Deciphering Structural and Functional Roles of Individual Disulfide Bonds of the Mitochondrial Sulfhydryl Oxidase Erv1p
Open Access
- 1 October 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (42) , 28754-28761
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Redox regulation of protein folding in the mitochondrial intermembrane spaceBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2009
- The MIA system for protein import into the mitochondrial intermembrane spaceBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2008
- Functional Characterization of Mia40p, the Central Component of the Disulfide Relay System of the Mitochondrial Intermembrane SpaceJournal of Biological Chemistry, 2007
- Gain of Function in an ERV/ALR Sulfhydryl Oxidase by Molecular Engineering of the Shuttle DisulfideJournal of Molecular Biology, 2006
- Disulfide Transfer between Two Conserved Cysteine Pairs Imparts Selectivity to Protein Oxidation by Ero1Molecular Biology of the Cell, 2006
- Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1pProceedings of the National Academy of Sciences, 2006
- A Disulfide Relay System in MitochondriaCell, 2005
- Protein Disulfide Bond Formation in ProkaryotesAnnual Review of Biochemistry, 2003
- The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centreEuropean Journal of Biochemistry, 2003
- Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol.Proceedings of the National Academy of Sciences, 1992