Year |
Citation |
Score |
2022 |
Dong X, Qin LY, Gong Z, Qin S, Zhou HX, Tang C. Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex. The Journal of Physical Chemistry Letters. 13: 792-800. PMID 35044179 DOI: 10.1021/acs.jpclett.1c03794 |
0.32 |
|
2020 |
Ghosh A, Zhou HX. Determinants for Fusion Speed of Biomolecular Droplets. Angewandte Chemie (International Ed. in English). PMID 32767698 DOI: 10.1002/Anie.202006711 |
0.323 |
|
2020 |
Paulino J, Yi M, Hung I, Gan Z, Wang X, Chekmenev EY, Zhou HX, Cross TA. Functional stability of water wire-carbonyl interactions in an ion channel. Proceedings of the National Academy of Sciences of the United States of America. PMID 32414918 DOI: 10.1073/Pnas.2001083117 |
0.318 |
|
2019 |
Ghosh A, Mazarakos K, Zhou HX. Three archetypical classes of macromolecular regulators of protein liquid-liquid phase separation. Proceedings of the National Academy of Sciences of the United States of America. PMID 31506351 DOI: 10.1073/Pnas.1907849116 |
0.303 |
|
2019 |
Qin S, Zhou HX. Calculation of Second Virial Coefficients of Atomistic Proteins Using Fast Fourier Transform. The Journal of Physical Chemistry. B. PMID 31490691 DOI: 10.1021/Acs.Jpcb.9B06808 |
0.361 |
|
2019 |
Nguemaha V, Qin S, Zhou H. Transfer Free Energies of Test Proteins Into Crowded Protein Solutions Have Simple Dependence on Crowder Concentration Frontiers in Molecular Biosciences. 6: 39. PMID 31192219 DOI: 10.3389/Fmolb.2019.00039 |
0.388 |
|
2019 |
Wu D, Zhou HX. Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein. Scientific Reports. 9: 6172. PMID 30992509 DOI: 10.1038/S41598-019-42717-6 |
0.364 |
|
2019 |
Ghosh A, Smith PES, Qin S, Yi M, Zhou HX. Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein. Biochemistry. PMID 30950267 DOI: 10.1021/Acs.Biochem.9B00154 |
0.417 |
|
2019 |
Paulino J, Pang X, Hung I, Zhou HX, Cross TA. Influenza A M2 Channel Clustering at High Protein/Lipid Ratios: Viral Budding Implications. Biophysical Journal. PMID 30819568 DOI: 10.1016/J.Bpj.2019.01.042 |
0.385 |
|
2018 |
Guo C, Zhou HX. Fatty Acids Compete with Aβ in Binding to Serum Albumin by Quenching its Conformational Flexibility. Biophysical Journal. PMID 30580919 DOI: 10.1016/J.Bpj.2018.11.3133 |
0.319 |
|
2018 |
Nguemaha V, Qin S, Zhou H. Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein-Crowder Attraction. Journal of Physical Chemistry B. 122: 11262-11270. PMID 30230839 DOI: 10.1021/Acs.Jpcb.8B07066 |
0.388 |
|
2018 |
Hicks A, Zhou HX. Temperature-induced collapse of a disordered peptide observed by three sampling methods in molecular dynamics simulations. The Journal of Chemical Physics. 149: 072313. PMID 30134733 DOI: 10.1063/1.5027409 |
0.311 |
|
2018 |
Zhou HX, Nguemaha V, Mazarakos K, Qin S. Why Do Disordered and Structured Proteins Behave Differently in Phase Separation? Trends in Biochemical Sciences. PMID 29716768 DOI: 10.1016/J.Tibs.2018.03.007 |
0.338 |
|
2018 |
Nguemaha V, Zhou HX. Liquid-Liquid Phase Separation of Patchy Particles Illuminates Diverse Effects of Regulatory Components on Protein Droplet Formation. Scientific Reports. 8: 6728. PMID 29712961 DOI: 10.1038/S41598-018-25132-1 |
0.327 |
|
2018 |
Banks A, Qin S, Weiss KL, Stanley CB, Zhou HX. Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding. Biophysical Journal. 114: 1067-1079. PMID 29539394 DOI: 10.1016/J.Bpj.2018.01.011 |
0.422 |
|
2018 |
Campitelli P, Guo J, Zhou HX, Ozkan SB. A Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1. The Journal of Physical Chemistry. B. PMID 29361231 DOI: 10.1021/Acs.Jpcb.7B11971 |
0.355 |
|
2018 |
Zhou HX, Pang X. Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation. Chemical Reviews. PMID 29319301 DOI: 10.1021/Acs.Chemrev.7B00305 |
0.412 |
|
2017 |
Nguyen TH, Zhou HX, Minh DDL. Using the fast fourier transform in binding free energy calculations. Journal of Computational Chemistry. PMID 29270990 DOI: 10.1002/Jcc.25139 |
0.341 |
|
2017 |
Ou L, Matthews M, Pang X, Zhou HX. The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase. The Febs Journal. PMID 28805312 DOI: 10.1111/Febs.14197 |
0.387 |
|
2017 |
Pang X, Zhou HX. Structural Modeling for the Open State of an NMDA Receptor. Journal of Structural Biology. PMID 28739483 DOI: 10.1016/J.Jsb.2017.07.005 |
0.334 |
|
2017 |
Pang X, Zhou HX. Rate Constants and Mechanisms of Protein-Ligand Binding. Annual Review of Biophysics. PMID 28375732 DOI: 10.1146/Annurev-Biophys-070816-033639 |
0.355 |
|
2017 |
Zhou HX. Gating Motions and Stationary Gating Properties of Ionotropic Glutamate Receptors: Computation Meets Electrophysiology. Accounts of Chemical Research. PMID 28186717 DOI: 10.1021/Acs.Accounts.6B00598 |
0.399 |
|
2017 |
Campitelli P, Zhou H, Ghirlanda G, Ozkan SB. Dynamic Flexibility Index Sheds Light on Pin1 Allostery Biophysical Journal. 112: 317a. DOI: 10.1016/J.Bpj.2016.11.1720 |
0.376 |
|
2016 |
Guo C, Zhou HX. Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791125 DOI: 10.1073/Pnas.1610142113 |
0.327 |
|
2016 |
Qin S, Zhou HX. Protein folding, binding, and droplet formation in cell-like conditions. Current Opinion in Structural Biology. 43: 28-37. PMID 27771543 DOI: 10.1016/J.Sbi.2016.10.006 |
0.415 |
|
2016 |
Dai J, Zhou HX. Semiclosed Conformations of the Ligand-Binding Domains of NMDA Receptors during Stationary Gating. Biophysical Journal. 111: 1418-1428. PMID 27705765 DOI: 10.1016/J.Bpj.2016.08.010 |
0.364 |
|
2016 |
Guo J, Zhou HX. Allosteric activation of SENP1 by SUMO1 β-grasp domain involves a dock-and-coalesce mechanism. Elife. 5. PMID 27576863 DOI: 10.7554/Elife.18249 |
0.355 |
|
2016 |
Batra J, Tjong H, Zhou HX. Electrostatic effects on the folding stability of FKBP12. Protein Engineering, Design & Selection : Peds. PMID 27381026 DOI: 10.1093/Protein/Gzw014 |
