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713 related items for PubMed ID: 10369668

  • 1. 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]

  • 2. Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli.
    Hennecke J, Sillen A, Huber-Wunderlich M, Engelborghs Y, Glockshuber R.
    Biochemistry; 1997 May 27; 36(21):6391-400. PubMed ID: 9174355
    [Abstract] [Full Text] [Related]

  • 3. An engineered pathway for the formation of protein disulfide bonds.
    Masip L, Pan JL, Haldar S, Penner-Hahn JE, DeLisa MP, Georgiou G, Bardwell JC, Collet JF.
    Science; 2004 Feb 20; 303(5661):1185-9. PubMed ID: 14976313
    [Abstract] [Full Text] [Related]

  • 4. Enzymatic catalysis of disulfide formation.
    Noiva R.
    Protein Expr Purif; 1994 Feb 20; 5(1):1-13. PubMed ID: 7909462
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.
    Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U.
    Acta Crystallogr D Biol Crystallogr; 2004 Feb 15; 60(Pt 2):304-9. PubMed ID: 14747707
    [Abstract] [Full Text] [Related]

  • 7. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.
    Mössner E, Huber-Wunderlich M, Glockshuber R.
    Protein Sci; 1998 May 15; 7(5):1233-44. PubMed ID: 9605329
    [Abstract] [Full Text] [Related]

  • 8. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 15; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

  • 9. 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]

  • 10. 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]

  • 11. Pathways of disulfide bond formation in Escherichia coli.
    Messens J, Collet JF.
    Int J Biochem Cell Biol; 2006 Jan 23; 38(7):1050-62. PubMed ID: 16446111
    [Abstract] [Full Text] [Related]

  • 12. Mechanism of the electron transfer catalyst DsbB from Escherichia coli.
    Grauschopf U, Fritz A, Glockshuber R.
    EMBO J; 2003 Jul 15; 22(14):3503-13. PubMed ID: 12853466
    [Abstract] [Full Text] [Related]

  • 13. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm.
    Debarbieux L, Beckwith J.
    Proc Natl Acad Sci U S A; 1998 Sep 01; 95(18):10751-6. PubMed ID: 9724776
    [Abstract] [Full Text] [Related]

  • 14. 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]

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

  • 16. Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: evidence that chaperone activity is the prime effect of thioredoxin.
    Jurado P, de Lorenzo V, Fernández LA.
    J Mol Biol; 2006 Mar 17; 357(1):49-61. PubMed ID: 16427080
    [Abstract] [Full Text] [Related]

  • 17. Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.
    Inaba K, Ito K.
    EMBO J; 2002 Jun 03; 21(11):2646-54. PubMed ID: 12032077
    [Abstract] [Full Text] [Related]

  • 18. Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin.
    Dartigalongue C, Nikaido H, Raina S.
    EMBO J; 2000 Nov 15; 19(22):5980-8. PubMed ID: 11080145
    [Abstract] [Full Text] [Related]

  • 19. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
    Nakamoto H, Bardwell JC.
    Biochim Biophys Acta; 2004 Nov 11; 1694(1-3):111-9. PubMed ID: 15546661
    [Abstract] [Full Text] [Related]

  • 20. A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.
    Huber D, Cha MI, Debarbieux L, Planson AG, Cruz N, López G, Tasayco ML, Chaffotte A, Beckwith J.
    Proc Natl Acad Sci U S A; 2005 Dec 27; 102(52):18872-7. PubMed ID: 16357193
    [Abstract] [Full Text] [Related]

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