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244 related items for PubMed ID: 11080145

  • 1. 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]

  • 2. The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli.
    Sardesai AA, Genevaux P, Schwager F, Ang D, Georgopoulos C.
    EMBO J; 2003 Apr 01; 22(7):1461-6. PubMed ID: 12660153
    [Abstract] [Full Text] [Related]

  • 3. 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 01; 26(1):121-32. PubMed ID: 9383195
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli.
    Lippa AM, Goulian M.
    J Bacteriol; 2012 Mar 15; 194(6):1457-63. PubMed ID: 22267510
    [Abstract] [Full Text] [Related]

  • 6. 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 15; 183(3):980-8. PubMed ID: 11208797
    [Abstract] [Full Text] [Related]

  • 7. The dsbA-dsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance.
    Hayashi S, Abe M, Kimoto M, Furukawa S, Nakazawa T.
    Microbiol Immunol; 2000 Feb 15; 44(1):41-50. PubMed ID: 10711598
    [Abstract] [Full Text] [Related]

  • 8. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.
    Pan JL, Sliskovic I, Bardwell JC.
    J Mol Biol; 2008 Apr 11; 377(5):1433-42. PubMed ID: 18325532
    [Abstract] [Full Text] [Related]

  • 9. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.
    Missiakas D, Schwager F, Raina S.
    EMBO J; 1995 Jul 17; 14(14):3415-24. PubMed ID: 7628442
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. The dithiol:disulfide oxidoreductases DsbA and DsbB of Rhodobacter capsulatus are not directly involved in cytochrome c biogenesis, but their inactivation restores the cytochrome c biogenesis defect of CcdA-null mutants.
    Deshmukh M, Turkarslan S, Astor D, Valkova-Valchanova M, Daldal F.
    J Bacteriol; 2003 Jun 26; 185(11):3361-72. PubMed ID: 12754234
    [Abstract] [Full Text] [Related]

  • 12. The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli.
    Knoke LR, Zimmermann J, Lupilov N, Schneider JF, Celebi B, Morgan B, Leichert LI.
    Redox Biol; 2023 Aug 26; 64():102800. PubMed ID: 37413765
    [Abstract] [Full Text] [Related]

  • 13. Oversynthesis of a new Escherichia coli small RNA suppresses export toxicity of DsbA'-PhoA unfoldable periplasmic proteins.
    Guigueno A, Dassa J, Belin P, Boquet PL.
    J Bacteriol; 2001 Feb 26; 183(4):1147-58. PubMed ID: 11157926
    [Abstract] [Full Text] [Related]

  • 14. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA.
    Bader MW, Hiniker A, Regeimbal J, Goldstone D, Haebel PW, Riemer J, Metcalf P, Bardwell JC.
    EMBO J; 2001 Apr 02; 20(7):1555-62. PubMed ID: 11285220
    [Abstract] [Full Text] [Related]

  • 15. [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 02; 18(3):261-6. PubMed ID: 12192853
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
    Kadokura H, Beckwith J.
    EMBO J; 2002 May 15; 21(10):2354-63. PubMed ID: 12006488
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. 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]

  • 20. Proteome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, dsbA.
    Malhotra S, Silo-Suh LA, Mathee K, Ohman DE.
    J Bacteriol; 2000 Dec 20; 182(24):6999-7006. PubMed ID: 11092861
    [Abstract] [Full Text] [Related]

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