Modulation of the ATPase Activity of the Molecular Chaperone DnaK by Peptides and the DnaJ and GrpE Heat Shock Proteins
Open Access
- 1 March 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (9) , 4563-4569
- https://doi.org/10.1074/jbc.270.9.4563
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Specificity of DnaK-peptide BindingJournal of Molecular Biology, 1994
- Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum.Molecular Biology of the Cell, 1993
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- 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
- Calculation of protein extinction coefficients from amino acid sequence dataAnalytical Biochemistry, 1989
- A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular ProteinsScience, 1989
- Peptide Binding and Release by Proteins Implicated as Catalysts of Protein AssemblyScience, 1989
- Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication.Proceedings of the National Academy of Sciences, 1988