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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
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
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
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This phenomenon is associated with a range ofExpand
Designing conditions for in vitro formation of amyloid protofilaments and fibrils.
We have been able to convert a small alpha/beta protein, acylphosphatase, from its soluble and native form into insoluble amyloid fibrils of the type observed in a range of pathological conditions.Expand
Amyloid formation by globular proteins under native conditions.
The conversion of proteins from their soluble states into well-organized fibrillar aggregates is associated with a wide range of pathological conditions, including neurodegenerative diseases andExpand
Prediction of aggregation-prone regions in structured proteins.
We present a method for predicting the regions of the sequences of peptides and proteins that are most important in promoting their aggregation and amyloid formation. The method extends previousExpand
Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins
The conversion from soluble states into cross-β fibrillar aggregates is a property shared by many different proteins and peptides and was hence conjectured to be a generic feature of polypeptide chains. Expand
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.
Increasing evidence indicates that many peptides and proteins can be converted in vitro into highly organised amyloid structures, provided that the appropriate experimental conditions can be found.Expand
A causative link between the structure of aberrant protein oligomers and their toxicity.
The aberrant assembly of peptides and proteins into fibrillar aggregates proceeds through oligomeric intermediates that are thought to be the primary pathogenic species in many protein depositionExpand