John M. Louis

11.8k total citations
226 papers, 9.7k citations indexed

About

John M. Louis is a scholar working on Molecular Biology, Virology and Infectious Diseases. According to data from OpenAlex, John M. Louis has authored 226 papers receiving a total of 9.7k indexed citations (citations by other indexed papers that have themselves been cited), including 132 papers in Molecular Biology, 105 papers in Virology and 98 papers in Infectious Diseases. Recurrent topics in John M. Louis's work include HIV Research and Treatment (105 papers), HIV/AIDS drug development and treatment (88 papers) and Protein Structure and Dynamics (58 papers). John M. Louis is often cited by papers focused on HIV Research and Treatment (105 papers), HIV/AIDS drug development and treatment (88 papers) and Protein Structure and Dynamics (58 papers). John M. Louis collaborates with scholars based in United States, Hungary and France. John M. Louis's co-authors include G. Marius Clore, Rieko Ishima, William A. Eaton, Angela M. Gronenborn, Ad Bax, Irene T. Weber, Hoi Sung Chung, Dennis A. Torchia, Robert W. Harrison and Carole A. Bewley and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

John M. Louis

221 papers receiving 9.6k citations

Peers

John M. Louis

VIROL

SPECT

Paul T. Wingfield United States

Alexander Wlodawer United States

Rodolfo Ghirlando United States

Stephen J. Stahl United States

Scott C. Blanchard United States

Myron F. Goodman United States

Tom Alber United States

Peter S. Kim United States

David G. Myszka United States

Thomas A. Steitz United States

Paul T. Wingfield United States

John M. Louis

9.8k ×1.7

2.6k ×0.8

VIROL

2.3k ×0.7

2.0k ×1.8

1.7k ×2.0

SPECT

Citations per year, relative to John M. Louis John M. Louis (= 1×) peers Paul T. Wingfield

Countries citing papers authored by John M. Louis

Since Specialization

Citations

This map shows the geographic impact of John M. Louis'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 John M. Louis with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites John M. Louis more than expected).

Fields of papers citing papers by John M. Louis

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John M. Louis. 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 John M. Louis. The network helps show where John M. Louis may publish in the future.

Co-authorship network of co-authors of John M. Louis

This figure shows the co-authorship network connecting the top 25 collaborators of John M. Louis. A scholar is included among the top collaborators of John M. Louis 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 John M. Louis. John M. Louis is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Gerlits, Oksana, Stephen M. Keable, Leighton Coates, et al.. (2025). Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir. Communications Biology. 8(1). 1061–1061.

Louis, John M., et al.. (2025). Chemical Analysis of Deep-Lung Fluid Derived from Exhaled Breath Particles. Analytical Chemistry. 97(7). 4128–4136. 1 indexed citations

Aniana, Annie, et al.. (2024). Characterization of alternate encounter assemblies of SARS-CoV-2 main protease. Journal of Biological Chemistry. 300(9). 107675–107675. 5 indexed citations

Kovalevsky, Andrey, Annie Aniana, Rodolfo Ghirlando, et al.. (2024). Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors. Journal of Medicinal Chemistry. 67(20). 18478–18490. 5 indexed citations

Shen, Yang, Melody Smith, John M. Louis, & Ad Bax. (2024). Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins. Journal of Biomolecular NMR. 79(1). 47–57.

Kovalevsky, Andrey, Annie Aniana, Leighton Coates, et al.. (2023). Contribution of the catalytic dyad of SARS-CoV-2 main protease to binding covalent and noncovalent inhibitors. Journal of Biological Chemistry. 299(7). 104886–104886. 16 indexed citations

Aniana, Annie, Nashaat T. Nashed, Rodolfo Ghirlando, et al.. (2023). Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursors. Communications Biology. 6(1). 1159–1159. 16 indexed citations

Kneller, Daniel W., Hui Li, G.N. Phillips, et al.. (2022). Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease. Nature Communications. 13(1). 93 indexed citations

Nashed, Nashaat T., Daniel W. Kneller, Leighton Coates, et al.. (2022). Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domain. Communications Biology. 5(1). 976–976. 26 indexed citations

10.

Nashed, Nashaat T., et al.. (2022). Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor. Communications Biology. 5(1). 160–160. 37 indexed citations

11.

Kneller, Daniel W., Qiu Zhang, Leighton Coates, John M. Louis, & Andrey Kovalevsky. (2021). Michaelis-like complex of SARS-CoV-2 main protease visualized by room-temperature X-ray crystallography. IUCrJ. 8(6). 973–979. 26 indexed citations

12.

Alderson, T. Reid, Elias Adriaenssens, Bob Asselbergh, et al.. (2021). A weakened interface in the P182L variant of HSP27 associated with severe Charcot‐Marie‐Tooth neuropathy causes aberrant binding to interacting proteins. The EMBO Journal. 40(8). e103811–e103811. 15 indexed citations

13.

Henry, Eric R., et al.. (2021). MWC allosteric model explains unusual hemoglobin-oxygen binding curves from sickle cell drug binding. Biophysical Journal. 120(12). 2543–2551. 9 indexed citations

14.

Lorieau, Justin L., John M. Louis, & Ad Bax. (2010). The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Proceedings of the National Academy of Sciences. 107(25). 11341–11346. 142 indexed citations

15.

Chung, Hoi Sung, John M. Louis, & William A. Eaton. (2010). Distinguishing between Protein Dynamics and Dye Photophysics in Single-Molecule FRET Experiments. Biophysical Journal. 98(4). 696–706. 53 indexed citations

16.

Chung, Hoi Sung, John M. Louis, & William A. Eaton. (2009). Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories. Proceedings of the National Academy of Sciences. 106(29). 11837–11844. 236 indexed citations

17.

Louis, John M., Rieko Ishima, Annie Aniana, & Jane M. Sayer. (2009). Revealing the dimer dissociation and existence of a folded monomer of the mature HIV‐2 protease. Protein Science. 18(12). 2442–2453. 22 indexed citations

18.

Chill, Jordan H., John M. Louis, Frank Delaglio, & Ad Bax. (2007). Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(12). 3260–3270. 29 indexed citations

19.

Barrientos, Laura G., John M. Louis, Istvan Botos, et al.. (2002). The Domain-Swapped Dimer of Cyanovirin-N Is in a Metastable Folded State. Structure. 10(5). 673–686. 105 indexed citations

20.

Tőzsér, József, Gábor Zahuczky, Péter Bagossi, et al.. (2000). Comparison of the substrate specificity of the human T‐cell leukemia virus and human immunodeficiency virus proteinases. European Journal of Biochemistry. 267(20). 6287–6295. 52 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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