Christopher Martin Dobson

Christopher Martin Dobson | JRNLClub

Research Statement

AI generated · 3d ago

Christopher Martin Dobson's research centres on the mechanisms by which proteins misfold and assemble into amyloid fibrils, and how these processes underlie human disease. His most-cited work includes a widely cited review of protein misfolding, functional amyloid and human disease (over 6,400 citations) and a foundational account of protein folding and misfolding (over 4,700 citations), alongside later syntheses of amyloid formation and its links to disease over the past decade. Across these, the recurring question is how sequence, evolution and environment determine whether a polypeptide folds correctly or aggregates. Beyond those reviews, his indexed outputs include the inherent toxicity of protein aggregates as a common mechanism for misfolding diseases and work on secondary nucleation driving the proliferation of amyloid-β42 aggregates, connecting kinetic theory to neurodegeneration. Related contributions address the analytical kinetics of breakable filament assembly and rationalizing how mutations alter peptide and protein aggregation rates. No software, datasets, patents or grants appear in the indexed record; the contribution is a sustained line of inquiry linking folding theory, aggregation kinetics and disease.

Most Cited Works

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

Giuliana Fusco, Serene W Chen, Philip T F Williamson, Roberta Cascella, Michele Perni, James A Jarvis, Cristina Cecchi, Michele Vendruscolo, Fabrizio Chiti, Nunilo Cremades, Liming Ying, Christopher M Dobson, Alfonso De Simone

Science2017

694Citations

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

Suman De, David C Wirthensohn, Patrick Flagmeier

Research Areas

Protein Structure and DynamicsAlzheimer's disease research and treatmeAdvanced NMR Techniques and ApplicationsPrion Diseases and Protein MisfoldingProtein purification and stability

Loading ORCID activity...

Christopher Martin Dobson

Sources

Research Statement

Most Cited Works

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

Research Areas

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease