Self-association and Chaperone Activity of Hsp27 Are Thermally Activated
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
1. The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”
2. Small heat shock proteins are molecular chaperones.
3. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
4. Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins
5. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
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