High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA , selB and selC genes 1 1Edited by M. Gottesman
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (5) , 1003-1016
- https://doi.org/10.1006/jmbi.1999.3085
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Preparation and assay of mammalian thioredoxin and thioredoxin reductasePublished by Elsevier ,1999
- The 58 kDa mouse selenoprotein is a BCNU‐sensitive thioredoxin reductaseFEBS Letters, 1997
- The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coliProceedings of the National Academy of Sciences, 1997
- Efficient Reduction of Lipoamide and Lipoic Acid by Mammalian Thioredoxin ReductaseBiochemical and Biophysical Research Communications, 1996
- Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.Proceedings of the National Academy of Sciences, 1996
- 1-Chloro-2,4-dinitrobenzene Is an Irreversible Inhibitor of Human Thioredoxin ReductasePublished by Elsevier ,1995
- Overproduction of a selenocysteine‐containing polypeptide in Escherichia coli: the fdhF gene productMolecular Microbiology, 1992
- Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressorJournal of Molecular Biology, 1991
- Selenocysteine: the 21st amino acidMolecular Microbiology, 1991
- One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution.Proceedings of the National Academy of Sciences, 1989