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Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCharacterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in SolutionTatyana I. Igumenova, Kendra King Frederick, and A. Joshua WandView Author Information Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059 Cite this: Chem. Rev. 2006, 106, 5, 1672–1699Publication Date (Web):April 26, 2006Publication History Received20 March 2006Published online26 April 2006Published inissue 1 May 2006https://pubs.acs.org/doi/10.1021/cr040422hhttps://doi.org/10.1021/cr040422hresearch-articleACS PublicationsCopyright © 2006 American Chemical SocietyRequest reuse permissionsArticle Views3160Altmetric-Citations279LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Alkyls,Magnetic properties,Order,Peptides and proteins,Protein dynamics Get e-Alerts
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Citations
Cites
The Principles of Nuclear Magnetism
Abragam, A., & Hebel, L. C. (1961) · American Journal of Physics · doi:10.1119/1.1937646 · Cited by 15,792
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a009 · Cited by 3,777
The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules
Lipari, G. (1982) · Journal of the American Chemical Society · Cited by 2,525
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Lipari, G., & Szabo, A. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00381a010 · Cited by 1,837
Kay, L. E., Torchia, D. A., & Bax, A. (1989) · Biochemistry · doi:10.1021/bi00449a003 · Cited by 1,768
Sattler, M. (1999) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(98)00025-9 · Cited by 1,722
Protein NMR Spectroscopy: Principles and Practice
Cavanagh, J. (1995) · Cited by 1,636
Hydrogen exchange and structural dynamics of proteins and nucleic acids
Englander, S. W., & Kallenbach, N. R. (1983) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005217 · Cited by 1,356
Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families
Lockless, S. W., & Ranganathan, R. (1999) · Science · doi:10.1126/science.286.5438.295 · Cited by 1,303
Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., & Gronenborn, A. M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00168a070 · Cited by 1,046
Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,033
Conformational Substates in Proteins
Frauenfelder, H., Parak, F., & Young, R. D. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002315 · Cited by 993
Backbone Dynamics of Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme
Mandel, A. M., Akke, M., & Palmer, III (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0073 · Cited by 990
Protein NMR Spectroscopy. Principles and Practice
Kalbitzer, H. R. (1997) · Zeitschrift für Physikalische Chemie · doi:10.1524/zpch.1997.202.part_1_2.297 · Cited by 971
Nuclear Spin Relaxation in Ellipsoids Undergoing Rotational Brownian Motion
Woessner, D. E. (1962) · The Journal of Chemical Physics · doi:10.1063/1.1701390 · Cited by 904
Evolutionarily conserved networks of residues mediate allosteric communication in proteins
Süel, G. M., Lockless, S. W., Wall, M. A., & Ranganathan, R. (2003) · Nature Structural Biology · doi:10.1038/nsb881 · Cited by 821
Allostery without conformational change: A plausible model
Cooper, A., & Dryden, D. T. F. (1984) · European Biophysics Journal · doi:10.1007/bf00276625 · Cited by 736
Tugarinov, V., Hwang, P. M., Ollerenshaw, J. E., & Kay, L. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja030153x · Cited by 649
Rotational diffusion anisotropy of human ubiquitin from 15N NMR relaxation
Tjandra, N., Feller, S. E., Pastor, R. W., & Bax, A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00155a020 · Cited by 589
Palmer, A. G., Rance, M., & Wright, P. E. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00012a001 · Cited by 562
Energetics of Ligand Binding to Proteins
Weber, G. (1975) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60410-6 · Cited by 523
Rate Theories and Puzzles of Hemeprotein Kinetics
Frauenfelder, H., & Wolynes, P. G. (1985) · Science · doi:10.1126/science.4012322 · Cited by 488
Optimal isotope labelling for NMR protein structure determinations
Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Mei Ono, A., & Güntert, P. (2006) · Nature · doi:10.1038/nature04525 · Cited by 485
Yang, D., & Kay, L. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0581 · Cited by 458
Jarymowycz, V. A., & Stone, M. J. (2006) · Chemical Reviews · doi:10.1021/cr040421p · Cited by 412
Mapping of spectral density functions using heteronuclear NMR relaxation measurements
Peng, J. W., & Wagner, G. (1992) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(92)90135-t · Cited by 379
Palmer, A. G., & Massi, F. (2006) · Chemical Reviews · doi:10.1021/cr0404287 · Cited by 357
Akke, M., Brueschweiler, R., & Palmer, A. G. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00074a073 · Cited by 352
Long-Range Motional Restrictions in a Multidomain Zinc-Finger Protein from Anisotropic Tumbling
Brüschweiler, R., Liao, X., & Wright, P. E. (1995) · Science · doi:10.1126/science.7754375 · Cited by 322
Dynamical Mapping of E. coli Thioredoxin via 13C NMR Relaxation Analysis
LeMaster, D. M., & Kushlan, D. M. (1996) · Journal of the American Chemical Society · doi:10.1021/ja960877r · Cited by 319
Peng, J. W., & Wagner, G. (1992) · Biochemistry · doi:10.1021/bi00151a027 · Cited by 315
Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex.
