The human protein disulphide isomerase family: substrate interactions and functional properties

By L. Ellgaard, L. Ruddock. EMBO Reports, 2005

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Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation (2009, background): “To date, three of these have been published, TMX (202), TMX2 (205), and TMX3 (111), with TMX4 appearing in reviews (9, 71).”
Multiple catalytically active thioredoxin folds: a winning strategy for many functions (2010, background): “Even if many of the residues that are implicated in ERp57–CRT interactions are conserved in ERp72 [18], no experimental evidence has been found to suggest a direct interaction between ERp72 and CNX or CRT [28, 84].”
Endoplasmic Reticulum Stress and Associated ROS (2016, background): “There are 20 oxidoreductases that are reported to catalyze disulfide bonds and are the correct sequence of pairs of cysteine residues with varying redox potential and substrate specificity [23,24].”
Protein quality control in the early secretory pathway (2008, background): “The precise role(s) of these molecules, as well as the mechanisms controlling their redox state and activity, remain to be clarified (Ellgaard and Ruddock, 2005).”
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells (2019, background): “Protein disulfide isomerase (PDI) catalyzes thiol-disulfide exchange reactions, which form a native disulfide bond in proteins [70].”