0.384 |
|
2016 |
Qin S, Zhou HX. Fast Method for Computing Chemical Potentials and Liquid-Liquid Phase Equilibria of Macromolecular Solutions. The Journal of Physical Chemistry. B. PMID 27327881 DOI: 10.1021/Acs.Jpcb.6B01607 |
0.304 |
|
2016 |
Pang X, Zhou HX. Mechanism and rate constants of the Cdc42 GTPase binding with intrinsically disordered effectors. Proteins. PMID 26879470 DOI: 10.1002/Prot.25018 |
0.38 |
|
2016 |
Guo J, Zhou HX. Protein Allostery and Conformational Dynamics. Chemical Reviews. PMID 26876046 DOI: 10.1021/Acs.Chemrev.5B00590 |
0.411 |
|
2016 |
Wright AK, Batsomboon P, Dai J, Hung I, Zhou HX, Dudley GB, Cross TA. Differential Binding of Rimantadine Enantiomers to Influenza A M2 Proton Channel. Journal of the American Chemical Society. PMID 26804976 DOI: 10.1021/Jacs.5B13129 |
0.345 |
|
2016 |
Banks A, Weiss K, Stanley C, Zhou H. Small Angle Neutron Scattering of the Intrinsically Disordered Protein FlgM under Crowded Conditions Biophysical Journal. 110: 560a. DOI: 10.1016/J.Bpj.2015.11.2993 |
0.345 |
|
2016 |
Smith PES, Zhou H. Conformations and Exchange Dynamics of FlgM, an Intrinsically Disordered Protein, in Dilute and Crowded Conditions Studied by NMR Spectroscopy Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.2985 |
0.395 |
|
2016 |
Wu D, Zhou H. Characterizing protein-protein Nonspecific Interactions by Static Light Scattering Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.298 |
0.381 |
|
2016 |
Cross TA, Fu R, Ekanayake EV, Miao Y, Paulino J, Anna W, Dai J, Zhou H. Functional, Dynamic and Structural Understanding of M2 Proton Channel from Influenza A and its Inhibition Biophysical Journal. 110: 192a. DOI: 10.1016/J.Bpj.2015.11.1069 |
0.366 |
|
2015 |
Miao Y, Fu R, Zhou HX, Cross TA. Dynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional Mechanism. Structure (London, England : 1993). PMID 26526851 DOI: 10.1016/J.Str.2015.09.011 |
0.348 |
|
2015 |
Pang X, Zhou HX. Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A. Biophysical Journal. 109: 1706-15. PMID 26488662 DOI: 10.1016/J.Bpj.2015.08.039 |
0.317 |
|
2015 |
Guo J, Zhou HX. Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions. Biophysical Journal. 108: 2771-4. PMID 26083915 DOI: 10.1016/J.Bpj.2015.04.035 |
0.34 |
|
2015 |
Dai J, Wollmuth LP, Zhou HX. Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors. The Journal of Physical Chemistry. B. PMID 25793415 DOI: 10.1021/Acs.Jpcb.5B00521 |
0.333 |
|
2015 |
Guo J, Pang X, Zhou H. Two Pathways Mediate Inter-Domain Allosteric Regulation in Pin1 Structure. 23: 237-247. PMID 25543254 DOI: 10.1016/J.Str.2014.11.009 |
0.365 |
|
2015 |
Dai J, Zhou HX. Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors. Structure (London, England : 1993). 23: 228-36. PMID 25543253 DOI: 10.1016/J.Str.2014.11.012 |
0.312 |
|
2015 |
Qin S, Zhou H. The Nonrandom Nature of Weak Interactions between Proteins and Bystander Macromolecules in Cellular Environments Biophysical Journal. 108: 1-6. DOI: 10.1016/J.Bpj.2014.11.653 |
0.4 |
|
2015 |
Ghosh A, Zhou H. Macromolecular Crowder and Ligand Compete for the Closed Domain Cleft of Maltose Binding Protein Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.342 |
0.381 |
|
2015 |
Miao Y, Fu R, Zhou H, Qin H, Cross TA. pH Titration and Acid Activation of the Full-Length Influenza a M2 Proton Channel in Lipid Bilayers Biophysical Journal. 108: 246a. DOI: 10.1016/J.Bpj.2014.11.1365 |
0.306 |
|
2014 |
Qin S, Zhou H. Further Development of the FFT-based Method for Atomistic Modeling of Protein Folding and Binding under Crowding: Optimization of Accuracy and Speed Journal of Chemical Theory and Computation. 10: 2824-2835. PMID 25061446 DOI: 10.1021/Ct5001878 |
0.354 |
|
2014 |
Greives N, Zhou H. Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit Proceedings of the National Academy of Sciences of the United States of America. 111: 10197-10202. PMID 24982141 DOI: 10.1073/Pnas.1407545111 |
0.405 |
|
2014 |
Kazi R, Dai J, Sweeney C, Zhou HX, Wollmuth LP. Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents. Nature Neuroscience. 17: 914-22. PMID 24859202 DOI: 10.1038/Nn.3724 |
0.317 |
|
2014 |
Pang X, Zhou HX. Design rules for selective binding of nuclear localization signals to minor site of importin α Plos One. 9. PMID 24609064 DOI: 10.1371/Journal.Pone.0091025 |
0.308 |
|
2014 |
Jean-Francois FL, Dai J, Yu L, Myrick A, Rubin E, Fajer PG, Song L, Zhou HX, Cross TA. Binding of MgtR, a Salmonella transmembrane regulatory peptide, to MgtC, a Mycobacterium tuberculosis virulence factor: a structural study. Journal of Molecular Biology. 426: 436-46. PMID 24140750 DOI: 10.1016/J.Jmb.2013.10.014 |
0.327 |
|
2014 |
Pang X, Zhou HX. Distinct mechanisms of a phosphotyrosyl peptide binding to two SH2 domains Journal of Theoretical and Computational Chemistry. 13. DOI: 10.1142/S0219633614400033 |
0.302 |
|
2014 |
Kazi R, Dai J, Daniel M, Zhou H, Wollmuth LP. Energetic Coupling of the Ligand Binding Domain to Pore Opening in NMDA Receptors Biophysical Journal. 106: 29a. DOI: 10.1016/J.Bpj.2013.11.212 |
0.332 |
|
2013 |
Qin S, Zhou H. Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins. Journal of Physical Chemistry Letters. 4: 3429-3434. PMID 24312701 DOI: 10.1021/Jz401817X |
0.394 |
|
2013 |
Qin S, Zhou H. FFT-Based Method for Modeling Protein Folding and Binding under Crowding: Benchmarking on Ellipsoidal and All-Atom Crowders Journal of Chemical Theory and Computation. 9: 4633-4643. PMID 24187527 DOI: 10.1021/Ct4005195 |
0.418 |
|
2013 |
