B, Wüthrich K. Useful Information from Axial Peak Magnetization in Projected NMR Experiments Journal of the American Chemical Society. 118: 8146-8147. DOI: 10.1021/Ja961015T |
0.535 |
|
| 1996 |
Wider G, Riek R, Wüthrich K. Diffusion filters for separation of solvent-protein and protein-protein nuclear Overhauser effects (HYDRA) Journal of the American Chemical Society. 118: 11629-11634. DOI: 10.1021/Ja9607188 |
0.572 |
|
| 1996 |
Szyperski T, Bailey JE, Wüthrich K. Detecting and dissecting metabolic fluxes using biosynthetic fractional 13C labeling and two-dimensional NMR spectroscopy Trends in Biotechnology. 14: 453-459. DOI: 10.1016/S0167-7799(96)10056-1 |
0.532 |
|
| 1995 |
Dötsch V, Wider G, Siegal G, Wüthrich K. Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor. Febs Letters. 366: 6-10. PMID 7789518 DOI: 10.1016/0014-5793(95)00459-M |
0.663 |
|
| 1995 |
Johansson J, Szyperski T, Wüthrich K. Pulmonary surfactant-associated polypeptide SP-C in lipid micelles: CD studies of intact SP-C and NMR secondary structure determination of depalmitoyl-SP-C(1-17) Febs Letters. 362: 261-265. PMID 7729509 DOI: 10.1016/0014-5793(95)00216-V |
0.51 |
|
| 1995 |
Schiffer CA, Dötsch V, Wüthrich K, van Gunsteren WF. Exploring the role of the solvent in the denaturation of a protein: a molecular dynamics study of the DNA binding domain of the 434 repressor. Biochemistry. 34: 15057-67. PMID 7578118 DOI: 10.1021/Bi00046A011 |
0.639 |
|
| 1995 |
Dötsch V, Wider G, Siegal G, Wüthrich K. Salt-stabilized globular protein structure in 7 M aqueous urea solution. Febs Letters. 372: 288-90. PMID 7556686 DOI: 10.1016/0014-5793(95)01004-X |
0.685 |
|
| 1995 |
Smith PE, van Schaik RC, Szyperski T, Wüthrich K, van Gunsteren WF. Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations. Journal of Molecular Biology. 246: 356-65. PMID 7532721 DOI: 10.1006/Jmbi.1994.0090 |
0.518 |
|
| 1995 |
Szyperski T, Braun D, Fernandez C, Bartels C, Wuthrich K. A Novel Reduced-Dimensionality Triple-Resonance Experiment for Efficient Polypeptide Backbone Assignment, 3D HN N Journal of Magnetic Resonance, Series B. 108: 197-203. DOI: 10.1006/Jmrb.1995.1124 |
0.504 |
|
| 1995 |
Luginbühl P, Szyperski T, Wüthrich K. Statistical Basis for the Use of13CαChemical Shifts in Protein Structure Determination Journal of Magnetic Resonance, Series B. 109: 229-233. DOI: 10.1006/Jmrb.1995.0016 |
0.539 |
|
| 1994 |
Bushweller JH, Holmgren A, Wüthrich K. Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments. European Journal of Biochemistry. 218: 327-34. PMID 8269921 DOI: 10.1111/J.1432-1033.1993.Tb18381.X |
0.594 |
|
| 1994 |
Johansson J, Szyperski T, Curstedt T, Wüthrich K. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix. Biochemistry. 33: 6015-23. PMID 8180229 DOI: 10.1021/Bi00185A042 |
0.565 |
|
| 1994 |
O'Connell JF, Bender R, Engels JW, Koller KP, Scharf M, Wüthrich K. The nuclear-magnetic-resonance solution structure of the mutant alpha-amylase inhibitor [R19L] Tendamistat and comparison with wild-type Tendamistat. European Journal of Biochemistry. 220: 763-70. PMID 8143730 DOI: 10.1111/J.1432-1033.1994.TB18677.X |
0.333 |
|
| 1994 |
Bushweller JH, Billeter M, Holmgren A, Wüthrich K. The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione. Journal of Molecular Biology. 235: 1585-97. PMID 8107093 DOI: 10.1006/Jmbi.1994.1108 |
0.636 |
|
| 1994 |
Spitzfaden C, Braun W, Wider G, Widmer H, Wüthrich K. Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex. Journal of Biomolecular Nmr. 4: 463-82. PMID 8075536 DOI: 10.1007/BF00156614 |
0.306 |
|
| 1994 |
Szyperski T, Antuch W, Schick M, Betz A, Stone SR, Wüthrich K. Transient hydrogen bonds identified on the surface of the NMR solution structure of Hirudin. Biochemistry. 33: 9303-10. PMID 8049231 DOI: 10.1021/Bi00197A034 |
0.544 |
|
| 1994 |
Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wüthrich K. NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proceedings of the National Academy of Sciences of the United States of America. 91: 11343-7. PMID 7972061 DOI: 10.1073/Pnas.91.24.11343 |
0.601 |
|
| 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 Letters. 352: 251-7. PMID 7925983 DOI: 10.1016/0014-5793(94)00941-4 |
0.355 |
|
| 1994 |
Wüthrich K. NMR assignments as a basis for structural characterization of denatured states of globular proteins Current Opinion in Structural Biology. 4: 93-99. DOI: 10.1016/S0959-440X(94)90065-5 |
0.37 |
|
| 1994 |
Bartels C, Wüthrich K. A spectral correlation function for efficient sequential NMR assignments of uniformly 15N-labeled proteins Journal of Biomolecular Nmr. 4: 775-785. DOI: 10.1007/BF00398408 |
0.327 |
|
| 1994 |
Szyperski T, Pellecchia M, Wuthrich K. 3D α/α/(CO)NHN, a Projected 4D NMR Experiment for Sequential Correlation of Polypeptide 1Hα/, 13Cα/ and Backbone 15N and 1HN Chemical-Shifts Journal of Magnetic Resonance, Series B. 105: 188-191. DOI: 10.1006/Jmrb.1994.1121 |
0.48 |
|
| 1994 |
Dotsch V, Wider G, Wuthrich K. Phase-Sensitive Spectra in a Single Scan with Coherence Selection by Pulsed Field Gradients Journal of Magnetic Resonance, Series A. 109: 263-264. DOI: 10.1006/Jmra.1994.1167 |
0.583 |
|
| 1994 |
Wider G, Dotsch V, Wuthrich K. Self-Compensating Pulsed Magnetic-Field Gradients for Short Recovery Times Journal of Magnetic Resonance, Series A. 108: 255-258. DOI: 10.1006/Jmra.1994.1120 |
0.585 |
|
| 1993 |
Brown LR, Mronga S, Bradshaw RA, Ortenzi C, Luporini P, Wüthrich K. Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi. Journal of Molecular Biology. 231: 800-16. PMID 8515452 DOI: 10.1006/Jmbi.1993.1327 |
0.328 |
|
| 1993 |
O'Connell JF, Bougis PE, Wüthrich K. Determination of the nuclear-magnetic-resonance solution structure of cardiotoxin CTX IIb from Naja mossambica mossambica. European Journal of Biochemistry. 213: 891-900. PMID 8504828 DOI: 10.1111/J.1432-1033.1993.TB17833.X |
0.303 |
|
| 1993 |
Szyperski T, Wider G, Bushweller JH, Wüthrich K. 3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins. Journal of Biomolecular Nmr. 3: 127-32. PMID 8448432 DOI: 10.1007/Bf00242481 |
0.704 |
|
| 1993 |
Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K. NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2. Febs Letters. 335: 18-26. PMID 8243660 DOI: 10.1016/0014-5793(93)80431-S |
