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146 related items for PubMed ID: 8218303

  • 1. 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]

  • 2. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 16; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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]

  • 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. 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]

  • 7. 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]

  • 8. 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]

  • 9. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine.
    Wunderlich M, Otto A, Maskos K, Mücke M, Seckler R, Glockshuber R.
    J Mol Biol; 1995 Mar 17; 247(1):28-33. PubMed ID: 7897659
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase.
    Darby NJ, Creighton TE.
    Biochemistry; 1995 Mar 21; 34(11):3576-87. PubMed ID: 7893654
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 13. 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]

  • 14. 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]

  • 15. Why is DsbA such an oxidizing disulfide catalyst?
    Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC.
    Cell; 1995 Dec 15; 83(6):947-55. PubMed ID: 8521518
    [Abstract] [Full Text] [Related]

  • 16. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase.
    Lundström-Ljung J, Holmgren A.
    J Biol Chem; 1995 Apr 07; 270(14):7822-8. PubMed ID: 7713872
    [Abstract] [Full Text] [Related]

  • 17. Monitoring Oxidative Folding of a Single Protein Catalyzed by the Disulfide Oxidoreductase DsbA.
    Kahn TB, Fernández JM, Perez-Jimenez R.
    J Biol Chem; 2015 Jun 05; 290(23):14518-27. PubMed ID: 25897077
    [Abstract] [Full Text] [Related]

  • 18. Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli.
    Hennecke J, Sillen A, Huber-Wunderlich M, Engelborghs Y, Glockshuber R.
    Biochemistry; 1997 May 27; 36(21):6391-400. PubMed ID: 9174355
    [Abstract] [Full Text] [Related]

  • 19. 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]

  • 20. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.
    Ostermeier M, De Sutter K, Georgiou G.
    J Biol Chem; 1996 May 03; 271(18):10616-22. PubMed ID: 8631865
    [Abstract] [Full Text] [Related]

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