Changes in Oligomerization Are Essential for the Chaperone Activity of a Small Heat Shock Protein in Vivo and in Vitro
Open Access
- 1 November 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (48), 46310-46318
- https://doi.org/10.1074/jbc.m208926200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Crystal structure and assembly of a eukaryotic small heat shock protein.Nature Structural & Molecular Biology, 2001
- Structure and function of the small heat shock protein/α-crystallin family of molecular chaperonesAdvances in Protein Chemistry, 2001
- Hsp26: a temperature-regulated chaperoneThe EMBO Journal, 1999
- Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activityBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia coliViability under Heat and Cold Stress1Plant Physiology, 1999
- Crystal structure of a small heat-shock proteinNature, 1998
- Genealogy of the α-crystallin—small heat-shock protein superfamilyInternational Journal of Biological Macromolecules, 1998
- A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent stateThe EMBO Journal, 1997
- Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivationThe EMBO Journal, 1997
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992