dc.contributor.author | Sevier, Carolyn S. | |
dc.date.accessioned | 2011-01-14T16:45:27Z | |
dc.date.available | 2011-01-14T16:45:27Z | |
dc.date.issued | 2010-03 | |
dc.date.submitted | 2010-02 | |
dc.identifier.issn | 1540-8140 | |
dc.identifier.issn | 0021-9525 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/60570 | |
dc.description.abstract | 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. | en_US |
dc.language.iso | en_US | |
dc.publisher | Rockefeller University Press | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1083/jcb.201002114 | en_US |
dc.rights | Article 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.source | Rockefeller UP | en_US |
dc.title | New insights into oxidative folding | en_US |
dc.type | Article | en_US |
dc.identifier.citation | Sevier, Carolyn S. “New insights into oxidative folding.” The Journal of Cell Biology 188.6 (2010): 757 -758. Copyright © 2010 by The Rockefeller University Press | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Biology | en_US |
dc.contributor.approver | Sevier, Carolyn S. | |
dc.contributor.mitauthor | Sevier, Carolyn S. | |
dc.relation.journal | Journal of Cell Biology | en_US |
dc.eprint.version | Final published version | en_US |
dc.identifier.pmid | 20308423 | |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | Sevier, Carolyn S. | en |
mit.license | PUBLISHER_POLICY | en_US |
mit.metadata.status | Complete | |