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...

We studied diaphragm function in a total of 64 normal subjects, who had no past or present respiratory or neuromuscular impairment. We measured transdiaphragmatic pressure (Pdi) during maximal sniffs and compared these values with Pdi during maximal static inspiratory efforts (PImax.). The range of Pdi during maximal sniffs (82-204 cm H2O) had better defined lower limits than Pdi during PImax. ...

Protein disulphide isomerase (PDI) shows chaperone and anti-chaperone activities in assisting refolding of denatured and reduced lysozyme in redox Hepes buffer, but only chaperone activity in phosphate buffer and redox Hepes buffer containing 0.1 M NaCl. In non-redox Hepes buffer its anti-chaperone activity is very weak. PDI displays its anti-chaperone activity only for those substrates showing...

e19651 Background: Cancer patients (CP) are frequently exposed to polypharmacy, which may increase their risk for drug interactions. Our study aims were to 1) determine and compare the prevalence and clinical significance of potential drug interactions (PDI) in CP vs. non-cancer patients (NCP) and 2) identify clinical risk factors associated with PDI in CP. METHODS Self-reported prescription ...