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261 related items for PubMed ID: 17366881

  • 1. [Study on disulfide bond formation protein A in Escherichia coli].
    Luo M, Guan YX, Yao SJ.
    Sheng Wu Gong Cheng Xue Bao; 2007 Jan; 23(1):7-15. PubMed ID: 17366881
    [Abstract] [Full Text] [Related]

  • 2. Conversion of a catalytic into a structural disulfide bond by circular permutation.
    Hennecke J, Glockshuber R.
    Biochemistry; 1998 Dec 15; 37(50):17590-7. PubMed ID: 9860875
    [Abstract] [Full Text] [Related]

  • 3. 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 15; 7(3):196-9. PubMed ID: 10700276
    [Abstract] [Full Text] [Related]

  • 4. Crystal structure of the DsbA protein required for disulphide bond formation in vivo.
    Martin JL, Bardwell JC, Kuriyan J.
    Nature; 1993 Sep 30; 365(6445):464-8. PubMed ID: 8413591
    [Abstract] [Full Text] [Related]

  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. Pathways of disulfide bond formation in Escherichia coli.
    Messens J, Collet JF.
    Int J Biochem Cell Biol; 2006 Jun 15; 38(7):1050-62. PubMed ID: 16446111
    [Abstract] [Full Text] [Related]

  • 7. Structure of reduced DsbA from Escherichia coli in solution.
    Schirra HJ, Renner C, Czisch M, Huber-Wunderlich M, Holak TA, Glockshuber R.
    Biochemistry; 1998 May 05; 37(18):6263-76. PubMed ID: 9572841
    [Abstract] [Full Text] [Related]

  • 8. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding.
    Guddat LW, Bardwell JC, Zander T, Martin JL.
    Protein Sci; 1997 Jun 05; 6(6):1148-56. PubMed ID: 9194175
    [Abstract] [Full Text] [Related]

  • 9. 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 05; 63(Pt 4):465-71. PubMed ID: 17372350
    [Abstract] [Full Text] [Related]

  • 10. Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    Biochemistry; 1996 Sep 03; 35(35):11386-95. PubMed ID: 8784194
    [Abstract] [Full Text] [Related]

  • 11. Enzymatic catalysis of disulfide formation.
    Noiva R.
    Protein Expr Purif; 1994 Feb 03; 5(1):1-13. PubMed ID: 7909462
    [Abstract] [Full Text] [Related]

  • 12. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
    Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL.
    Protein Sci; 1997 Sep 03; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli.
    Skórko-Glonek J, Sobiecka-Szkatuła A, Lipińska B.
    Acta Biochim Pol; 2006 Jul 18; 53(3):585-9. PubMed ID: 17019443
    [Abstract] [Full Text] [Related]

  • 15. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding.
    Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J.
    Science; 2004 Jan 23; 303(5657):534-7. PubMed ID: 14739460
    [Abstract] [Full Text] [Related]

  • 16. DsbA directs efficient expression of outer membrane secretin EscC of the enteropathogenic Escherichia coli type III secretion apparatus.
    Miki T, Okada N, Kim Y, Abe A, Danbara H.
    Microb Pathog; 2008 Feb 23; 44(2):151-8. PubMed ID: 17933489
    [Abstract] [Full Text] [Related]

  • 17. [Redox properties and conformational changes of DsbA protein from Escherichia coli periplasm].
    Li Q, Hu HY.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai); 2002 Sep 23; 34(5):583-8. PubMed ID: 12198560
    [Abstract] [Full Text] [Related]

  • 18. Disulfide bond formation system in Escherichia coli.
    Inaba K.
    J Biochem; 2009 Nov 23; 146(5):591-7. PubMed ID: 19567379
    [Abstract] [Full Text] [Related]

  • 19. 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
    [Abstract] [Full Text] [Related]

  • 20. Heterologous expression of lipase in Escherichia coli is limited by folding and disulfide bond formation.
    Xu Y, Yasin A, Tang R, Scharer JM, Moo-Young M, Chou CP.
    Appl Microbiol Biotechnol; 2008 Nov 06; 81(1):79-87. PubMed ID: 18758768
    [Abstract] [Full Text] [Related]

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