World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
73
Citations
14345
World Ranking
5133
National Ranking
1591

Biology and Biochemistry

D-Index
73
Citations
14465
World Ranking
6081
National Ranking
2861

Overview

John M. Louis is affiliated with the National Institutes of Health in the United States. Their research spans multiple areas within biochemistry, genetics, molecular biology, and medicine, with specific focus on molecular biology and infectious diseases.

Their scholarly output encompasses a range of topics, including:

  • Protein Structure and Dynamics
  • SARS-CoV-2 and COVID-19 Research
  • Computational Drug Discovery Methods
  • HIV Research and Treatment
  • RNA and Protein Synthesis Mechanisms
  • Enzyme Structure and Function
  • Advanced NMR Techniques and Applications

Their frequent publication venues include:

  • Communications Biology
  • Proceedings of the National Academy of Sciences
  • Journal of Molecular Biology
  • Biophysical Journal
  • Nature Communications

Recent papers authored or co-authored by John M. Louis highlight research in virology, drug discovery, and protein dynamics. Key publications are:

  • Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease, 2022, Nature Communications
  • Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor, 2022, Communications Biology
  • Structural, Electronic, and Electrostatic Determinants for Inhibitor Binding to Subsites S1 and S2 in SARS-CoV-2 Main Protease, 2021, Journal of Medicinal Chemistry
  • Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease, 2020, Proceedings of the National Academy of Sciences
  • Structures of brain-derived 42-residue amyloid-β fibril polymorphs with unusual molecular conformations and intermolecular interactions, 2023, Proceedings of the National Academy of Sciences

John M. Louis collaborates regularly with several researchers, indicating consistent teamwork across multiple studies. Frequent co-authors include:

  • Andrey Kovalevsky
  • Leighton Coates
  • Annie Aniana
  • Rodolfo Ghirlando
  • Nashaat T. Nashed

The main fields of study connected to their work are:

  • Biochemistry, Genetics and Molecular Biology
  • Medicine

Within these broad areas, subfields such as molecular biology, infectious diseases, computational theory and mathematics, virology, and materials chemistry are significant components of their research focus.

Best Publications

  • Single-molecule fluorescence experiments determine protein folding transition path times.

    Hoi Sung Chung;Kevin McHale;John M. Louis;William A. Eaton

  • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations.

    Kusai A. Merchant;Robert B. Best;John M. Louis;Irina V. Gopich

  • Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function.

    Rieko Ishima;Darón I Freedberg;Yun-Xing Wang;John M Louis

  • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles.

    James J. Chou;Sander Gaemers;Bernard Howder;John M. Louis

  • Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories

    Hoi Sung Chung;John M. Louis;William A. Eaton

  • High Resolution Crystal Structures of HIV-1 Protease with a Potent Non-Peptide Inhibitor (Uic-94017) Active Against Multi-Drug-Resistant Clinical Strains.

    Yunfeng Tie;Peter I. Boross;Peter I. Boross;Yuan-Fang Wang;Laquasha Gaddis

  • Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations.

    Darón I. Freedberg;Rieko Ishima;Jaison Jacob;Yun-Xing Wang

  • Autoprocessing of HIV-1 protease is tightly coupled to protein folding.

    Louis Jm;Clore Gm;Gronenborn Am

  • Structure and dynamics of KH domains from FBP bound to single-stranded DNA

    Demetrios T. Braddock;John M. Louis;James L. Baber;David Levens

  • Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping.

    Fan Yang;Carole A Bewley;John M Louis;Kirk R Gustafson

  • NMR study of the tetrameric KcsA potassium channel in detergent micelles

    Jordan H. Chill;John M. Louis;Christopher Miller;Ad Bax

  • Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction

    Jim F. White;Justin Grodnitzky;John M. Louis;Loc B. Trinh

  • CAR2, a prestalk cAMP receptor required for normal tip formation and late development of Dictyostelium discoideum.

    C L Saxe;G T Ginsburg;J M Louis;R Johnson

  • The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.

    Laura G. Barrientos;John M. Louis;Istvan Botos;Toshiyuki Mori

  • Design of a Novel Peptide Inhibitor of HIV Fusion That Disrupts the Internal Trimeric Coiled-coil of gp41

    Carole A. Bewley;John M. Louis;Rodolfo Ghirlando;G. Marius Clore

  • The structure of a replication initiator unites diverse aspects of nucleic acid metabolism

    Ramon Campos-Olivas;John M Louis;Danielle Clerot;Bruno Gronenborn

  • The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface

    Justin L. Lorieau;John M. Louis;Ad Bax

  • Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114.

    Andrey Y. Kovalevsky;Fengling Liu;Sofiya Leshchenko;Arun K. Ghosh

  • Structural and kinetic analysis of drug resistant mutants of HIV‐1 protease

    Bhuvaneshwari Mahalingam;John M. Louis;Charles C. Reed;Jill M. Adomat

  • Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease

    Unknown

  • Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occurring point mutation.

    E C Murphy;V B Zhurkin;J M Louis;G Cornilescu

Frequent Co-Authors

G. Marius Clore
G. Marius Clore National Institutes of Health
Angela M. Gronenborn
Angela M. Gronenborn University of Pittsburgh
Ad Bax
Ad Bax National Institutes of Health
Irene T. Weber
Irene T. Weber Georgia State University
Jane M. Sayer
Jane M. Sayer National Institutes of Health
Stephen Oroszlan
Stephen Oroszlan National Institutes of Health
Dennis A. Torchia
Dennis A. Torchia National Institutes of Health
Carole A. Bewley
Carole A. Bewley National Institutes of Health
Rodolfo Ghirlando
Rodolfo Ghirlando National Institutes of Health
Terry D. Copeland
Terry D. Copeland National Institutes of Health

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