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Volumn 8, Issue 13, 1998, Pages

Protein folding: A missing redox link in the endoplasmic reticulum

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EID: 0032543557     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0960-9822(98)70295-7     Document Type: Article
Times cited : (30)

References (9)
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  • 2
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    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR, Kaiser CA: The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Molecular Cell 1998, 1:161-170.
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    • Frand, A.R.1    Kaiser, C.A.2
  • 3
    • 0031610364 scopus 로고    scopus 로고
    • Ero1 p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ, Weissmann JS: Ero1 p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Molecular Cell 1998, 1:171-182.
    • (1998) Molecular Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissmann, J.S.3
  • 4
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    • Protein disulphide bond synthesis: A possible intracellular mechanism
    • Ziegler DM, Poulsen LL: Protein disulphide bond synthesis: a possible intracellular mechanism. Trends Biochem Sci 1977, 2:79-81.
    • (1977) Trends Biochem Sci , vol.2 , pp. 79-81
    • Ziegler, D.M.1    Poulsen, L.L.2
  • 6
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF: Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 7
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    • On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes
    • Creighton TE, Bagley CJ, Cooper L, Darby NJ, Freedman RB, Kemmink J, Sheikh A: On the biosynthesis of bovine pancreatic trypsin inhibitor (BPTI). Structure, processing, folding and disulphide bond formation of the precursor in vitro and in microsomes. J Mol Biol 1993, 232:1176-1196.
    • (1993) J Mol Biol , vol.232 , pp. 1176-1196
    • Creighton, T.E.1    Bagley, C.J.2    Cooper, L.3    Darby, N.J.4    Freedman, R.B.5    Kemmink, J.6    Sheikh, A.7
  • 8
    • 0027250528 scopus 로고
    • Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes
    • Marquadt T, Hebert DN, Helenius A: Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes. J Biol Chem 1993, 268:19618-19625.
    • (1993) J Biol Chem , vol.268 , pp. 19618-19625
    • Marquadt, T.1    Hebert, D.N.2    Helenius, A.3
  • 9
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    • PDI and glutathione-mediated reduction of the glutathionylated variant of human lysozyme
    • Hayano T, Inaka K, Otsu M, Taniyama Y, Miki K, Matsushima M, Kikuchi M: PDI and glutathione-mediated reduction of the glutathionylated variant of human lysozyme. FEBS Lett 1993, 328:203-208.
    • (1993) FEBS Lett , vol.328 , pp. 203-208
    • Hayano, T.1    Inaka, K.2    Otsu, M.3    Taniyama, Y.4    Miki, K.5    Matsushima, M.6    Kikuchi, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.