Wand, A. J., Lee, A. L., & Kinnear, S. (2000) · Nature Structural Biology · doi:10.1038/71280 · Cited by 305
Self-citationDynamic activation of protein function: a view emerging from NMR spectroscopy.
Wand, A. J. (2001) · Nature Structural Biology · doi:10.1038/nsb1101-926 · Cited by 302
Self-citationSelective Methyl Group Protonation of Perdeuterated Proteins
Rosen, M. K., Gardner, K. H., Willis, R. C., Parris, W. E., Pawson, T., & Kay, L. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0603 · Cited by 301
Lee, L. K., Rance, M., Chazin, W. J., & Palmer, A. G. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018631009583 · Cited by 294
Microscopic origins of entropy, heat capacity and the glass transition in proteins
Lee, A. L., & Wand, A. J. (2001) · Nature · doi:10.1038/35078119 · Cited by 291
Self-citationNMR studies of protein structure and dynamics
Kay, L. E. (2005) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2004.11.021 · Cited by 284
Gurd, F. R. N., & Rothges, T. M. (1979) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60459-3 · Cited by 280
Muhandiram, D. R., Yamazaki, T., Sykes, B. D., & Kay, L. E. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00151a018 · Cited by 279
NMR Residual Dipolar Couplings as Probes of Biomolecular Dynamics
Tolman, J. R., & Ruan, K. (2006) · Chemical Reviews · doi:10.1021/cr040429z · Cited by 256
Ottiger, M., & Bax, A. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9826791 · Cited by 254
Gardner, K. H., & Kay, L. E. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9706514 · Cited by 250
Edgington, E. (1998) · Technometrics · doi:10.1080/00401706.1998.10485213 · Cited by 243
Motional model analyses of protein and peptide dynamics using 13C and 15N NMR relaxation
Daragan, V. A., & Mayo, K. H. (1997) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(97)00006-x · Cited by 242
Ligand-dependent Dynamics and Intramolecular Signaling in a PDZ Domain
Fuentes, E. J., Der, C. J., & Lee, A. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.010 · Cited by 237
Nicholson, L. K., Kay, L. E., Baldisseri, D. M., Arango, J., Young, P. E., Bax, A., & Torchia, D. A. (1992) · Biochemistry · doi:10.1021/bi00138a003 · Cited by 236
McIntosh, L. P., & Dahlquist, F. W. (1990) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005400 · Cited by 233
New developments in isotope labeling strategies for protein solution NMR spectroscopy
Goto, N. K., & Kay, L. E. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00135-4 · Cited by 224
Hilser, V. J., Dowdy, D., Oas, T. G., & Freire, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.9903 · Cited by 215
Influence of vibrational motion on solid state line shapes and NMR relaxation
Henry, E. R., & Szabo, A. (1985) · The Journal of Chemical Physics · doi:10.1063/1.448692 · Cited by 211
Insights into the local residual entropy of proteins provided by NMR relaxation
Li, Z., Raychaudhuri, S., & Wand, A. J. (1996) · Protein Science · doi:10.1002/pro.5560051228 · Cited by 210
Self-citationNMR studies of Brownian tumbling and internal motions in proteins
Korzhnev, D. M., Billeter, M., Arseniev, A. S., & Orekhov, V. Y. (2001) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(00)00028-5 · Cited by 209
Methyl TROSY: explanation and experimental verification
Ollerenshaw, J. E., Tugarinov, V., & Kay, L. E. (2003) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1256 · Cited by 208
