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New insights into oxidative folding

Author(s)
Sevier, Carolyn S.
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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.

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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.
Date issued
2010-03
URI
http://hdl.handle.net/1721.1/60570
Department
Massachusetts Institute of Technology. Department of Biology
Journal
Journal of Cell Biology
Publisher
Rockefeller University Press
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
Version: Final published version
ISSN
1540-8140
0021-9525

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