A Bacterial Thioredoxin-like Protein That Is Exposed to the Periplasm Has Redox Properties Comparable with Those of Cytoplasmic Thioredoxins
Open Access
- 1 November 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (44), 26178-26183
- https://doi.org/10.1074/jbc.270.44.26178
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Expression, purification and functional properties of a soluble form of Bradyrhizobium japonicum TlpA, a thioredoxin‐like proteinEuropean Journal of Biochemistry, 1994
- Cytochrome c biogenesis in bacteria: a possible pathway begins to emergeMolecular Microbiology, 1994
- The Redox Properties of Protein Disulfide Isomerase (DsbA) of Escherichia coli Result from a Tense Conformation of its Oxidized FormJournal of Molecular Biology, 1993
- Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxinBiochemistry, 1993
- Identification of a protein required for disulfide bond formation in vivoCell, 1991
- Genetic analysis of the cytochrome c‐aa3 branch of the Bradyrhizobium japonicum respiratory chainMolecular Microbiology, 1990
- Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolutionJournal of Molecular Biology, 1990
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesJournal of Molecular Biology, 1986
- Selective N-bromosuccinimide oxidation of the nonfluorescent tryptophan-31 in the active center of thioredoxin from Escherichia coliBiochemistry, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970