Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin

Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms. Surprisingly, ERO1-deficient mammalian cells exhibit only a modest delay in disulfide bond formation. T...

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Bibliographic Details
Main Author: Zito, Ester (author)
Other Authors: Melo, Eduardo (author), Yang, Yun (author), Wahlander, Asa (author), Neubert, Thomas A. (author), Ron, David (author)
Format: article
Language:eng
Published: 2018
Subjects:
Disulfide bond formation
Thiol oxidase
Redox state
Human cells
Stress
Gene
Ero1
Death
Mitochondria
Homeostasis
Online Access:http://hdl.handle.net/10400.1/11253
Country:Portugal
Oai:oai:sapientia.ualg.pt:10400.1/11253

Internet

http://hdl.handle.net/10400.1/11253

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