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166 related items for PubMed ID: 9254601

  • 1. 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]

  • 2. [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 19; 18(3):261-6. PubMed ID: 12192853
    [Abstract] [Full Text] [Related]

  • 3. The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.
    Wunderlich M, Jaenicke R, Glockshuber R.
    J Mol Biol; 1993 Oct 20; 233(4):559-66. PubMed ID: 8411164
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. 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 06; 53(3):585-9. PubMed ID: 17019443
    [Abstract] [Full Text] [Related]

  • 6. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 06; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

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  • 8. 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]

  • 9. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.
    Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G.
    J Bacteriol; 2001 Feb 03; 183(3):980-8. PubMed ID: 11208797
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. Preferential binding of an unfolded protein to DsbA.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    EMBO J; 1996 Jan 15; 15(2):392-98. PubMed ID: 8617214
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 13. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.
    Hiniker A, Collet JF, Bardwell JC.
    J Biol Chem; 2005 Oct 07; 280(40):33785-91. PubMed ID: 16087673
    [Abstract] [Full Text] [Related]

  • 14. 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 07; 67(2):336-49. PubMed ID: 18036138
    [Abstract] [Full Text] [Related]

  • 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. 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]

  • 17. The disulfide bond formation (Dsb) system.
    Ito K, Inaba K.
    Curr Opin Struct Biol; 2008 Aug 27; 18(4):450-8. PubMed ID: 18406599
    [Abstract] [Full Text] [Related]

  • 18. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins.
    Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S.
    Mol Microbiol; 1997 Oct 27; 26(1):121-32. PubMed ID: 9383195
    [Abstract] [Full Text] [Related]

  • 19. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.
    Missiakas D, Georgopoulos C, Raina S.
    EMBO J; 1994 Apr 15; 13(8):2013-20. PubMed ID: 8168498
    [Abstract] [Full Text] [Related]

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

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