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Journal Abstract Search

127 related items for PubMed ID: 10047491

  • 1. 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]

  • 2. 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]

  • 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. 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]

  • 5. Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.
    Otzen DE, Fersht AR.
    Biochemistry; 1998 Jun 02; 37(22):8139-46. PubMed ID: 9609709
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. 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 02; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 8. 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 02; 6(6):1148-56. PubMed ID: 9194175
    [Abstract] [Full Text] [Related]

  • 9. 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]

  • 10. Circular permutation of granulocyte colony-stimulating factor.
    Feng Y, Minnerly JC, Zurfluh LL, Joy WD, Hood WF, Abegg AL, Grabbe ES, Shieh JJ, Thurman TL, McKearn JP, McWherter CA.
    Biochemistry; 1999 Apr 06; 38(14):4553-63. PubMed ID: 10194377
    [Abstract] [Full Text] [Related]

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  • 12. [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 06; 34(5):583-8. PubMed ID: 12198560
    [Abstract] [Full Text] [Related]

  • 13. Systematic circular permutation of an entire protein reveals essential folding elements.
    Iwakura M, Nakamura T, Yamane C, Maki K.
    Nat Struct Biol; 2000 Jul 06; 7(7):580-5. PubMed ID: 10876245
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  • 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]

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  • 17. 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]

  • 18. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 01; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

  • 19. The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond.
    Parrini C, Bemporad F, Baroncelli A, Gianni S, Travaglini-Allocatelli C, Kohn JE, Ramazzotti M, Chiti F, Taddei N.
    J Mol Biol; 2008 Jun 20; 379(5):1107-18. PubMed ID: 18495159
    [Abstract] [Full Text] [Related]

  • 20. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding.
    Kadokura H, Tian H, Zander T, Bardwell JC, Beckwith J.
    Science; 2004 Jan 23; 303(5657):534-7. PubMed ID: 14739460
    [Abstract] [Full Text] [Related]

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