The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a weak protein oxidoreductase
- 12 May 2006
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 343 (3) , 780-786
- https://doi.org/10.1016/j.bbrc.2006.03.028
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding SiteJournal of Biological Chemistry, 2003
- Identity and Functions of CxxC-Derived MotifsBiochemistry, 2003
- Physiological functions of thioredoxin and thioredoxin reductaseEuropean Journal of Biochemistry, 2000
- Thioredoxin 2 Is Involved in the Oxidative Stress Response inEscherichia coliJournal of Biological Chemistry, 2000
- Electron Avenue: Pathways of Disulfide Bond Formation and IsomerizationCell, 1999
- Cloning, Expression, and Characterization of a NovelEscherichia coli ThioredoxinJournal of Biological Chemistry, 1997
- The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasmJournal of Biological Chemistry, 1997
- A Novel Function of Escherichia coli Chaperone DnaJJournal of Biological Chemistry, 1995
- Mutations that Allow Disulfide Bond Formation in the Cytoplasm of Escherichia coliScience, 1993
- Thioredoxin-catalyzed refolding of disulfide-containing proteins.Proceedings of the National Academy of Sciences, 1986