• Publications
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Protein misfolding, functional amyloid, and human disease.
Peptides or proteins convert under some conditions from their soluble forms into highly ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging fromExpand
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Protein folding and misfolding
  • C. Dobson
  • Chemistry, Medicine
  • Nature
  • 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 multipleExpand
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Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
Pulse field gradient NMR methods have been used to determine the effective hydrodynamic radii of a range of native and nonnative protein conformations. From these experimental data, empiricalExpand
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
A range of human degenerative conditions, including Alzheimer's disease, light-chain amyloidosis and the spongiform encephalopathies, is associated with the deposition in tissue of proteinaceousExpand
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The amyloid state and its association with protein misfolding diseases
Nature Reviews Molecular Cell Biology 15, 384–396 (2014) In the legend of figure 2 of the above article (page 388), the sentence “The spacing between polypeptide chains along the fibril axis isExpand
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Rationalization of the effects of mutations on peptide andprotein aggregation rates
In order for any biological system to function effectively, it is essential to avoid the inherent tendency of proteins to aggregate and form potentially harmful deposits. In each of the variousExpand
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Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic feature of more than 20 degenerative conditions affecting either the central nervous system or a variety ofExpand
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The protofilament structure of insulin amyloid fibrils
Under solution conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-β structure.Expand
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
The generation of toxic oligomers during the aggregation of the amyloid-β (Aβ) peptide Aβ42 into amyloid fibrils and plaques has emerged as a central feature of the onset and progression ofExpand
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Protein misfolding, evolution and disease.
  • C. Dobson
  • Philosophy, Medicine
  • Trends in biochemical sciences
  • 1 September 1999
I acknowledge very valuable discussions on this article with John Ellis and Carol Robinson. I am grateful to Jose Jiminez and Helen Saibil for providing Figure 3Figure 3 and to Adam Rostom forExpand
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