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Christopher M. Dobson

Christopher M. Dobson

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Best Scientists
2025
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Chemistry
UK
2022

D-Index & Metrics

Best Scientists

D-Index
183
Citations
146867
World Ranking
546
National Ranking
58

Chemistry

D-Index
183
Citations
142180
World Ranking
34
National Ranking
1

Research.com Recognitions

  • 2025 - Research.com Best Scientists Award
  • 2022 - Research.com Chemistry in United Kingdom Leader Award
  • 2013 - Member of the National Academy of Sciences
  • 2005 - Davy Medal, Royal Society of London (UK) For his work on the application of NMR and other structural methods for studying protein folding and misfolding, especially the formation of amyloid fibrils, leading to novel insights on protein structure and folding
  • 1999 - Interdisciplinary Prize, Royal Society of Chemistry (UK)
  • 1981 - Corday–Morgan Prize, Royal Society of Chemistry (UK)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Christopher M. Dobson was affiliated with the University of Cambridge in the United Kingdom. Their research primarily focused on the fields of Medicine and Biochemistry, Genetics, and Molecular Biology, with significant contributions in the subfields of Molecular Biology, Physiology, Neurology, Biomedical Engineering, and Computational Theory and Mathematics.

The main research topics covered by Christopher M. Dobson included:

  • Alzheimer's disease research and treatments
  • Protein Structure and Dynamics
  • Parkinson's Disease Mechanisms and Treatments
  • Computational Drug Discovery Methods
  • Endoplasmic Reticulum Stress and Disease
  • Prion Diseases and Protein Misfolding
  • Microfluidic and Capillary Electrophoresis Applications

The researcher contributed to several notable papers in high-impact journals, including:

  • "Half a century of amyloids: past, present and future" (2020) published in Chemical Society Reviews
  • "Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide" (2020) published in Nature Chemistry
  • "The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells" (2021) published in Nature Communications
  • "Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies" (2020) published in Nature Structural & Molecular Biology
  • "Kinetic diversity of amyloid oligomers" (2020) published in Proceedings of the National Academy of Sciences

Frequent co-authors included Michele Vendruscolo, Tuomas P. J. Knowles, Janet R. Kumita, Catherine K. Xu, and Francesco Simone Ruggeri. Dobson's work appeared regularly in publication venues such as bioRxiv (Cold Spring Harbor Laboratory), Apollo (University of Cambridge), Proceedings of the National Academy of Sciences, Communications Biology, and Biophysical Journal.

Throughout their career, Christopher M. Dobson received several awards and honors, including being named a Member of the National Academy of Sciences in 2013. Other distinctions included the Davy Medal from the Royal Society of London in 2005 for research on protein folding and amyloid fibrils, the Interdisciplinary Prize from the Royal Society of Chemistry in 1999, the Corday-Morgan Prize from the Royal Society of Chemistry in 1981, and membership in the European Molecular Biology Organization (EMBO).

Best Publications

  • Protein Misfolding, Functional Amyloid, and Human Disease

    Fabrizio Chiti;Christopher M. Dobson

  • Protein folding and misfolding

    Christopher M. Dobson

  • Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

    Fabrizio Chiti;Christopher M. Dobson

  • The amyloid state and its association with protein misfolding diseases

    Tuomas P. J. Knowles;Michele Vendruscolo;Christopher M. Dobson

  • Protein misfolding, evolution and disease

    Christopher M. Dobson

  • Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

    Samuel I. A. Cohen;Sara Linse;Leila M. Luheshi;Erik Hellstrand

  • Designing conditions for in vitro formation of amyloid protofilaments and fibrils

    Fabrizio Chiti;Paul Webster;Niccolò Taddei;Anne Clark

  • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

    David R. Booth;Margaret Sunde;Vittorio Bellotti;Vittorio Bellotti;Carol V. Robinson

  • Rationalization of the effects of mutations on peptide and protein aggregation rates.

    Fabrizio Chiti;Massimo Stefani;Niccolò Taddei;Giampietro Ramponi

  • Chemical space and biology.

    Christopher M. Dobson

  • An analytical solution to the kinetics of breakable filament assembly

    Tuomas P. J. Knowles;Christopher A. Waudby;Glyn L. Devlin;Samuel I. A. Cohen

  • Principles of protein folding, misfolding and aggregation

    Christopher M Dobson

  • The structural basis of protein folding and its links with human disease

    Christopher M. Dobson

  • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.

    Deborah K. Wilkins;Shaun B. Grimshaw;Véronique Receveur;Christopher M. Dobson

  • Protein Folding: A Perspective from Theory and Experiment.

    Christopher M. Dobson;Andrej Šali;Martin Karplus

  • The protofilament structure of insulin amyloid fibrils

    José L. Jiménez;Ewan J. Nettleton;Mario Bouchard;Carol V. Robinson

  • Amyloid fibrils from muscle myoglobin

    Marcus Fändrich;Matthew A. Fletcher;Christopher M. Dobson

  • Direct observation of the interconversion of normal and toxic forms of α-synuclein.

    Nunilo Cremades;Samuel I.A. Cohen;Emma Deas;Andrey Y. Abramov

  • Amyloid formation by globular proteins under native conditions

    Fabrizio Chiti;Christopher M Dobson

  • The folding of hen lysozyme involves partially structured intermediates and multiple pathways.

    Sheena E. Radford;Christopher M. Dobson;Philip A. Evans

  • Amyloid fibril formation by an SH3 domain

    Guijarro Ji;Sunde M;Jones Ja;Campbell Id

  • Erratum: The amyloid state and its association with protein misfolding diseases

    Tuomas P. J. Knowles;Michele Vendruscolo;Christopher M. Dobson

Frequent Co-Authors

Michele Vendruscolo
Michele Vendruscolo University of Cambridge
Tuomas P. J. Knowles
Tuomas P. J. Knowles University of Cambridge
Fabrizio Chiti
Fabrizio Chiti University of Florence
Carol V. Robinson
Carol V. Robinson University of Oxford
Christina Redfield
Christina Redfield University of Oxford
Sara Linse
Sara Linse Lund University
David Klenerman
David Klenerman University of Cambridge
Sheena E. Radford
Sheena E. Radford University of Leeds
Paolo Arosio
Paolo Arosio ETH Zurich
Mark E. Welland
Mark E. Welland University of Cambridge

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