Two Conserved Cysteine Triads in Human Ero1α Cooperate for Efficient Disulfide Bond Formation in the Endoplasmic Reticulum
Open Access
- 1 July 2004
- journal article
- Published by Elsevier BV
- Vol. 279 (29), 30047-30052
- https://doi.org/10.1074/jbc.m403192200
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Oxidative protein folding in eukaryotesThe Journal of cell biology, 2004
- The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1‐LαEuropean Journal of Biochemistry, 2003
- Formation and transfer of disulphide bonds in living cellsNature Reviews Molecular Cell Biology, 2002
- Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulumHistochemistry and Cell Biology, 2002
- Endoplasmic Reticulum Oxidoreductin 1-Lβ (ERO1-Lβ), a Human Gene Induced in the Course of the Unfolded Protein ResponseJournal of Biological Chemistry, 2000
- ERO1-L, a Human Protein That Favors Disulfide Bond Formation in the Endoplasmic ReticulumJournal of Biological Chemistry, 2000
- Ero1p Oxidizes Protein Disulfide Isomerase in a Pathway for Disulfide Bond Formation in the Endoplasmic ReticulumMolecular Cell, 1999
- ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and CalnexinMolecular Biology of the Cell, 1999
- The ERO1 Gene of Yeast Is Required for Oxidation of Protein Dithiols in the Endoplasmic ReticulumMolecular Cell, 1998
- Ero1p: A Novel and Ubiquitous Protein with an Essential Role in Oxidative Protein Folding in the Endoplasmic ReticulumMolecular Cell, 1998