Protein misfolding, functional amyloid, and human disease.

By Fabrizio Chiti, Christopher M. Dobson. Annual Review of Biochemistry, 2006

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Cellular strategies for controlling protein aggregation (2010, background): “Such mutations are responsible for various 'conformational diseases', such as type II diabetes, Huntington's disease and familial forms (which are inherited and have a higher probability of developing in the affected family) of Parkinson's disease and Alzheimer's diseas”
Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans (2010, background): “Why might this be? Many recent studies show that low-MW oligomers formed by diseasemisfolded proteins are at least as, if not more, toxic as high-MW, visible, aggregates [43,84,85,86].”
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. (2011, background): “Like natural amyloidogenic proteins, they populate a range of prefibrillar aggregation intermediates, which are likely to represent the primary toxic agents in aggregation diseases (Chiti and Dobson, 2006; Jahn and Radford, 2008).”
Amyloid formation by globular proteins under native conditions. (2009, background): “131" language="eng" publish="issue" relation="no"> A wide range of human pathologies are associated with the conversion of polypeptide chains from their soluble states into well-organized fibrillar aggregates having extensive β-sheet structur”