Ronald M. Levy

Chemistry Rutgers University, New Brunswick, New Brunswick, NJ, United States 
"Ronald Levy"
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Martin J. Kushmerick grad student 1973-1976 Harvard
 (Regulation of vertebrate striated muscle contraction in the presence and absence of calcium.)
Martin Karplus post-doc 1976-1980 Harvard
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Li M, Oliveira Passos D, Shan Z, et al. (2023) Mechanisms of HIV-1 integrase resistance to dolutegravir and potent inhibition of drug-resistant variants. Science Advances. 9: eadg5953
Gizzio J, Thakur A, Haldane A, et al. (2022) Evolutionary divergence in the conformational landscapes of tyrosine vs serine/threonine kinases. Elife. 11
Choudhuri I, Biswas A, Haldane A, et al. (2022) Contingency and Entrenchment of Drug-Resistance Mutations in HIV Viral Proteins. The Journal of Physical Chemistry. B. 126: 10622-10636
Haldane A, Levy RM. (2021) Mi3-GPU: MCMC-based inverse Ising inference on GPUs for protein covariation analysis Computer Physics Communications. 260: 107312
Tse C, Wickstrom L, Kvaratskhelia M, et al. (2020) Exploring the Free-Energy Landscape and Thermodynamics of Protein-Protein Association. Biophysical Journal
Zhang BW, Matubayasi N, Levy RM. (2020) Cavity Particle in Aqueous Solution with a Hydrophobic Solute: Structure, Energetics, and Functionals. The Journal of Physical Chemistry. B
Levy RM. (2020) Insights into the energy landscapes of chromosome organization proteins from coevolutionary sequence variation and structural modeling. Proceedings of the National Academy of Sciences of the United States of America
Narayan B, Fathizadeh A, Templeton C, et al. (2019) The transition between active and inactive conformations of Abl kinase studied by rock climbing and Milestoning. Biochimica Et Biophysica Acta. General Subjects. 129508
Cui D, Zhang BW, Tan Z, et al. (2019) Ligand Binding Thermodynamic Cycles: Hysteresis, LWHAM, and the Overlapping States Matrix. Journal of Chemical Theory and Computation
Sakae Y, Zhang BW, Levy RM, et al. (2019) Absolute Protein Binding Free Energy Simulations for Ligands with Multiple Poses, a Thermodynamic Path That Avoids Exhaustive Enumeration of the Poses. Journal of Computational Chemistry
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