How does a protein fold? A S˘ ali, E Shakhnovich, M Karplus nature 369 (6477), 248-251, 1994 | 1276 | 1994 |
Kinetics of protein folding: A lattice model study of the requirements for folding to the native state A Šali, E Shakhnovich, M Karplus Journal of molecular biology 235 (5), 1614-1636, 1994 | 702 | 1994 |
Engineering of stable and fast-folding sequences of model proteins. EI Shakhnovich, AM Gutin Proceedings of the National Academy of Sciences 90 (15), 7195-7199, 1993 | 673 | 1993 |
Specific nucleus as the transition state for protein folding: evidence from the lattice model VI Abkevich, AM Gutin, EI Shakhnovich Biochemistry 33 (33), 10026-10036, 1994 | 621 | 1994 |
On the transition coordinate for protein folding R Du, VS Pande, AY Grosberg, T Tanaka, ES Shakhnovich The Journal of chemical physics 108 (1), 334-350, 1998 | 572 | 1998 |
The role of topological constraints in the kinetics of collapse of macromolecules AY Grosberg, SK Nechaev, EI Shakhnovich Journal de physique 49 (12), 2095-2100, 1988 | 518 | 1988 |
Theoretical studies of protein-folding thermodynamics and kinetics EI Shakhnovich Current opinion in structural biology 7 (1), 29-40, 1997 | 508 | 1997 |
Proteins with selected sequences fold into unique native conformation EI Shakhnovich Physical Review Letters 72 (24), 3907, 1994 | 506 | 1994 |
Estimating the Entropic Cost of Self-Assembly of Multiparticle Hydrogen-Bonded Aggregates Based on the Cyanuric Acid⊙ Melamine Lattice M Mammen, EI Shakhnovich, JM Deutch, GM Whitesides The Journal of Organic Chemistry 63 (12), 3821-3830, 1998 | 474 | 1998 |
Common activation mechanism of class A GPCRs Q Zhou, D Yang, M Wu, Y Guo, W Guo, L Zhong, X Cai, A Dai, W Jang, ... Elife 8, e50279, 2019 | 467 | 2019 |
Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function LA Mirny, EI Shakhnovich Journal of molecular biology 291 (1), 177-196, 1999 | 467 | 1999 |
Protein folding theory: from lattice to all-atom models L Mirny, E Shakhnovich Annual review of biophysics and biomolecular structure 30 (1), 361-396, 2001 | 459 | 2001 |
Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet E Shakhnovich Chemical reviews 106 (5), 1559-1588, 2006 | 435 | 2006 |
SMoG: de novo design method based on simple, fast, and accurate free energy estimates. 1. Methodology and supporting evidence RS DeWitte, EI Shakhnovich Journal of the American Chemical Society 118 (47), 11733-11744, 1996 | 413 | 1996 |
Formation of unique structure in polypeptide chains: theoretical investigation with the aid of a replica approach EI Shakhnovich, AM Gutin Biophysical chemistry 34 (3), 187-199, 1989 | 408 | 1989 |
Protein folding bottlenecks: A lattice Monte Carlo simulation E Shakhnovich, G Farztdinov, AM Gutin, M Karplus Physical review letters 67 (12), 1665, 1991 | 377 | 1991 |
Discrete molecular dynamics studies of the folding of a protein-like model NV Dokholyan, SV Buldyrev, HE Stanley, EI Shakhnovich Folding and design 3 (6), 577-587, 1998 | 370 | 1998 |
A test of lattice protein folding algorithms. K Yue, KM Fiebig, PD Thomas, HS Chan, EI Shakhnovich, KA Dill Proceedings of the National Academy of Sciences 92 (1), 325-329, 1995 | 359 | 1995 |
Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition EI Shakhnovich, AV Finkelstein Biopolymers: Original Research on Biomolecules 28 (10), 1667-1680, 1989 | 358 | 1989 |
Topological determinants of protein folding NV Dokholyan, L Li, F Ding, EI Shakhnovich Proceedings of the National Academy of Sciences 99 (13), 8637-8641, 2002 | 357 | 2002 |