Unique Structural Features of a Novel Class of Small Heat Shock Proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference69 articles.
1. Alpha-crystallin can function as a molecular chaperone.
2. Small heat shock proteins are molecular chaperones.
3. Structure and in Vitro Molecular Chaperone Activity of Cytosolic Small Heat Shock Proteins from Pea
4. Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation
5. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.
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3. The Caenorhabditis elegans 12‐kDa small heat shock proteins with little in vitro chaperone activity play crucial roles for its dauer formation, longevity, and reproduction;Protein Science;2021-07-31
4. The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase;Journal of Biological Chemistry;2020-03
5. Small heat shock proteins: Simplicity meets complexity;Journal of Biological Chemistry;2019-02
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