title: Defining the protein-protein interactions of the mammalian endoplasmic reticulum oxidoreductases (EROs).
abstract: The ER (endoplasmic reticulum) is the site of protein folding for all eukaryotic secreted and plasma membrane proteins. Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. This review will examine what we know about ERO function, and will then consider ERO interactions and their implications for mammalian oxidative protein folding.
authors.affiliation: Department of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, UK.
authors.forename: S
authors.initials: S
authors.lastname: Dias-Gunasekara
authors.forename: A M
authors.initials: AM
authors.lastname: Benham
mesh_terms: D000818:Animals; D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry; D014018:Tissue Distribution
chemical_list: D004220:Disulfides; D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D010088:Oxidoreductases