Miklos AC, Sumpter M, Zhou HX. Competitive interactions of ligands and macromolecular crowders with maltose binding protein. Plos One. 8: e74969. PMID 24124463 DOI: 10.1371/Journal.Pone.0074969 |
0.41 |
|
2013 |
Heymann G, Dai J, Li M, Silberberg SD, Zhou HX, Swartz KJ. Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels. Proceedings of the National Academy of Sciences of the United States of America. 110: E4045-54. PMID 24082111 DOI: 10.1073/Pnas.1311071110 |
0.33 |
|
2013 |
Dong H, Yi M, Cross TA, Zhou HX. Ab initio calculations and validation of the pH-dependent structures of the His37-Trp41 quartet, the heart of acid activation and proton conductance in the M2 protein of Influenza A virus. Chemical Science (Royal Society of Chemistry : 2010). 4: 2776-2787. PMID 23930201 DOI: 10.1039/C3Sc50293G |
0.344 |
|
2013 |
Qin S, Mittal J, Zhou HX. Folding free energy surfaces of three small proteins under crowding: validation of the postprocessing method by direct simulation. Physical Biology. 10: 045001. PMID 23912849 DOI: 10.1088/1478-3975/10/4/045001 |
0.38 |
|
2013 |
Qin S, Zhou H. Using the concept of transient complex for affinity predictions in CAPRI rounds 20-27 and beyond. Proteins. 81: 2229-2236. PMID 23873496 DOI: 10.1002/Prot.24366 |
0.377 |
|
2013 |
Zhou HX, Bates PA. Modeling protein association mechanisms and kinetics. Current Opinion in Structural Biology. 23: 887-93. PMID 23850142 DOI: 10.1016/J.Sbi.2013.06.014 |
0.359 |
|
2013 |
Moretti R, Fleishman SJ, Agius R, Torchala M, Bates PA, Kastritis PL, Rodrigues JP, Trellet M, Bonvin AM, Cui M, Rooman M, Gillis D, Dehouck Y, Moal I, Romero-Durana M, ... ... Zhou HX, et al. Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions. Proteins. 81: 1980-7. PMID 23843247 DOI: 10.1002/Prot.24356 |
0.346 |
|
2013 |
Zhou H, Qin S. Simulation and Modeling of Crowding Effects on the Thermodynamic and Kinetic Properties of Proteins with Atomic Details. Biophysical Reviews. 5: 207-215. PMID 23710260 DOI: 10.1007/S12551-013-0101-7 |
0.425 |
|
2013 |
Dai J, Zhou HX. An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions. Biophysical Journal. 104: 2170-81. PMID 23708357 DOI: 10.1016/J.Bpj.2013.04.013 |
0.326 |
|
2013 |
Qin S, Zhou H. PI2PE: A Suite of Web Servers for Predictions Ranging From Protein Structure to Binding Kinetics. Biophysical Reviews. 5: 41-46. PMID 23526172 DOI: 10.1007/S12551-012-0086-7 |
0.398 |
|
2013 |
Zhou HX, Cross TA. Influences of membrane mimetic environments on membrane protein structures Annual Review of Biophysics. 42: 361-392. PMID 23451886 DOI: 10.1146/Annurev-Biophys-083012-130326 |
0.329 |
|
2013 |
Zhou H. Influence of crowded cellular environments on protein folding, binding, and oligomerization: Biological consequences and potentials of atomistic modeling Febs Letters. 587: 1053-1061. PMID 23395796 DOI: 10.1016/J.Febslet.2013.01.064 |
0.387 |
|
2013 |
Zhou HX, Cross TA. Modeling the membrane environment has implications for membrane protein structure and function: Influenza A M2 protein Protein Science. 22: 381-394. PMID 23389890 DOI: 10.1002/Pro.2232 |
0.377 |
|
2013 |
Zhou H. Polymer crowders and protein crowders act similarly on protein folding stability Febs Letters. 587: 394-397. PMID 23353683 DOI: 10.1016/J.Febslet.2013.01.030 |
0.34 |
|
2013 |
Pang X, Zhou HX. Poisson-Boltzmann calculations: Van der Waals or molecular surface? Communications in Computational Physics. 13: 1-12. DOI: 10.4208/Cicp.270711.140911S |
0.307 |
|
2013 |
Yi M, Dong H, Zhou H. Molecular Basis for the Ion Selectivity of Gap Junction Channels Elucidated by Molecular Dynamics Simulations Biophysical Journal. 104: 4-9. DOI: 10.1016/J.Bpj.2012.11.2283 |
0.304 |
|
2013 |
Kazi R, Dai J, Jin T, Zhou H, Wollmuth LP. Biophysical Coupling Mechanisms in NMDA Receptor Gating Biophysical Journal. 104: 273a-274a. DOI: 10.1016/J.Bpj.2012.11.1534 |
0.338 |
|
2012 |
Qin S, Cai L, Zhou H. A method for computing association rate constants of atomistically represented proteins under macromolecular crowding Physical Biology. 9: 66008-66008. PMID 23197255 DOI: 10.1088/1478-3975/9/6/066008 |
0.404 |
|
2012 |
Pang X, Zhou KH, Qin S, Zhou H. Prediction and Dissection of Widely-Varying Association Rate Constants of Actin-Binding Proteins Plos Computational Biology. 8. PMID 23055910 DOI: 10.1371/Journal.Pcbi.1002696 |
0.398 |
|
2012 |
Greives N, Zhou H. BDflex: a method for efficient treatment of molecular flexibility in calculating protein-ligand binding rate constants from brownian dynamics simulations. Journal of Chemical Physics. 137: 135105-135105. PMID 23039617 DOI: 10.1063/1.4756913 |
0.373 |
|
2012 |
Phillip Y, Harel M, Khait R, Qin S, Zhou HX, Schreiber G. Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents Biophysical Journal. 103: 1011-1019. PMID 23009850 DOI: 10.1016/J.Bpj.2012.08.009 |
0.375 |
|
2012 |
Du J, Dong H, Zhou HX. Size matters in activation/inhibition of ligand-gated ion channels. Trends in Pharmacological Sciences. 33: 482-93. PMID 22789930 DOI: 10.1016/J.Tips.2012.06.005 |
0.328 |
|
2012 |
Zhou H, Pang X, Lu C. Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets Physical Chemistry Chemical Physics. 14: 10466-10476. PMID 22744607 DOI: 10.1039/C2Cp41196B |
0.39 |
|
2012 |
Dong H, Sharma M, Zhou HX, Cross TA. Glycines: Role in α-helical membrane protein structures and a potential indicator of native conformation Biochemistry. 51: 4779-4789. PMID 22650985 DOI: 10.1021/Bi300090X |
0.359 |
|
2012 |
Cross TA, Dong H, Sharma M, Busath DD, Zhou HX. M2 protein from Influenza A: From multiple structures to biophysical and functional insights Current Opinion in Virology. 2: 128-133. PMID 22482709 DOI: 10.1016/J.Coviro.2012.01.005 |
0.369 |
|
2012 |
