Journal
PRION
Volume 3, Issue 2, Pages 51-58Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/pri.3.2.8587
Keywords
chaperone; heat shock protein; protein aggregation; amyloid; Hsp70; Hsp40; prion
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Funding
- American Heart Association
- National Institutes of Health Pre-doctoral Training Grant [5T32GM008581-09]
- National Institutes of Health Grant [5R01GM067785-06]
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The self-association of misfolded or damaged proteins into ordered amyloid-like aggregates characterizes numerous neurodegenerative disorders. Insoluble amyloid plaques are diagnostic of many disease states. Yet soluble, oligomeric intermediates in the aggregation pathway appear to represent the toxic culprit. Molecular chaperones regulate the fate of misfolded proteins and thereby influence their aggregation state. Chaperones conventionally antagonize aggregation of misfolded, disease proteins and assist in refolding or degradation pathways. Recent work suggests that chaperones may also suppress neurotoxicity by converting toxic, soluble oligomers into benign aggregates. Chaperones can therefore suppress or promote aggregation of disease proteins to ameliorate the proteotoxic accumulation of soluble, assembly intermediates.
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