Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)-Reference-Cited by-同舟云学术

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Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)

Published:2010-02-26 Issue:5 Volume:15 Page:619-629
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Gilady Susanna Y.,Bui Michael,Lynes Emily M.,Benson Matthew D.,Watts Russell,Vance Jean E.,Simmen Thomas

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s12192-010-0174-1.pdf

Reference50 articles.

1. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (2002) ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 21:835–844

2. Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R (2003) Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J 22:5015–5022

3. Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, Braakman I (2000) The CXXCXXC motif determines the folding, structure and stability of human Ero1-L alpha. Embo J 19:4493–4502

4. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R (2000) ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275:4827–4833

5. Camacho P, Lechleiter JD (1995) Calreticulin inhibits repetitive intracellular Ca2+ waves. Cell 82:765–771

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