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Journal Abstract Search

485 related items for PubMed ID: 24483600

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  • 4. Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.
    Kojima R, Okumura M, Masui S, Kanemura S, Inoue M, Saiki M, Yamaguchi H, Hikima T, Suzuki M, Akiyama S, Inaba K.
    Structure; 2014 Mar 04; 22(3):431-43. PubMed ID: 24462249
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  • 6. Salmonella enterica BcfH Is a Trimeric Thioredoxin-Like Bifunctional Enzyme with Both Thiol Oxidase and Disulfide Isomerase Activities.
    Subedi P, Paxman JJ, Wang G, Hor L, Hong Y, Verderosa AD, Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B.
    Antioxid Redox Signal; 2021 Jul 04; 35(1):21-39. PubMed ID: 33607928
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  • 7. Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.
    Hudson DA, Gannon SA, Thorpe C.
    Free Radic Biol Med; 2015 Mar 04; 80():171-82. PubMed ID: 25091901
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  • 8. 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
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  • 9. Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase.
    Rancy PC, Thorpe C.
    Biochemistry; 2008 Nov 18; 47(46):12047-56. PubMed ID: 18937500
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  • 10. Enzymatic catalysis of disulfide formation.
    Noiva R.
    Protein Expr Purif; 1994 Feb 18; 5(1):1-13. PubMed ID: 7909462
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  • 11. 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
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  • 12. 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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  • 13. Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72.
    Kozlov G, Azeroual S, Rosenauer A, Määttänen P, Denisov AY, Thomas DY, Gehring K.
    J Mol Biol; 2010 Aug 27; 401(4):618-25. PubMed ID: 20600112
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  • 14. The oxidoreductase behavior of protein disulfide isomerase impedes fold maturation of endoplasmic reticulum-processed proteins in the pivotal structure-coupled step of oxidative folding: implications for subcellular protein trafficking.
    Gonzalez V, Pal R, Narayan M.
    Biochemistry; 2010 Jul 27; 49(29):6282-9. PubMed ID: 20568731
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  • 15. Methods to identify the substrates of thiol-disulfide oxidoreductases.
    Fujimoto T, Inaba K, Kadokura H.
    Protein Sci; 2019 Jan 27; 28(1):30-40. PubMed ID: 30341785
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  • 16. Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding.
    Kramer B, Ferrari DM, Klappa P, Pöhlmann N, Söling HD.
    Biochem J; 2001 Jul 01; 357(Pt 1):83-95. PubMed ID: 11415439
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  • 17. Pathways of disulfide bond formation in Escherichia coli.
    Messens J, Collet JF.
    Int J Biochem Cell Biol; 2006 Jul 01; 38(7):1050-62. PubMed ID: 16446111
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  • 18. Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone.
    Wang L, Wang X, Wang CC.
    Free Radic Biol Med; 2015 Jun 01; 83():305-13. PubMed ID: 25697778
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  • 19. Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding.
    Okumura M, Noi K, Kanemura S, Kinoshita M, Saio T, Inoue Y, Hikima T, Akiyama S, Ogura T, Inaba K.
    Nat Chem Biol; 2019 May 01; 15(5):499-509. PubMed ID: 30992562
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  • 20. Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum.
    Okumura M, Kadokura H, Inaba K.
    Free Radic Biol Med; 2015 Jun 01; 83():314-22. PubMed ID: 25697777
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