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Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

219 related items for PubMed ID: 9407079

  • 21.
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  • 22. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.
    Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE.
    Curr Biol; 1997 Apr 01; 7(4):239-45. PubMed ID: 9094311
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  • 23. Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site.
    Quan H, Fan G, Wang CC.
    J Biol Chem; 1995 Jul 21; 270(29):17078-80. PubMed ID: 7615500
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  • 24. Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate.
    Hawkins HC, Blackburn EC, Freedman RB.
    Biochem J; 1991 Apr 15; 275 ( Pt 2)(Pt 2):349-53. PubMed ID: 2025222
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  • 27. Isomerase and chaperone activities of protein disulfide isomerase are both required for its function as a foldase.
    Wang CC.
    Biochemistry (Mosc); 1998 Apr 15; 63(4):407-12. PubMed ID: 9556523
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  • 29. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.
    Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H.
    Cell; 2006 Jan 13; 124(1):61-73. PubMed ID: 16413482
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  • 33. PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.
    van Lith M, Hartigan N, Hatch J, Benham AM.
    J Biol Chem; 2005 Jan 14; 280(2):1376-83. PubMed ID: 15475357
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  • 36. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.
    Koivunen P, Pirneskoski A, Karvonen P, Ljung J, Helaakoski T, Notbohm H, Kivirikko KI.
    EMBO J; 1999 Jan 04; 18(1):65-74. PubMed ID: 9878051
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