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203 related items for PubMed ID: 9860875

  • 1. 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]

  • 2. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
    Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL.
    Protein Sci; 1997 Sep 15; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 3. Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.
    Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U.
    Acta Crystallogr D Biol Crystallogr; 2004 Feb 15; 60(Pt 2):304-9. PubMed ID: 14747707
    [Abstract] [Full Text] [Related]

  • 4. Structure of reduced DsbA from Escherichia coli in solution.
    Schirra HJ, Renner C, Czisch M, Huber-Wunderlich M, Holak TA, Glockshuber R.
    Biochemistry; 1998 May 05; 37(18):6263-76. PubMed ID: 9572841
    [Abstract] [Full Text] [Related]

  • 5. 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]

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

  • 7. 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]

  • 8. Random circular permutation of DsbA reveals segments that are essential for protein folding and stability.
    Hennecke J, Sebbel P, Glockshuber R.
    J Mol Biol; 1999 Mar 05; 286(4):1197-215. PubMed ID: 10047491
    [Abstract] [Full Text] [Related]

  • 9. On the role of the cis-proline residue in the active site of DsbA.
    Charbonnier JB, Belin P, Moutiez M, Stura EA, Quéméneur E.
    Protein Sci; 1999 Jan 05; 8(1):96-105. PubMed ID: 10210188
    [Abstract] [Full Text] [Related]

  • 10. A single dipeptide sequence modulates the redox properties of a whole enzyme family.
    Huber-Wunderlich M, Glockshuber R.
    Fold Des; 1998 Jan 05; 3(3):161-71. PubMed ID: 9562546
    [Abstract] [Full Text] [Related]

  • 11. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 05; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

  • 12. Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.
    Mössner E, Huber-Wunderlich M, Glockshuber R.
    Protein Sci; 1998 May 05; 7(5):1233-44. PubMed ID: 9605329
    [Abstract] [Full Text] [Related]

  • 13. [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 05; 34(5):583-8. PubMed ID: 12198560
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.
    Ondo-Mbele E, Vivès C, Koné A, Serre L.
    J Mol Biol; 2005 Apr 01; 347(3):555-63. PubMed ID: 15755450
    [Abstract] [Full Text] [Related]

  • 16. Pathways of disulfide bond formation in Escherichia coli.
    Messens J, Collet JF.
    Int J Biochem Cell Biol; 2006 Apr 01; 38(7):1050-62. PubMed ID: 16446111
    [Abstract] [Full Text] [Related]

  • 17. Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.
    Inaba K, Ito K.
    EMBO J; 2002 Jun 03; 21(11):2646-54. PubMed ID: 12032077
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. 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]

  • 20. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 20; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

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