Substrate Recognition by the ClpA Chaperone Component of ClpAP Protease
Open Access
- 1 November 2000
- journal article
- Published by Elsevier
- Vol. 275 (45), 35361-35367
- https://doi.org/10.1074/jbc.m006288200
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- ClpB Cooperates with DnaK, DnaJ, and GrpE in Suppressing Protein AggregationJournal of Biological Chemistry, 1999
- Hsp104, Hsp70, and Hsp40Cell, 1998
- The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperoneProceedings of the National Academy of Sciences, 1997
- Mechanism of protein remodeling by ClpA chaperoneProceedings of the National Academy of Sciences, 1997
- Protein quality control: triage by chaperones and proteases.Genes & Development, 1997
- Disassembly of the Mu transposase tetramer by the ClpX chaperone.Genes & Development, 1995
- The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.The EMBO Journal, 1995
- A molecular chaperone, ClpA, functions like DnaK and DnaJ.Proceedings of the National Academy of Sciences, 1994
- Protein disaggregation mediated by heat-shock protein Hspl04Nature, 1994
- The Clp proteins: proteolysis regulators or molecular chaperones?Journal of Bacteriology, 1992