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2000 | 2 |
2024 | 0 |
PubMed for id: 461191
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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. 2000 Sep;11(9):2833-43. doi: 10.1091/mbc.11.9.2833.
Mol Biol Cell. 2000.
PMID: 10982384
Free PMC article.
Pathways for protein disulphide bond formation.
Frand AR, Cuozzo JW, Kaiser CA.
Frand AR, et al.
Trends Cell Biol. 2000 May;10(5):203-10. doi: 10.1016/s0962-8924(00)01745-1.
Trends Cell Biol. 2000.
PMID: 10754564
Review.
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Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
Pollard MG, Travers KJ, Weissman JS.
Pollard MG, et al.
Mol Cell. 1998 Jan;1(2):171-82. doi: 10.1016/s1097-2765(00)80018-0.
Mol Cell. 1998.
PMID: 9659914
Free article.
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