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Rockefeller University Press, Journal of Cell Biology, 6(188), p. 757-758, 2010

DOI: 10.1083/jcb.201002114

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New insights into oxidative folding

Journal article published in 2010 by Carolyn S. Sevier ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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-alpha and -beta) in oxidative folding. Their analysis reveals a selective role for ERO1-beta in insulin production and a surprisingly minor contribution for either ERO1 isoform on immunoglobulin folding and secretion.