Year |
Citation |
Score |
2015 |
Cumberworth A, Bui JM, Gsponer J. Free energies of solvation in the context of protein folding: Implications for implicit and explicit solvent models. Journal of Computational Chemistry. PMID 26558440 DOI: 10.1002/Jcc.24235 |
0.336 |
|
2014 |
Thomas D, Koopmans T, Lakowski TM, Kreinin H, Vhuiyan MI, Sedlock SA, Bui JM, Martin NI, Frankel A. Protein arginine N-methyltransferase substrate preferences for different nη-substituted arginyl peptides. Chembiochem : a European Journal of Chemical Biology. 15: 1607-13. PMID 25044481 DOI: 10.1002/Cbic.201402045 |
0.32 |
|
2014 |
Bui JM, Gsponer J. Phosphorylation of an intrinsically disordered segment in Ets1 shifts conformational sampling toward binding-competent substates. Structure (London, England : 1993). 22: 1196-203. PMID 25017730 DOI: 10.1016/J.Str.2014.06.002 |
0.47 |
|
2009 |
Bui JM, Gsponer J, Vendruscolo M, Dobson CM. Analysis of sub-tauc and supra-tauc motions in protein Gbeta1 using molecular dynamics simulations. Biophysical Journal. 97: 2513-20. PMID 19883594 DOI: 10.1016/J.Bpj.2009.07.061 |
0.45 |
|
2008 |
Gsponer J, Christodoulou J, Cavalli A, Bui JM, Richter B, Dobson CM, Vendruscolo M. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure (London, England : 1993). 16: 736-46. PMID 18462678 DOI: 10.1016/J.Str.2008.02.017 |
0.366 |
|
2008 |
Bui JM, Andrew McCammon J. Intrinsic conformational flexibility of acetylcholinesterase. Chemico-Biological Interactions. 175: 303-4. PMID 18452905 DOI: 10.1016/J.Cbi.2008.03.002 |
0.446 |
|
2006 |
Bui JM, McCammon JA. Protein complex formation by acetylcholinesterase and the neurotoxin fasciculin-2 appears to involve an induced-fit mechanism. Proceedings of the National Academy of Sciences of the United States of America. 103: 15451-6. PMID 17021015 DOI: 10.1073/Pnas.0605355103 |
0.613 |
|
2006 |
Bui JM, Radic Z, Taylor P, McCammon JA. Conformational transitions in protein-protein association: binding of fasciculin-2 to acetylcholinesterase. Biophysical Journal. 90: 3280-7. PMID 16473897 DOI: 10.1529/Biophysj.105.075564 |
0.603 |
|
2005 |
Bui JM, McCammon JA. Acetylcholinesterase: pivotal roles of its long omega loop (Cys69-Cys96) in regulating substrate binding. Chemico-Biological Interactions. 157: 357-9. PMID 16429484 DOI: 10.1016/J.Cbi.2005.10.049 |
0.397 |
|
2005 |
Senapati S, Bui JM, McCammon JA. Induced fit in mouse acetylcholinesterase upon binding a femtomolar inhibitor: a molecular dynamics study. Journal of Medicinal Chemistry. 48: 8155-62. PMID 16366597 DOI: 10.1021/Jm050669M |
0.592 |
|
2005 |
Minh DD, Bui JM, Chang CE, Jain T, Swanson JM, McCammon JA. The entropic cost of protein-protein association: a case study on acetylcholinesterase binding to fasciculin-2. Biophysical Journal. 89: L25-7. PMID 16100267 DOI: 10.1529/Biophysj.105.069336 |
0.6 |
|
2004 |
Bui JM, Tai K, McCammon JA. Acetylcholinesterase: enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2. Journal of the American Chemical Society. 126: 7198-205. PMID 15186156 DOI: 10.1021/Ja0485715 |
0.622 |
|
2003 |
Bui JM, Henchman RH, McCammon JA. The dynamics of ligand barrier crossing inside the acetylcholinesterase gorge. Biophysical Journal. 85: 2267-72. PMID 14507691 DOI: 10.1016/S0006-3495(03)74651-7 |
0.617 |
|
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