Ronald M. Levy

16.0k total citations · 1 hit paper
232 papers, 12.6k citations indexed

About

Ronald M. Levy is a scholar working on Molecular Biology, Atomic and Molecular Physics, and Optics and Spectroscopy. According to data from OpenAlex, Ronald M. Levy has authored 232 papers receiving a total of 12.6k indexed citations (citations by other indexed papers that have themselves been cited), including 153 papers in Molecular Biology, 69 papers in Atomic and Molecular Physics, and Optics and 40 papers in Spectroscopy. Recurrent topics in Ronald M. Levy's work include Protein Structure and Dynamics (116 papers), Spectroscopy and Quantum Chemical Studies (60 papers) and Enzyme Structure and Function (32 papers). Ronald M. Levy is often cited by papers focused on Protein Structure and Dynamics (116 papers), Spectroscopy and Quantum Chemical Studies (60 papers) and Enzyme Structure and Function (32 papers). Ronald M. Levy collaborates with scholars based in United States, Japan and France. Ronald M. Levy's co-authors include Emilio Gallicchio, Martin Karplus, Anthony K. Felts, Michael Andrec, Richard A. Friesner, Karsten Krogh‐Jespersen, Douglas B. Kitchen, Howard Alper, Nobuyuki Matubayasi and Francisco Figueirido and has published in prestigious journals such as Nature, Science and New England Journal of Medicine.

In The Last Decade

Ronald M. Levy

230 papers receiving 12.3k citations

Hit Papers

Integrated Modeling Program, Applied Chemical Theory (IMP... 2005 2026 2012 2019 2005 250 500 750 1000

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Ronald M. Levy United States 64 8.2k 3.7k 2.7k 1.8k 1.3k 232 12.6k
Thomas Fox Germany 28 9.2k 1.1× 3.0k 0.8× 3.4k 1.2× 1.8k 1.0× 1.5k 1.1× 56 15.1k
S. Swaminathan United States 30 11.7k 1.4× 2.5k 0.7× 3.2k 1.2× 1.8k 1.0× 1.2k 0.9× 54 16.8k
Johan Åqvist Sweden 57 9.5k 1.2× 2.2k 0.6× 2.3k 0.8× 1.1k 0.6× 1.8k 1.4× 204 13.4k
Pedro E. M. Lopes United States 23 7.2k 0.9× 2.2k 0.6× 2.1k 0.8× 1.1k 0.6× 1.2k 0.9× 40 11.6k
Robert E. Bruccoleri United States 30 13.8k 1.7× 2.5k 0.7× 3.8k 1.4× 1.9k 1.0× 1.4k 1.0× 58 18.8k
Henk Bekker Netherlands 11 9.0k 1.1× 1.9k 0.5× 2.5k 0.9× 1.1k 0.6× 1.2k 0.9× 20 15.5k
Robert D. Skeel United States 36 12.4k 1.5× 2.9k 0.8× 3.3k 1.2× 1.5k 0.8× 1.8k 1.4× 105 20.9k
Gerrit Groenhof Finland 39 9.5k 1.2× 3.5k 0.9× 3.2k 1.2× 1.3k 0.7× 1.4k 1.1× 87 18.7k
David J. States United States 32 13.9k 1.7× 2.6k 0.7× 3.7k 1.4× 3.0k 1.7× 1.2k 0.9× 75 20.1k
Hsing Lee United States 7 10.3k 1.2× 3.6k 1.0× 3.5k 1.3× 1.6k 0.9× 1.2k 0.9× 8 19.2k

Countries citing papers authored by Ronald M. Levy

Since Specialization
Citations

This map shows the geographic impact of Ronald M. Levy's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Ronald M. Levy with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Ronald M. Levy more than expected).

Fields of papers citing papers by Ronald M. Levy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald M. Levy. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Ronald M. Levy. The network helps show where Ronald M. Levy may publish in the future.

