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Journal Abstract Search

219 related items for PubMed ID: 9407079

  • 1. A 21-kDa C-terminal fragment of protein-disulfide isomerase has isomerase, chaperone, and anti-chaperone activities.
    Puig A, Primm TP, Surendran R, Lee JC, Ballard KD, Orkiszewski RS, Makarov V, Gilbert HF.
    J Biol Chem; 1997 Dec 26; 272(52):32988-94. PubMed ID: 9407079
    [Abstract] [Full Text] [Related]

  • 2. Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.
    Lyles MM, Gilbert HF.
    J Biol Chem; 1994 Dec 09; 269(49):30946-52. PubMed ID: 7983029
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  • 3. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine.
    Walker KW, Lyles MM, Gilbert HF.
    Biochemistry; 1996 Feb 13; 35(6):1972-80. PubMed ID: 8639681
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  • 4. A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.
    Lundström J, Krause G, Holmgren A.
    J Biol Chem; 1992 May 05; 267(13):9047-52. PubMed ID: 1577742
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  • 5. Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth.
    Xiao R, Solovyov A, Gilbert HF, Holmgren A, Lundström-Ljung J.
    J Biol Chem; 2001 Jul 27; 276(30):27975-80. PubMed ID: 11375405
    [Abstract] [Full Text] [Related]

  • 6. A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain.
    Wilkinson B, Xiao R, Gilbert HF.
    J Biol Chem; 2005 Mar 25; 280(12):11483-7. PubMed ID: 15649885
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  • 13. Catalysis of protein disulfide bond isomerization in a homogeneous substrate.
    Kersteen EA, Barrows SR, Raines RT.
    Biochemistry; 2005 Sep 13; 44(36):12168-78. PubMed ID: 16142915
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  • 14. 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 13; 7(3):196-9. PubMed ID: 10700276
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  • 15. Thioredoxin domain non-equivalence and anti-chaperone activity of protein disulfide isomerase mutants in vivo.
    Whiteley EM, Hsu TA, Betenbaugh MJ.
    J Biol Chem; 1997 Sep 05; 272(36):22556-63. PubMed ID: 9278409
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  • 16. The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.
    Puig A, Lyles MM, Noiva R, Gilbert HF.
    J Biol Chem; 1994 Jul 22; 269(29):19128-35. PubMed ID: 7913469
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  • 17. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase.
    Schwaller M, Wilkinson B, Gilbert HF.
    J Biol Chem; 2003 Feb 28; 278(9):7154-9. PubMed ID: 12486139
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  • 18. 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
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  • 19. The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability.
    Luz JM, Lennarz WJ.
    Biochem Biophys Res Commun; 1998 Jul 30; 248(3):621-7. PubMed ID: 9703976
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  • 20. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.
    Darby NJ, Creighton TE.
    Biochemistry; 1995 Sep 19; 34(37):11725-35. PubMed ID: 7547904
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