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EMBO Journal
Volumn 28, Issue 3, 2009, Pages 169-170
A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway
Author keywords

[No Author keywords available]
Indexed keywords

CYSTEINE; DISULFIDE ISOMERASE; FUNGAL PROTEIN; FUNGAL PROTEIN ERO1; ISOMERASE; OXYGEN; SECRETORY PROTEIN; UNCLASSIFIED DRUG;
EID: 59649129599     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.293     Document Type: Short Survey
Times cited : (5)
References (5)
  • 1
    • 56549083161 scopus 로고    scopus 로고
    • A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells
    • Appenzeller-Herzog C, Riemer J, Christensen B, Sørensen ES, Ellgaard L (2008) A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells. EMBO J 27: 2977-2987
    • (2008) EMBO J , vol.27 , pp. 2977-2987
    • Appenzeller-Herzog, C.1    Riemer, J.2    Christensen, B.3    Sørensen, E.S.4    Ellgaard, L.5
  • 2
    • 56549124032 scopus 로고    scopus 로고
    • Low reduction potential of Ero1alpha 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 Ero1alpha 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
  • 3
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass R, Ruddock LW, Klappa P, Freedman RB (2004) A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 279: 5257-5262
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 4
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard L, Ruddock LW (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6: 28-32
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 5
    • 31044452359 scopus 로고    scopus 로고
    • Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
    • Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C, Fass D (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. PNAS 103: 299-304
    • (2006) PNAS , vol.103 , pp. 299-304
    • Gross, E.1    Sevier, C.S.2    Heldman, N.3    Vitu, E.4    Bentzur, M.5    Kaiser, C.A.6    Thorpe, C.7    Fass, D.8

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.