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A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway

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Freedman, R. B.. (2009) A non-catalytic disulphide bond regulating redox flux in the ER oxidative folding pathway. EMBO Journal, Vol.28 . pp. 169-170. ISSN 0261-4189

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Official URL: http://dx.doi.org/10.1038/emboj.2008.293

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH301 Biology
Divisions:	Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Library of Congress Subject Headings (LCSH):	Endoplasmic reticulum
Journal or Publication Title:	EMBO Journal
Publisher:	Nature Publishing Group
ISSN:	0261-4189
Date:	2009
Volume:	Vol.28
Page Range:	pp. 169-170
Identification Number:	10.1038/emboj.2008.293
Status:	Peer Reviewed
Access rights to Published version:	Open Access
References:	Appenzeller-Herzog C, Riemer J, Christensen B, S^rensen ES, Ellgaard L (2008) A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells. EMBO J 27: 2977–2987 Baker KM, Chakravarthi S, Langton KP, Sheppard AM, Lu H, Bulleid NJ (2008) Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. EMBO J 27: 2988–2997 Bass R, Ruddock LW, Klappa P, Freedman RB (2004) A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 279: 5257–5262 Ellgaard L, Ruddock LW (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6: 28–32 Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C, Fass D (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. PNAS 103: 299–304
URI:	http://wrap.warwick.ac.uk/id/eprint/439