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Protein misfolding, functional amyloid, and human disease.
TLDR
Protein folding and misfolding
- C. Dobson
- BiologyNature
- 18 December 2003
The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple…
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
- D. K. Wilkins, S. Grimshaw, V. Receveur, C. Dobson, J. A. Jones, L. J. Smith
- Chemistry, BiologyBiochemistry
- 24 November 1999
TLDR
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
- M. Bucciantini, E. Giannoni, M. Stefani
- BiologyNature
- 4 April 2002
TLDR
Rationalization of the effects of mutations on peptide andprotein aggregation rates
- F. Chiti, M. Stefani, N. Taddei, G. Ramponi, C. Dobson
- BiologyNature
- 14 August 2003
TLDR
The amyloid state and its association with protein misfolding diseases
- T. Knowles, M. Vendruscolo, C. Dobson
- BiologyNature Reviews Molecular Cell Biology
- 1 July 2014
TLDR
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
- M. Stefani, C. Dobson
- BiologyJournal of Molecular Medicine
- 27 August 2003
TLDR
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
TLDR
Protein misfolding, evolution and disease.
- C. Dobson
- MedicineTrends in biochemical sciences
- 1 September 1999
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
- Samuel I. A. Cohen, S. Linse, T. Knowles
- Biology, ChemistryProceedings of the National Academy of Sciences
- 23 May 2013
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