Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation
Small heat-shock proteins (sHsps) are molecular chaperones that play an important protective role against cellular protein misfolding by interacting with partially unfolded proteins on their off-folding pathway, preventing their aggregation. Polyglutamine (polyQ) repeat expansion leads to the formation of fibrillar protein aggregates and neuronal cell death in nine diseases, including Huntington disease and the spinocerebellar ataxias (SCAs). There is evidence that sHsps have a role in...[Show more]
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|Source:||PNAS - Proceedings of the National Academy of Sciences of the United States of America|
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