Results 41 to 50 of about 83,411 (273)
Inactivation of mammalian Ero 1α 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.
Appenzeller-Herzog+22 more
core +1 more source
Immunoproteomic to identify antigens in the intestinal mucosa of Crohn's disease patients. [PDF]
Incidences of Crohn disease (CD) have increased significantly in the last decade. Immunoproteomics are a promising method to identify biomarkers of different diseases. In the present study, we used immunoproteomics to study proteins of intestinal mucosal
Zheng Zhou+6 more
doaj +1 more source
BACKGROUND Protein disulfide isomerase (PDI) is a thiol isomerase secreted by vascular cells that is required for thrombus formation. Quercetin flavonoids inhibit PDI activity and block platelet accumulation and fibrin generation at the site of a ...
J. Zwicker+15 more
semanticscholar +1 more source
Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]
The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian+6 more
core +3 more sources
Chaperone members of the protein disulfide isomerase family can catalyze the thiol-disulfide exchange reaction with pairs of cysteines. There are 14 protein disulfide isomerase family members, but the ability to catalyze a thiol disulfide exchange ...
W. Lucca-Junior+2 more
doaj +1 more source
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
Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio+1 more
core +1 more source
Tissue factor activation (decryption) has been proposed to be dependent on the cysteine 186-cysteine 209 allosteric disulfide in the tissue factor extracellular domain.
Lisa G. van den Hengel+3 more
doaj +1 more source
Expression of Functional Human Sialyltransferases ST3Gal1 and ST6Gal1 in Escherichia coli. [PDF]
Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and participate in the synthesis of the core structure oligosaccharides of human milk.
Maria Elena Ortiz-Soto, Jürgen Seibel
doaj +1 more source
Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]
Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio+7 more
core +1 more source