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Journal Abstract Search


90 related items for PubMed ID: 7783200

  • 1. A molecular model for the redox potential difference between thioredoxin and DsbA, based on electrostatics calculations.
    Gane PJ, Freedman RB, Warwicker J.
    J Mol Biol; 1995 Jun 02; 249(2):376-87. PubMed ID: 7783200
    [Abstract] [Full Text] [Related]

  • 2. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 02; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

  • 3. Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.
    Foloppe N, Sagemark J, Nordstrand K, Berndt KD, Nilsson L.
    J Mol Biol; 2001 Jul 06; 310(2):449-70. PubMed ID: 11428900
    [Abstract] [Full Text] [Related]

  • 4. Crystal structure of the DsbA protein required for disulphide bond formation in vivo.
    Martin JL, Bardwell JC, Kuriyan J.
    Nature; 1993 Sep 30; 365(6445):464-8. PubMed ID: 8413591
    [Abstract] [Full Text] [Related]

  • 5. 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 30; 6(6):1148-56. PubMed ID: 9194175
    [Abstract] [Full Text] [Related]

  • 6. 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 30; 7(5):1233-44. PubMed ID: 9605329
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. 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 20; 60(Pt 2):304-9. PubMed ID: 14747707
    [Abstract] [Full Text] [Related]

  • 9. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase.
    Kortemme T, Darby NJ, Creighton TE.
    Biochemistry; 1996 Nov 19; 35(46):14503-11. PubMed ID: 8931546
    [Abstract] [Full Text] [Related]

  • 10. 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 19; 7(10):2065-80. PubMed ID: 9792093
    [Abstract] [Full Text] [Related]

  • 11. Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family.
    Kortemme T, Creighton TE.
    J Mol Biol; 1995 Nov 10; 253(5):799-812. PubMed ID: 7473753
    [Abstract] [Full Text] [Related]

  • 12. The zinc center influences the redox and thermodynamic properties of Escherichia coli thioredoxin 2.
    El Hajjaji H, Dumoulin M, Matagne A, Colau D, Roos G, Messens J, Collet JF.
    J Mol Biol; 2009 Feb 13; 386(1):60-71. PubMed ID: 19073194
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. 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]

  • 15. 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]

  • 16. 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]

  • 17. Enzymatic catalysis of disulfide formation.
    Noiva R.
    Protein Expr Purif; 1994 Feb 05; 5(1):1-13. PubMed ID: 7909462
    [Abstract] [Full Text] [Related]

  • 18. Role of the variable active site residues in the function of thioredoxin family oxidoreductases.
    Carvalho AT, Fernandes PA, Swart M, Van Stralen JN, Bickelhaupt FM, Ramos MJ.
    J Comput Chem; 2009 Apr 15; 30(5):710-24. PubMed ID: 18780356
    [Abstract] [Full Text] [Related]

  • 19. Calculations of electrostatic interactions and pKas in the active site of Escherichia coli thioredoxin.
    Dillet V, Dyson HJ, Bashford D.
    Biochemistry; 1998 Jul 14; 37(28):10298-306. PubMed ID: 9665738
    [Abstract] [Full Text] [Related]

  • 20. Probing the flexibility of the DsbA oxidoreductase from Vibrio cholerae--a 15N - 1H heteronuclear NMR relaxation analysis of oxidized and reduced forms of DsbA.
    Horne J, d'Auvergne EJ, Coles M, Velkov T, Chin Y, Charman WN, Prankerd R, Gooley PR, Scanlon MJ.
    J Mol Biol; 2007 Aug 17; 371(3):703-16. PubMed ID: 17585933
    [Abstract] [Full Text] [Related]


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