Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase

In the mammalian endoplasmic reticulum, oxidoreductin-1α (Ero1α) generates protein disulfide bonds and transfers them specifically to canonical protein-disulfide isomerase (PDI) to sustain oxidative protein folding. This oxidative process is coupled to the reduction of O(2) to H(2)O(2) on the bound...

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Bibliografische gegevens
Gepubliceerd in:J Biol Chem
Hoofdauteurs: Kanemura, Shingo, Okumura, Masaki, Yutani, Katsuhide, Ramming, Thomas, Hikima, Takaaki, Appenzeller-Herzog, Christian, Akiyama, Shuji, Inaba, Kenji
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: American Society for Biochemistry and Molecular Biology 2016
Onderwerpen:
Protein Structure and Folding
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC5104921/
https://ncbi.nlm.nih.gov/pubmed/27703014
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.735662
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