Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases
- 20 July 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 310 (4) , 907-918
- https://doi.org/10.1006/jmbi.2001.4721
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- The NMR solution structure of human glutaredoxin in the fully reduced formJournal of Molecular Biology, 1998
- Thioredoxin —a fold for all reasonsStructure, 1995
- [29] GlutaredoxinPublished by Elsevier ,1995
- Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductaseBiochemistry, 1993
- Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14.fwdarw.S) and its mixed disulfide with glutathioneBiochemistry, 1992
- Sequence-specific1H n.m.r. assignments and determination of the three-dimensional structure of reduced escherichia coli glutaredoxinJournal of Molecular Biology, 1991
- The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pairEuropean Journal of Biochemistry, 1984
- The primary structure of Escherichia coli glutaredoxinEuropean Journal of Biochemistry, 1983
- Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.Proceedings of the National Academy of Sciences, 1979
- Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.Proceedings of the National Academy of Sciences, 1976