Pan, H., Lee, J. C., & Hilser, V. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220240297 · Cited by 202
Correlation between Dynamics and High Affinity Binding in an SH2 Domain Interaction
Kay, L. E., Muhandiram, D. R., Farrow, N. A., Aubin, Y., & Forman-Kay, J. D. (1996) · Biochemistry · doi:10.1021/bi9522312 · Cited by 202
Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins
Tugarinov, V., & Kay, L. E. (2005) · ChemBioChem · doi:10.1002/cbic.200500110 · Cited by 198
Millet, O., Muhandiram, D. R., Skrynnikov, N. R., & Kay, L. E. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012497y · Cited by 182
An Effective Method for the Discrimination of Motional Anisotropy and Chemical Exchange
Kneller, J. M., Lu, M., & Bracken, C. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017461k · Cited by 167
Protein NMR relaxation: theory, applications and outlook
Fischer, M. W. F., Majumdar, A. K., & Zuiderweg, E. R. P. (1998) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(98)00023-5 · Cited by 159
Fast internal main-chain dynamics of human ubiquitin
Schneider, D. M., Dellwo, M. J., & Wand, A. J. (1992) · Biochemistry · doi:10.1021/bi00129a013 · Cited by 157
Self-citationWand, A. J., Urbauer, J. L., McEvoy, R. P., & Urbauer, R. J. B. (1996) · Biochemistry · doi:10.1021/bi9530144 · Cited by 146
Self-citationInsights into the Mobility of Methyl-Bearing Side Chains in Proteins from 3JCC and 3JCN Couplings
Chou, J. J., Case, D. A., & Bax, A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029972s · Cited by 134
New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins
Brüschweiler, R. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00036-8 · Cited by 133
The use of model selection in the model-free analysis of protein dynamics
d’Auvergne, E. J., & Gooley, P. R. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1021902006114 · Cited by 130
Allosteric determinants in guanine nucleotide-binding proteins
Hatley, M. E., Lockless, S. W., Gibson, S. K., Gilman, A. G., & Ranganathan, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1835919100 · Cited by 130
Skrynnikov, N. R., Millet, Ó., & Kay, L. E. (2002) · Journal of the American Chemical Society · doi:10.1021/ja012498q · Cited by 126
Efficient production of isotopically labeled proteins by cell-free synthesis: A practical protocol
Torizawa, T., Shimizu, M., Taoka, M., Miyano, H., & Kainosho, M. (2004) · Journal of Biomolecular NMR · doi:10.1007/s10858-004-3534-2 · Cited by 125
Wand, A. J., Urbauer, J. L., McEvoy, R. P., & Urbauer, R. J. B. (2011) · PubMed · doi:10.13018/bmr6466 · Cited by 123
Self-citationEnergetics of Target Peptide Binding by Calmodulin Reveals Different Modes of Binding
Brokx, R. D., López, M. M., Vogel, H. J., & Makhatadze, G. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011026200 · Cited by 118
Gagné, S. M., Tsuda, S., Spyracopoulos, L., Kay, L. E., & Sykes, B. D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1723 · Cited by 116
Chatfield, D. C., Szabó, A., & Brooks, B. R. (1998) · Journal of the American Chemical Society · doi:10.1021/ja972215n · Cited by 114
Correlation between binding and dynamics at SH2 domain interfaces
Kay, L. E., Muhandiram, D. R., Wolf, G., Shoelson, S. E., & Forman-Kay, J. D. (1998) · Nature Structural Biology · doi:10.1038/nsb0298-156 · Cited by 111
A rate process with an entropy barrier
Zhou, H., & Zwanzig, R. W. (1991) · The Journal of Chemical Physics · doi:10.1063/1.460427 · Cited by 110
