These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

100 related items for PubMed ID: 8411164

  • 1. 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]

  • 2. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.
    Wunderlich M, Glockshuber R.
    Protein Sci; 1993 May 20; 2(5):717-26. PubMed ID: 8495194
    [Abstract] [Full Text] [Related]

  • 3. [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 20; 34(5):583-8. PubMed ID: 12198560
    [Abstract] [Full Text] [Related]

  • 4. Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    Biochemistry; 1996 Sep 03; 35(35):11386-95. PubMed ID: 8784194
    [Abstract] [Full Text] [Related]

  • 5. Preferential binding of an unfolded protein to DsbA.
    Frech C, Wunderlich M, Glockshuber R, Schmid FX.
    EMBO J; 1996 Jan 15; 15(2):392-98. PubMed ID: 8617214
    [Abstract] [Full Text] [Related]

  • 6. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.
    Joly JC, Swartz JR.
    Biochemistry; 1997 Aug 19; 36(33):10067-72. PubMed ID: 9254601
    [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 19; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. 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]

  • 10. On the non-respect of the thermodynamic cycle by DsbA variants.
    Moutiez M, Burova TV, Haertlé T, Quéméneur E.
    Protein Sci; 1999 Jan 02; 8(1):106-12. PubMed ID: 10210189
    [Abstract] [Full Text] [Related]

  • 11. 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 02; 7(5):1233-44. PubMed ID: 9605329
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 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. 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]

  • 15. 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 15; 6(6):1148-56. PubMed ID: 9194175
    [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. Protein folding activities of Escherichia coli protein disulfide isomerase.
    Joly JC, Swartz JR.
    Biochemistry; 1994 Apr 12; 33(14):4231-6. PubMed ID: 8155639
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. 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]

  • 20. Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH.
    Wunderlich M, Otto A, Seckler R, Glockshuber R.
    Biochemistry; 1993 Nov 16; 32(45):12251-6. PubMed ID: 8218303
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 5.