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222 related items for PubMed ID: 19968787

  • 1. 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; 75(1):13-28. PubMed ID: 19968787
    [Abstract] [Full Text] [Related]

  • 2. 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
    [Abstract] [Full Text] [Related]

  • 3. Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli.
    Skórko-Glonek J, Sobiecka-Szkatuła A, Lipińska B.
    Acta Biochim Pol; 2006 Nov 20; 53(3):585-9. PubMed ID: 17019443
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  • 4. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
    McCarthy AA, Haebel PW, Törrönen A, Rybin V, Baker EN, Metcalf P.
    Nat Struct Biol; 2000 Mar 20; 7(3):196-9. PubMed ID: 10700276
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  • 6. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.
    Joly JC, Swartz JR.
    Biochemistry; 1997 Aug 19; 36(33):10067-72. PubMed ID: 9254601
    [Abstract] [Full Text] [Related]

  • 7. Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate.
    Ke H, Zhang S, Li J, Howlett GJ, Wang CC.
    Biochemistry; 2006 Dec 19; 45(50):15100-10. PubMed ID: 17154548
    [Abstract] [Full Text] [Related]

  • 8. 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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  • 9. Laboratory evolution of one disulfide isomerase to resemble another.
    Hiniker A, Ren G, Heras B, Zheng Y, Laurinec S, Jobson RW, Stuckey JA, Martin JL, Bardwell JC.
    Proc Natl Acad Sci U S A; 2007 Jul 10; 104(28):11670-5. PubMed ID: 17609373
    [Abstract] [Full Text] [Related]

  • 10. [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 10; 18(3):261-6. PubMed ID: 12192853
    [Abstract] [Full Text] [Related]

  • 11. DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.
    Maskos K, Huber-Wunderlich M, Glockshuber R.
    J Mol Biol; 2003 Jan 17; 325(3):495-513. PubMed ID: 12498799
    [Abstract] [Full Text] [Related]

  • 12. Editing disulphide bonds: error correction using redox currencies.
    Ito K.
    Mol Microbiol; 2010 Jan 17; 75(1):1-5. PubMed ID: 19906178
    [Abstract] [Full Text] [Related]

  • 13. Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.
    Segatori L, Paukstelis PJ, Gilbert HF, Georgiou G.
    Proc Natl Acad Sci U S A; 2004 Jul 06; 101(27):10018-23. PubMed ID: 15220477
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  • 15. In vivo substrate specificity of periplasmic disulfide oxidoreductases.
    Hiniker A, Bardwell JC.
    J Biol Chem; 2004 Mar 26; 279(13):12967-73. PubMed ID: 14726535
    [Abstract] [Full Text] [Related]

  • 16. DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli.
    Grimshaw JP, Stirnimann CU, Brozzo MS, Malojcic G, Grütter MG, Capitani G, Glockshuber R.
    J Mol Biol; 2008 Jul 18; 380(4):667-80. PubMed ID: 18565543
    [Abstract] [Full Text] [Related]

  • 17. Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG.
    Yeh SM, Koon N, Squire C, Metcalf P.
    Acta Crystallogr D Biol Crystallogr; 2007 Apr 18; 63(Pt 4):465-71. PubMed ID: 17372350
    [Abstract] [Full Text] [Related]

  • 18. The oxidase DsbA folds a protein with a nonconsecutive disulfide.
    Messens J, Collet JF, Van Belle K, Brosens E, Loris R, Wyns L.
    J Biol Chem; 2007 Oct 26; 282(43):31302-7. PubMed ID: 17702751
    [Abstract] [Full Text] [Related]

  • 19. The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
    Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora JP, Messens J, Bardwell JC, Collet JF.
    Mol Microbiol; 2008 Jan 26; 67(2):336-49. PubMed ID: 18036138
    [Abstract] [Full Text] [Related]

  • 20. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.
    Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P.
    EMBO J; 2002 Sep 16; 21(18):4774-84. PubMed ID: 12234918
    [Abstract] [Full Text] [Related]

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