Mutant AhpC Peroxiredoxins Suppress Thiol-Disulfide Redox Deficiencies and Acquire Deglutathionylating Activity
- 1 January 2008
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 29 (1) , 36-45
- https://doi.org/10.1016/j.molcel.2007.11.029
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (R01 GM041883, R01 GM050389)
This publication has 20 references indexed in Scilit:
- Cysteine Reactivity and Thiol−Disulfide Interchange Pathways in AhpF and AhpC of the Bacterial Alkyl Hydroperoxide Reductase SystemBiochemistry, 2007
- A Novel Monothiol Glutaredoxin (Grx4) from Escherichia coli Can Serve as a Substrate for Thioredoxin ReductaseJournal of Biological Chemistry, 2005
- PeroxiredoxinsBiological Chemistry, 2002
- Regulation of Thioredoxin Peroxidase Activity by C-terminal TruncationArchives of Biochemistry and Biophysics, 2002
- Bridge over Troubled WatersCell, 1999
- Roles for the Two Cysteine Residues of AhpC in Catalysis of Peroxide Reduction by Alkyl Hydroperoxide Reductase from Salmonella typhimuriumBiochemistry, 1997
- Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studiesJournal of Bacteriology, 1995
- Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon.Proceedings of the National Academy of Sciences, 1992
- OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins.Proceedings of the National Academy of Sciences, 1989
- Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimuriumCell, 1985