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Chemistry

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Research.com Recognitions

  • 2026 - Research.com Chemistry in United Kingdom Leader Award
  • 2025 - Research.com Best Scientists Award
  • 2025 - Research.com Chemistry in United Kingdom Leader Award
  • 2022 - Research.com Chemistry in United Kingdom Leader Award
  • 1998 - Davy Medal, Royal Society of London (UK) In recognition for his pioneering work on the analysis of proteins by combining the methods and ideas of physical-organic chemistry with those of protein engineering thus illuminating such processes as enzymatic catalysis, protein folding, protein-protein interactions and those macromolecule interactions in general that are dominated by the chemistry of the noncovalent bond
  • 1993 - Member of the National Academy of Sciences
  • 1989 - Member of Academia Europaea
  • 1988 - Fellow of the American Academy of Arts and Sciences
  • 1983 - Fellow of the Royal Society, United Kingdom
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Alan R. Fersht is affiliated with the University of Cambridge in the United Kingdom. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology, with significant contributions to Medicine.

The main areas of study include molecular biology, oncology, physiology, immunology, and geriatrics and gerontology. Their research topics focus on:

  • PARP inhibition in cancer therapy
  • DNA repair mechanisms
  • Genomics and chromatin dynamics
  • RNA research and splicing
  • RNA modifications and cancer
  • Calcium signaling and nucleotide metabolism
  • Toxin mechanisms and immunotoxins

Frequent collaborators include Magdalena Murawska, Charlotte Blessing, Imke K. Mandemaker, Claudia Gonzalez-Leal, and G. Knobloch.

Common publication venues for their work are:

  • Molecular Cell
  • Nature Structural & Molecular Biology
  • Cell Reports
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications

Selected recent papers include:

  • ADP-ribosyltransferases, an update on function and nomenclature, 2021, FEBS Journal
  • The Oncogenic Helicase ALC1 Regulates PARP Inhibitor Potency by Trapping PARP2 at DNA Breaks, 2020, Molecular Cell
  • The taming of PARP1 and its impact on NAD+ metabolism, 2020, Molecular Metabolism
  • Crosstalk between Drp1 phosphorylation sites during mitochondrial remodeling and their impact on metabolic adaptation, 2021, Cell Reports
  • The histone chaperone FACT facilitates heterochromatin spreading by regulating histone turnover and H3K9 methylation states, 2021, Cell Reports

Among their recognitions, Alan R. Fersht has been awarded the Davy Medal by the Royal Society of London in 1998. The award citation highlights pioneering work in protein analysis through combining physical-organic chemistry with protein engineering, illuminating enzymatic catalysis, protein folding, protein-protein interactions, and macromolecular interactions dominated by noncovalent chemistry.

They have been elected a member or fellow of several prestigious organizations, including the National Academy of Sciences (1993), Academia Europaea (1989), the American Academy of Arts and Sciences (1988), the Royal Society, United Kingdom (1983), The Academy of Medical Sciences, United Kingdom, and the European Molecular Biology Organization (EMBO).

Best Publications

  • Enzyme structure and mechanism

    Alan Fersht

  • Structure and Mechanism in Protein Science : a guide to enzyme catalysis and protein folding

    Alan Fersht

  • Structure and Mechanism in Protein Science

    Alan Fersht

  • Hydrogen bonding and biological specificity analysed by protein engineering

    Alan R. Fersht;Jian-Ping Shi;Jack Knill-Jones;Denise M. Lowe

  • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

    Sophie E. Jackson;Alan R. Fersht

  • Awakening guardian angels: drugging the p53 pathway

    Christopher J. Brown;Sonia Lain;Chandra S. Verma;Alan R. Fersht

  • Structure and Function of a Human TAFII250 Double Bromodomain Module

    Raymond H. Jacobson;Andreas G. Ladurner;David S. King;Robert Tjian

  • The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding

    Laura S. Itzhaki;Daniel E. Otzen;Alan R. Fersht

  • The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding

    Alan R. Fersht;Andreas T Matouschek;Luis Serrano

  • Mapping the transition state and pathway of protein folding by protein engineering

    Andreas T Matouschek;James T. Kellis;Luis Serrano;Alan R. Fersht

  • Rescuing the function of mutant p53

    Alex N. Bullock;Alan R. Fersht

  • Structural Biology of the Tumor Suppressor p53

    Andreas C. Joerger;Alan R. Fersht

  • Nucleation mechanisms in protein folding.

    Alan R Fersht

  • Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles

    Gideon Schreiber;Alan R. Fersht

  • The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

    Paul J. Carter;Greg Winter;Anthony J. Wilkinson;Alan R. Fersht

  • Rapid, electrostatically assisted association of proteins

    Gideon Schreiber;Alan R. Fersht

  • Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

    Alan R. Fersht

  • PRIMA-1 Reactivates Mutant p53 by Covalent Binding to the Core Domain

    Jeremy M.R. Lambert;Jeremy M.R. Lambert;Petr Gorzov;Dimitry B. Veprintsev;Maja Söderqvist

  • The hydrogen bond in molecular recognition

    Alan R. Fersht

  • Is there a unifying mechanism for protein folding

    Valerie Daggett;Alan R. Fersht

  • Protein folding and unfolding at atomic resolution.

    Alan R. Fersht;Valerie Daggett

Frequent Co-Authors

Stefan M.V. Freund
Stefan M.V. Freund MRC Laboratory of Molecular Biology
Christopher M. Johnson
Christopher M. Johnson MRC Laboratory of Molecular Biology
Luis Serrano
Luis Serrano Centre for Genomic Regulation
Valerie Daggett
Valerie Daggett University of Washington
Ashley M. Buckle
Ashley M. Buckle Monash University
Dmitry B. Veprintsev
Dmitry B. Veprintsev University of Nottingham
Gideon Schreiber
Gideon Schreiber Weizmann Institute of Science
Andreas T Matouschek
Andreas T Matouschek The University of Texas at Austin
Jane Clarke
Jane Clarke University of Cambridge
Neil M. Ferguson
Neil M. Ferguson Imperial College London

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