A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway
- PMID: 19194483
- PMCID: PMC2637342
- DOI: 10.1038/emboj.2008.293
A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway
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Comment on
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A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells.EMBO J. 2008 Nov 19;27(22):2977-87. doi: 10.1038/emboj.2008.202. Epub 2008 Oct 2. EMBO J. 2008. PMID: 18833192 Free PMC article.
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Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.EMBO J. 2008 Nov 19;27(22):2988-97. doi: 10.1038/emboj.2008.230. Epub 2008 Oct 30. EMBO J. 2008. PMID: 18971943 Free PMC article.
References
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- 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 - PubMed
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