| Principles of docking: An overview of search algorithms and a guide to scoring functions I Halperin, B Ma, H Wolfson, R Nussinov Proteins: Structure, Function, and Bioinformatics 47 (4), 409-443, 2002 | 1830 | 2002 |
| Is allostery an intrinsic property of all dynamic proteins? K Gunasekaran, B Ma, R Nussinov Proteins: Structure, Function, and Bioinformatics 57 (3), 433-443, 2004 | 1022 | 2004 |
| Aβ (1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease Y Xiao, B Ma, D McElheny, S Parthasarathy, F Long, M Hoshi, R Nussinov, ... Nature structural & molecular biology 22 (6), 499-505, 2015 | 872 | 2015 |
| Principles of protein− protein interactions: what are the preferred ways for proteins to interact? O Keskin, A Gursoy, B Ma, R Nussinov Chemical reviews 108 (4), 1225-1244, 2008 | 822 | 2008 |
| Folding funnels, binding funnels, and protein function CJ Tsai, S Kumar, B Ma, R Nussinov Protein Science 8 (6), 1181-1190, 1999 | 811 | 1999 |
| Protein–protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces B Ma, T Elkayam, H Wolfson, R Nussinov Proceedings of the National Academy of Sciences 100 (10), 5772-5777, 2003 | 750 | 2003 |
| Folding funnels and binding mechanisms B Ma, S Kumar, CJ Tsai, R Nussinov Protein engineering 12 (9), 713-720, 1999 | 729 | 1999 |
| Folding and binding cascades: dynamic landscapes and population shifts S Kumar, B Ma, CJ Tsai, N Sinha, R Nussinov Protein science 9 (1), 10-19, 2000 | 714 | 2000 |
| Hot regions in protein–protein interactions: the organization and contribution of structurally conserved hot spot residues O Keskin, B Ma, R Nussinov Journal of molecular biology 345 (5), 1281-1294, 2005 | 654 | 2005 |
| Amyloid oligomers: A joint experimental/computational perspective on Alzheimer’s disease, Parkinson’s disease, type II diabetes, and amyotrophic lateral sclerosis PH Nguyen, A Ramamoorthy, BR Sahoo, J Zheng, P Faller, JE Straub, ... Chemical reviews 121 (4), 2545-2647, 2021 | 533 | 2021 |
| Multiple diverse ligands binding at a single protein site: a matter of pre‐existing populations B Ma, M Shatsky, HJ Wolfson, R Nussinov Protein science 11 (2), 184-197, 2002 | 530 | 2002 |
| Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ16–22, Aβ16–35, and Aβ10–35): sequence effects B Ma, R Nussinov Proceedings of the National Academy of Sciences 99 (22), 14126-14131, 2002 | 515 | 2002 |
| The origin of allosteric functional modulation: multiple pre-existing pathways A Del Sol, CJ Tsai, B Ma, R Nussinov Structure 17 (8), 1042-1050, 2009 | 425 | 2009 |
| Folding and binding cascades: shifts in energy landscapes CJ Tsai, B Ma, R Nussinov Proceedings of the National Academy of Sciences 96 (18), 9970-9972, 1999 | 417 | 1999 |
| Conservation of polar residues as hot spots at protein interfaces Z Hu, B Ma, H Wolfson, R Nussinov Proteins: Structure, Function, and Bioinformatics 39 (4), 331-342, 2000 | 415 | 2000 |
| Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell G Wei, W Xi, R Nussinov, B Ma Chemical reviews 116 (11), 6516-6551, 2016 | 375 | 2016 |
| Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states Y Miller, B Ma, R Nussinov Proceedings of the National Academy of Sciences 107 (21), 9490-9495, 2010 | 358 | 2010 |
| Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape Y Miller, B Ma, R Nussinov Chemical reviews 110 (8), 4820-4838, 2010 | 331 | 2010 |
| Simulations as analytical tools to understand protein aggregation and predict amyloid conformation B Ma, R Nussinov Current opinion in chemical biology 10 (5), 445-452, 2006 | 266 | 2006 |
| Protein–protein interactions: hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: implications for docking X Li, O Keskin, B Ma, R Nussinov, J Liang Journal of molecular biology 344 (3), 781-795, 2004 | 257 | 2004 |
