These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

160 related items for PubMed ID: 9724776

  • 1. 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]

  • 2. 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]

  • 3. Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm.
    Eser M, Masip L, Kadokura H, Georgiou G, Beckwith J.
    Proc Natl Acad Sci U S A; 2009 Feb 03; 106(5):1572-7. PubMed ID: 19164554
    [Abstract] [Full Text] [Related]

  • 4. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.
    Stewart EJ, Aslund F, Beckwith J.
    EMBO J; 1998 Oct 01; 17(19):5543-50. PubMed ID: 9755155
    [Abstract] [Full Text] [Related]

  • 5. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
    Rietsch A, Bessette P, Georgiou G, Beckwith J.
    J Bacteriol; 1997 Nov 01; 179(21):6602-8. PubMed ID: 9352906
    [Abstract] [Full Text] [Related]

  • 6. A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins.
    Loferer H, Wunderlich M, Hennecke H, Glockshuber R.
    J Biol Chem; 1995 Nov 03; 270(44):26178-83. PubMed ID: 7592822
    [Abstract] [Full Text] [Related]

  • 7. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.
    Stewart EJ, Katzen F, Beckwith J.
    EMBO J; 1999 Nov 01; 18(21):5963-71. PubMed ID: 10545108
    [Abstract] [Full Text] [Related]

  • 8. Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant.
    Masip L, Klein-Marcuschamer D, Quan S, Bardwell JC, Georgiou G.
    J Biol Chem; 2008 Jan 11; 283(2):840-8. PubMed ID: 18003618
    [Abstract] [Full Text] [Related]

  • 9. On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.
    Debarbieux L, Beckwith J.
    J Bacteriol; 2000 Feb 11; 182(3):723-7. PubMed ID: 10633106
    [Abstract] [Full Text] [Related]

  • 10. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD.
    Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D.
    Biochemistry; 2002 Jun 04; 41(22):6920-7. PubMed ID: 12033924
    [Abstract] [Full Text] [Related]

  • 11. 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 04; 64():102800. PubMed ID: 37413765
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 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
    [Abstract] [Full Text] [Related]

  • 14. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.
    Derman AI, Prinz WA, Belin D, Beckwith J.
    Science; 1993 Dec 10; 262(5140):1744-7. PubMed ID: 8259521
    [Abstract] [Full Text] [Related]

  • 15. Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.
    Ke N, Landeta C, Wang X, Boyd D, Eser M, Beckwith J.
    J Bacteriol; 2018 Aug 15; 200(16):. PubMed ID: 29784887
    [Abstract] [Full Text] [Related]

  • 16. 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 15; 26(1):121-32. PubMed ID: 9383195
    [Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli.
    van Straaten M, Missiakas D, Raina S, Darby NJ.
    FEBS Lett; 1998 May 29; 428(3):255-8. PubMed ID: 9654144
    [Abstract] [Full Text] [Related]

  • 20. TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.
    Hemmis CW, Berkmen M, Eser M, Schildbach JF.
    J Bacteriol; 2011 Sep 29; 193(18):4588-97. PubMed ID: 21742866
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 8.