0.625 |
|
| 1993 |
Szyperski T, Luginbühl P, Otting G, Güntert P, Wüthrich K. Protein dynamics studied by rotating frame 15N spin relaxation times. Journal of Biomolecular Nmr. 3: 151-64. PMID 7682879 DOI: 10.1007/Bf00178259 |
0.534 |
|
| 1993 |
Szyperski T, Güntert P, Stone SR, Wüthrich K. Nuclear magnetic resonance solution structure of hirudin(1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain. Journal of Molecular Biology. 228: 1193-205. PMID 1335515 DOI: 10.1016/0022-2836(92)90325-E |
0.572 |
|
| 1993 |
Xia TH, Bushweller JH, Sodano P, Billeter M, Björnberg O, Holmgren A, Wüthrich K. NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Science : a Publication of the Protein Society. 1: 310-21. PMID 1304339 DOI: 10.1002/Pro.5560010302 |
0.61 |
|
| 1992 |
Montelione GT, Wüthrich K, Burgess AW, Nice EC, Wagner G, Gibson KD, Scheraga HA. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints. Biochemistry. 31: 236-49. PMID 1731873 DOI: 10.1021/Bi00116A033 |
0.753 |
|
| 1992 |
Eccles C, Güntert P, Billeter M, Wüthrich K. Efficient analysis of protein 2D NMR spectra using the software package EASY. Journal of Biomolecular Nmr. 1: 111-30. PMID 1726780 DOI: 10.1007/BF01877224 |
0.344 |
|
| 1992 |
Neri D, Wider G, Wüthrich K. 1H, 15N and 13C NMR assignments of the 434 repressor fragments 1-63 and 44-63 unfolded in 7 M urea Febs Letters. 303: 129-135. PMID 1607010 DOI: 10.1016/0014-5793(92)80504-A |
0.348 |
|
| 1992 |
Neri D, Wider G, Wüthrich K. Complete 15N and 1H NMR assignments for the amino-terminal bmain of the phage 434 repressor in the urea-unfolded form Proceedings of the National Academy of Sciences of the United States of America. 89: 4397-4401. PMID 1584772 |
0.377 |
|
| 1992 |
Neri D, Billeter M, Wider G, Wüthrich K. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science (New York, N.Y.). 257: 1559-63. PMID 1523410 DOI: 10.1126/SCIENCE.1523410 |
0.367 |
|
| 1992 |
Szyperski T, Güntert P, Stone SR, 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 nuclear magnetic resonance solution structure of hirudin(1-51). Journal of Molecular Biology. 228: 1206-11. PMID 1474586 DOI: 10.1016/0022-2836(92)90326-F |
0.595 |
|
| 1992 |
Braun W, Vasák M, Robbins AH, Stout CD, Wagner G, Kägi JH, Wüthrich K. Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2. Proceedings of the National Academy of Sciences of the United States of America. 89: 10124-8. PMID 1438200 DOI: 10.1073/Pnas.89.21.10124 |
0.547 |
|
| 1992 |
Brown LR, Wüthrich K. Nuclear magnetic resonance solution structure of the alpha-neurotoxin from the black mamba (Dendroaspis polylepis polylepis). Journal of Molecular Biology. 227: 1118-35. PMID 1433289 DOI: 10.1016/0022-2836(92)90525-O |
0.306 |
|
| 1992 |
Billeter M, Neri D, Otting G, Qian YQ, Wüthrich K. Precise vicinal coupling constants 3JHN alpha in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments. Journal of Biomolecular Nmr. 2: 257-74. PMID 1392569 DOI: 10.1007/BF01875320 |
0.366 |
|
| 1992 |
Bushweller JH, Aslund F, Wüthrich K, Holmgren A. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione. Biochemistry. 31: 9288-93. PMID 1390715 DOI: 10.1021/bi00153a023 |
0.614 |
|
| 1992 |
Liepinsh E, Otting G, Wüthrich K. NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins Journal of Biomolecular Nmr. 2: 447-465. PMID 1384851 DOI: 10.1007/BF02192808 |
0.375 |
|
| 1992 |
Szyperski T, Neri D, Leiting B, Otting G, Wüthrich K. Support of 1H NMR assignments in proteins by biosynthetically directed fractional 13C-labeling. Journal of Biomolecular Nmr. 2: 323-34. PMID 1324756 DOI: 10.1007/Bf01874811 |
0.555 |
|
| 1992 |
Neri D, Billeter M, Wüthrich K. Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure Journal of Molecular Biology. 223: 743-767. PMID 1311771 DOI: 10.1016/0022-2836(92)90987-U |
0.322 |
|
| 1992 |
Szyperski T, Güntert P, Otting G, Wüthrich K. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets Journal of Magnetic Resonance (1969). 99: 552-560. DOI: 10.1016/0022-2364(92)90209-P |
0.538 |
|
| 1991 |
Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K. The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution. Biochemistry. 30: 6563-74. PMID 2054355 DOI: 10.1021/BI00240A029 |
0.33 |
|
| 1991 |
Sodano P, Xia TH, Bushweller JH, Björnberg O, Holmgren A, Billeter M, Wüthrich K. Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin. Journal of Molecular Biology. 221: 1311-24. PMID 1942053 DOI: 10.1016/0022-2836(91)90935-Y |
0.577 |
|
| 1991 |
Sodano P, Chary KV, Björnberg O, Holmgren A, Kren B, Fuchs JA, Wüthrich K. Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form. European Journal of Biochemistry. 200: 369-77. PMID 1889405 DOI: 10.1111/J.1432-1033.1991.Tb16194.X |
0.316 |
|
| 1991 |
Wüthrich K. Six years of protein structure determination by NMR spectroscopy: what have we learned? Ciba Foundation Symposium. 161: 136-145; discussion . PMID 1726080 |
0.309 |
|
| 1991 |
Wüthrich K. NMR Structures of proteins in solution Journal of Inorganic Biochemistry. 43: 78. DOI: 10.1016/0162-0134(91)84075-K |
0.303 |
|
| 1990 |
Neri D, Szyperski T, Otting G, Senn H, Wüthrich K. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry. 28: 7510-6. PMID 2692701 DOI: 10.1021/Bi00445A003 |
0.562 |
|
| 1990 |
Wüthrich K. Determination of three-dimensional protein structures in solution by nuclear magnetic resonance: an overview. Methods in Enzymology. 177: 125-31. PMID 2691844 DOI: 10.1016/0076-6879(89)77008-7 |
0.308 |
|
| 1990 |
Widmer H, Billeter M, Wüthrich K. Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy. Proteins. 6: 357-71. PMID 2576133 DOI: 10.1002/PROT.340060403 |
0.346 |
|
| 1990 |
Messerle BA, Schäffer A, Vasák M, Kägi JH, Wüthrich K. Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 214: 765-79. PMID 2388267 DOI: 10.1016/0022-2836(90)90291-S |
0.338 |
|
| 1990 |
Gruetter R, Boesch C, Müri M, Martin E, Wüthrich K. A simple design for a double-tunable probe head for imaging and spectroscopy at high fields. Magnetic Resonance in Medicine. 15: 128-34. PMID 2374493 DOI: 10.1002/Mrm.1910150114 |
0.746 |
|
| 1990 |
