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Journal Abstract Search

149 related items for PubMed ID: 8155639

  • 1. Protein folding activities of Escherichia coli protein disulfide isomerase.
    Joly JC, Swartz JR.
    Biochemistry; 1994 Apr 12; 33(14):4231-6. PubMed ID: 8155639
    [Abstract] [Full Text] [Related]

  • 2. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA).
    Wunderlich M, Glockshuber R.
    J Biol Chem; 1993 Nov 25; 268(33):24547-50. PubMed ID: 7693702
    [Abstract] [Full Text] [Related]

  • 3. Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH.
    Wunderlich M, Otto A, Seckler R, Glockshuber R.
    Biochemistry; 1993 Nov 16; 32(45):12251-6. PubMed ID: 8218303
    [Abstract] [Full Text] [Related]

  • 4. The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.
    Wunderlich M, Jaenicke R, Glockshuber R.
    J Mol Biol; 1993 Oct 20; 233(4):559-66. PubMed ID: 8411164
    [Abstract] [Full Text] [Related]

  • 5. Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    Biochemistry; 1996 Sep 03; 35(35):11386-95. PubMed ID: 8784194
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.
    Zapun A, Creighton TE.
    Biochemistry; 1994 May 03; 33(17):5202-11. PubMed ID: 7513556
    [Abstract] [Full Text] [Related]

  • 8. DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding.
    Frech C, Schmid FX.
    J Biol Chem; 1995 Mar 10; 270(10):5367-74. PubMed ID: 7890650
    [Abstract] [Full Text] [Related]

  • 9. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.
    Zapun A, Cooper L, Creighton TE.
    Biochemistry; 1994 Feb 22; 33(7):1907-14. PubMed ID: 8110795
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 17; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

  • 12. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.
    Zapun A, Bardwell JC, Creighton TE.
    Biochemistry; 1993 May 18; 32(19):5083-92. PubMed ID: 8494885
    [Abstract] [Full Text] [Related]

  • 13. Preferential binding of an unfolded protein to DsbA.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    EMBO J; 1996 Jan 15; 15(2):392-98. PubMed ID: 8617214
    [Abstract] [Full Text] [Related]

  • 14. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product.
    Akiyama Y, Kamitani S, Kusukawa N, Ito K.
    J Biol Chem; 1992 Nov 05; 267(31):22440-5. PubMed ID: 1429594
    [Abstract] [Full Text] [Related]

  • 15. A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.
    de Crouy-Chanel A, Kohiyama M, Richarme G.
    J Biol Chem; 1995 Sep 29; 270(39):22669-72. PubMed ID: 7559385
    [Abstract] [Full Text] [Related]

  • 16. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.
    Jacob-Dubuisson F, Pinkner J, Xu Z, Striker R, Padmanhaban A, Hultgren SJ.
    Proc Natl Acad Sci U S A; 1994 Nov 22; 91(24):11552-6. PubMed ID: 7972100
    [Abstract] [Full Text] [Related]

  • 17. Identification of a protein required for disulfide bond formation in vivo.
    Bardwell JC, McGovern K, Beckwith J.
    Cell; 1991 Nov 01; 67(3):581-9. PubMed ID: 1934062
    [Abstract] [Full Text] [Related]

  • 18. 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 01; 64():102800. PubMed ID: 37413765
    [Abstract] [Full Text] [Related]

  • 19. 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]

  • 20. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
    Zapun A, Missiakas D, Raina S, Creighton TE.
    Biochemistry; 1995 Apr 18; 34(15):5075-89. PubMed ID: 7536035
    [Abstract] [Full Text] [Related]

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