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 format...

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Main Authors: Robertson, Amy L., Headey, Stephen J., Saunders, Helen M., Ecroyd, Heath, Scanlon, Martin J., Carver, John A., Bottomley, Stephen P.
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2010
Fag:
Biological Sciences
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2890844/
https://ncbi.nlm.nih.gov/pubmed/20484674
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0914773107
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