Wüthrich K. Structure and dynamics in proteins of pharmacological interest Biochemical Pharmacology. 40: 55-62. PMID 2372312 DOI: 10.1016/0006-2952(90)90178-N |
0.333 |
|
| 1990 |
Wüthrich K. Protein structure determination in solution by NMR spectroscopy Journal of Biological Chemistry. 265: 22059-22062. PMID 2266107 |
0.318 |
|
| 1990 |
Vendrell J, Wider G, Avilés FX, Wüthrich K. Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B. Biochemistry. 29: 7515-22. PMID 2223783 DOI: 10.1021/BI00484A600 |
0.304 |
|
| 1990 |
Gruetter R, Boesch C, Martin E, Wüthrich K. A method for rapid evaluation of saturation factors in in vivo surface coil NMR spectroscopy using B1-insensitive pulse cycles. Nmr in Biomedicine. 3: 265-71. PMID 2092742 DOI: 10.1002/Nbm.1940030605 |
0.766 |
|
| 1989 |
Wüthrich K. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science (New York, N.Y.). 243: 45-50. PMID 2911719 DOI: 10.1126/SCIENCE.2911719 |
0.32 |
|
| 1989 |
Haruyama H, Wüthrich K. Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance Biochemistry. 28: 4301-4312. PMID 2765488 |
0.371 |
|
| 1989 |
Boesch C, Gruetter R, Martin E, Duc G, Wüthrich K. Variations in the in vivo P-31 MR spectra of the developing human brain during postnatal life. Work in progress. Radiology. 172: 197-9. PMID 2740503 DOI: 10.1148/Radiology.172.1.2740503 |
0.753 |
|
| 1989 |
Celda B, Widmer H, Leupin W, Chazin WJ, Denny WA, Wüthrich K. Conformational studies of d-(AAAAATTTTT)2 using constraints from nuclear overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional 1H nuclear magnetic resonance spectra Biochemistry. 28: 1462-1471. PMID 2719909 DOI: 10.1021/Bi00430A006 |
0.534 |
|
| 1988 |
Arseniev A, Schultze P, Wörgötter E, Braun W, Wagner G, Vasák M, Kägi JH, Wüthrich K. Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. Journal of Molecular Biology. 201: 637-57. PMID 3418714 DOI: 10.1016/0022-2836(88)90644-4 |
0.541 |
|
| 1988 |
Steinmetz WE, Bougis PE, Rochat H, Redwine OD, Braun W, Wüthrich K. 1H nuclear-magnetic-resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins. European Journal of Biochemistry. 172: 101-16. PMID 3345756 DOI: 10.1111/J.1432-1033.1988.TB13861.X |
0.309 |
|
| 1988 |
Schultze P, Wörgötter E, Braun W, Wagner G, Vasák M, Kägi JH, Wüthrich K. Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 203: 251-68. PMID 3184190 DOI: 10.1016/0022-2836(88)90106-4 |
0.549 |
|
| 1988 |
Martin E, Boesch C, Duc G, Wüthrich K, Brunner P, Fanconi A. [Magnetic resonance in pediatric research and clinical practice. I. What can we expect from this new method?]. Helvetica Paediatrica Acta. 43: 53-74. PMID 3049466 |
0.567 |
|
| 1988 |
Widmer H, Wagner G, Schweitz H, Lazdunski M, Wüthrich K. The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence-specific 1H-NMR assignments. European Journal of Biochemistry / Febs. 171: 177-92. PMID 2892680 DOI: 10.1111/J.1432-1033.1988.Tb13774.X |
0.624 |
|
| 1988 |
Grütter R, Otting G, Wüthrich K, Leupin W. OR3 operator of bacteriophage lambda in a 23 base-pair DNA fragment: sequence-specific 1H NMR assignments for the non-labile protons and comparison with the isolated 17 base-pair operator. European Biophysics Journal : Ebj. 16: 279-86. PMID 2853668 DOI: 10.1007/BF00254064 |
0.656 |
|
| 1988 |
Montelione GT, Wüthrich K, Scheraga HA. Sequence-specific 1H NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor. Biochemistry. 27: 2235-43. PMID 2837287 DOI: 10.1021/bi00406a064 |
0.686 |
|
| 1987 |
Leupin W, Wagner G, Denny WA, Wüthrich K. Assignment of the 13C nuclear magnetic resonance spectrum of a short DNA-duplex with 1H-detected two-dimensional heteronuclear correlation spectroscopy. Nucleic Acids Research. 15: 267-75. PMID 3822804 DOI: 10.1093/Nar/15.1.267 |
0.579 |
|
| 1987 |
Lee KH, Fitton JE, Wüthrich K. Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 911: 144-153. PMID 3801489 DOI: 10.1016/0167-4838(87)90003-3 |
0.312 |
|
| 1987 |
Vasák M, Wörgötter E, Wagner G, Kägi JH, Wüthrich K. Metal co-ordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2. Journal of Molecular Biology. 196: 711-9. PMID 3681973 DOI: 10.1016/0022-2836(87)90042-8 |
0.506 |
|
| 1987 |
Otting G, Marchot P, Bougis PE, Rochat H, Wüthrich K. Monitoring the purification by high-performance liquid chromatography of cardiotoxins from Naja mossambica mossambica using phase-sensitive two-dimensional nuclear magnetic resonance. European Journal of Biochemistry. 168: 603-7. PMID 3665936 DOI: 10.1111/J.1432-1033.1987.Tb13459.X |
0.301 |
|
| 1987 |
Wörgötter E, Wagner G, Vasák M, Kägi JH, Wüthrich K. Sequence-specific 1H-NMR assignments in rat-liver metallothionein-2. European Journal of Biochemistry / Febs. 167: 457-66. PMID 3653102 DOI: 10.1111/J.1432-1033.1987.Tb13359.X |
0.581 |
|
| 1987 |
Montelione GT, Wüthrich K, Nice EC, Burgess AW, Scheraga HA. Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry. Proceedings of the National Academy of Sciences of the United States of America. 84: 5226-30. PMID 3496602 DOI: 10.1073/Pnas.84.15.5226 |
0.684 |
|
| 1987 |
Otting G, Grütter R, Leupin W, Minganti C, Ganesh KN, Sproat BS, Gait MJ, Wüthrich K. Sequential NMR assignments of labile protons in DNA using two-dimensional nuclear-Overhauser-enhancement spectroscopy with three jump-and-return pulse sequences. European Journal of Biochemistry / Febs. 166: 215-20. PMID 3036520 DOI: 10.1111/j.1432-1033.1987.tb13504.x |
0.651 |
|
| 1987 |
Wagner G, Frey MH, Neuhaus D, Wörgötter E, Braun W, Vasak M, Kägi JH, Wüthrich K. Spatial structure of rabbit liver metallothionein-2 in solution by NMR. Experientia. Supplementum. 52: 149-57. PMID 2959501 DOI: 10.1007/978-3-0348-6784-9_8 |
0.525 |
|
| 1987 |
Otting G, Steinmetz WE, Bougis PE, Rochat H, Wüthrich K. Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica. European Journal of Biochemistry. 168: 609-20. PMID 2822421 DOI: 10.1111/J.1432-1033.1987.TB13460.X |
0.387 |
|
| 1987 |
Siekmann J, Wenzel HR, Schröder W, Schutt H, Truscheit E, Arens A, Rauenbusch E, Chazin WJ, Wüthrich K, Tschesche H. Pyroglutamyl-aprotinin, a new aprotinin homologue from bovine lungs--isolation, properties, sequence analysis and characterization using 1H nuclear magnetic resonance in solution Biological Chemistry Hoppe-Seyler. 368: 1589-1596. PMID 2450551 DOI: 10.1515/Bchm3.1987.368.2.1589 |