Pang X, Zhou HX. A common model for cytokine receptor activation: Combined scissor-like rotation and self-rotation of receptor dimer induced by class I cytokine Plos Computational Biology. 8. PMID 22412367 DOI: 10.1371/Journal.Pcbi.1002427 |
0.313 |
|
2012 |
Du J, Dong H, Zhou HX. Gating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulations. Proceedings of the National Academy of Sciences of the United States of America. 109: 4140-5. PMID 22378652 DOI: 10.1073/Pnas.1119546109 |
0.302 |
|
2012 |
Pang X, Zhou H. A Common Model for Cytokine Receptor Activation: Combined Scissor-Like Rotation and Self-Rotation of Receptor Dimer Induced by Class I Cytokine Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.3620 |
0.313 |
|
2012 |
Qin S, Zhou H. Atomistic Modeling of Excluded-Volume and Soft Interactions in Crowded Environments Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.2598 |
0.4 |
|
2012 |
Zhou KH, Pang X, Qin S, Zhou H. Prediction and Analysis of the Widely-Varying Association Rates of Actin-Binding Proteins Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.2039 |
0.383 |
|
2012 |
Qin H, Miao Y, Fu R, Sharma M, Can T, Busath DD, Zhou H, Cross TA. Structural Insights for the Full Length Influenza A M2 Proton Channel in Native E. Coli Membranes Biophysical Journal. 102: 265a. DOI: 10.1016/J.Bpj.2011.11.1456 |
0.343 |
|
2011 |
Barreda JL, Zhou H. Theory and simulation of diffusion-influenced, stochastically gated ligand binding to buried sites Journal of Chemical Physics. 135: 145101-145101. PMID 22010732 DOI: 10.1063/1.3645000 |
0.376 |
|
2011 |
Pang X, Qin S, Zhou H. Rationalizing 5000-Fold Differences in Receptor-Binding Rate Constants of Four Cytokines Biophysical Journal. 101: 1175-1183. PMID 21889455 DOI: 10.1016/J.Bpj.2011.06.056 |
0.359 |
|
2011 |
Berezhkovskii AM, Szabo A, Zhou H. Diffusion-influenced ligand binding to buried sites in macromolecules and transmembrane channels. Journal of Chemical Physics. 135: 75103-75103. PMID 21861586 DOI: 10.1063/1.3609973 |
0.347 |
|
2011 |
Qin S, Zhou H. Structural Models of Protein-DNA Complexes Based on Interface Prediction and Docking Current Protein & Peptide Science. 12: 531-539. PMID 21787304 DOI: 10.2174/138920311796957694 |
0.354 |
|
2011 |
Dong H, Zhou HX. Atomistic mechanism for the activation and desensitization of an AMPA-subtype glutamate receptor. Nature Communications. 2: 354. PMID 21673675 DOI: 10.1038/Ncomms1362 |
0.335 |
|
2011 |
Zhou H. Rapid search for specific sites on DNA through conformational switch of nonspecifically bound proteins Proceedings of the National Academy of Sciences of the United States of America. 108: 8651-8656. PMID 21543711 DOI: 10.1073/Pnas.1101555108 |
0.377 |
|
2011 |
Zhou H. Equivalence of two approaches for modeling ion permeation through a transmembrane channel with an internal binding site. Journal of Chemical Physics. 134: 135101-135101. PMID 21476774 DOI: 10.1063/1.3575585 |
0.321 |
|
2011 |
Cai L, Zhou H. Theory and simulation on the kinetics of protein–ligand binding coupled to conformational change Journal of Chemical Physics. 134: 105101-105101. PMID 21405192 DOI: 10.1063/1.3561694 |
0.396 |
|
2011 |
Zhou H. A Theory for the Proton Transport of the Influenza Virus M2 Protein: Extensive Test against Conductance Data Biophysical Journal. 100: 912-921. PMID 21320435 DOI: 10.1016/J.Bpj.2011.01.002 |
0.357 |
|
2011 |
Cross TA, Sharma M, Yi M, Zhou HX. Influence of solubilizing environments on membrane protein structures Trends in Biochemical Sciences. 36: 117-125. PMID 20724162 DOI: 10.1016/J.Tibs.2010.07.005 |
0.341 |
|
2011 |
Sharma M, Li C, Busath DD, Zhou HX, Cross TA. Drug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins Biochimica Et Biophysica Acta - Biomembranes. 1808: 538-546. PMID 20655872 DOI: 10.1016/J.Bbamem.2010.07.015 |
0.375 |
|
2011 |
Lee W, Zeng X, Zhou H, Bennett V, Yang W, Marszalek P. Full Reconstruction of a Vectorial Protein Folding Pathway by Afm and Smd: Insights Into the Co-Translational Folding of the Nascent-Polypeptide-Chain Biophysical Journal. 100: 483a. DOI: 10.1016/J.Bpj.2010.12.2829 |
0.381 |
|
2011 |
Qin S, Zhou H. Automated Prediction of Protein-Protein Association Rate Constants Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.2295 |
0.393 |
|
2011 |
Can T, Miao Y, Sharma M, Luca S, Qin H, Hung I, Truong M, Busath D, Zhou H, Cross T. Solid-State NMR Study on the Conductance Mechanism and Acid Activation of M2 Proton Channel Biophysical Journal. 100: 384a. DOI: 10.1016/J.Bpj.2010.12.2283 |
0.362 |
|
2011 |
Sharma M, Yi M, Dong H, Peterson E, Qin H, Busath DD, Zhou H, Cross TA. Influenza A/M2 Proton Channel: Structure in a Lipid Bilayer Provides Insights into the Conductance Mechanism Biophysical Journal. 100: 383a. DOI: 10.1016/J.Bpj.2010.12.2282 |
0.363 |
|
2010 |
Sharma M, Yi M, Dong H, Qin H, Peterson E, Busath DD, Zhou HX, Cross TA. Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer Science. 330: 509-512. PMID 20966252 DOI: 10.1126/Science.1191750 |
0.358 |
|
2010 |
Lee W, Zeng X, Zhou HX, Bennett V, Yang W, Marszalek PE. Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations. The Journal of Biological Chemistry. 285: 38167-72. PMID 20870713 DOI: 10.1074/Jbc.M110.179697 |
0.377 |
|
2010 |
Zhou H. Rate theories for biologists Quarterly Reviews of Biophysics. 43: 219-293. PMID 20691138 DOI: 10.1017/S0033583510000120 |
0.302 |
|
2010 |
Zhou H. Diffusion-Influenced Transport of Ions across a Transmembrane Channel with an Internal Binding Site Journal of Physical Chemistry Letters. 1: 1973-1976. PMID 20625440 DOI: 10.1021/Jz100683T |
0.357 |
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2010 |
