The Fe/S Assembly Protein IscU Behaves as a Substrate for the Molecular Chaperone Hsc66 from Escherichia coli
Open Access
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (3), 1696-1700
- https://doi.org/10.1074/jbc.m009542200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- Interaction of Hsp70 chaperones with substratesNature Structural & Molecular Biology, 1997
- Chaperone-assisted protein foldingCurrent Opinion in Structural Biology, 1997
- Kinetics of Peptide Binding to the Bovine 70 kDa Heat Shock Cognate Protein, a Molecular ChaperoneBiochemistry, 1996
- The Role of ATP in the Functional Cycle of the DnaK Chaperone SystemJournal of Molecular Biology, 1995
- Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock ProteinPublished by Elsevier ,1995
- Kinetics of Molecular Chaperone ActionScience, 1994
- Specificity of DnaK-peptide BindingJournal of Molecular Biology, 1994
- ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysisNature, 1993
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990