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Journal Abstract Search

219 related items for PubMed ID: 2394726

  • 1. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.
    Wells WW, Xu DP, Yang YF, Rocque PA.
    J Biol Chem; 1990 Sep 15; 265(26):15361-4. PubMed ID: 2394726
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  • 2. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.
    Jung CH, Thomas JA.
    Arch Biochem Biophys; 1996 Nov 01; 335(1):61-72. PubMed ID: 8914835
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  • 3. The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin).
    Washburn MP, Wells WW.
    Biochemistry; 1999 Jan 05; 38(1):268-74. PubMed ID: 9890907
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  • 4. Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase.
    Washburn MP, Wells WW.
    Biochem Biophys Res Commun; 1999 Apr 13; 257(2):567-71. PubMed ID: 10198252
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  • 5. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins.
    Yoshitake S, Nanri H, Fernando MR, Minakami S.
    J Biochem; 1994 Jul 13; 116(1):42-6. PubMed ID: 7798184
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  • 6. Sensitivity of protein sulfhydryl repair enzymes to oxidative stress.
    Starke DW, Chen Y, Bapna CP, Lesnefsky EJ, Mieyal JJ.
    Free Radic Biol Med; 1997 Jul 13; 23(3):373-84. PubMed ID: 9214573
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  • 7. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity.
    Lundström J, Holmgren A.
    J Biol Chem; 1990 Jun 05; 265(16):9114-20. PubMed ID: 2188973
    [Abstract] [Full Text] [Related]

  • 8. Dehydroascorbate reduction.
    Wells WW, Xu DP.
    J Bioenerg Biomembr; 1994 Aug 05; 26(4):369-77. PubMed ID: 7844111
    [Abstract] [Full Text] [Related]

  • 9. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
    Gravina SA, Mieyal JJ.
    Biochemistry; 1993 Apr 06; 32(13):3368-76. PubMed ID: 8461300
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  • 11. Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.
    Washburn MP, Wells WW.
    Free Radic Biol Med; 1997 Apr 06; 23(4):563-70. PubMed ID: 9215802
    [Abstract] [Full Text] [Related]

  • 12. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.
    Lundström J, Holmgren A.
    Biochemistry; 1993 Jul 06; 32(26):6649-55. PubMed ID: 8329391
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  • 16. Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione.
    Peltoniemi MJ, Karala AR, Jurvansuu JK, Kinnula VL, Ruddock LW.
    J Biol Chem; 2006 Nov 03; 281(44):33107-14. PubMed ID: 16956877
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  • 19. Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase.
    Soute BA, Groenen-van Dooren MM, Holmgren A, Lundström J, Vermeer C.
    Biochem J; 1992 Jan 01; 281 ( Pt 1)(Pt 1):255-9. PubMed ID: 1731762
    [Abstract] [Full Text] [Related]

  • 20. Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphides.
    Mannervik B, Axelsson K, Sundewall AC, Holmgren A.
    Biochem J; 1983 Aug 01; 213(2):519-23. PubMed ID: 6351844
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