2023 - Research.com Microbiology in United Kingdom Leader Award
2014 - Member of the National Academy of Sciences
1992 - Member of Academia Europaea
1987 - Robert Koch Prize
1984 - Fellow of the Royal Society, United Kingdom
Member of the European Molecular Biology Organization (EMBO)
Fellow of The Academy of Medical Sciences, United Kingdom
His primary scientific interests are in Virus, Virology, Biochemistry, Protein structure and Influenza A virus. His research in Virus intersects with topics in Transcription, Mutant and Glycoprotein. John J. Skehel combines subjects such as Antibody and Antigen with his study of Virology.
The various areas that he examines in his Protein structure study include Conformational change, Peptide sequence and Lipid bilayer fusion. His Lipid bilayer fusion research integrates issues from Ectodomain and Protein folding. His Influenza A virus study combines topics from a wide range of disciplines, such as Receptor, N-Acetylneuraminic acid and Binding site.
John J. Skehel spends much of his time researching Virology, Virus, Hemagglutinin, Biochemistry and Lipid bilayer fusion. His work carried out in the field of Virology brings together such families of science as Antibody and Antigen. His studies in Virus integrate themes in fields like Molecular biology and Glycoprotein.
The study incorporates disciplines such as T cell, Conformational change, Stereochemistry, Epitope and Binding site in addition to Hemagglutinin. The concepts of his Lipid bilayer fusion study are interwoven with issues in Viral entry, Biophysics and Ectodomain. John J. Skehel has included themes like Receptor and Influenza A virus subtype H5N1 in his Viral protein study.
John J. Skehel mostly deals with Virology, Virus, Hemagglutinin, Influenza A virus and Receptor. The Neuraminidase, Influenza A virus subtype H5N1 and Orthomyxoviridae research he does as part of his general Virology study is frequently linked to other disciplines of science, such as H5N1 genetic structure, therefore creating a link between diverse domains of science. Many of his studies on Virus involve topics that are commonly interrelated, such as Binding site.
His research integrates issues of Epitope, Biophysics and Lipid bilayer fusion in his study of Hemagglutinin. His Receptor research is multidisciplinary, incorporating perspectives in Protein structure, Plasma protein binding, Avidity and Viral protein. As a part of the same scientific family, he mostly works in the field of Biochemistry, focusing on Viral entry and, on occasion, Glycoprotein and Simian immunodeficiency virus.
His primary areas of investigation include Virology, Virus, Influenza A virus, Hemagglutinin and Receptor. His study in Virology is interdisciplinary in nature, drawing from both Antibody and Monoclonal antibody. John J. Skehel has researched Virus in several fields, including Sialic acid, Binding site and Microbiology.
Hemagglutinin is the subject of his research, which falls under Biochemistry. His Receptor study which covers Viral protein that intersects with Plasma protein binding, Mutant and Avidity. His Lipid bilayer research focuses on Viral entry and how it relates to Simian immunodeficiency virus, Gp41 and Glycoprotein.
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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.
Annual Review of Biochemistry (1987)
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.
Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
Ola Blixt;Steve Head;Tony Mondala;Christopher Scanlan.
Proceedings of the National Academy of Sciences of the United States of America (2004)
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.
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.
Proceedings of the National Academy of Sciences of the United States of America (1982)
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.
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.
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