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811 related items for PubMed ID: 19965429

  • 1. A periplasmic reducing system protects single cysteine residues from oxidation.
    Depuydt M, Leonard SE, Vertommen D, Denoncin K, Morsomme P, Wahni K, Messens J, Carroll KS, Collet JF.
    Science; 2009 Nov 20; 326(5956):1109-11. PubMed ID: 19965429
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  • 2. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling.
    Shouldice SR, Cho SH, Boyd D, Heras B, Eser M, Beckwith J, Riggs P, Martin JL, Berkmen M.
    Mol Microbiol; 2010 Jan 20; 75(1):13-28. PubMed ID: 19968787
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  • 3. [A new protein system protects single cysteines against oxidative stress].
    Collet JF.
    Bull Mem Acad R Med Belg; 2010 Jan 20; 165(5-6):299-305. PubMed ID: 21513117
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  • 11. Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.
    Jonda S, Huber-Wunderlich M, Glockshuber R, Mössner E.
    EMBO J; 1999 Jun 15; 18(12):3271-81. PubMed ID: 10369668
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  • 14. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.
    Heras B, Edeling MA, Schirra HJ, Raina S, Martin JL.
    Proc Natl Acad Sci U S A; 2004 Jun 15; 101(24):8876-81. PubMed ID: 15184683
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  • 18. [Escherichia coli disulfide-forming related proteins: structures, functions and their application in gene engineering for expressing heterologous proteins in Escherichia coli].
    Zhang Z, Huang HL.
    Sheng Wu Gong Cheng Xue Bao; 2002 May 15; 18(3):261-6. PubMed ID: 12192853
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  • 19. High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study.
    Stirnimann CU, Rozhkova A, Grauschopf U, Böckmann RA, Glockshuber R, Capitani G, Grütter MG.
    J Mol Biol; 2006 May 05; 358(3):829-45. PubMed ID: 16545842
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