0.509 |
|
| 1987 |
Wagner G, Braun W, Havel TF, Schaumann T, Go N, Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. Journal of Molecular Biology. 196: 611-39. PMID 2445992 DOI: 10.1016/0022-2836(87)90037-4 |
0.585 |
|
| 1987 |
Wagner G, Brühwiler D, Wüthrich K. Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance. Journal of Molecular Biology. 196: 227-31. PMID 2443716 DOI: 10.1016/0022-2836(87)90524-9 |
0.56 |
|
| 1987 |
Chazin WJ, Wüthrich K. Optimization of homonuclear relayed coherence transfer experiments with proteins in H2O solution Journal of Magnetic Resonance (1969). 72: 358-363. DOI: 10.1016/0022-2364(87)90300-3 |
0.455 |
|
| 1986 |
Wagner G, Neuhaus D, Wörgötter E, Vasák M, Kägi JH, Wüthrich K. Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2. Journal of Molecular Biology. 187: 131-5. PMID 3959079 DOI: 10.1016/0022-2836(86)90413-4 |
0.581 |
|
| 1986 |
Braun W, Wagner G, Wörgötter E, Vasák M, Kägi JH, Wüthrich K. Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution. Journal of Molecular Biology. 187: 125-9. PMID 3959078 DOI: 10.1016/0022-2836(86)90412-2 |
0.53 |
|
| 1986 |
Leupin W, Chazin WJ, Hyberts S, Denny WA, Wüthrich K. NMR studies of the complex between the decadeoxynucleotide d-(GCATTAATGC)2 and a minor-groove-binding drug Biochemistry. 25: 5902-5910. PMID 3790493 DOI: 10.1021/Bi00368A010 |
0.475 |
|
| 1986 |
Chazin WJ, Wüthrich K, Hyberts S, Rance M, Denny WA, Leupin W. 1H nuclear magnetic resonance assignments for d-(GCATTAATGC)2 using experimental refinements of established procedures Journal of Molecular Biology. 190: 439-453. PMID 3783707 DOI: 10.1016/0022-2836(86)90014-8 |
0.697 |
|
| 1986 |
Wagner G, Wüthrich K. Observation of internal motility of proteins by nuclear magnetic resonance in solution. Methods in Enzymology. 131: 307-26. PMID 3773764 DOI: 10.1016/0076-6879(86)31047-4 |
0.557 |
|
| 1986 |
Wagner G, Neuhaus D, Wörgötter E, Vasák M, Kägi JH, Wüthrich K. Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2. European Journal of Biochemistry / Febs. 157: 275-89. PMID 3709538 DOI: 10.1111/J.1432-1033.1986.Tb09666.X |
0.567 |
|
| 1986 |
Montelione GT, Wüthrich K, Nice EC, Burgess AW, Scheraga HA. Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance. Proceedings of the National Academy of Sciences of the United States of America. 83: 8594-8. PMID 3490668 DOI: 10.1073/Pnas.83.22.8594 |
0.651 |
|
| 1986 |
Roder H, Wuthrich K. Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons Proteins: Structure, Function and Genetics. 1: 34-42. PMID 2835760 DOI: 10.1002/Prot.340010107 |
0.335 |
|
| 1986 |
Müller N, Ernst RR, Wüthrich K. Multiple-Quantum-Filtered Two-Dimensional Correlated NMR Spectroscopy of Proteins Journal of the American Chemical Society. 108: 6482-6492. DOI: 10.1021/Ja00281A006 |
0.653 |
|
| 1986 |
Otting G, Senn H, Wagner G, Wüthrich K. Editing of 2D 1H NMR spectra using X half-filters. combined use with residue-selective 15N labeling of proteins Journal of Magnetic Resonance (1969). 70: 500-505. DOI: 10.1016/0022-2364(86)90144-7 |
0.571 |
|
| 1986 |
Otting G, Widmer H, Wagner G, Wüthrich K. Origin of τ2 and τ2 ridges in 2D NMR spectra and procedures for suppression Journal of Magnetic Resonance (1969). 66: 187-193. DOI: 10.1016/0022-2364(86)90122-8 |
0.513 |
|
| 1985 |
Neuhaus D, Wagner G, Vasák M, Kägi JH, Wüthrich K. Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Rabbit metallothionein-2. European Journal of Biochemistry / Febs. 151: 257-73. PMID 2992961 DOI: 10.1111/j.1432-1033.1985.tb09096.x |
0.582 |
|
| 1985 |
Havel TF, Wüthrich K. An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution Journal of Molecular Biology. 182: 281-294. PMID 2582141 DOI: 10.1016/0022-2836(85)90346-8 |
0.375 |
|
| 1985 |
Roder H, Wagner G, Wüthrich K. Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor. Biochemistry. 24: 7407-11. PMID 2417626 DOI: 10.1021/Bi00346A056 |
0.573 |
|
| 1985 |
Roder H, Wagner G, Wüthrich K. Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. Biochemistry. 24: 7396-407. PMID 2417625 DOI: 10.1021/Bi00346A055 |
0.55 |
|
| 1985 |
Chazin WJ, Goldenberg DP, Creighton TE, Wüthrich K. Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution. European Journal of Biochemistry / Febs. 152: 429-37. PMID 2414103 DOI: 10.1111/J.1432-1033.1985.Tb09215.X |
0.602 |
|
| 1985 |
Billeter M, Engeli M, Wüthrich K. Interactive program for investigation of protein structures based on 1H NMR experiments Journal of Molecular Graphics. 3: 79-83. DOI: 10.1016/0263-7855(85)80014-X |
0.311 |
|
| 1985 |
Rance M, Sørensen OW, Leupin W, Kogler H, Wüthrich K, Ernst RR. Uniform excitation of multiple-quantum coherence. Application to two-dimensional double-quantum spectroscopy Journal of Magnetic Resonance (1969). 61: 67-80. DOI: 10.1016/0022-2364(85)90268-9 |
0.61 |
|
| 1985 |
Rance M, Bodenhausen G, Wagner G, Wüthrich K, Ernst RR. A systematic approach to the suppression of J cross peaks in 2D exchange and 2D NOE spectroscopy Journal of Magnetic Resonance (1969). 62: 497-510. DOI: 10.1016/0022-2364(85)90218-5 |
0.71 |
|
| 1985 |
Müller N, Bodenhausen G, Wüthrich K, Ernst RR. The appearance of forbidden cross peaks in two-dimensional nuclear magnetic resonance spectra due to multiexponential T2 relaxation Journal of Magnetic Resonance (1969). 65: 531-534. DOI: 10.1016/0022-2364(85)90142-8 |
0.671 |
|
| 1985 |
Denk W, Wagner G, Rance M, Wüthrich K. Combined suppression of diagonal peaks and t1 ridges in two-dimensional nuclear overhauser enhancement spectra Journal of Magnetic Resonance (1969). 62: 350-355. DOI: 10.1016/0022-2364(85)90074-5 |
0.644 |
|
| 1984 |
Williamson MP, Marion D, Wüthrich K. Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance Journal of Molecular Biology. 173: 341-359. PMID 6699915 DOI: 10.1016/0022-2836(84)90125-6 |
0.35 |
|
| 1984 |
Zuiderweg ER, Billeter M, Boelens R, Scheek RM, Wüthrich K, Kaptein R. Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain. Febs Letters. 174: 243-7. PMID 6381097 DOI: 10.1016/0014-5793(84)81166-7 |
0.668 |
|
| 1984 |
Wagner G, Stassinopoulou CI, Wüthrich K. Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor. European Journal of Biochemistry / Febs. 145: 431-6. PMID 6209139 DOI: 10.1111/J.1432-1033.1984.Tb08572.X |
