Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40
Open Access
- 1 August 1996
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 271 (32), 19617-19624
- https://doi.org/10.1074/jbc.271.32.19617
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- The role of molecular chaperones in protein folding.The FASEB Journal, 1995
- The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure TopologyBiochemistry, 1995
- Specificity of DnaK-peptide BindingJournal of Molecular Biology, 1994
- Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiPCell, 1993
- ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysisNature, 1993
- MOLECULAR CHAPERONE FUNCTIONS OF HEAT-SHOCK PROTEINSAnnual Review of Biochemistry, 1993
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Protein folding in the cellNature, 1992
- Peptide-binding specificity of the molecular chaperone BiPNature, 1991
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990