Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases. [PDF]
Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Shepherd C, Oka OB, Bulleid NJ.
europepmc +3 more sources
Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress. [PDF]
The endoplasmic reticulum (ER) is responsible for protein folding, modification, and trafficking. Accumulation of unfolded or misfolded proteins represents the condition of ER stress and triggers the unfolded protein response (UPR), a key mechanism ...
Lee S+10 more
europepmc +4 more sources
Cis-nonProline peptides: Genuine occurrences and their functional roles. [PDF]
Abstract While cis peptides preceding proline can occur about 5% of the time, cis peptides preceding any other residue (“cis‐nonPro” peptides) are an extremely rare feature in protein structures, of considerable importance for two opposite reasons. On one hand, their genuine occurrences are mostly found at sites critical to biological function, from ...
Richardson JS+5 more
europepmc +2 more sources
Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation [PDF]
The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined.
Altmann, Berid+13 more
core +3 more sources
Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases [PDF]
OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet ...
Ali, Marfoua S.+14 more
core +1 more source
A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis [PDF]
Background: Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangement of disulphide bonds in newly folded proteins entering the secretory pathway to ensure correct protein folding.
Bicknell, A. B.+8 more
core +1 more source
Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis [PDF]
Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotype is
Alun Jones+43 more
core +1 more source
Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy [PDF]
published_or_final_versio
Chong, CM+13 more
core +1 more source
Inhibition of thiol isomerase activity diminishes endothelial activation of plasminogen, but not of protein C [PDF]
Highlights •A range of thiol isomerase enzymes were expressed by HMEC-1 endothelial cells. •Inhibition of thiol isomerases reduced plasminogen activation on HMEC-1 cells.
Gordge, M.P.+7 more
core +1 more source
Influence of ellagitannins extracted by pomegranate fruit on disulfide isomerase PDIA3 activity [PDF]
Pomegranate fruit is a functional food of high interest for human health due to its wide range of phytochemicals with antioxidant properties are implicated in the prevention of inflammation and cancer. Ellagitannins, such as punicalagin and ellagic acid,
Altieri, Fabio+6 more
core +1 more source