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Microbiology

D-Index
112
Citations
59801
World Ranking
220
National Ranking
30

Overview

J.J. Skehel is affiliated with The Francis Crick Institute in the United Kingdom and has contributed extensively to the field of medicine, particularly within infectious diseases. Their research covers a range of topics including viral infections, molecular biology, and epidemiology.

The main fields of study for Skehel include:

  • Medicine

Their subfields of study comprise:

  • Infectious Diseases
  • Epidemiology
  • Animal Science and Zoology
  • Molecular Biology
  • Immunology

The key topics of Skehel's work include:

  • SARS-CoV-2 and COVID-19 Research
  • Animal Virus Infections Studies
  • Influenza Virus Research Studies
  • Viral Infections and Outbreaks Research
  • Viral gastroenteritis research and epidemiology
  • Lipid Membrane Structure and Behavior
  • RNA and protein synthesis mechanisms

A selection of recent publications demonstrates the focus and range of their research:

  • Structural transitions in influenza haemagglutinin at membrane fusion pH (2020), published in Nature
  • Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion (2020), published in Nature
  • SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects (2020), published in Nature Structural & Molecular Biology
  • The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2 (2021), published in Proceedings of the National Academy of Sciences
  • Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2 (2021), published in Nature Communications

Skehel frequently collaborates with several co-authors, including:

  • S.J. Gamblin
  • Stephen R. Martin
  • Peter B. Rosenthal
  • D.J. Benton
  • Antoni G. Wrobel

Their work is regularly published in the following venues:

  • Reviews in Medical Virology
  • Nature
  • Nature Communications
  • Research Square
  • Nature Structural & Molecular Biology

Best Publications

  • Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin

    John J. Skehel;Don C. Wiley

  • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.

    I. A. Wilson;J. J. Skehel;D. C. Wiley

  • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

    D. C. Wiley;I. A. Wilson;J. J. Skehel

  • Atomic structure of the ectodomain from HIV-1 gp41

    W. Weissenhorn;A. Dessen;S. C. Harrison;S. C. Harrison;J. J. Skehel

  • The Structure and Function of the Hemagglutinin Membrane Glycoprotein of Influenza Virus

    Don C. Wiley;John J. Skehel

  • Structure of influenza haemagglutinin at the pH of membrane fusion

    Per A. Bullough;Frederick M. Hughson;John J. Skehel;Don C. Wiley;Don C. Wiley

  • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid

    W. Weis;J. H. Brown;S. Cusack;S. Cusack;J. C. Paulson

  • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins

    Davide Corti;Jarrod Voss;Steven J. Gamblin;Giosiana Codoni

  • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

    Ola Blixt;Steve Head;Tony Mondala;Christopher Scanlan

  • The molecular basis of the specific anti-influenza action of amantadine.

    A J Hay;A J Wolstenholme;J J Skehel;M H Smith

  • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design

    Rupert J. Russell;Lesley F. Haire;David J. Stevens;Patrick J. Collins

  • Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion.

    J J Skehel;P M Bayley;E B Brown;S R Martin

  • The structure and receptor binding properties of the 1918 influenza hemagglutinin.

    S. J. Gamblin;L. F. Haire;R. J. Russell;D. J. Stevens

  • Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity

    G. N. Rogers;J. C. Paulson;R. S. Daniels;J. J. Skehel

  • Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion.

    Donald J. Benton;Antoni G. Wrobel;Pengqi Xu;Pengqi Xu;Chloë Roustan

  • Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors

    Shinya Yamada;Yasuo Suzuki;Takashi Suzuki;Mai Q. Le

  • Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins

    Steven J. Gamblin;John J. Skehel

  • Structure of an unliganded simian immunodeficiency virus gp120 core.

    Bing Chen;Erik M. Vogan;Erik M. Vogan;Haiyun Gong;John J. Skehel

  • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation.

    Jue Chen;Kon Ho Lee;David A Steinhauer;David J Stevens

  • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs.

    Ya Ha;David J. Stevens;John J. Skehel;Don C. Wiley

  • A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody

    J J Skehel;D J Stevens;R S Daniels;A R Douglas

Frequent Co-Authors

Olivier Diat
Olivier Diat Institut de Chimie

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