Co-authorship network of co-authors of Ronald M. Levy

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald M. Levy. A scholar is included among the top collaborators of Ronald M. Levy based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Ronald M. Levy. Ronald M. Levy is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
2.
Choudhuri, Indrani, Tao Jing, Avik Biswas, et al.. (2025). BPS2025 - Structural and mechanistic insights into cabotegravir resistance in HIV-1 integrase. Biophysical Journal. 124(3). 176a–177a.
3.
Levy, Ronald M., et al.. (2025). BPS2025 - Phylogenetic corrections and higher-order sequence statistics in protein families: The Potts model and MSA transformer showdown. Biophysical Journal. 124(3). 487a–487a. 1 indexed citations
4.
Thakur, Abhishek, et al.. (2024). Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases. Nature Communications. 15(1). 6545–6545. 5 indexed citations
5.
Passos, Dario Oliveira, Steven J. Smith, Avik Biswas, et al.. (2023). Mechanisms of HIV-1 integrase resistance to dolutegravir and potent inhibition of drug-resistant variants. Science Advances. 9(29). eadg5953–eadg5953. 17 indexed citations
6.
Levy, Ronald M., Nobuyuki Matubayasi, & Bin W. Zhang. (2020). Solvation Thermodynamics from the Perspective of Endpoints DFT. The Journal of Physical Chemistry B. 124(52). 11771–11782. 4 indexed citations
7.
Zhang, Bin W., Nobuyuki Matubayasi, & Ronald M. Levy. (2020). Cavity Particle in Aqueous Solution with a Hydrophobic Solute: Structure, Energetics, and Functionals. The Journal of Physical Chemistry B. 124(25). 5220–5237. 1 indexed citations
8.
Ishii, Yoshiki, Naoki Yamamoto, Nobuyuki Matubayasi, et al.. (2019). Spatially-Decomposed Free Energy of Solvation Based on the Endpoint Density-Functional Method. Journal of Chemical Theory and Computation. 15(5). 2896–2912. 13 indexed citations
9.
Zhang, Bin W., Di Cui, Nobuyuki Matubayasi, & Ronald M. Levy. (2018). The Excess Chemical Potential of Water at the Interface with a Protein from End Point Simulations. The Journal of Physical Chemistry B. 122(17). 4700–4707. 8 indexed citations
10.
Haldane, Allan, William F. Flynn, Peng He, & Ronald M. Levy. (2018). Coevolutionary Landscape of Kinase Family Proteins: Sequence Probabilities and Functional Motifs. Biophysical Journal. 114(1). 21–31. 19 indexed citations
11.
Cui, Di, Bin W. Zhang, Nobuyuki Matubayasi, & Ronald M. Levy. (2017). The Role of Interfacial Water in Protein–Ligand Binding: Insights from the Indirect Solvent Mediated Potential of Mean Force. Journal of Chemical Theory and Computation. 14(2). 512–526. 25 indexed citations
12.
Gallicchio, Emilio, Haoyuan Chen, Michael Fitzgerald, et al.. (2015). BEDAM binding free energy predictions for the SAMPL4 octa-acid host challenge. Journal of Computer-Aided Molecular Design. 29(4). 315–325. 16 indexed citations
13.
Andrec, Michael, David A. Snyder, Zhiyong Zhou, et al.. (2007). A large data set comparison of protein structures determined by crystallography and NMR: Statistical test for structural differences and the effect of crystal packing. Proteins Structure Function and Bioinformatics. 69(3). 449–465. 96 indexed citations
14.
Gallicchio, Emilio, et al.. (2005). Conformational Equilibria and Free Energy Profiles for the Allosteric Transition of the Ribose-binding Protein. Journal of Molecular Biology. 353(1). 196–210. 66 indexed citations
15.
Gallicchio, Emilio & Ronald M. Levy. (2004). AGBNP: An analytic implicit solvent model suitable for molecular dynamics simulations and high‐resolution modeling. Journal of Computational Chemistry. 25(4). 479–499. 270 indexed citations
16.
Andrec, Michael & Ronald M. Levy. (2002). Protein sequential resonance assignments by combinatorial enumeration using 13Cα chemical shifts and their (i, i−1) sequential connectivities. Journal of Biomolecular NMR. 23(4). 263–270. 15 indexed citations
17.
Andrec, Michael, G.T. Montelione, & Ronald M. Levy. (2000). Lipari–Szabo mapping: A graphical approach to Lipari–Szabo analysis of NMR relaxation data using reduced spectral density mapping. Journal of Biomolecular NMR. 18(2). 83–100. 15 indexed citations
18.
Matubayasi, Nobuyuki, et al.. (1998). Protein hydration and unfolding – insights from experimental partial specific volumes and unfolded protein models. PubMed. 3(2). 105–118. 84 indexed citations
19.
Kominos, Dorothea, et al.. (1993). Global folding of proteins using a limited number of distance constraints. Protein Engineering Design and Selection. 6(6). 605–614. 31 indexed citations
20.
Metzler, William J., et al.. (1990). Determining local conformational variations in DNA. Journal of Molecular Biology. 214(3). 711–736. 63 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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