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280 related items for PubMed ID: 16357193

  • 1. 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]

  • 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. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation.
    Huber D, Boyd D, Xia Y, Olma MH, Gerstein M, Beckwith J.
    J Bacteriol; 2005 May 15; 187(9):2983-91. PubMed ID: 15838024
    [Abstract] [Full Text] [Related]

  • 4. The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway.
    Schierle CF, Berkmen M, Huber D, Kumamoto C, Boyd D, Beckwith J.
    J Bacteriol; 2003 Oct 15; 185(19):5706-13. PubMed ID: 13129941
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. 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]

  • 7. F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues.
    Elton TC, Holland SJ, Frost LS, Hazes B.
    J Bacteriol; 2005 Dec 20; 187(24):8267-77. PubMed ID: 16321931
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. [Study on disulfide bond formation protein A in Escherichia coli].
    Luo M, Guan YX, Yao SJ.
    Sheng Wu Gong Cheng Xue Bao; 2007 Jan 17; 23(1):7-15. PubMed ID: 17366881
    [Abstract] [Full Text] [Related]

  • 10. A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.
    Ribnicky B, Van Blarcom T, Georgiou G.
    J Mol Biol; 2007 Jun 08; 369(3):631-9. PubMed ID: 17462668
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.
    Debarbieux L, Beckwith J.
    J Bacteriol; 2000 Feb 01; 182(3):723-7. PubMed ID: 10633106
    [Abstract] [Full Text] [Related]

  • 13. Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli.
    Cho SH, Beckwith J.
    J Bacteriol; 2006 Jul 01; 188(14):5066-76. PubMed ID: 16816179
    [Abstract] [Full Text] [Related]

  • 14. 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
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57.
    Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, Holmgren A.
    Biochemistry; 1997 Mar 04; 36(9):2622-36. PubMed ID: 9054569
    [Abstract] [Full Text] [Related]

  • 17. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones.
    Levy R, Weiss R, Chen G, Iverson BL, Georgiou G.
    Protein Expr Purif; 2001 Nov 04; 23(2):338-47. PubMed ID: 11676610
    [Abstract] [Full Text] [Related]

  • 18. 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 04; 179(21):6602-8. PubMed ID: 9352906
    [Abstract] [Full Text] [Related]

  • 19. 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 04; 183(3):980-8. PubMed ID: 11208797
    [Abstract] [Full Text] [Related]

  • 20. Effect of folding on the export of ribose-binding protein studied with the genetically isolated suppressors for the signal sequence mutation.
    Song T, Park C.
    J Mol Biol; 1995 Oct 20; 253(2):304-12. PubMed ID: 7563091
    [Abstract] [Full Text] [Related]

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