Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?

FEBS Letters
Eva Margittai, Gábor Bánhegyi

Abstract

Oxidative protein folding in the luminal compartment of the endoplasmic reticulum is thought to be mediated by a proteinaceous electron relay system composed by PDI and ER oxidoreductin 1 (Ero1), transferring electrons from the cysteinyl residues of substrate proteins to oxygen. However, recent observations revealed that Ero1 isoforms are dispensable. Endoplasmic reticulum is known as a generator and accumulator of low molecular weight oxidants; some of them have already been shown to promote oxidative folding. On the basis of these observations a new theory of oxidative folding is proposed where the oxidative power is provided by the stochastic contribution of prooxidants.

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Citations

Aug 13, 2011·Accounts of Chemical Research·Alexander R LippertChristopher J Chang
Mar 1, 2012·Antioxidants & Redox Signaling·Éva MargittaiGábor Bánhegyi
Dec 8, 2011·Antioxidants & Redox Signaling·Kazutaka Araki, Kenji Inaba
Dec 7, 2011·Antioxidants & Redox Signaling·Gábor BánhegyiMiklós Csala
Aug 31, 2011·Cold Spring Harbor Perspectives in Biology·Kazutaka Araki, Kazuhiro Nagata
Nov 30, 2011·TheScientificWorldJournal·Beatriz S StolfCelio X C Santos
Sep 13, 2012·The Plant Journal : for Cell and Molecular Biology·Alessio LombardiAldo Ceriotti
Aug 31, 2010·The EMBO Journal·Christian Appenzeller-HerzogLars Ellgaard
Feb 14, 2015·Free Radical Biology & Medicine·Éva MargittaiGábor Bánhegyi
Dec 15, 2010·Current Opinion in Cell Biology·Matthias J Feige, Linda M Hendershot
Jul 13, 2017·Chemical Reviews·Deborah Fass, Colin Thorpe
Jul 6, 2014·The Journal of Biological Chemistry·Pawel StockiDavid B Williams
Nov 20, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Mahesh Narayan

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