Year |
Citation |
Score |
2012 |
Craig PO, Hoffman RM, Lätzer J, Weinkam P, Komives EA, Wolynes PG. Analysis of Native H/D Exchange Dynamics in EX1/EX2 Conditions using Structure Based Model Simulations Biophysical Journal. 102: 448a. DOI: 10.1016/J.Bpj.2011.11.2459 |
0.713 |
|
2011 |
Craig PO, Lätzer J, Weinkam P, Hoffman RM, Ferreiro DU, Komives EA, Wolynes PG. Prediction of native-state hydrogen exchange from perfectly funneled energy landscapes. Journal of the American Chemical Society. 133: 17463-72. PMID 21913704 DOI: 10.1021/Ja207506Z |
0.643 |
|
2010 |
Craig PO, Lätzer J, Weinkam P, Hoffman R, Komives E, Wolynes P. Prediction of H Exchange from Perfectly Funneled Structure Based Models Biophysical Journal. 98: 638a. DOI: 10.1016/J.Bpj.2009.12.3493 |
0.737 |
|
2009 |
Hegler JA, Lätzer J, Shehu A, Clementi C, Wolynes PG. Restriction versus guidance in protein structure prediction. Proceedings of the National Academy of Sciences of the United States of America. 106: 15302-7. PMID 19706384 DOI: 10.1073/Pnas.0907002106 |
0.633 |
|
2008 |
Lätzer J, Shen T, Wolynes PG. Conformational switching upon phosphorylation: a predictive framework based on energy landscape principles. Biochemistry. 47: 2110-22. PMID 18198897 DOI: 10.1021/Bi701350V |
0.624 |
|
2007 |
Sutto L, Lätzer J, Hegler JA, Ferreiro DU, Wolynes PG. Consequences of localized frustration for the folding mechanism of the IM7 protein. Proceedings of the National Academy of Sciences of the United States of America. 104: 19825-30. PMID 18077415 DOI: 10.1073/Pnas.0709922104 |
0.676 |
|
2007 |
Lätzer J, Papoian GA, Prentiss MC, Komives EA, Wolynes PG. Induced fit, folding, and recognition of the NF-kappaB-nuclear localization signals by IkappaBalpha and IkappaBbeta. Journal of Molecular Biology. 367: 262-74. PMID 17257619 DOI: 10.1016/J.Jmb.2006.12.006 |
0.662 |
|
2006 |
Lätzer J, Eastwood MP, Wolynes PG. Simulation studies of the fidelity of biomolecular structure ensemble recreation. The Journal of Chemical Physics. 125: 214905. PMID 17166047 DOI: 10.1063/1.2375121 |
0.539 |
|
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