Dong H, Qin S, Zhou HX. Effects of macromolecular crowding on protein conformational changes. Plos Computational Biology. 6: e1000833. PMID 20617196 DOI: 10.1371/Journal.Pcbi.1000833 |
0.426 |
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2010 |
Tjong H, Zhou H. The Folding Transition-State Ensemble of a Four-Helix Bundle Protein: Helix Propensity as a Determinant and Macromolecular Crowding as a Probe Biophysical Journal. 98: 2273-2280. PMID 20483336 DOI: 10.1016/J.Bpj.2010.01.052 |
0.344 |
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2010 |
Qin S, Zhou H. Generalized fundamental measure theory for atomistic modeling of macromolecular crowding. Physical Review E. 81: 31919-31919. PMID 20365782 DOI: 10.1103/Physreve.81.031919 |
0.37 |
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2010 |
Zhou H. From induced fit to conformational selection: a continuum of binding mechanism controlled by the timescale of conformational transitions. Biophysical Journal. 98. PMID 20303846 DOI: 10.1016/J.Bpj.2009.11.029 |
0.347 |
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2010 |
Zeng X, Hu H, Zhou HX, Marszalek PE, Yang W. Equilibrium sampling for biomolecules under mechanical tension. Biophysical Journal. 98: 733-40. PMID 20159170 DOI: 10.1016/J.Bpj.2009.11.004 |
0.304 |
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2010 |
Zhou HX, McCammon JA. The gates of ion channels and enzymes Trends in Biochemical Sciences. 35: 179-185. PMID 19926290 DOI: 10.1016/J.Tibs.2009.10.007 |
0.305 |
|
2010 |
Qin S, Zhou H. An Fft-Based Method for Modeling Crowding Effects when Both Test Proteins and Crowders are Represented at the Atomic Level Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.3487 |
0.397 |
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2010 |
Peterson E, Yi M, Zhou H, Sharma M, Cross TA, Busath D. Acid-Activation, Proton Transport Rate Saturation, and pH-Dependence of Amantadine Block for Influenza a M2 Protein Truncate (22-62) Biophysical Journal. 98: 503a. DOI: 10.1016/J.Bpj.2009.12.2739 |
0.322 |
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2010 |
Sharma M, Yi M, Peterson E, Inouye D, Velez A, Can T, Qin H, Busath DD, Zhou H, Cross TA. Structural and Functional Studies of M2 Proton Channel From Influenza A Virus Biophysical Journal. 98: 47a-48a. DOI: 10.1016/J.Bpj.2009.12.273 |
0.367 |
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2010 |
Dong H, Qin S, Zhou H. Crowding Effects on Protein Conformational Changes Biophysical Journal. 98: 25a. DOI: 10.1016/J.Bpj.2009.12.147 |
0.422 |
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2010 |
Zhou H. Atomistic Simulations of Macromolecular Crowding Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.032 |
0.397 |
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2009 |
Maniccia AW, Yang W, Johnson JA, Li S, Tjong H, Zhou HX, Shaket LA, Yang JJ. Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins. Pmc Biophysics. 2: 11. PMID 20025729 DOI: 10.1186/1757-5036-2-11 |
0.326 |
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2009 |
Batra J, Xu K, Qin S, Zhou H. Effect of Macromolecular Crowding on Protein Binding Stability: Modest Stabilization and Significant Biological Consequences Biophysical Journal. 97: 906-911. PMID 19651049 DOI: 10.1016/J.Bpj.2009.05.032 |
0.389 |
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2009 |
Yi M, Cross TA, Zhou HX. Conformational heterogeneity of the M2 proton channel and a structural model for channel activation Proceedings of the National Academy of Sciences of the United States of America. 106: 13311-13316. PMID 19633188 DOI: 10.1073/Pnas.0906553106 |
0.382 |
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2009 |
Zhou HX, Gilson MK. Theory of free energy and entropy in noncovalent binding. Chemical Reviews. 109: 4092-107. PMID 19588959 DOI: 10.1021/Cr800551W |
0.364 |
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2009 |
Qin S, Zhou H. Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability. Biophysical Journal. 97: 12-19. PMID 19580740 DOI: 10.1016/J.Bpj.2009.03.066 |
0.416 |
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2009 |
Batra J, Xu K, Zhou H. Nonadditive effects of mixed crowding on protein stability. Proteins. 77: 133-138. PMID 19408299 DOI: 10.1002/Prot.22425 |
0.339 |
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2009 |
Qin S, Zhou H. Dissection of the high rate constant for the binding of a ribotoxin to the ribosome. Proceedings of the National Academy of Sciences of the United States of America. 106: 6974-6979. PMID 19346475 DOI: 10.1073/Pnas.0900291106 |
0.378 |
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2009 |
Zhou H. Crowding Effects of Membrane Proteins Journal of Physical Chemistry B. 113: 7995-8005. PMID 19323472 DOI: 10.1021/Jp8107446 |
0.302 |
|
2009 |
Zhou H. Association and dissociation kinetics of colicin E3 and immunity protein 3: convergence of theory and experiment. Protein Science. 12: 2379-2382. PMID 14500897 DOI: 10.1110/Ps.03216203 |
0.351 |
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2009 |
Yi M, Cross TA, Zhou H. Conformational Heterogeneity Of The M2 Proton Channel: A Model For Channel Activation Biophysical Journal. 96: 668a. DOI: 10.1016/J.Bpj.2008.12.3530 |
0.367 |
|
2009 |
Batra J, Xu K, Zhou H. Effect of Macromolecular Crowding on Protein Folding Stability Biophysical Journal. 96: 5-8. DOI: 10.1016/J.Bpj.2008.12.3081 |
0.389 |
|
2009 |
Tjong H, Batra J, Zhou H. Computational Model to Predict Folding Stability of FKBP Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.1497 |
0.406 |
|
2008 |
