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Journal Abstract Search

100 related items for PubMed ID: 8411164

  • 21. Mechanism of the electron transfer catalyst DsbB from Escherichia coli.
    Grauschopf U, Fritz A, Glockshuber R.
    EMBO J; 2003 Jul 15; 22(14):3503-13. PubMed ID: 12853466
    [Abstract] [Full Text] [Related]

  • 22. 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]

  • 23. 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]

  • 24. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA).
    Wunderlich M, Glockshuber R.
    J Biol Chem; 1993 Nov 25; 268(33):24547-50. PubMed ID: 7693702
    [Abstract] [Full Text] [Related]

  • 25. 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 25; 60(Pt 2):304-9. PubMed ID: 14747707
    [Abstract] [Full Text] [Related]

  • 26. 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]

  • 27. 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]

  • 28. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
    Martin JL, Waksman G, Bardwell JC, Beckwith J, Kuriyan J.
    J Mol Biol; 1993 Apr 05; 230(3):1097-100. PubMed ID: 8478925
    [Abstract] [Full Text] [Related]

  • 29. 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]

  • 30. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.
    Guddat LW, Bardwell JC, Martin JL.
    Structure; 1998 Jun 15; 6(6):757-67. PubMed ID: 9655827
    [Abstract] [Full Text] [Related]

  • 31. 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]

  • 32. Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties.
    Jacobi A, Huber-Wunderlich M, Hennecke J, Glockshuber R.
    J Biol Chem; 1997 Aug 29; 272(35):21692-9. PubMed ID: 9268296
    [Abstract] [Full Text] [Related]

  • 33. 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 29; 8(1):96-105. PubMed ID: 10210188
    [Abstract] [Full Text] [Related]

  • 34. 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]

  • 35. Human carbonic anhydrase IV: in vitro activation and purification of disulfide-bonded enzyme following expression in Escherichia coli.
    Waheed A, Pham T, Won M, Okuyama T, Sly WS.
    Protein Expr Purif; 1997 Mar 30; 9(2):279-87. PubMed ID: 9056493
    [Abstract] [Full Text] [Related]

  • 36. Effect of redox state on the folding free energy of a thermostable electron-transfer metalloprotein: the CuA domain of cytochrome oxidase from Thermus thermophilus.
    Wittung-Stafshede P, Malmstrom BG, Sanders D, Fee JA, Winkler JR, Gray HB.
    Biochemistry; 1998 Mar 03; 37(9):3172-7. PubMed ID: 9485471
    [Abstract] [Full Text] [Related]

  • 37. Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate.
    Ke H, Zhang S, Li J, Howlett GJ, Wang CC.
    Biochemistry; 2006 Dec 19; 45(50):15100-10. PubMed ID: 17154548
    [Abstract] [Full Text] [Related]

  • 38. Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase.
    Ruoppolo M, Freedman RB, Pucci P, Marino G.
    Biochemistry; 1996 Oct 22; 35(42):13636-46. PubMed ID: 8885843
    [Abstract] [Full Text] [Related]

  • 39. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.
    Kobayashi T, Ito K.
    EMBO J; 1999 Mar 01; 18(5):1192-8. PubMed ID: 10064586
    [Abstract] [Full Text] [Related]

  • 40. Catalysis of the oxidative folding of bovine pancreatic ribonuclease A by protein disulfide isomerase.
    Shin HC, Scheraga HA.
    J Mol Biol; 2000 Jul 21; 300(4):995-1003. PubMed ID: 10891284
    [Abstract] [Full Text] [Related]

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