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Journal Abstract Search

487 related items for PubMed ID: 9755155

  • 1. 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]

  • 2. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.
    Prinz WA, Aslund F, Holmgren A, Beckwith J.
    J Biol Chem; 1997 Jun 20; 272(25):15661-7. PubMed ID: 9188456
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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 10; 179(21):6602-8. PubMed ID: 9352906
    [Abstract] [Full Text] [Related]

  • 5. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.
    Bessette PH, Aslund F, Beckwith J, Georgiou G.
    Proc Natl Acad Sci U S A; 1999 Nov 23; 96(24):13703-8. PubMed ID: 10570136
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  • 6. 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]

  • 7. 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
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  • 11. trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression.
    Sardesai AA, Gowrishankar J.
    J Bacteriol; 2001 Jan 01; 183(1):86-93. PubMed ID: 11114904
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  • 12. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.
    Jung CH, Thomas JA.
    Arch Biochem Biophys; 1996 Nov 01; 335(1):61-72. PubMed ID: 8914835
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  • 13. 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
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  • 14. Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
    Veine DM, Mulrooney SB, Wang PF, Williams CH.
    Protein Sci; 1998 Jun 03; 7(6):1441-50. PubMed ID: 9655349
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  • 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. Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli.
    Mössner E, Huber-Wunderlich M, Rietsch A, Beckwith J, Glockshuber R, Aslund F.
    J Biol Chem; 1999 Sep 03; 274(36):25254-9. PubMed ID: 10464247
    [Abstract] [Full Text] [Related]

  • 17. 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
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  • 18. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol.
    Höög JO, Jörnvall H, Holmgren A, Carlquist M, Persson M.
    Eur J Biochem; 1983 Oct 17; 136(1):223-32. PubMed ID: 6352262
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  • 19. Mechanism of the prokaryotic transmembrane disulfide reduction pathway and its in vitro reconstitution from purified components.
    Malojčić G, Geertsma ER, Brozzo MS, Glockshuber R.
    Angew Chem Int Ed Engl; 2012 Jul 09; 51(28):6900-3. PubMed ID: 22674494
    [Abstract] [Full Text] [Related]

  • 20. Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae.
    Trotter EW, Grant CM.
    Eukaryot Cell; 2005 Feb 09; 4(2):392-400. PubMed ID: 15701801
    [Abstract] [Full Text] [Related]

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