Yang, D., Mittermaier, A., Mok, Y., & Kay, L. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1588 · Cited by 109
Ishima, R., Petkova, A. T., Louis, J. M., & Torchia, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0104711 · Cited by 100
Kay, L. E., & Torchia, D. A. (1991) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(91)90167-r · Cited by 97
Best, R. B., Clarke, J., & Karplus, M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.03.001 · Cited by 96
Energetics of target peptide recognition by calmodulin: A calorimetric study
Wintrode, P. L., & Privalov, P. L. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0785 · Cited by 94
Lee, A. L., Flynn, P. F., & Wand, A. J. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983758f · Cited by 88
Self-citationSolution structure and dynamics of a designed hydrophobic core variant of ubiquitin
Johnson, E. C., Lazar, G. A., Desjarlais, J. R., & Handel, T. M. (1999) · Structure · doi:10.1016/s0969-2126(99)80123-3 · Cited by 88
Katoh, E., Louis, J. M., Yamazaki, T., Gronenborn, A. M., Torchia, D. A., & Ishima, R. (2003) · Protein Science · doi:10.1110/ps.0300703 · Cited by 88
Biosynthetic 13C Labeling of Aromatic Side Chains in Proteins for NMR Relaxation Measurements
Teilum, K., Brath, U., Lundström, P., & Akke, M. (2006) · Journal of the American Chemical Society · doi:10.1021/ja055660o · Cited by 82
Temperature Dependence of the Internal Dynamics of a Calmodulin−Peptide Complex
Lee, A. L., Sharp, K. A., Kranz, J. K., Song, X.-J., & Wand, A. J. (2002) · Biochemistry · doi:10.1021/bi026380d · Cited by 82
Self-citationClarkson, M. W., & Lee, A. L. (2004) · Biochemistry · doi:10.1021/bi0494424 · Cited by 81
Henry, G. D., Weiner, J. H., & Sykes, B. D. (1986) · Biochemistry · doi:10.1021/bi00351a012 · Cited by 79
Constantine, K. L., Friedrichs, M. S., Wittekind, M. G., et al. (1998) · Biochemistry · doi:10.1021/bi980203o · Cited by 79
Schnell, J. R., Dyson, H. J., & Wright, P. E. (2003) · Biochemistry · doi:10.1021/bi035464z · Cited by 78
Lee, A. L., & Wand, A. J. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008304220445 · Cited by 76
Self-citationTugarinov, V., & Kay, L. E. (2005) · Biochemistry · doi:10.1021/bi0519809 · Cited by 74
Mittermaier, A., Varani, L., Muhandiram, D. R., Kay, L. E., & Varani, G. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3311 · Cited by 74
Vugmeyster, L., Trott, O., McKnight, C. J., Raleigh, D. P., & Palmer, A. G. I. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00537-5 · Cited by 69
The Origin of Protein Sidechain Order Parameter Distributions
Best, R. B., Clarke, J., & Karplus, M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja049078w · Cited by 64
Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins
Ollerenshaw, J. E., Tugarinov, V., Skrynnikov, N. R., & Kay, L. E. (2005) · Journal of Biomolecular NMR · doi:10.1007/s10858-005-2614-2 · Cited by 64
Dynamics and Entropy of a Calmodulin−Peptide Complex Studied by NMR and Molecular Dynamics
Prabhu, N. V., Lee, A. L., Wand, A. J., & Sharp, K. A. (2002) · Biochemistry · doi:10.1021/bi026544q · Cited by 61
Self-citationImproved labeling strategy for 13C relaxation measurements of methyl groups in proteins
Lee, A. L., Urbauer, J. L., & Wand, A. J. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018311013338 · Cited by 58
Self-citationMillet, Ó., Mittermaier, A., Baker, D. A., & Kay, L. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00471-6 · Cited by 56