0.585 |
|
| 1984 |
Stassinopoulou CI, Wagner G, Wüthrich K. Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein. European Journal of Biochemistry / Febs. 145: 423-30. PMID 6209138 DOI: 10.1111/J.1432-1033.1984.Tb08571.X |
0.599 |
|
| 1984 |
Ebina S, Wüthrich K. Amide proton titration shifts in bull seminal inhibitor IIA by two-dimensional correlated 1H nuclear magnetic resonance (COSY). Manifestation of conformational equilibria involving carboxylate groups Journal of Molecular Biology. 179: 283-288. PMID 6094827 DOI: 10.1016/0022-2836(84)90469-8 |
0.315 |
|
| 1984 |
Neuhaus D, Wagner G, Vasák M, Kägi JH, Wüthrich K. 113CD-1H spin-spin couplings in homonuclear 1H correlated spectroscopy of metallothionein. Identification of the cysteine 1H spin systems. European Journal of Biochemistry / Febs. 143: 659-67. PMID 6090138 DOI: 10.1111/J.1432-1033.1984.Tb08419.X |
0.559 |
|
| 1984 |
Senn H, Billeter M, Wüthrich K. The spatial structure of the axially bound methionine in solution conformations of horse ferrocytochrome c and Pseudomonas aeruginosa ferrocytochrome c 551 by 1H NMR European Biophysics Journal. 11: 3-15. PMID 6088217 DOI: 10.1007/BF00253853 |
0.323 |
|
| 1984 |
Pardi A, Billeter M, Wüthrich K. Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure. Journal of Molecular Biology. 180: 741-51. PMID 6084720 DOI: 10.1016/0022-2836(84)90035-4 |
0.568 |
|
| 1984 |
Wüthrich K, Billeter M, Braun W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances Journal of Molecular Biology. 180: 715-740. PMID 6084719 DOI: 10.1016/0022-2836(84)90034-2 |
0.354 |
|
| 1984 |
Wüthrich K, Wagner G. Internal dynamics of proteins Trends in Biochemical Sciences. 9: 152-154. DOI: 10.1016/0968-0004(84)90124-5 |
0.553 |
|
| 1984 |
Senn H, Cusanovich MA, Wüthrich K. 1H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 785: 46-53. DOI: 10.1016/0167-4838(84)90232-2 |
0.302 |
|
| 1984 |
Neuhaus D, Wider G, Wagner G, Wüthrich K. X-relayed 1H-1H correlated spectroscopy Journal of Magnetic Resonance (1969). 57: 164-168. DOI: 10.1016/0022-2364(84)90250-6 |
0.481 |
|
| 1984 |
Rance M, Wagner G, Sørensen OW, Wüthrich K, Ernst RR. Application of ω1-decoupled 2D correlation spectra to the study of proteins Journal of Magnetic Resonance (1969). 59: 250-261. DOI: 10.1016/0022-2364(84)90169-0 |
0.747 |
|
| 1984 |
Wider G, Macura S, Kumar A, Ernst R, Wüthrich K. Homonuclear two-dimensional 1H NMR of proteins. Experimental procedures Journal of Magnetic Resonance (1969). 56: 207-234. DOI: 10.1016/0022-2364(84)90099-4 |
0.532 |
|
| 1984 |
Bodenhausen G, Wagner G, Rance M, Sørensen OW, Wüthrich K, Ernst RR. Longitudinal two-spin order in 2D exchange spectroscopy (NOESY) Journal of Magnetic Resonance (1969). 59: 542-550. DOI: 10.1016/0022-2364(84)90092-1 |
0.726 |
|
| 1983 |
Štrop P, ?echova D, Wüthrich K, Kendrew JC. Preliminary structural comparison of the proteinase isoinhibitors IIA and IIB from bull seminal plasma based on individual assignments of the 1H nuclear magnetic resonance spectra by two-dimensional nuclear magnetic resonance at 500 MHz Journal of Molecular Biology. 166: 669-676. PMID 6864794 DOI: 10.1016/S0022-2836(83)80291-5 |
0.365 |
|
| 1983 |
Wagner G, Wüthrich K. [Dynamics of protein structures]. Die Naturwissenschaften. 70: 105-14. PMID 6855917 DOI: 10.1007/BF00401593 |
0.56 |
|
| 1983 |
Hosur RV, Wider G, Wüthrich K. Sequential individual resonance assignments in the 1H nuclear-magnetic-resonance spectrum of cardiotoxin VII2 from Naja mossambica mossambica. European Journal of Biochemistry. 130: 497-508. PMID 6825705 DOI: 10.1111/J.1432-1033.1983.TB07178.X |
0.667 |
|
| 1983 |
Wüthrich K. Sequential individual resonance assignments in the 1H-nmr spectra of polypeptides and proteins Biopolymers - Peptide Science Section. 22: 131-138. PMID 6673752 |
0.336 |
|
| 1983 |
Rance M, Sørensen OW, Bodenhausen G, Wagner G, Ernst RR, Wüthrich K. Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering. Biochemical and Biophysical Research Communications. 117: 479-85. PMID 6661238 DOI: 10.1016/0006-291X(83)91225-1 |
0.714 |
|
| 1983 |
Wüthrich K, Wagner G. Nuclear magnetic resonance studies of mobility in proteins. Ciba Foundation Symposium. 93: 310-28. PMID 6551231 DOI: 10.1002/9780470720752.ch17 |
0.545 |
|
| 1983 |
Zuiderweg ER, Kaptein R, Wüthrich K. Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy. European Journal of Biochemistry / Febs. 137: 279-92. PMID 6360686 DOI: 10.1111/J.1432-1033.1983.Tb07827.X |
0.73 |
|
| 1983 |
Zuiderweg ER, Kaptein R, Wüthrich K. Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution. Proceedings of the National Academy of Sciences of the United States of America. 80: 5837-41. PMID 6351066 DOI: 10.1073/Pnas.80.19.5837 |
0.714 |
|
| 1983 |
Wüthrich K, Billeter M, Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. Journal of Molecular Biology. 169: 949-61. PMID 6313936 DOI: 10.1016/S0022-2836(83)80144-2 |
0.327 |
|
| 1983 |
Strop P, Wider G, Wüthrich K. Assignment of the 1H nuclear magnetic resonance spectrum of the proteinase inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic resonance at 500 MHz. Journal of Molecular Biology. 166: 641-65. PMID 6306250 DOI: 10.1016/S0022-2836(83)80289-7 |
0.341 |
|
| 1983 |
Štrop P, Wüthrich K, Kendrew JC. Characterization of the proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance. Stability, amide proton exchange and mobility of aromatic residues Journal of Molecular Biology. 166: 631-640. PMID 6306249 DOI: 10.1016/S0022-2836(83)80288-5 |
0.323 |
|
| 1983 |
Senn H, Eugster A, Wüthrich K. Determination of the coordination geometry at the heme iron in three cytochromes c from Saccharomyces cerevisiae and from Candida krusei based on individual 1H-NMR assignments for heme c and the axially coordinated amino acids. Biochimica Et Biophysica Acta. 743: 58-68. PMID 6297596 DOI: 10.1016/0167-4838(83)90418-1 |
0.361 |
|
| 1983 |
Pardi A, Wagner G, Wüthrich K. Protein conformation and proton nuclear-magnetic-resonance chemical shifts. European Journal of Biochemistry / Febs. 137: 445-54. PMID 6198174 DOI: 10.1111/J.1432-1033.1983.Tb07848.X |
