title: Protein disulfide isomerase a multifunctional protein with multiple physiological roles.
abstract: Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone. Originally, PDI was identified in the lumen of the endoplasmic reticulum and subsequently detected at additional locations, such as cell surfaces and the cytosol. This review will provide an overview of the recent advances in relating the structural features of PDI to its multiple catalytic roles as well as its physiological and pathophysiological functions related to redox regulation and protein folding.
authors.affiliation: Chemistry and Biochemistry Department, University of Windsor Windsor, ON, Canada.
authors.forename: Hyder
authors.initials: H
authors.lastname: Ali Khan
authors.affiliation: Chemistry and Biochemistry Department, University of Windsor Windsor, ON, Canada.
authors.forename: Bulent
authors.initials: B
authors.lastname: Mutus
keywords: PDI; cell surface; chaperone; disulfides; endoplasmic reticulum; oxidoreductase; protein disulfide isomerase