Backbone Dynamics of trp Repressor Studied by 15N NMR Relaxation
Zheng, Z., Czaplicki, J., & Jardetzky, O. (1995) · Biochemistry · doi:10.1021/bi00015a035 · Cited by 54
Prompers, J. J., & Brüschweiler, R. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp0026033 · Cited by 53
Prediction of methyl-side Chain Dynamics in Proteins
Ming, D., & Brüschweiler, R. (2004) · Journal of Biomolecular NMR · doi:10.1023/b:jnmr.0000032612.70767.35 · Cited by 51
Ensemble‐based signatures of energy propagation in proteins: A new view of an old phenomenon
Liu, T., Whitten, S. T., & Hilser, V. J. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20749 · Cited by 51
Finerty, P. J., Muhandiram, R., & Forman-Kay, J. D. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00803-3 · Cited by 43
Walsh, S. T. R., Lee, A. L., DeGrado, W. F., & Wand, A. J. (2001) · Biochemistry · doi:10.1021/bi0105274 · Cited by 40
Self-citationBest, R. B., Rutherford, T. J., Freund, S. M. V., & Clarke, J. (2004) · Biochemistry · doi:10.1021/bi035658e · Cited by 39
Mittermaier, A., & Kay, L. E. (2004) · Protein Science · doi:10.1110/ps.03502504 · Cited by 39
Vugmeyster, L., Raleigh, D. P., Palmer, A. G. I., & Vugmeister, B. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja029480f · Cited by 38
Flynn, P. F., Urbauer, R. J. B., Zhang, H., et al. (2001) · Biochemistry · doi:10.1021/bi0102252 · Cited by 38
Ishima, R., Louis, J. M., & Torchia, D. A. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1012482426306 · Cited by 32
Mittermaier, A., Davidson, A. R., & Kay, L. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034856q · Cited by 32
Backbone and Side Chain Dynamics of Mutant Calmodulin−Peptide Complexes
Igumenova, T. I., Lee, A. L., & Wand, A. J. (2005) · Biochemistry · doi:10.1021/bi050832f · Cited by 31
Self-citationFinerty, P. J., Mittermaier, A., Muhandiram, R., Kay, L. E., & Forman-Kay, J. D. (2004) · Biochemistry · doi:10.1021/bi048641k · Cited by 29
Daragan, V. A., Kloczewiak, M. A., & Mayo, K. H. (1993) · Biochemistry · doi:10.1021/bi00091a007 · Cited by 27
On the Dynamic Origins of Allosteric Activation
Wand, A. J. (2001) · Science · doi:10.1126/science.293.5534.1395a · Cited by 23
Self-citationMeasurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins
Liu, W., Zheng, Y., Cistola, D. P., & Yang, D. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1025884922203 · Cited by 22
Methyl Side-Chain Dynamics in Proteins Using Selective Enrichment with a Single Isotopomer
Chaykovski, M. M., Bae, L. C., Cheng, M.-C., Murray, J. H., Tortolani, K. E., Zhang, R., Seshadri, K., Findlay, J. B. C., Hsieh, S., Kalverda, A. P., et al. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0368608 · Cited by 15
Model selection for the interpretation of protein side chain methyl dynamics
Choy, W., & Kay, L. E. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1023065310430 · Cited by 14
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Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561
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Metadata
- Authors
- Igumenova, T. I., Frederick, K. K., & Wand, A. J.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-04-26
- Volume
- 106
- Issue
- 5
- Pages
- 1672-1699
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W1976391576
- Cited by
- 314
- References
- 119
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.