0.729 |
|
| 1983 |
Wider G, Hosur R, Wüthrich K. Suppression of the solvent resonance in 2D NMR spectra of proteins in H2O solution Journal of Magnetic Resonance (1969). 52: 130-135. DOI: 10.1016/0022-2364(83)90263-9 |
0.589 |
|
| 1983 |
Wagner G, Pardi A, Wüthrich K. Hydrogen bond length and 1H NMR chemical shifts in proteins Journal of the American Chemical Society. 105: 5948-5949. |
0.573 |
|
| 1982 |
Wider G, Lee KH, Wüthrich K. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles Journal of Molecular Biology. 155: 367-388. PMID 7077677 DOI: 10.1016/0022-2836(82)90010-9 |
0.347 |
|
| 1982 |
Billeter M, Braun W, Wüthrich K. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. Journal of Molecular Biology. 155: 321-46. PMID 7077676 DOI: 10.1016/0022-2836(82)90008-0 |
0.341 |
|
| 1982 |
Wüthrich K, Wider G, Wagner G, Braun W. Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. Journal of Molecular Biology. 155: 311-9. PMID 7077675 DOI: 10.1016/0022-2836(82)90007-9 |
0.586 |
|
| 1982 |
Brown LR, Braun W, Kumar A, Wüthrich K. High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface. Biophysical Journal. 37: 319-28. PMID 6275926 DOI: 10.1016/S0006-3495(82)84680-8 |
0.328 |
|
| 1982 |
Wagner G, Wüthrich K. Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. Journal of Molecular Biology. 160: 343-61. PMID 6184480 DOI: 10.1016/0022-2836(82)90180-2 |
0.602 |
|
| 1982 |
Wagner G, Wüthrich K. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. Journal of Molecular Biology. 155: 347-66. PMID 6176717 DOI: 10.1016/0022-2836(82)90009-2 |
0.593 |
|
| 1982 |
Macura S, Wuthrich K, Ernst R. Separation and suppression of coherent transfer effects in two-dimensional NOE and chemical exchange spectroscopy Journal of Magnetic Resonance (1969). 46: 269-282. DOI: 10.1016/0022-2364(82)90142-1 |
0.536 |
|
| 1982 |
Macura S, Wüthrich K, Ernst RR. The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules Journal of Magnetic Resonance (1969). 47: 351-357. DOI: 10.1016/0022-2364(82)90128-7 |
0.494 |
|
| 1981 |
Steinmetz WE, Moonen C, Kumar A, Lazdunski M, Visser L, Carlsson FH, Wüthrich K. 1H nuclear-magnetic-resonance studies of the conformation of cardiotoxin VII2 from Naja mossambica mossambica. European Journal of Biochemistry / Febs. 120: 467-75. PMID 7333275 DOI: 10.1111/J.1432-1033.1981.Tb05725.X |
0.597 |
|
| 1981 |
Brown LR, Wüthrich K. Melittin bound to dodecylphosphocholine micelles 1H-NMR assignments and global conformational features Bba - Biomembranes. 647: 95-111. PMID 7295724 DOI: 10.1016/0005-2736(81)90298-4 |
0.337 |
|
| 1981 |
Wüthrich K, Wagner G, Richarz R, Braun W. Correlations between internal mobility and stability of globular proteins. Biophysical Journal. 32: 549-60. PMID 7248460 DOI: 10.1016/S0006-3495(80)84989-7 |
0.614 |
|
| 1981 |
Nagayama K, Wüthrich K. Structural interpretation of vicinal proton-proton coupling constants 3JH alpha H beta in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy European Journal of Biochemistry. 115: 653-657. PMID 6165586 |
0.55 |
|
| 1981 |
Wagner G, Kumar A, Wüthrich K. Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 2. Combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidation of polypeptide secondary structures. European Journal of Biochemistry. 114: 375-84. PMID 6163631 DOI: 10.1111/j.1432-1033.1981.tb05157.x |
0.607 |
|
| 1981 |
Nagayama K, Wüthrich K. Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino-acid residues European Journal of Biochemistry. 114: 365-374. PMID 6163630 |
0.547 |
|
| 1981 |
Baumann R, Kumar A, Ernst R, Wüthrich K. Improvement of 2D NOE and 2D correlated spectra by triangular multiplication Journal of Magnetic Resonance (1969). 44: 76-83. DOI: 10.1016/0022-2364(81)90190-6 |
0.438 |
|
| 1981 |
Bösch C, Kumar A, Baumann R, Ernst RR, Wüthrich K. Comparison of selective proton-proton overhauser effects in biological macromolecules observed by one-dimensional and two-dimensional NMR experiments Journal of Magnetic Resonance (1969). 42: 159-163. DOI: 10.1016/0022-2364(81)90021-4 |
0.487 |
|
| 1981 |
Wider G, Baumann R, Nagayama K, Ernst RR, Wüthrich K. Strong spin-spin coupling in the two-dimensional J-resolved 360-MHz 1H NMR spectra of the common amino acids Journal of Magnetic Resonance (1969). 42: 73-87. DOI: 10.1016/0022-2364(81)90011-1 |
0.645 |
|
| 1980 |
Kumar A, Ernst RR, Wüthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochemical and Biophysical Research Communications. 95: 1-6. PMID 7417242 DOI: 10.1016/0006-291X(80)90695-6 |
0.527 |
|
| 1980 |
Wüthrich K, Eugster A, Wagner G. p2H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 1438 Journal of Molecular Biology. 144: 601-604. PMID 6265651 DOI: 10.1016/0022-2836(80)90342-3 |
0.559 |
|
| 1980 |
Senn H, Keller RM, Wüthrich K. Different chirality of the axial methionine in homologous cytochromes c determined by 1H NMR and CD spectroscopy Biochemical and Biophysical Research Communications. 92: 1362-1369. PMID 6245651 DOI: 10.1016/0006-291X(80)90436-2 |
0.372 |
|
| 1980 |
Richarz R, Nagayama K, Wüthrich K. Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogue Biochemistry. 19: 5189-5196. PMID 6160872 |
0.47 |
|
| 1980 |
Kumar A, Wagner G, Ernst RR, Wüthrich K. Studies of J-connectives and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments. Biochemical and Biophysical Research Communications. 96: 1156-63. PMID 6159893 DOI: 10.1016/0006-291X(80)90073-X |
0.669 |
|
| 1980 |
Lauterwein J, Bösch C, Brown LR, Wüthrich K. Physicochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochimica Et Biophysica Acta. 556: 244-64. PMID 534626 DOI: 10.1016/0005-2736(79)90046-4 |
0.332 |
|
| 1980 |
Vasák M, Nagayama K, Wüthrich K, Mertens ML, Kägi JH. Creatine kinase. Nuclear magnetic resonance and fluorescence evidence for interaction of adenosine 5'-diphosphate with aromatic residue(s). Biochemistry. 18: 5050-5. PMID 497170 DOI: 10.1021/bi00590a004 |
0.471 |
|
| 1980 |
Nagayama K, Kumar A, Wüthrich K, Ernst R. Experimental techniques of two-dimensional correlated spectroscopy Journal of Magnetic Resonance (1969). 40: 321-334. DOI: 10.1016/0022-2364(80)90255-3 |
0.613 |
|
| 1979 |