Tjong H, Zhou H. Accurate Calculations of Binding, Folding, and Transfer Free Energies by a Scaled Generalized Born Method. Journal of Chemical Theory and Computation. 4: 1733-1744. PMID 23468599 DOI: 10.1021/Ct8001656 |
0.316 |
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2008 |
Li S, Yang W, Maniccia AW, Barrow D, Tjong H, Zhou HX, Yang JJ. Rational design of a conformation-switchable Ca2+- and Tb3+-binding protein without the use of multiple coupled metal-binding sites. The Febs Journal. 275: 5048-61. PMID 18785925 DOI: 10.1111/J.1742-4658.2008.06638.X |
0.354 |
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2008 |
Yuan JM, Chyan CL, Zhou HX, Chung TY, Peng H, Ping G, Yang G. The effects of macromolecular crowding on the mechanical stability of protein molecules. Protein Science : a Publication of the Protein Society. 17: 2156-66. PMID 18780817 DOI: 10.1110/Ps.037325.108 |
0.361 |
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2008 |
Yi M, Tjong H, Zhou HX. Spontaneous conformational change and toxin binding in alpha7 acetylcholine receptor: insight into channel activation and inhibition. Proceedings of the National Academy of Sciences of the United States of America. 105: 8280-5. PMID 18541920 DOI: 10.1073/Pnas.0710530105 |
0.38 |
|
2008 |
Tjong H, Zhou H. Prediction of Protein Solubility from Calculation of Transfer Free Energy Biophysical Journal. 95: 2601-2609. PMID 18515380 DOI: 10.1529/Biophysj.107.127746 |
0.339 |
|
2008 |
Zhou H. Effect of Mixed Macromolecular Crowding Agents on Protein Folding Proteins. 72: 1109-1113. PMID 18506780 DOI: 10.1002/Prot.22111 |
0.327 |
|
2008 |
Zhou H. A minimum-reaction-flux solution to master-equation models of protein folding. Journal of Chemical Physics. 128: 195104-195104. PMID 18500902 DOI: 10.1063/1.2929824 |
0.314 |
|
2008 |
Yi M, Cross TA, Zhou HX. A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine. The Journal of Physical Chemistry. B. 112: 7977-9. PMID 18476738 DOI: 10.1021/Jp800171M |
0.309 |
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2008 |
Alsallaq R, Zhou H. Protein association with circular DNA: rate enhancement by nonspecific binding. Journal of Chemical Physics. 128: 115108-115108. PMID 18361623 DOI: 10.1063/1.2888996 |
0.319 |
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2008 |
Qin S, Zhou H. Prediction of salt and mutational effects on the association rate of U1A protein and U1 small nuclear RNA stem/loop II. Journal of Physical Chemistry B. 112: 5955-5960. PMID 18154282 DOI: 10.1021/Jp075919K |
0.366 |
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2008 |
Nymeyer H, Zhou HX. A method to determine dielectric constants in nonhomogeneous systems: application to biological membranes. Biophysical Journal. 94: 1185-93. PMID 17951302 DOI: 10.1529/Biophysj.107.117770 |
0.333 |
|
2008 |
Alsallaq R, Zhou H. Electrostatic rate enhancement and transient complex of protein-protein association. Proteins. 71: 320-335. PMID 17932929 DOI: 10.1002/Prot.21679 |
0.375 |
|
2008 |
Li C, Yi M, Hu J, Zhou HX, Cross TA. Solid-state NMR and MD simulations of the antiviral drug amantadine solubilized in DMPC bilayers Biophysical Journal. 94: 1295-1302. PMID 17890391 DOI: 10.1529/Biophysj.107.112482 |
0.312 |
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2008 |
Zhou H. Protein folding in confined and crowded environments Archives of Biochemistry and Biophysics. 469: 76-82. PMID 17719556 DOI: 10.1016/J.Abb.2007.07.013 |
0.405 |
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2008 |
Yang W, Nymeyer H, Zhou HX, Berg B, Brüschweiler R. Quantitative computer simulations of biomolecules: a snapshot. Journal of Computational Chemistry. 29: 668-72. PMID 17708535 DOI: 10.1002/Jcc.20819 |
0.354 |
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2008 |
Zhou HX, Rivas G, Minton AP. Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences Annual Review of Biophysics. 37: 375-397. DOI: 10.1146/Annurev.Biophys.37.032807.125817 |
0.303 |
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2008 |
Zhou H, Qin S, Tjong H. Modeling Protein–Protein and Protein–Nucleic Acid Interactions: Structure, Thermodynamics, and Kinetics Annual Reports in Computational Chemistry. 4: 67-87. DOI: 10.1016/S1574-1400(08)00004-2 |
0.347 |
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2007 |
Bhattacharya N, Yi M, Zhou HX, Logan TM. Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR. Journal of Molecular Biology. 374: 977-92. PMID 17976643 DOI: 10.1016/J.Jmb.2007.09.063 |
0.34 |
|
2007 |
Qin S, Zhou H. A holistic approach to protein docking. Proteins. 69: 743-749. PMID 17803232 DOI: 10.1002/Prot.21752 |
0.391 |
|
2007 |
Zhou H, Qin S. Interaction-site prediction for protein complexes Bioinformatics. 23: 2203-2209. PMID 17586545 DOI: 10.1093/Bioinformatics/Btm323 |
0.382 |
|
2007 |
Tjong H, Qin S, Zhou H. PI2PE: protein interface/interior prediction engine Nucleic Acids Research. 35: 357-362. PMID 17526530 DOI: 10.1093/Nar/Gkm231 |
0.388 |
|
2007 |
Qin S, Zhou H. Do electrostatic interactions destabilize protein–nucleic acid binding? Biopolymers. 86: 112-118. PMID 17326079 DOI: 10.1002/Bip.20708 |
0.401 |
|
2007 |
Tjong H, Zhou H. GBr(6): a parameterization-free, accurate, analytical generalized born method. Journal of Physical Chemistry B. 111: 3055-3061. PMID 17309289 DOI: 10.1021/Jp066284C |
0.344 |
|
2007 |
Alsallaq R, Zhou H. Prediction of protein-protein association rates from a transition-state theory. Structure. 15: 215-224. PMID 17292839 DOI: 10.1016/J.Str.2007.01.005 |
0.374 |
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2007 |
Tjong H, Zhou H. DISPLAR: an accurate method for predicting DNA-binding sites on protein surfaces Nucleic Acids Research. 35: 1465-1477. PMID 17284455 DOI: 10.1093/Nar/Gkm008 |
