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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

Official Date:

2009

Dates:

Date	Event
2009	UNSPECIFIED

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