Intact protein folding in the glutathione-depleted endoplasmic reticulum implicates alternative protein thiol reductants

Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxidation, but also relies on a parallel reductive process to edit disulfides during the maturation or degradation of secreted proteins. To critically examine the widely held assumption that reduced ER glu...

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Bibliographic Details
Main Author: Tsunoda, Satoshi (author)
Other Authors: Avezov, Edward (author), Zyryanova, Alisa (author), Konno, Tasuku (author), Leonardo Mendes-Silva (author), Melo, Eduardo (author), Harding, Heather P. (author), Ron, David (author)
Format: article
Language:eng
Published: 2018
Subjects:
Disulfide-bond formation
Localized peroxiredoxin
Oxidized glutathione
Reducing pathways
Redox
Isomerase
Er
Catalysis
Oxidation
Erdj5
Online Access:http://hdl.handle.net/10400.1/11452
Country:Portugal
Oai:oai:sapientia.ualg.pt:10400.1/11452

Internet

http://hdl.handle.net/10400.1/11452

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