Inhibition of Protein Disulfide Isomerase in Thrombosis [PDF]
Basic & Clinical Pharmacology & Toxicology, 2016 AbstractThis MiniReview addresses our current understanding of the mechanisms by which protein disulfide isomerase (PDI) mediates thrombus formation and discusses the potential of blocking thrombosis by targeting PDI. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic reticulum (ER) where they serve a critical role ...
Roelof H, Bekendam, Robert, Flaumenhaft
openaire +2 more sources
The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses
BMC Plant Biology, 2021 Background Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response.
Ying Lu +6 more
doaj +1 more source
Influence of ellagitannins extracted by pomegranate fruit on disulfide isomerase PDIA3 activity [PDF]
, 2019 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
A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion
Cell Reports, 2019 Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe +6 more
doaj +1 more source
Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase
Frontiers in Cell and Developmental Biology, 2020 Aggregates of α-synuclein contribute to the etiology of Parkinson’s Disease. Protein disulfide isomerase (PDI), a chaperone and oxidoreductase, blocks the aggregation of α-synuclein.
Albert Serrano +7 more
doaj +1 more source
A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding. [PDF]
PLoS ONE, 2014 Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI).
Li Zhu +4 more
doaj +1 more source
Immunoproteomic to identify antigens in the intestinal mucosa of Crohn's disease patients. [PDF]
PLoS ONE, 2013 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
Brazilian Journal of Medical and Biological Research, 2009 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
Folding of small disulfide-rich proteins : clarifying the puzzle [PDF]
, 2006 Premi a l'excel·lència investigadora. Àmbit de les Ciències Experimentals. 2008The process by which small proteins fold to their native conformations has been intensively studied over the last few decades.
Apuy +73 more
core +2 more sources
Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]
, 2016 Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa +2 more
core +1 more source