PDIA2 has a dual function in promoting androgen deprivation therapy induced venous thrombosis events and castrate resistant prostate cancer progression.
Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC).
Human major histocompatibility complex class 1 antigens (HLA-A B C) are potential binding partners of PDIA2 suggesting an involvement for PDIA2 in antigen presentation.
The redox-regulated open/closed conformational switch of hPDI endows the protein with versatile target-binding capacities for its enzymatic and chaperone functions.
surface-associated PDI is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation
Data show that diabetic patients had a greater number of transferase-mediated dUTP nick-end labeling-positive cells than nondiabetic patients despite a greater myocardial protein disulfide isomerase (PDI)expression suggesting altered PDI function.
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