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204 related items for PubMed ID: 9562546

  • 1. A single dipeptide sequence modulates the redox properties of a whole enzyme family.
    Huber-Wunderlich M, Glockshuber R.
    Fold Des; 1998; 3(3):161-71. PubMed ID: 9562546
    [Abstract] [Full Text] [Related]

  • 2. 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; 7(5):1233-44. PubMed ID: 9605329
    [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. Determination of the DeltapKa between the active site cysteines of thioredoxin and DsbA.
    Carvalho AT, Fernandes PA, Ramos MJ.
    J Comput Chem; 2006 Jun 15; 27(8):966-75. PubMed ID: 16586531
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. 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]

  • 7. Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.
    Netto LE, de Oliveira MA, Tairum CA, da Silva Neto JF.
    Free Radic Res; 2016 Jun 15; 50(2):206-45. PubMed ID: 26573728
    [Abstract] [Full Text] [Related]

  • 8. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.
    Jung CH, Thomas JA.
    Arch Biochem Biophys; 1996 Nov 01; 335(1):61-72. PubMed ID: 8914835
    [Abstract] [Full Text] [Related]

  • 9. 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]

  • 10. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.
    Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G.
    J Bacteriol; 2001 Feb 29; 183(3):980-8. PubMed ID: 11208797
    [Abstract] [Full Text] [Related]

  • 11. Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases.
    Siedler F, Rudolph-Böhner S, Doi M, Musiol HJ, Moroder L.
    Biochemistry; 1993 Jul 27; 32(29):7488-95. PubMed ID: 8338847
    [Abstract] [Full Text] [Related]

  • 12. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.
    Lundström J, Holmgren A.
    Biochemistry; 1993 Jul 06; 32(26):6649-55. PubMed ID: 8329391
    [Abstract] [Full Text] [Related]

  • 13. 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 06; 6(9):1893-900. PubMed ID: 9300489
    [Abstract] [Full Text] [Related]

  • 14. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria.
    Aslund F, Berndt KD, Holmgren A.
    J Biol Chem; 1997 Dec 05; 272(49):30780-6. PubMed ID: 9388218
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 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. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase.
    Lundström-Ljung J, Birnbach U, Rupp K, Söling HD, Holmgren A.
    FEBS Lett; 1995 Jan 09; 357(3):305-8. PubMed ID: 7835433
    [Abstract] [Full Text] [Related]

  • 18. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase.
    Lundström-Ljung J, Holmgren A.
    J Biol Chem; 1995 Apr 07; 270(14):7822-8. PubMed ID: 7713872
    [Abstract] [Full Text] [Related]

  • 19. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol.
    Höög JO, Jörnvall H, Holmgren A, Carlquist M, Persson M.
    Eur J Biochem; 1983 Oct 17; 136(1):223-32. PubMed ID: 6352262
    [Abstract] [Full Text] [Related]

  • 20. The CXC motif: a functional mimic of protein disulfide isomerase.
    Woycechowsky KJ, Raines RT.
    Biochemistry; 2003 May 13; 42(18):5387-94. PubMed ID: 12731880
    [Abstract] [Full Text] [Related]

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