New insights into oxidative folding

The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-α and -β) in...

Descripción completa

Detalles Bibliográficos
Autor principal: Sevier, Carolyn S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
Reviews
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845070/
https://www.ncbi.nlm.nih.gov/pubmed/20308423
http://dx.doi.org/10.1083/jcb.201002114
_version_ 1782179368671379456
author Sevier, Carolyn S.
author_facet Sevier, Carolyn S.
author_sort Sevier, Carolyn S.
collection PubMed
description The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-α and -β) in oxidative folding. Their analysis reveals a selective role for ERO1-β in insulin production and a surprisingly minor contribution for either ERO1 isoform on immunoglobulin folding and secretion.
format Text
id pubmed-2845070
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-28450702010-09-22 New insights into oxidative folding Sevier, Carolyn S. J Cell Biol Reviews The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-α and -β) in oxidative folding. Their analysis reveals a selective role for ERO1-β in insulin production and a surprisingly minor contribution for either ERO1 isoform on immunoglobulin folding and secretion. The Rockefeller University Press 2010-03-22 /pmc/articles/PMC2845070/ /pubmed/20308423 http://dx.doi.org/10.1083/jcb.201002114 Text en © 2010 Sevier This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Reviews
Sevier, Carolyn S.
New insights into oxidative folding
title New insights into oxidative folding
title_full New insights into oxidative folding
title_fullStr New insights into oxidative folding
title_full_unstemmed New insights into oxidative folding
title_short New insights into oxidative folding
title_sort new insights into oxidative folding
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845070/
https://www.ncbi.nlm.nih.gov/pubmed/20308423
http://dx.doi.org/10.1083/jcb.201002114
work_keys_str_mv AT seviercarolyns newinsightsintooxidativefolding

Ejemplares similares