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Volumn 19, Issue 10, 2010, Pages 1863-1876

Steps in reductive activation of the disulfide-generating enzyme Ero1p

Author keywords

Disulfide bond formation; Enzyme activation; Flavin adenine dinucleotide; Lag phase

Indexed keywords

DISULFIDE; ERO1P ENZYME; FUNGAL ENZYME; UNCLASSIFIED DRUG;

EID: 77957322919     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.473     Document Type: Article
Times cited : (22)

References (22)
  • 2
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR, Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1:161-170.
    • (1998) Mol Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 3
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ, Weissman JS (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1:171-182.
    • (1998) Mol Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 4
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide bond formation and the ER redox environment by feedback regulation of Ero1
    • Sevier CS, Qu H, Heldman N, Gross E, Fass D, Kaiser CA (2007) Modulation of cellular disulfide bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129:333-344.
    • (2007) Cell , vol.129 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 6
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • Gross E, Kastner DB, Kaiser CA, Fass D (2004) Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117:601-610.
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 8
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM (1971) The interpretation of protein structures: estimation of static accessibility. J Mol Biol 55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 9
    • 0034494605 scopus 로고    scopus 로고
    • Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum
    • Frand AR, Kaiser CA (2000) Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol Biol Cell 11:2833-2843.
    • (2000) Mol Biol Cell , vol.11 , pp. 2833-2843
    • Frand, A.R.1    Kaiser, C.A.2
  • 10
    • 33745761475 scopus 로고    scopus 로고
    • Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1
    • Sevier CS, Kaiser CA (2006) Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1. Mol Biol Cell 17:2256-2266.
    • (2006) Mol Biol Cell , vol.17 , pp. 2256-2266
    • Sevier, C.S.1    Kaiser, C.A.2
  • 11
    • 56549124032 scopus 로고    scopus 로고
    • Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation
    • Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H, Bulleid NJ (2008) Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation. EMBO J 27:2988-2997.
    • (2008) EMBO J , vol.27 , pp. 2988-2997
    • Baker, K.M.1    Chakravarthi, S.2    Langton, K.P.3    Sheppard, A.M.4    Lu, H.5    Bulleid, N.J.6
  • 12
    • 77953313165 scopus 로고    scopus 로고
    • Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum
    • Vitu E, Kim S, Sevier CS, Lutzky O, Heldman N, Bentzur M, Unger T, Yona M, Kaiser CA, Fass D (2010) Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum. J Biol Chem 285:18155-18165.
    • (2010) J Biol Chem , vol.285 , pp. 18155-18165
    • Vitu, E.1    Kim, S.2    Sevier, C.S.3    Lutzky, O.4    Heldman, N.5    Bentzur, M.6    Unger, T.7    Yona, M.8    Kaiser, C.A.9    Fass, D.10
  • 13
    • 0036142325 scopus 로고    scopus 로고
    • A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
    • DOI 10.1038/nsb740
    • Gross E, Sevier CS, Vala A, Kaiser CA, Fass D (2002) A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol 9:61-67. (Pubitemid 34049182)
    • (2002) Nature Structural Biology , vol.9 , Issue.1 , pp. 61-67
    • Gross, E.1    Sevier, C.S.2    Vala, A.3    Kaiser, C.A.4    Fass, D.5
  • 14
    • 0033525472 scopus 로고    scopus 로고
    • Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo
    • DOI 10.1006/jmbi.1999.2560
    • Westphal V, Darby NJ, Winther JR (1999) Functional properties of the two redox-active sites in yeast protein disulfide isomerase in vitro and in vivo. J Mol Biol 286:1229-1239. (Pubitemid 29116687)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.4 , pp. 1229-1239
    • Westphal, V.1    Darby, N.J.2    Winther, J.R.3
  • 15
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman GL. (1958) A colorimetric method for determining low concentrations of mercaptans. Arch Biochem Biophys 74:443-450.
    • (1958) Arch Biochem Biophys , vol.74 , pp. 443-450
    • Ellman, G.L.1
  • 16
    • 0031059866 scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1977) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1977) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • DOI 10.1021/ac950914h
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68:850-858. (Pubitemid 26101214)
    • (1996) Analytical Chemistry , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 38649131282 scopus 로고    scopus 로고
    • Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine
    • DOI 10.1021/pr070363z
    • Xu H, Zhang L, Freitas MA (2008) Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine. J Proteome Res 7:138-144. (Pubitemid 351171125)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 138-144
    • Xu, H.1    Zhang, L.2    Freitas, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.