Bundi A, Andreatta RH, Wüthrich K. Characterisation of a local structure in the synthetic parathyroid hormone fragment 1--34 by 1H nuclear-magnetic-resonance techniques. European Journal of Biochemistry. 91: 201-8. PMID 720337 DOI: 10.1111/j.1432-1033.1978.tb20952.x |
0.357 |
|
| 1979 |
Wagner G, Wüthrich K, Tschesche H. A 1H nuclear-magnetic-resonance study of the solution conformation of the isoinhibitor K from Helix pomatia. European Journal of Biochemistry. 89: 367-77. PMID 710398 DOI: 10.1111/j.1432-1033.1978.tb12538.x |
0.599 |
|
| 1979 |
Wagner G, Wüthrich K. Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins Journal of Molecular Biology. 134: 75-94. PMID 537062 DOI: 10.1016/0022-2836(79)90414-5 |
0.596 |
|
| 1979 |
Nagayama K, Wüthrich K, Ernst RR. Two-dimensional spin echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromolecules. Biochemical and Biophysical Research Communications. 90: 305-11. PMID 496980 DOI: 10.1016/0006-291X(79)91625-5 |
0.621 |
|
| 1979 |
Wagner G, Wüthrich K. Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor Journal of Molecular Biology. 130. PMID 469937 DOI: 10.1016/0022-2836(79)90550-3 |
0.591 |
|
| 1979 |
Nagayama K, Bachmann P, Ernst RR, Wüthrich K. Selective spin decoupling in the J-resolved two-dimensional 1H n.m.r. spectra of proteins. Biochemical and Biophysical Research Communications. 86: 218-25. PMID 435302 DOI: 10.1016/0006-291X(79)90403-0 |
0.621 |
|
| 1979 |
Wagner G, Kalb AJ, Wüthrich K. Conformational studies by 1H nuclear magnetic resonance of the basic pancreatic trypsin inhibitor after reduction of the disulfide bond between Cys-14 and Cys-38. Influence of charged protecting groups on the stability of the protein European Journal of Biochemistry. 95: 249-253. PMID 313338 DOI: 10.1111/J.1432-1033.1979.Tb12960.X |
0.535 |
|
| 1979 |
Wagner G, Tschesche H, Wüthrich K. The influence of localized chemical modifications of the basic pancreatic trypsin inhibitor on static and dynamic aspects of the molecular conformation in solution. European Journal of Biochemistry. 95: 239-48. PMID 313337 DOI: 10.1111/j.1432-1033.1979.tb12959.x |
0.599 |
|
| 1979 |
Dubs A, Wagner G, Wüthrich K. Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor. Biochimica Et Biophysica Acta. 577: 177-94. PMID 311660 DOI: 10.1016/0005-2795(79)90020-5 |
0.585 |
|
| 1979 |
Richarz R, Sehr P, Wagner G, Wüthrich K. Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor. Journal of Molecular Biology. 130: 19-30. PMID 38343 DOI: 10.1016/0022-2836(79)90549-7 |
0.545 |
|
| 1979 |
Wüthrich K, Wagner G. Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor Journal of Molecular Biology. 130: 1-18. PMID 38342 DOI: 10.1016/0022-2836(79)90548-5 |
0.578 |
|
| 1979 |
Lauterwein J, Lazdunski M, Wüthrich K. The 1H nuclear-magnetic-resonance spectra of Neurotoxin I and cardiotoxin Vii4 from Naja mossambica mossambica. European Journal of Biochemistry. 92: 361-71. PMID 33043 DOI: 10.1111/J.1432-1033.1978.Tb12755.X |
0.411 |
|
| 1979 |
Wüthrich K, Nagayama K, Ernst RR. Emerging techniques Two-dimensional NMR spectroscopy Trends in Biochemical Sciences. 4. DOI: 10.1016/0968-0004(79)90406-7 |
0.604 |
|
| 1979 |
Wagner G, Wuthrich K. Truncated driven nuclear overhauser effect (TOE). A new technique for studies of selective 1H1H overhauser effects in the presence of spin diffusion Journal of Magnetic Resonance (1969). 33: 675-680. DOI: 10.1016/0022-2364(79)90180-X |
0.472 |
|
| 1979 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. I. The non-amide protons Biopolymers. 18: 2911-2911. DOI: 10.1002/Bip.1979.360181118 |
0.52 |
|
| 1979 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. II. The amide resonances Biopolymers. 18: 2911-2911. DOI: 10.1002/Bip.1978.360170308 |
0.578 |
|
| 1978 |
Llinás M, Klein MP, Wüthrich K. Amide proton spin-lattice relaxation in polypeptides. A field-dependence study of the proton and nitrogen dipolar interactions in alumichrome. Biophysical Journal. 24: 849-62. PMID 737289 DOI: 10.1016/S0006-3495(78)85424-1 |
0.687 |
|
| 1978 |
Boesch C, Bundi A, Oppliger M, Wüthrich K. 1H nuclear-magnetic-resonance studies of the molecular conformation of monomeric glucagon in aqueous solution. European Journal of Biochemistry / Febs. 91: 209-14. PMID 720338 DOI: 10.1111/J.1432-1033.1978.Tb20953.X |
0.661 |
|
| 1978 |
Wagner G, Wüthrich K. Dynamic model of globular protein conformations based on NMR studies in solution [33] Nature. 275: 247-248. PMID 692702 DOI: 10.1038/275247a0 |
0.677 |
|
| 1978 |
Llinás M, Wüthrich K. A nitrogen-15 spin-lattice relaxation study of alumichrome Bba - Protein Structure. 532: 29-40. PMID 620055 DOI: 10.1016/0005-2795(78)90444-0 |
0.57 |
|
| 1978 |
Nagayama K, Wüthrich K. Two-dimensional NMR spectroscopy. A powerful tool for the investigation of biopolymers in solution. Die Naturwissenschaften. 64: 581-3. PMID 593403 DOI: 10.1007/BF00450641 |
0.468 |
|
| 1978 |
Wüthrich K, Wagner G, Richarz R, Perkins SJ. Individual assignments of the methyl resonances in the 1H nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor. Biochemistry. 17: 2253-63. PMID 307961 DOI: 10.1021/bi00605a001 |
0.606 |
|
| 1978 |
Perkins SJ, Wüthrich K. Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by 1H NMR at 360 MHz Bba - Protein Structure. 536: 406-420. PMID 30488 DOI: 10.1016/0005-2795(78)90498-1 |
0.309 |
|
| 1978 |
Brown LR, De Marco A, Richarz R, Wagner G, Wüthrich K. The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor. 1H and 13C nuclear-magnetic-resonance studies of the native and the transaminated inhibitor. European Journal of Biochemistry. 88: 87-95. PMID 27364 DOI: 10.1111/j.1432-1033.1978.tb12425.x |
0.626 |
|
| 1978 |
Wüthrich K, Wagner G. Internal motion in globular proteins Trends in Biochemical Sciences. 3: 227-230. DOI: 10.1016/S0968-0004(78)94607-8 |
0.568 |
|
| 1978 |
Nagayama K, Bachmann P, Wuthrich K, Ernst R. The use of cross-sections and of projections in two-dimensional NMR spectroscopy Journal of Magnetic Resonance (1969). 31: 133-148. DOI: 10.1016/0022-2364(78)90176-2 |
0.599 |
|
| 1978 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. II. The amide resonances Biopolymers. 17: 637-650. DOI: 10.1002/bip.1978.360170308 |
0.524 |
|
