| Studying “invisible” excited protein states in slow exchange with a major state conformation P Vallurupalli, G Bouvignies, LE Kay Journal of the American Chemical Society 134 (19), 8148-8161, 2012 | 485 | 2012 |
| Solution structure of a minor and transiently formed state of a T4 lysozyme mutant G Bouvignies, P Vallurupalli, DF Hansen, BE Correia, O Lange, A Bah, ... Nature 477 (7362), 111-114, 2011 | 311 | 2011 |
| Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings G Bouvignies, P Bernadó, S Meier, K Cho, S Grzesiek, R Brüschweiler, ... Proceedings of the National Academy of Sciences of the United States of …, 2005 | 288 | 2005 |
| Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy PRL Markwick, G Bouvignies, M Blackledge Journal of the American Chemical Society 129 (15), 4724-4730, 2007 | 185 | 2007 |
| Toward a unified representation of protein structural dynamics in solution PRL Markwick, G Bouvignies, L Salmon, JA McCammon, M Nilges, ... Journal of the American Chemical Society 131 (46), 16968-16975, 2009 | 122 | 2009 |
| Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways A Sekhar, JAO Rumfeldt, HR Broom, CM Doyle, G Bouvignies, ... elife 4, e07296, 2015 | 116 | 2015 |
| Protein Conformational Flexibility from Structure‐Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin L Salmon, G Bouvignies, P Markwick, N Lakomek, S Showalter, DW Li, ... Angewandte Chemie International Edition 48 (23), 4154-4157, 2009 | 114 | 2009 |
| Mapping the conformation of a client protein through the Hsp70 functional cycle A Sekhar, R Rosenzweig, G Bouvignies, LE Kay Proceedings of the National Academy of Sciences 112 (33), 10395-10400, 2015 | 101 | 2015 |
| Hsp70 biases the folding pathways of client proteins A Sekhar, R Rosenzweig, G Bouvignies, LE Kay Proceedings of the National Academy of Sciences 113 (20), E2794-E2801, 2016 | 97 | 2016 |
| A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding G Bouvignies, LE Kay Journal of biomolecular NMR 53, 303-310, 2012 | 93 | 2012 |
| Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings G Bouvignies, P Markwick, R Brüschweiler, M Blackledge Journal of the American Chemical Society 128 (47), 15100-15101, 2006 | 87 | 2006 |
| Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions A Sekhar, A Velyvis, G Zoltsman, R Rosenzweig, G Bouvignies, LE Kay Elife 7, e32764, 2018 | 79 | 2018 |
| Structure and dynamics of the MKK7–JNK signaling complex J Kragelj, A Palencia, MH Nanao, D Maurin, G Bouvignies, M Blackledge, ... Proceedings of the National Academy of Sciences 112 (11), 3409-3414, 2015 | 78 | 2015 |
| Increasing the Exchange Time-Scale That Can Be Probed by CPMG Relaxation Dispersion NMR P Vallurupalli, G Bouvignies, LE Kay The Journal of Physical Chemistry B, 2011 | 77 | 2011 |
| Measurement of proton chemical shifts in invisible states of slowly exchanging protein systems by chemical exchange saturation transfer G Bouvignies, LE Kay The Journal of Physical Chemistry B 116 (49), 14311-14317, 2012 | 75 | 2012 |
| 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics AJ Baldwin, TL Religa, DF Hansen, G Bouvignies, LE Kay Journal of the American Chemical Society, 2010 | 71 | 2010 |
| Visualizing side chains of invisible protein conformers by solution NMR G Bouvignies, P Vallurupalli, LE Kay Journal of molecular biology 426 (3), 763-774, 2014 | 68 | 2014 |
| Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy E Delaforge, J Kragelj, L Tengo, A Palencia, S Milles, G Bouvignies, ... Journal of the American Chemical Society 140 (3), 1148-1158, 2018 | 67 | 2018 |
| Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings G Bouvignies, PRL Markwick, M Blackledge Chemphyschem 8 (13), 1901-1909, 2007 | 61 | 2007 |
| Nuclear Magnetic Resonance Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Time Scales L Salmon, G Bouvignies, P Markwick, M Blackledge Biochemistry 50 (14), 2735-2747, 2011 | 59 | 2011 |
Lewis E KayUniversity of Toronto在 pound.med.utoronto.ca 的电子邮件经过验证