0.343 |
|
2007 |
Gilson MK, Zhou HX. Calculation of protein-ligand binding affinities. Annual Review of Biophysics and Biomolecular Structure. 36: 21-42. PMID 17201676 DOI: 10.1146/Annurev.Biophys.36.040306.132550 |
0.392 |
|
2007 |
Alsallaq R, Zhou H. Energy Landscape and Transition State of Protein-Protein Association Biophysical Journal. 92: 1486-1502. PMID 17142273 DOI: 10.1529/Biophysj.106.096024 |
0.4 |
|
2006 |
Zhou H. Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains. Biophysical Journal. 91: 3170-3181. PMID 16891373 DOI: 10.1529/Biophysj.106.090258 |
0.35 |
|
2006 |
Dong F, Zhou HX. Electrostatic contribution to the binding stability of protein-protein complexes Proteins: Structure, Function and Genetics. 65: 87-102. PMID 16856180 DOI: 10.1002/Prot.21070 |
0.41 |
|
2006 |
Huang X, Zhou HX. Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulations. Biophysical Journal. 91: 2451-63. PMID 16844745 DOI: 10.1529/Biophysj.106.082891 |
0.349 |
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2006 |
Hu J, Fu R, Nishimura K, Zhang L, Zhou HX, Busath DD, Vijayvergiya V, Cross TA. Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity Proceedings of the National Academy of Sciences of the United States of America. 103: 6865-6870. PMID 16632600 DOI: 10.1073/Pnas.0601944103 |
0.332 |
|
2005 |
Zhou H. How do biomolecular systems speed up and regulate rates Physical Biology. 2. PMID 16224118 DOI: 10.1088/1478-3975/2/3/R01 |
0.421 |
|
2005 |
Chen H, Zhou HX. Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data. Proteins. 61: 21-35. PMID 16080151 DOI: 10.1002/Prot.20514 |
0.367 |
|
2005 |
Zhou H. Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect. Proteins. 61: 69-78. PMID 16044460 DOI: 10.1002/Prot.20500 |
0.329 |
|
2005 |
Spencer DS, Xu K, Logan TM, Zhou H. Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study. Journal of Molecular Biology. 351: 219-232. PMID 15992823 DOI: 10.1016/J.Jmb.2005.05.029 |
0.379 |
|
2005 |
Chen H, Zhou HX. Prediction of solvent accessibility and sites of deleterious mutations from protein sequence. Nucleic Acids Research. 33: 3193-9. PMID 15937195 DOI: 10.1093/Nar/Gki633 |
0.327 |
|
2005 |
Huang X, Dong F, Zhou HX. Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel. Journal of the American Chemical Society. 127: 6836-49. PMID 15869307 DOI: 10.1021/Ja042641Q |
0.39 |
|
2005 |
Zhou H. A Model for the Mediation of Processivity of DNA-Targeting Proteins by Nonspecific Binding: Dependence on DNA Length and Presence of Obstacles Biophysical Journal. 88: 1608-1615. PMID 15596498 DOI: 10.1529/Biophysj.104.052688 |
0.308 |
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2004 |
Zhou H, Szabo A. Enhancement of association rates by nonspecific binding to DNA and cell membranes. Physical Review Letters. 93: 178101. PMID 15525128 DOI: 10.1103/Physrevlett.93.178101 |
0.321 |
|
2004 |
Zhou H. Protein folding and binding in confined spaces and in crowded solutions Journal of Molecular Recognition. 17: 368-375. PMID 15362094 DOI: 10.1002/Jmr.711 |
0.427 |
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2004 |
Zhou H. Improving the understanding of human genetic diseases through predictions of protein structures and protein-protein interaction sites. Current Medicinal Chemistry. 11: 539-549. PMID 15032602 DOI: 10.2174/0929867043455800 |
0.371 |
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2004 |
Zhou H. Polymer Models of Protein Stability, Folding, and Interactions† Biochemistry. 43: 2141-2154. PMID 14979710 DOI: 10.1021/Bi036269N |
0.42 |
|
2004 |
Zhou H. Loops, linkages, rings, catenanes, cages, and crowders: entropy-based strategies for stabilizing proteins. Accounts of Chemical Research. 37: 123-130. PMID 14967059 DOI: 10.1021/Ar0302282 |
0.367 |
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2003 |
Zhou H. Effect of backbone cyclization on protein folding stability: chain entropies of both the unfolded and the folded states are restricted. Journal of Molecular Biology. 332: 257-264. PMID 12946362 DOI: 10.1016/S0022-2836(03)00886-6 |
0.377 |
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2003 |
Zhou H. Effect of catenation on protein folding stability. Journal of the American Chemical Society. 125: 9280-9281. PMID 12889942 DOI: 10.1021/Ja0355978 |
0.348 |
|
2003 |
Dong F, Vijayakumar M, Zhou HX. Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar Biophysical Journal. 85: 49-60. PMID 12829463 DOI: 10.1016/S0006-3495(03)74453-1 |
0.345 |
|
2003 |
Zhou HX, Dong F. Electrostatic contributions to the stability of a thermophilic cold shock protein Biophysical Journal. 84: 2216-2222. PMID 12668430 DOI: 10.1016/S0006-3495(03)75027-9 |
0.39 |
|
2003 |
Zhou H. Direct test of the Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins. Journal of the American Chemical Society. 125: 2060-2061. PMID 12590529 DOI: 10.1021/Ja0298491 |
0.345 |
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2003 |
Zhou H. Theory for the rate of contact formation in a polymer chain with local conformational transitions Journal of Chemical Physics. 118: 2010-2015. DOI: 10.1063/1.1531588 |
0.337 |
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2002 |
Zhou H. Toward the physical basis of thermophilic proteins : linking of enriched polar interactions and reduced heat capacity of unfolding Biophysical Journal. 83: 3126-3133. PMID 12496083 DOI: 10.1016/S0006-3495(02)75316-2 |
0.332 |
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2002 |
Zhou H. Residual charge interactions in unfolded staphylococcal nuclease can be explained by the Gaussian-chain model. Biophysical Journal. 83: 2981-2986. PMID 12496071 DOI: 10.1016/S0006-3495(02)75304-6 |
