S-nitrosothiols (RSNOs) regulate several aspects of platelet physiology including inhibition of activation, adhesion and aggregation. PDI (protein disulphide-isomerase) has recently been found to be localized to the cell surface, where it exhibits both disulphide-exchange and denitrosation activities. The disulphide-exchange activity of PDI has been linked to aspects of platelet aggregation. Th...

Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC. Haploid pdi1 delta Saccharomyces cerevisiae are inviable, but can be complemented with either a wild-type rat PDI gene or a mutant gene coding for CGHS PDI (shufflease). In contrast, pdi1 delta yeast can...

Aims: To determine whether Percussion, diuresis and inversion (PDI) maneuver following shock wave lithotripsy (SWL) can enhance stone clearance from lower calyx as compared to SWL alone. Methods: 60 Patients with lower pole stones (8-15 mm) were randomized to SWL plus PDI (group A) or SWL alone (group B). Shock waves were delivered to all patients according to a standard protocol. Group A patie...

Protein disulphide isomerase (PDI) is a key multi-domain protein folding catalyst in the endoplasmic reticulum. The b' domain of PDI is essential for the non-covalent binding of incompletely folded protein substrates. Earlier, we defined the substrate binding site in the b' domain of human PDI by modelling and mutagenesis studies. Here, we show by fluorescence and NMR that recombinant human PDI...

BACKGROUND Portable Data for Imaging (PDI) is regularly used as a guideline for sharing medical imaging data between hospitals and other medical institutions. When a patient is referred to another location, the patient almost always brings PDI media on a CD or DVD. However, problems often occur when trying to view images on PDI discs inserted into computer terminals, and it is more efficient to...

The flavin-dependent quiescin-sulfhydryl oxidase (QSOX) inserts disulfide bridges into unfolded reduced proteins with the reduction of molecular oxygen to form hydrogen peroxide. This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase, four disulfide bonds and 105 disulfide isome...

Protein disulfide isomerases (PDI) are involved in catalyzing protein disulfide bonding and isomerization in the endoplasmic reticulum and functions as a chaperone to inhibit the aggregation of misfolded proteins. Brachypodium distachyon is a widely used model plant for temperate grass species such as wheat and barley. In this work, we report the first molecular characterization, phylogenies, a...

The purpose of this research was to determine whether prior activity affected the shape of a plaster cast taken of a transtibial residual limb. Plaster casts were taken twice on one day in 24 participants with transtibial limb loss, with 5 s between doffing and casting in one trial (PDI-5s) and 20 min in the other trial (PDI-20m). The ordering of the trials was randomized. The mean +/- standard...

Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and isomerization in compact folding intermediates. The high-resolution structures of the a and b domains of PDI are now known, and the overall domain architecture of PDI and its homologues can be inferred. The isolated a and a' domains of P...

Protein disulfide isomerase (PDI), secreted by platelets and endothelial cells on vascular injury, is required for thrombus formation. Using PDI variants that form mixed disulfide complexes with their substrates, we identify by kinetic trapping multiple substrate proteins, including vitronectin. Plasma vitronectin does not bind to αvβ3 or αIIbβ3 integrins on endothelial cells and platelets. The...