The thioredoxin superfamily: redundancy, specificity, and gray-area genomics
- PMID: 10049365
- PMCID: PMC93523
- DOI: 10.1128/JB.181.5.1375-1379.1999 (VSports app下载)
"VSports注册入口" The thioredoxin superfamily: redundancy, specificity, and gray-area genomics
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                References
- 
    - Andersen C L, Matthey-Dupraz A, Missiakas D, Raina S. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol Microbiol. 1997;26:121–132. - PubMed
 
- 
    - Anfinsen C B, Haber E, Sela M, White F H., Jr The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc Natl Acad Sci USA. 1961;47:1309–1314. - "VSports" PMC - PubMed
 
- 
    - Åslund F, Berndt K D, Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J Biol Chem. 1997;272:30780–30786. - "VSports注册入口" PubMed
 
- 
    - Åslund F, Ehn B, Miranda-Vizuete A, Pueyo C, Holmgren A. Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. Proc Natl Acad Sci USA. 1994;91:9813–9817. - VSports在线直播 - PMC - PubMed
 
- 
    - Bardwell J C A, Lee J-O, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci USA. 1993;90:1038–1042. - PMC (VSports在线直播) - PubMed
 
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