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Journal Abstract Search

96 related items for PubMed ID: 10210189

  • 1. On the non-respect of the thermodynamic cycle by DsbA variants.
    Moutiez M, Burova TV, Haertlé T, Quéméneur E.
    Protein Sci; 1999 Jan; 8(1):106-12. PubMed ID: 10210189
    [Abstract] [Full Text] [Related]

  • 2. 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; 8(1):96-105. PubMed ID: 10210188
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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]

  • 5. 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 17; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 6. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 17; 27(8):966-75. PubMed ID: 16586531
    [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. 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]

  • 9. 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 05; 60(Pt 2):304-9. PubMed ID: 14747707
    [Abstract] [Full Text] [Related]

  • 10. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 05; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. 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]

  • 13. 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 02; 7(10):2065-80. PubMed ID: 9792093
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. [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]

  • 16. 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]

  • 17. The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity.
    Meinhold D, Beach M, Shao Y, Osuna R, Colón W.
    Biochemistry; 2006 Aug 15; 45(32):9767-77. PubMed ID: 16893178
    [Abstract] [Full Text] [Related]

  • 18. Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex.
    Couprie J, Vinci F, Dugave C, Quéméneur E, Moutiez M.
    Biochemistry; 2000 Jun 06; 39(22):6732-42. PubMed ID: 10828992
    [Abstract] [Full Text] [Related]

  • 19. 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]

  • 20. Description of the topographical changes associated to the different stages of the DsbA catalytic cycle.
    Vinci F, Couprie J, Pucci P, Quéméneur E, Moutiez M.
    Protein Sci; 2002 Jul 15; 11(7):1600-12. PubMed ID: 12070313
    [Abstract] [Full Text] [Related]

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