Active Solubilization and Refolding of Stable Protein Aggregates By Cooperative Unfolding Action of Individual Hsp70 Chaperones
Open Access
- 1 September 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (36) , 37298-37303
- https://doi.org/10.1074/jbc.m405627200
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- Proteinaceous Infectious Behavior in Non-pathogenic Proteins Is Controlled by Molecular ChaperonesJournal of Biological Chemistry, 2002
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Characterization of a Lidless Form of the Molecular Chaperone DnaKJournal of Biological Chemistry, 2001
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- GrpE Accelerates Nucleotide Exchange of the Molecular Chaperone DnaK with an Associative Displacement MechanismBiochemistry, 1997
- Chaperone-assisted protein foldingCurrent Opinion in Structural Biology, 1997
- Substrate Shuttling Between the DnaK and GroEL Systems Indicates a Chaperone Network Promoting Protein FoldingJournal of Molecular Biology, 1996
- Polymerization of 70-kDa Heat Shock Protein by Yeast DnaJ in ATPJournal of Biological Chemistry, 1995