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dc.contributor.authorSevier, Carolyn S.
dc.date.accessioned2011-01-14T16:45:27Z
dc.date.available2011-01-14T16:45:27Z
dc.date.issued2010-03
dc.date.submitted2010-02
dc.identifier.issn1540-8140
dc.identifier.issn0021-9525
dc.identifier.urihttp://hdl.handle.net/1721.1/60570
dc.description.abstractThe 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.en_US
dc.language.isoen_US
dc.publisherRockefeller University Pressen_US
dc.relation.isversionofhttp://dx.doi.org/10.1083/jcb.201002114en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceRockefeller UPen_US
dc.titleNew insights into oxidative foldingen_US
dc.typeArticleen_US
dc.identifier.citationSevier, Carolyn S. “New insights into oxidative folding.” The Journal of Cell Biology 188.6 (2010): 757 -758. Copyright © 2010 by The Rockefeller University Pressen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.approverSevier, Carolyn S.
dc.contributor.mitauthorSevier, Carolyn S.
dc.relation.journalJournal of Cell Biologyen_US
dc.eprint.versionFinal published versionen_US
dc.identifier.pmid20308423
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsSevier, Carolyn S.en
mit.licensePUBLISHER_POLICYen_US
mit.metadata.statusComplete


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