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713 related items for PubMed ID: 10369668

  • 21. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

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

  • 23. Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli.
    Skórko-Glonek J, Sobiecka-Szkatuła A, Lipińska B.
    Acta Biochim Pol; 2006 Jan; 53(3):585-9. PubMed ID: 17019443
    [Abstract] [Full Text] [Related]

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

  • 25. Oxidative folding and reductive activities of EhPDI, a protein disulfide isomerase from Entamoeba histolytica.
    Mares RE, Magaña PD, Meléndez-López SG, Licea AF, Cornejo-Bravo JM, Ramos MA.
    Parasitol Int; 2009 Sep; 58(3):311-3. PubMed ID: 19361571
    [Abstract] [Full Text] [Related]

  • 26. [Redox properties and conformational changes of DsbA protein from Escherichia coli periplasm].
    Li Q, Hu HY.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai); 2002 Sep; 34(5):583-8. PubMed ID: 12198560
    [Abstract] [Full Text] [Related]

  • 27. 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
    [Abstract] [Full Text] [Related]

  • 28. Periplasmic chaperones used to enhance functional secretion of proteins in E. coli.
    Schlapschy M, Skerra A.
    Methods Mol Biol; 2011 Nov 01; 705():211-24. PubMed ID: 21125388
    [Abstract] [Full Text] [Related]

  • 29. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling.
    Shouldice SR, Cho SH, Boyd D, Heras B, Eser M, Beckwith J, Riggs P, Martin JL, Berkmen M.
    Mol Microbiol; 2010 Jan 01; 75(1):13-28. PubMed ID: 19968787
    [Abstract] [Full Text] [Related]

  • 30. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding.
    Guddat LW, Bardwell JC, Zander T, Martin JL.
    Protein Sci; 1997 Jun 01; 6(6):1148-56. PubMed ID: 9194175
    [Abstract] [Full Text] [Related]

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  • 32. 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]

  • 33. A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli.
    Schlapschy M, Grimm S, Skerra A.
    Protein Eng Des Sel; 2006 Aug 11; 19(8):385-90. PubMed ID: 16720693
    [Abstract] [Full Text] [Related]

  • 34. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
    McCarthy AA, Haebel PW, Törrönen A, Rybin V, Baker EN, Metcalf P.
    Nat Struct Biol; 2000 Mar 11; 7(3):196-9. PubMed ID: 10700276
    [Abstract] [Full Text] [Related]

  • 35. 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 11; 64():102800. PubMed ID: 37413765
    [Abstract] [Full Text] [Related]

  • 36. Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase.
    Zhan X, Schwaller M, Gilbert HF, Georgiou G.
    Biotechnol Prog; 1999 Aug 11; 15(6):1033-8. PubMed ID: 10585186
    [Abstract] [Full Text] [Related]

  • 37. Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopy.
    Couprie J, Remerowski ML, Bailleul A, Courçon M, Gilles N, Quéméneur E, Jamin N.
    Protein Sci; 1998 Oct 11; 7(10):2065-80. PubMed ID: 9792093
    [Abstract] [Full Text] [Related]

  • 38. A single dipeptide sequence modulates the redox properties of a whole enzyme family.
    Huber-Wunderlich M, Glockshuber R.
    Fold Des; 1998 Oct 11; 3(3):161-71. PubMed ID: 9562546
    [Abstract] [Full Text] [Related]

  • 39. 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]

  • 40. 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]

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