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Journal Abstract Search


758 related items for PubMed ID: 8784194

  • 1. 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]

  • 2. 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]

  • 3. Folding of horse cytochrome c in the reduced state.
    Bhuyan AK, Udgaonkar JB.
    J Mol Biol; 2001 Oct 05; 312(5):1135-60. PubMed ID: 11580255
    [Abstract] [Full Text] [Related]

  • 4. Disulfide formation and stability of a cysteine-rich repeat protein from Helicobacter pylori.
    Devi VS, Sprecher CB, Hunziker P, Mittl PR, Bosshard HR, Jelesarov I.
    Biochemistry; 2006 Feb 14; 45(6):1599-607. PubMed ID: 16460007
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  • 5. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 14; 2(5):717-26. PubMed ID: 8495194
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  • 8. 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
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  • 9. Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor.
    Ma LC, Anderson S.
    Biochemistry; 1997 Mar 25; 36(12):3728-36. PubMed ID: 9132026
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  • 10. Increased folding stability of TEM-1 beta-lactamase by in vitro selection.
    Kather I, Jakob RP, Dobbek H, Schmid FX.
    J Mol Biol; 2008 Oct 31; 383(1):238-51. PubMed ID: 18706424
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  • 11. 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
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  • 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
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  • 13. Oxidation of kinetically trapped thiols by protein disulfide isomerase.
    Walker KW, Gilbert HF.
    Biochemistry; 1995 Oct 17; 34(41):13642-50. PubMed ID: 7577954
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  • 14. 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]

  • 15. The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy.
    Kuwajima K, Yamaya H, Sugai S.
    J Mol Biol; 1996 Dec 13; 264(4):806-22. PubMed ID: 8980687
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  • 17. Folding and oxidation of the antibody domain C(H)3.
    Thies MJ, Talamo F, Mayer M, Bell S, Ruoppolo M, Marino G, Buchner J.
    J Mol Biol; 2002 Jun 21; 319(5):1267-77. PubMed ID: 12079363
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  • 18. Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange.
    Houry WA, Scheraga HA.
    Biochemistry; 1996 Sep 10; 35(36):11734-46. PubMed ID: 8794754
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  • 20. Conversion of a catalytic into a structural disulfide bond by circular permutation.
    Hennecke J, Glockshuber R.
    Biochemistry; 1998 Dec 15; 37(50):17590-7. PubMed ID: 9860875
    [Abstract] [Full Text] [Related]


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