Literature: Endoplasmic reticulum oxidoreductin 1 (IPR007266)
References used in this entry
The following publications were referred to in the abstract:
Pathways for protein disulphide bond formation.
Frand AR, Cuozzo JW, Kaiser CA.
Trends Cell Biol. 10 203-10 2000
PMID: 10754564 Related citations
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.
Mol. Biol. Cell 11 2833-43 2000
PMID: 10982384 Related citations
Balanced Ero1 activation and inactivation establishes ER redox homeostasis.
Kim S, Sideris DP, Sevier CS, Kaiser CA.
J. Cell Biol. 196 713-25 2012
PMID: 22412017 Related citations
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.
EMBO J. 27 2988-97 2008
PMID: 18971943 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.
Gross E, Kastner DB, Kaiser CA, Fass D.
Cell 117 601-10 2004
PMID: 15163408 Related citations
Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
Pollard MG, Travers KJ, Weissman JS.
Mol. Cell 1 171-82 1998
PMID: 9659914 Related citations