| 1978 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. I. The non-amide protons Biopolymers. 17: 617-636. DOI: 10.1002/Bip.1978.360170307 |
0.587 |
|
| 1977 |
Nagayama K, Wüthrich K, Bachmann P, Ernst RR. Two-dimensional J-resolved 1H n.m.r. spectroscopy for studies of biological macromolecules. Biochemical and Biophysical Research Communications. 78: 99-105. PMID 907694 DOI: 10.1016/0006-291X(77)91226-8 |
0.642 |
|
| 1977 |
Llinás M, Meier W, Wüthrich K. A carbon-13 spin lattice relaxation study of alumichrome at 25.1 MHz and 90.5 MHz. Biochimica Et Biophysica Acta. 492: 1-11. PMID 861244 DOI: 10.1016/0005-2795(77)90208-2 |
0.525 |
|
| 1977 |
De Marco A, Tschesche H, Wagner G, Wüthrich K. 1H Nmr studies at 360 MHz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI). Biophysics of Structure and Mechanism. 3: 303-15. PMID 20175 DOI: 10.1007/BF00535703 |
0.321 |
|
| 1977 |
Bundi A, Wüthrich K. 1H NMR titration shifts of amide proton resonances in polypeptide chains Febs Letters. 77: 11-14. PMID 15871 DOI: 10.1016/0014-5793(77)80182-8 |
0.304 |
|
| 1977 |
Keller RM, Wüthrich K. 1H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome c-552 from euglena gracilis Bba - Protein Structure. 491: 416-422. DOI: 10.1016/0005-2795(77)90284-7 |
0.334 |
|
| 1976 |
Keller R, Groudinsky O, Wüthrich K. Contact-shifted resonances in the 1H NMR spectra of cytochrome b5. Resonance identification and spin density distribution in the heme group. Biochimica Et Biophysica Acta. 427: 497-511. PMID 5127 DOI: 10.1016/0005-2795(76)90192-6 |
0.32 |
|
| 1976 |
Brown LR, De Marco A, Wagner G, Wüthrich K. A study of the lysyl residues in the basic pancreatic trypsin inhibitor using 1H nuclear magnetic resonance at 360 Mhz. European Journal of Biochemistry. 62: 103-7. PMID 2474 DOI: 10.1111/j.1432-1033.1976.tb10102.x |
0.653 |
|
| 1975 |
Wüthrich K, Wagner G. NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor Febs Letters. 50: 265-268. PMID 234403 DOI: 10.1016/0014-5793(75)80504-7 |
0.515 |
|
| 1975 |
Bundi A, Grathwohl C, Hochmann J, Keller RM, Wagner G, Wüthrich K. Proton NMR of the protected tetrapeptides TFA-Gly-Gly-l-X-l-Ala-OCH3, where X stands for One of the 20 common amino acids Journal of Magnetic Resonance (1969). 18: 191-198. DOI: 10.1016/0022-2364(75)90237-1 |
0.535 |
|
| 1975 |
Wüthrich K, Hochmann J, Keller RM, Wagner G, Brunori M, Giacometti C. 1H NMR relaxation in high-spin ferrous hemoproteins Journal of Magnetic Resonance (1969). 19: 111-113. DOI: 10.1016/0022-2364(75)90034-7 |
0.524 |
|
| 1975 |
Wagner G, De Marco A, Wüthrich K. Convolution difference 1H NMR spectra at 360 MHz of the basic pancreatic trypsin inhibitor Journal of Magnetic Resonance (1969). 20: 565-569. DOI: 10.1016/0022-2364(75)90015-3 |
0.534 |
|
| 1975 |
Wagner G, Wüthrich K. Proton NMR studies of the aromatic residues in the basic pancreatic trypsin inhibitor (BPTI) Journal of Magnetic Resonance (1969). 20: 435-445. DOI: 10.1016/0022-2364(75)90001-3 |
0.647 |
|
| 1971 |
Wüthrich K, Shulman R. Магнитный резонанс в биологии Uspekhi Fizicheskih Nauk. 105: 707-720. DOI: 10.3367/UFNr.0105.197112d.0707 |
0.478 |
|
| 1970 |
Shulman RG, Wüthrich K, Yamane T, Patel DJ, Blumberg WE. Nuclear magnetic resonance determination of ligand-induced conformational changes in myoglobin. Journal of Molecular Biology. 53: 143-57. PMID 5530399 DOI: 10.1016/0022-2836(70)90050-1 |
0.594 |
|
| 1970 |
Yamane T, Wüthrich K, Shulman RG, Ogawa S. Proton magnetic resonance studies of cyanoferrihemoglobins from different species. Journal of Molecular Biology. 49: 197-202. PMID 5465385 |
0.58 |
|
| 1970 |
Wüthrich K, Shulman RG, Yamane T, Wyluda BJ, Hugli TE, Gurd FR. High resolution proton magnetic resonance studies of cyanoferrimyoglobins and alkylated derivatives from different species. The Journal of Biological Chemistry. 245: 1947-53. PMID 5462360 |
0.587 |
|
| 1970 |
Wüthrich K, Shulman RG. Magnetic resonance in biology Physics Today. 23: 43-50. DOI: 10.1063/1.3022065 |
0.569 |
|
| 1970 |
Wüthrich K, Meiboom S, Snyder LC. Nuclear magnetic resonance spectroscopy of bicyclobutane The Journal of Chemical Physics. 52: 222-229. DOI: 10.1063/1.1672669 |
0.303 |
|
| 1969 |
Shulman RG, Wüthrich K, Yamane T, Antonini E, Brunori M. Nuclear magnetic resonances of reconstituted myoglobins. Proceedings of the National Academy of Sciences of the United States of America. 63: 623-8. PMID 5259755 |
0.628 |
|
| 1969 |
Wüthrich K, Shulman RG, Wyluda BJ, Caughey WS. Proton magnetic resonance studies of porphyrin iron (3) cyanides. Proceedings of the National Academy of Sciences of the United States of America. 62: 636-43. PMID 5256994 |
0.584 |
|
| 1969 |
Shulman RG, Ogawa S, Wüthrich K, Yamane T, Peisach J, Blumberg WE. The absence of "heme-heme" interactions in hemoglobin. Science (New York, N.Y.). 165: 251-7. PMID 4306914 DOI: 10.1126/Science.165.3890.251 |
0.516 |
|
| 1969 |
Connick RE, Wüthrich K. 17O nuclear magnetic relaxation in aqueous solutions of diamagnetic metal ions The Journal of Chemical Physics. 51: 4506-4508. |
0.616 |
|
| 1968 |
Wüthrich K, Shulman RG, Peisach J. High-resolution proton magnetic resonance spectra of sperm whale cyanometmyoglobin. Proceedings of the National Academy of Sciences of the United States of America. 60: 373-80. PMID 5248802 |
0.604 |
|
| 1968 |
Wüthrich K, Shulman RG, Yamane T. Proton magnetic resonance studies of human cyanomethemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 61: 1199-206. PMID 4303475 |
0.582 |
|
| 1968 |
Wüthrich K, Connick RE. Nuclear magnetic resonance studies of the coordination of vanadyl complexes in solution and the rate of elimination of coordinated water molecules Inorganic Chemistry. 7: 1377-1388. |
0.642 |
|
| 1967 |
Wüthrich K, Connick RE. Nuclear magnetic resonance relaxation of oxygen-17 in aqueous solutions of vanadyl perchlorate and the rate of elimination of water molecules from the first coordination sphere Inorganic Chemistry. 6: 583-590. |
0.64 |
|
| 1964 |
Wüthrich K, Loeliger H, Fallab S. [Electron spin resonance for research on the kinetics and mechanism of Cu2+-catalyzed reactions]. Experientia. 20: 599-601. PMID 4285556 DOI: 10.1007/BF02144805 |
0.551 |
|
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