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244 related items for PubMed ID: 9572841

  • 1. 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]

  • 2. NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
    Xia TH, Bushweller JH, Sodano P, Billeter M, Björnberg O, Holmgren A, Wüthrich K.
    Protein Sci; 1992 Mar 05; 1(3):310-21. PubMed ID: 1304339
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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]

  • 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 15; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 6. Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
    Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM.
    Biochemistry; 1997 Mar 04; 36(9):2517-30. PubMed ID: 9054557
    [Abstract] [Full Text] [Related]

  • 7. 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 04; 8(1):96-105. PubMed ID: 10210188
    [Abstract] [Full Text] [Related]

  • 8. 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 04; 7(10):2065-80. PubMed ID: 9792093
    [Abstract] [Full Text] [Related]

  • 9. 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]

  • 10. 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]

  • 11. 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 06; 6(6):1148-56. PubMed ID: 9194175
    [Abstract] [Full Text] [Related]

  • 12. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 06; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. [Study on disulfide bond formation protein A in Escherichia coli].
    Luo M, Guan YX, Yao SJ.
    Sheng Wu Gong Cheng Xue Bao; 2007 Jan 30; 23(1):7-15. PubMed ID: 17366881
    [Abstract] [Full Text] [Related]

  • 15. The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.
    Bushweller JH, Billeter M, Holmgren A, Wüthrich K.
    J Mol Biol; 1994 Feb 04; 235(5):1585-97. PubMed ID: 8107093
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.
    Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y.
    J Mol Biol; 1997 May 30; 269(1):142-53. PubMed ID: 9193006
    [Abstract] [Full Text] [Related]

  • 18. Determination of the structure of oxidised Desulfovibrio africanus ferredoxin I by 1H NMR spectroscopy and comparison of its solution structure with its crystal structure.
    Davy SL, Osborne MJ, Moore GR.
    J Mol Biol; 1998 Apr 03; 277(3):683-706. PubMed ID: 9533888
    [Abstract] [Full Text] [Related]

  • 19. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
    McCarthy AA, Haebel PW, Törrönen A, Rybin V, Baker EN, Metcalf P.
    Nat Struct Biol; 2000 Mar 03; 7(3):196-9. PubMed ID: 10700276
    [Abstract] [Full Text] [Related]

  • 20. 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]

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