Year |
Citation |
Score |
2017 |
Gavazzi D, Portman JJ. The Folding Mechanism and Kinetics of the Domains of α-Spectrin: Results from a Variational Model Biophysical Journal. 112: 497a-498a. DOI: 10.1016/J.Bpj.2016.11.2691 |
0.37 |
|
2017 |
Ruzmetov TA, Portman JJ. Exploring the Role of Flexibility in Binding Kinetics and Affinity of pKID-Kix through Coarse Grained Simulations Biophysical Journal. 112: 208a. DOI: 10.1016/J.Bpj.2016.11.1147 |
0.491 |
|
2016 |
Nandigrami P, Portman JJ. Comparing allosteric transitions in the domains of calmodulin through coarse-grained simulations. The Journal of Chemical Physics. 144: 105102. PMID 26979706 DOI: 10.1063/1.4943130 |
0.46 |
|
2016 |
Nandigrami P, Portman JJ. Coarse-grained molecular simulations of allosteric cooperativity. The Journal of Chemical Physics. 144: 105101. PMID 26979705 DOI: 10.1063/1.4943043 |
0.489 |
|
2016 |
Nandigrami P, Portman JJ. Calculating Multi-Body Cooperativity Parameters for Calcium Binding to Calmodulin through Coarse-Grained Simulations Biophysical Journal. 110: 55a. DOI: 10.1016/J.Bpj.2015.11.362 |
0.477 |
|
2014 |
Ruzmetov T, Portman JJ. Influence of Desolvation Barriers in Coupled Folding and Binding Kinetics of pKID-KIX Biophysical Journal. 106: 482a. DOI: 10.1016/J.Bpj.2013.11.2724 |
0.494 |
|
2013 |
Tripathi S, Portman JJ. Allostery and folding of the N-terminal receiver domain of protein NtrC. The Journal of Physical Chemistry. B. 117: 13182-93. PMID 23961720 DOI: 10.1021/Jp403181P |
0.427 |
|
2013 |
Nandigrami P, Portman JJ. Exploring Kinetic Scenarios for Allosteric Transitions of Calmodulin through Coarse-Grained Simulations Biophysical Journal. 104: 58a. DOI: 10.1016/J.Bpj.2012.11.358 |
0.464 |
|
2012 |
Ray S, Qureshi MH, Malcolm D, Celik U, Portman JJ, Balci H. What Structural Elements make a G-Quadruplex Physiologically Viable? Biophysical Journal. 102: 483a. DOI: 10.1016/J.Bpj.2011.11.2646 |
0.448 |
|
2012 |
Nandigrami P, Portman JJ. Conformational Flexibility and the Mechanism of Allosteric Transitions in Calmodulin Biophysical Journal. 102: 449a. DOI: 10.1016/J.Bpj.2011.11.2462 |
0.514 |
|
2011 |
Tripathi S, Portman JJ. Conformational flexibility and the mechanisms of allosteric transitions in topologically similar proteins. The Journal of Chemical Physics. 135: 075104. PMID 21861587 DOI: 10.1063/1.3625636 |
0.443 |
|
2011 |
Tripathi S, Portman JJ. Allostery and Folding Mechanisms of the N-Terminal Receiver Domain of Protein NTRC Biophysical Journal. 100: 18a. DOI: 10.1016/J.Bpj.2010.12.308 |
0.47 |
|
2010 |
Portman JJ. Cooperativity and protein folding rates. Current Opinion in Structural Biology. 20: 11-5. PMID 20093004 DOI: 10.1016/J.Sbi.2009.12.013 |
0.522 |
|
2009 |
Tripathi S, Portman JJ. Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin. Proceedings of the National Academy of Sciences of the United States of America. 106: 2104-9. PMID 19190183 DOI: 10.1073/Pnas.0806872106 |
0.466 |
|
2008 |
Qi X, Portman JJ. Capillarity-like growth of protein folding nuclei. Proceedings of the National Academy of Sciences of the United States of America. 105: 11164-9. PMID 18678894 DOI: 10.1073/Pnas.0711527105 |
0.448 |
|
2008 |
Tripathi S, Portman JJ. Inherent flexibility and protein function: The open/closed conformational transition in the N-terminal domain of calmodulin. The Journal of Chemical Physics. 128: 205104. PMID 18513047 DOI: 10.1063/1.2928634 |
0.514 |
|
2008 |
Shen T, Zong C, Portman JJ, Wolynes PG. Variationally determined free energy profiles for structural models of proteins: characteristic temperatures for folding and trapping. The Journal of Physical Chemistry. B. 112: 6074-82. PMID 18376882 DOI: 10.1021/Jp076280N |
0.628 |
|
2007 |
Qi X, Portman JJ. Excluded volume, local structural cooperativity, and the polymer physics of protein folding rates. Proceedings of the National Academy of Sciences of the United States of America. 104: 10841-6. PMID 17569785 DOI: 10.1073/Pnas.0609321104 |
0.511 |
|
2003 |
Portman JJ. Non-Gaussian dynamics from a simulation of a short peptide: Loop closure rates and effective diffusion coefficients Journal of Chemical Physics. 118: 2381-2391. DOI: 10.1063/1.1532728 |
0.365 |
|
2001 |
Portman JJ, Takada S, Wolynes PG. Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics Journal of Chemical Physics. 114: 5082-5096. DOI: 10.1063/1.1334663 |
0.586 |
|
2001 |
Portman JJ, Takada S, Wolynes PG. Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach Journal of Chemical Physics. 114: 5069-5081. DOI: 10.1063/1.1334662 |
0.606 |
|
2000 |
Shoemaker BA, Portman JJ, Wolynes PG. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proceedings of the National Academy of Sciences of the United States of America. 97: 8868-73. PMID 10908673 DOI: 10.1073/Pnas.160259697 |
0.639 |
|
1999 |
Portman JJ, Wolynes PG. Complementary variational approximations for intermittency and reaction dynamics in fluctuating environments Journal of Physical Chemistry A. 103: 10602-10610. DOI: 10.1021/Jp992334K |
0.459 |
|
1998 |
Portman JJ, Takada S, Wolynes PG. Variational theory for site resolved protein folding free energy surfaces Physical Review Letters. 81: 5237-5240. DOI: 10.1103/Physrevlett.81.5237 |
0.588 |
|
1997 |
Takada S, Portman JJ, Wolynes PG. An elementary mode coupling theory of random heteropolymer dynamics. Proceedings of the National Academy of Sciences of the United States of America. 94: 2318-21. PMID 9122192 DOI: 10.1073/Pnas.94.6.2318 |
0.469 |
|
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