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Journal Abstract Search

402 related items for PubMed ID: 1577742

  • 21. Redox properties of a thioredoxin-like Arabidopsis protein, AtTDX.
    Kim SG, Chi YH, Lee JS, Schlesinger SR, Zabet-Moghaddam M, Chung JS, Knaff DB, Kim ST, Lee SY, Kim SK.
    Biochim Biophys Acta; 2010 Dec; 1804(12):2213-21. PubMed ID: 20849982
    [Abstract] [Full Text] [Related]

  • 22. Enzymatic catalysis of disulfide formation.
    Noiva R.
    Protein Expr Purif; 1994 Feb; 5(1):1-13. PubMed ID: 7909462
    [Abstract] [Full Text] [Related]

  • 23. Conserved residues flanking the thiol/disulfide centers of protein disulfide isomerase are not essential for catalysis of thiol/disulfide exchange.
    Lu X, Gilbert HF, Harper JW.
    Biochemistry; 1992 May 05; 31(17):4205-10. PubMed ID: 1567868
    [Abstract] [Full Text] [Related]

  • 24. A 21-kDa C-terminal fragment of protein-disulfide isomerase has isomerase, chaperone, and anti-chaperone activities.
    Puig A, Primm TP, Surendran R, Lee JC, Ballard KD, Orkiszewski RS, Makarov V, Gilbert HF.
    J Biol Chem; 1997 Dec 26; 272(52):32988-94. PubMed ID: 9407079
    [Abstract] [Full Text] [Related]

  • 25. Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding.
    Cabrele C, Fiori S, Pegoraro S, Moroder L.
    Chem Biol; 2002 Jun 26; 9(6):731-40. PubMed ID: 12079785
    [Abstract] [Full Text] [Related]

  • 26. Salmonella enterica BcfH Is a Trimeric Thioredoxin-Like Bifunctional Enzyme with Both Thiol Oxidase and Disulfide Isomerase Activities.
    Subedi P, Paxman JJ, Wang G, Hor L, Hong Y, Verderosa AD, Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B.
    Antioxid Redox Signal; 2021 Jul 26; 35(1):21-39. PubMed ID: 33607928
    [Abstract] [Full Text] [Related]

  • 27. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase.
    Lyles MM, Gilbert HF.
    Biochemistry; 1991 Jan 22; 30(3):619-25. PubMed ID: 1988051
    [Abstract] [Full Text] [Related]

  • 28. 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
    [Abstract] [Full Text] [Related]

  • 29. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer.
    Lyles MM, Gilbert HF.
    Biochemistry; 1991 Jan 22; 30(3):613-9. PubMed ID: 1988050
    [Abstract] [Full Text] [Related]

  • 30. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen.
    Kumar S, Björnstedt M, Holmgren A.
    Eur J Biochem; 1992 Jul 15; 207(2):435-39. PubMed ID: 1321713
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  • 37. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria.
    Aslund F, Berndt KD, Holmgren A.
    J Biol Chem; 1997 Dec 05; 272(49):30780-6. PubMed ID: 9388218
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  • 38. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.
    Kulp MS, Frickel EM, Ellgaard L, Weissman JS.
    J Biol Chem; 2006 Jan 13; 281(2):876-84. PubMed ID: 16368681
    [Abstract] [Full Text] [Related]

  • 39. The thioredoxin antioxidant system.
    Lu J, Holmgren A.
    Free Radic Biol Med; 2014 Jan 13; 66():75-87. PubMed ID: 23899494
    [Abstract] [Full Text] [Related]

  • 40. Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
    Veine DM, Mulrooney SB, Wang PF, Williams CH.
    Protein Sci; 1998 Jun 13; 7(6):1441-50. PubMed ID: 9655349
    [Abstract] [Full Text] [Related]

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