0.342 |
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2002 |
Dong F, Zhou HX. Electrostatic contributions to T4 lysozyme stability: Solvent-exposed charges versus semi-buried salt bridges Biophysical Journal. 83: 1341-1347. PMID 12202359 DOI: 10.1016/S0006-3495(02)73904-0 |
0.333 |
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2002 |
Zhou H. Residual electrostatic effects in the unfolded state of the N-terminal domain of L9 can be attributed to nonspecific nonlocal charge-charge interactions. Biochemistry. 41: 6533-6538. PMID 12009918 DOI: 10.1021/Bi025580M |
0.323 |
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2002 |
Zhou H. A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins. Proceedings of the National Academy of Sciences of the United States of America. 99: 3569-3574. PMID 11891295 DOI: 10.1073/Pnas.052030599 |
0.413 |
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2002 |
Zhou H. Model for the Binding of the Inactivation N-Terminal to the Ion Pore of Shaker Potassium Channel: Both Electrostatic Attraction and Covalent Linkage Are Required for Rapid Inactivation Journal of Physical Chemistry B. 106: 2393-2397. DOI: 10.1021/Jp013859R |
0.341 |
|
2002 |
Zhou H. Dimensions of denatured protein chains from hydrodynamic data Journal of Physical Chemistry B. 106: 5769-5775. DOI: 10.1021/Jp013403+ |
0.338 |
|
2001 |
Zhou H, Wang G. Predicted structures of two proteins involved in human diseases. Cell Biochemistry and Biophysics. 35: 35-47. PMID 11898854 DOI: 10.1385/Cbb:35:1:35 |
0.347 |
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2001 |
Zhou H. A unified picture of protein hydration: prediction of hydrodynamic properties from known structures. Biophysical Chemistry. 93: 171-179. PMID 11804724 DOI: 10.1016/S0301-4622(01)00219-8 |
0.386 |
|
2001 |
Zhou H. The Affinity-Enhancing Roles of Flexible Linkers in Two-Domain DNA-Binding Proteins † Biochemistry. 40: 15069-15073. PMID 11735389 DOI: 10.1021/Bi015795G |
0.334 |
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2001 |
Zhou H. Disparate ionic-strength dependencies of on and off rates in protein-protein association. Biopolymers. 59: 427-433. PMID 11598877 DOI: 10.1002/1097-0282(200111)59:6<427::Aid-Bip1047>3.0.Co;2-7 |
0.361 |
|
2001 |
Zhou HX, Shan Y. Prediction of protein interaction sites from sequence profile and residue neighbor list Proteins: Structure, Function and Genetics. 44: 336-343. PMID 11455607 DOI: 10.1002/Prot.1099 |
0.374 |
|
2001 |
Zhou H. Single-chain versus dimeric protein folding: thermodynamic and kinetic consequences of covalent linkage. Journal of the American Chemical Society. 123: 6730-6731. PMID 11439075 DOI: 10.1021/Ja015990I |
0.359 |
|
2001 |
Zhou H. Loops in Proteins Can Be Modeled as Worm-Like Chains Journal of Physical Chemistry B. 105: 6763-6766. DOI: 10.1021/Jp011355N |
0.377 |
|
2001 |
Vijayakumar M, Zhou HX. Salt bridges stabilize the folded structure of barnase Journal of Physical Chemistry B. 105: 7334-7340. DOI: 10.1021/Jp011214L |
0.345 |
|
2000 |
Shan Y, Zhou HX. Correspondence of potentials of mean force in proteins and in liquids Journal of Chemical Physics. 113: 4794-4798. DOI: 10.1063/1.1288920 |
0.351 |
|
2000 |
Vijayakumar M, Zhou H. Prediction of Residue−Residue Pair Frequencies in Proteins Journal of Physical Chemistry B. 104: 9755-9764. DOI: 10.1021/Jp001757F |
0.377 |
|
1998 |
Zhou HX, Wlodek ST, McCammon JA. Conformation gating as a mechanism for enzyme specificity. Proceedings of the National Academy of Sciences of the United States of America. 95: 9280-3. PMID 9689071 DOI: 10.1073/Pnas.95.16.9280 |
0.356 |
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1998 |
Vijayakumar M, Wong KY, Schreiber G, Fersht AR, Szabo AP, Zhou H. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. Journal of Molecular Biology. 278: 1015-1024. PMID 9600858 DOI: 10.1006/Jmbi.1998.1747 |
0.399 |
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1998 |
Zhou HX, Briggs JM, Tara S, McCammon JA. Correlation between rate of enzyme-substrate diffusional encounter and average Boltzmann factor around active site. Biopolymers. 45: 355-60. PMID 9530014 DOI: 10.1002/(Sici)1097-0282(19980415)45:5<355::Aid-Bip4>3.0.Co;2-K |
0.32 |
|
1998 |
Zhou H. Theory of the diffusion-influenced substrate binding rate to a buried and gated active site Journal of Chemical Physics. 108: 8146-8154. DOI: 10.1063/1.476255 |
0.324 |
|
1997 |
Zhou HX, Vijayakumar M. Modeling of protein conformational fluctuations in pK(a) predictions Journal of Molecular Biology. 267: 1002-1011. PMID 9135126 DOI: 10.1006/Jmbi.1997.0895 |
0.355 |
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1993 |
Schaad O, Zhou HX, Szabo A, Eaton WA, Henry ER. Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin. Proceedings of the National Academy of Sciences of the United States of America. 90: 9547-51. PMID 8415739 DOI: 10.1073/Pnas.90.20.9547 |
0.385 |
|
1993 |
Zhou H. Brownian dynamics study of the influences of electrostatic interaction and diffusion on protein-protein association kinetics Biophysical Journal. 64: 1711-1726. PMID 8396447 DOI: 10.1016/S0006-3495(93)81543-1 |
0.385 |
|
1991 |
Zhou H, Szabo A. Comparison between molecular dynamics simulations and the Smoluchowski theory of reactions in a hard‐sphere liquid Journal of Chemical Physics. 95: 5948-5952. DOI: 10.1063/1.461616 |
0.317 |
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1991 |
Zhou HX, Zwanzig R. A rate process with an entropy barrier The Journal of Chemical Physics. 94: 6147-6152. DOI: 10.1063/1.460427 |
0.307 |
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