Refolding of Substrates Bound to Small Hsps Relies on a Disaggregation Reaction Mediated Most Efficiently by ClpB/DnaK
Open Access
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (33) , 31033-31042
- https://doi.org/10.1074/jbc.m303587200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Subunit Exchange of Multimeric Protein ComplexesJournal of Biological Chemistry, 2002
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone NetworkMicrobiology and Molecular Biology Reviews, 2002
- Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock ProteinsJournal of Biological Chemistry, 2000
- A Small Heat Shock Protein Cooperates with Heat Shock Protein 70 Systems to Reactivate a Heat-Denatured ProteinPlant Physiology, 2000
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- The Dynamics of Hsp25 Quaternary StructureJournal of Biological Chemistry, 1999
- Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperonesTrends in Biochemical Sciences, 1994
- Folding in vivo of bacterial cytoplasmic proteins: Role of GroELCell, 1993
- Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeastBiochemistry, 1991