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Robin J. Leatherbarrow

Robin J. Leatherbarrow

D-Index & Metrics

Chemistry

D-Index
57
Citations
7296
World Ranking
11422
National Ranking
644

Biology and Biochemistry

D-Index
57
Citations
7253
World Ranking
14121
National Ranking
1106

Overview

Robin J. Leatherbarrow is affiliated with Imperial College London in the United Kingdom. Their research primarily focuses on medical and biochemical sciences, emphasizing public health, epidemiology, and molecular biology.

Their work covers key areas such as enzyme function and inhibition, as well as specific studies on diseases caused by Trypanosoma species and Leishmaniasis. These topics reflect a concentration on infectious disease mechanisms and potential therapeutic targets.

Leatherbarrow has contributed to research published in the Journal of Medicinal Chemistry. A notable publication includes the paper titled "Novel Thienopyrimidine Inhibitors of Leishmania N-Myristoyltransferase with On-Target Activity in Intracellular Amastigotes" from 2020.

Frequently collaborating with other researchers, Leatherbarrow's coauthors include:

  • Andrew Bell
  • Zhiyong Yu
  • J.A. Hutton
  • Megan H. Wright
  • J.A. Brannigan

Their research has been recognized through citations primarily focused on medicinal chemistry and parasitology, showing active engagement in advancing knowledge related to enzyme inhibitors affecting parasite viability.

Main research areas encompass:

  • Research on Leishmaniasis Studies
  • Trypanosoma species research and implications
  • Enzyme function and inhibition

Fields of study associated with Leatherbarrow's work include:

  • Medicine
  • Biochemistry, Genetics and Molecular Biology

Subfields contributing to their scientific contributions are:

  • Public Health, Environmental and Occupational Health
  • Epidemiology
  • Molecular Biology

Best Publications

  • Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor.

    Robin J. Leatherbarrow;Thomas W. Rademacher;Raymond A. Dwek;Jennifer M. Woof

  • Using linear and non-linear regression to fit biochemical data

    Robin J. Leatherbarrow

  • Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering

    Robin J. Leatherbarrow;Alan R. Fersht;Greg Winter

  • Validation of N -myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach

    Megan H. Wright;Barbara Clough;Mark D. Rackham;Kaveri Rangachari

  • Kinetics of Protein-Protein Interactions at the Surface of an Optical Biosensor

    P.R. Edwards;A. Gill;D.V. Pollardknight;M. Hoare

  • Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.

    Alan R. Fersht;Robin J. Leatherbarrow;Tim N. C. Wells

  • Crystal structure of foot-and-mouth disease virus 3C protease: New insights into catalytic mechanism and cleavage specificity

    James R. Birtley;Stephen R. Knox;Agnès M. Jaulent;Peter Brick

  • Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A

    R J Leatherbarrow;P D Dean

  • Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides

    Panumart Thongyoo;Núria Roqué-Rosell;Robin J. Leatherbarrow;Edward W. Tate

  • N-Myristoyl transferase-mediated protein labelling in vivo.

    William P. Heal;Sasala R. Wickramasinghe;Robin J. Leatherbarrow;Edward W. Tate

  • Potent Inhibitors of β-Tryptase and Human Leukocyte Elastase Based on the MCoTI-II Scaffold

    Panumart Thongyoo;Camille Bonomelli;Robin J. Leatherbarrow;Edward W. Tate

  • Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships

    Alan R. Fersht;Robin J. Leatherbarrow;Tim N. C. Wells

  • Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus.

    Aurélie Mousnier;Aurélie Mousnier;Andrew S. Bell;Dawid P. Swieboda;Julia Morales-Sanfrutos

  • N-Myristoyltransferase from Leishmania Donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis.

    James A. Brannigan;Barbara A. Smith;Zhiyong Yu;Andrzej M. Brzozowski

  • Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase

    Alan R Fersht;Robin J Leatherbarrow;Tim N.C Wells

  • Determination of Association Rate Constants by an Optical Biosensor Using Initial Rate Analysis

    Paul R. Edwards;Robin J. Leatherbarrow

  • Structural and Mutagenic Analysis of Foot-and-Mouth Disease Virus 3C Protease Reveals the Role of the β-Ribbon in Proteolysis

    Trevor R. Sweeney;Núria Roqué-Rosell;James R. Birtley;Robin J. Leatherbarrow

  • Selective inhibitors of protozoan protein N-myristoyltransferases as starting points for tropical disease medicinal chemistry programs.

    Andrew S. Bell;James E. Mills;Gareth P. Williams;James A. Brannigan

  • Selection of Chymotrypsin Inhibitors from a Conformationally-constrained Combinatorial Peptide Library

    Jeffrey D. McBride;Neil Freeman;Neil Freeman;Gonzalo J. Domingo;Gonzalo J. Domingo;Robin J. Leatherbarrow;Robin J. Leatherbarrow

  • Peptide mimics of the Bowman-Birk inhibitor reactive site loop.

    Jeffrey D. McBride;Emma M. Watson;Arnd B. E. Brauer;Agnès M. Jaulent

  • On to the second generation

    Robin J. Leatherbarrow

Frequent Co-Authors

Edward W. Tate
Edward W. Tate Imperial College London
Anthony A. Holder
Anthony A. Holder The Francis Crick Institute
Deborah F. Smith
Deborah F. Smith University of York
Anthony J. Wilkinson
Anthony J. Wilkinson University of York
Stephen Matthews
Stephen Matthews Imperial College London
Stephen Curry
Stephen Curry Imperial College London
Raymond A. Dwek
Raymond A. Dwek University of Oxford
Andrew G. Livingston
Andrew G. Livingston Queen Mary University of London
Brian J. Sutton
Brian J. Sutton King's College London
Patricia A. Zunszain
Patricia A. Zunszain King's College London

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