World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
80
Citations
31740
World Ranking
4005
National Ranking
299

Research.com Recognitions

  • 2011 - Fellow of the Royal Society, United Kingdom

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • DNA

The scientist’s investigation covers issues in Biochemistry, Virology, Virus, Orthomyxoviridae and Influenza A virus. AMP-activated protein kinase, AMPK, Protein structure, Protein kinase A and Methylation are the subjects of his Biochemistry studies. His work in the fields of Hemagglutinin overlaps with other areas such as Heterosubtypic immunity.

His Hemagglutinin research includes themes of Neutralizing antibody and Monoclonal antibody. He works in the field of Virus, namely Neuraminidase. His studies in Orthomyxoviridae integrate themes in fields like Influenza A virus subtype H5N1, Receptor and Viral protein.

His most cited work include:

  • The structural basis for 14-3-3:phosphopeptide binding specificity. (1375 citations)
  • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins (940 citations)
  • Role of the polycomb protein EED in the propagation of repressive histone marks (825 citations)

What are the main themes of his work throughout his whole career to date?

His scientific interests lie mostly in Virology, Biochemistry, Virus, Severe acute respiratory syndrome coronavirus 2 and Receptor. His study on Hemagglutinin, Neuraminidase, Viral protein and Hemagglutinin is often connected to Oseltamivir as part of broader study in Virology. His research related to Histone methyltransferase, Phosphorylation, AMP-activated protein kinase, Protein kinase A and Methylation might be considered part of Biochemistry.

Steven J. Gamblin has included themes like Histone H2A, Histone methylation, Histone H1 and Stereochemistry in his Histone methyltransferase study. His work in Virus addresses issues such as Binding site, which are connected to fields such as Protein structure. Many of his studies involve connections with topics such as Plasma protein binding and Receptor.

He most often published in these fields:

  • Virology (43.15%)
  • Biochemistry (19.18%)
  • Virus (15.07%)

What were the highlights of his more recent work (between 2018-2021)?

  • Severe acute respiratory syndrome coronavirus 2 (13.70%)
  • Virology (43.15%)
  • Spike (8.90%)

In recent papers he was focusing on the following fields of study:

Steven J. Gamblin focuses on Severe acute respiratory syndrome coronavirus 2, Virology, Spike, Glycoprotein and Biophysics. With his scientific publications, his incorporates both Virology and Coronavirus. His Glycoprotein research is multidisciplinary, incorporating elements of Protein structure, Virus, Endosome and Cell biology.

As a part of the same scientific study, Steven J. Gamblin usually deals with the Virus, concentrating on Receptor and frequently concerns with Protein folding. His research in Endosome intersects with topics in Hemagglutinin, Protein subunit, Membrane, Influenza A virus and Viral replication. His Cell biology study integrates concerns from other disciplines, such as Chromatin, Antibody, Epigenetics and Binding site.

Between 2018 and 2021, his most popular works were:

  • Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion. (128 citations)
  • SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. (128 citations)
  • G-tract RNA removes Polycomb repressive complex 2 from genes. (32 citations)

In his most recent research, the most cited papers focused on:

  • Gene
  • Enzyme
  • DNA

Steven J. Gamblin spends much of his time researching Glycoprotein, Virology, Severe acute respiratory syndrome coronavirus 2, Furin and Cleavage. His Glycoprotein research incorporates themes from Protein structure, Antibody, Binding site and Cell biology. His Neutralization study in the realm of Virology interacts with subjects such as 2019-20 coronavirus outbreak.

He combines subjects such as Virus, Virus genetics, Plasma protein binding and Protein folding with his study of Furin. His Virus research is multidisciplinary, incorporating perspectives in Mutant and Cryo-electron microscopy. His work carried out in the field of Cleavage brings together such families of science as Receptor, Biophysics and Lipid bilayer fusion.

Best Publications

  • The structural basis for 14-3-3:phosphopeptide binding specificity.

    Michael B Yaffe;Katrin Rittinger;Stefano Volinia;Paul R Caron

  • 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

  • Role of the polycomb protein EED in the propagation of repressive histone marks

    Raphael Margueron;Neil Justin;Katsuhito Ohno;Miriam L. Sharpe

  • Structure and mechanism of DNA topoisomerase II

    James M. Berger;Steven J. Gamblin;Steven J. Gamblin;Stephen C. Harrison;James C. Wang

  • Structure of mammalian AMPK and its regulation by ADP

    Bing Xiao;Matthew J. Sanders;Matthew J. Sanders;Elizabeth Underwood;Richard J. Heath

  • 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

  • Regulation of p53 activity through lysine methylation

    Sergei Chuikov;Julia K. Kurash;Jonathan R. Wilson;Bing Xiao

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

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

  • 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

  • Structural basis for AMP binding to mammalian AMP-activated protein kinase

    Bing Xiao;Richard Heath;Richard Heath;Peter Saiu;Fiona C. Leiper

  • Structural Analysis of 14-3-3 Phosphopeptide Complexes Identifies a Dual Role for the Nuclear Export Signal of 14-3-3 in Ligand Binding

    Katrin Rittinger;Joe Budman;Jian Xu;Stefano Volinia

  • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

    Bing Xiao;Stephen J. Smerdon;David H. Jones;Guy G. Dodson;Guy G. Dodson

  • Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants.

    Patrick J. Collins;Lesley F. Haire;Yi Pu Lin;Junfeng Liu

  • Structural Basis of Ampk Regulation by Small Molecule Activators.

    Bing Xiao;Matthew J. Sanders;David Carmena;Nicola J. Bright

  • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue

    Katrin Rittinger;Philip A. Walker;John F. Eccleston;Stephen J. Smerdon

  • The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1.

    D W Rodgers;S J Gamblin;B A Harris;S Ray

  • SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.

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

  • Pre-existing and de novo humoral immunity to SARS-CoV-2 in humans

    Kevin Ng;Nikhil Faulkner;Georgina Cornish;Annachiara Rosa

Frequent Co-Authors

Stephen R. Martin
Stephen R. Martin The Francis Crick Institute
Stephen J. Smerdon
Stephen J. Smerdon University of Birmingham
John J. Skehel
John J. Skehel The Francis Crick Institute
David Carling
David Carling Imperial College London
John W. McCauley
John W. McCauley The Francis Crick Institute
Guy Dodson
Guy Dodson University of York
William R. Taylor
William R. Taylor The Francis Crick Institute
Antonio Lanzavecchia
Antonio Lanzavecchia Istituto Nazionale Genetica Molecolare
G. Michael Blackburn
G. Michael Blackburn University of Sheffield
Richard B. Sessions
Richard B. Sessions University of Bristol

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