Molecular crowding enhances native state stability and refolding rates of globular proteins MS Cheung, D Klimov, D Thirumalai Proceedings of the National Academy of Sciences 102 (13), 4753-4758, 2005 | 643 | 2005 |
Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties T Veitshans, D Klimov, D Thirumalai Folding and Design 2 (1), 1-22, 1997 | 469 | 1997 |
Dissecting the assembly of Aβ16–22 amyloid peptides into antiparallel β sheets DK Klimov, D Thirumalai Structure 11 (3), 295-307, 2003 | 433 | 2003 |
Emerging ideas on the molecular basis of protein and peptide aggregation D Thirumalai, DK Klimov, RI Dima Current opinion in structural biology 13 (2), 146-159, 2003 | 421 | 2003 |
Mechanisms and kinetics of β-hairpin formation DK Klimov, D Thirumalai Proceedings of the National Academy of Sciences 97 (6), 2544-2549, 2000 | 306 | 2000 |
Viscosity dependence of the folding rates of proteins DK Klimov, D Thirumalai Physical review letters 79 (2), 317, 1997 | 272 | 1997 |
EARLY EVENTS IN RNA FOLDING D Thirumalai, N Lee, SA Woodson, DK Klimov Annual review of physical chemistry 52 (1), 751-762, 2001 | 253 | 2001 |
Criterion that determines the foldability of proteins DK Klimov, D Thirumalai Physical review letters 76 (21), 4070, 1996 | 252 | 1996 |
Simulations of β-hairpin folding confined to spherical pores using distributed computing DK Klimov, D Newfield, D Thirumalai Proceedings of the National Academy of Sciences 99 (12), 8019-8024, 2002 | 215 | 2002 |
Native topology determines force-induced unfolding pathways in globular proteins DK Klimov, D Thirumalai Proceedings of the National Academy of Sciences 97 (13), 7254-7259, 2000 | 196 | 2000 |
Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models D Thirumalai, DK Klimov Current opinion in structural Biology 9 (2), 197-207, 1999 | 193 | 1999 |
Aqueous urea solution destabilizes Aβ16–22 oligomers DK Klimov, JE Straub, D Thirumalai Proceedings of the National Academy of Sciences 101 (41), 14760-14765, 2004 | 188 | 2004 |
Cooperativity in protein folding: from lattice models with sidechains to real proteins DK Klimov, D Thirumalai Folding and Design 3 (2), 127-139, 1998 | 162 | 1998 |
Factors governing the foldability of proteins DK Klimov, D Thirumalai Proteins: Structure, Function, and Bioinformatics 26 (4), 411-441, 1996 | 148 | 1996 |
Stretching single-domain proteins: phase diagram and kinetics of force-induced unfolding DK Klimov, D Thirumalai Proceedings of the National Academy of Sciences 96 (11), 6166-6170, 1999 | 131 | 1999 |
Lattice models for proteins reveal multiple folding nuclei for nucleation-collapse mechanism DK Klimov, D Thirumalai Journal of Molecular Biology 282 (2), 471-492, 1998 | 121 | 1998 |
Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules D Thirumalai, DK Klimov, SA Woodson Theoretical Chemistry Accounts 96, 14-22, 1997 | 118 | 1997 |
Replica exchange simulations of the thermodynamics of Aβ fibril growth T Takeda, DK Klimov Biophysical journal 96 (2), 442-452, 2009 | 114 | 2009 |
Probing the mechanisms of fibril formation using lattice models MS Li, DK Klimov, JE Straub, D Thirumalai The Journal of chemical physics 129 (17), 2008 | 112 | 2008 |
Caging helps proteins fold D Thirumalai, DK Klimov, GH Lorimer Proceedings of the National Academy of Sciences 100 (20), 11195-11197, 2003 | 105 | 2003 |