Results 31 to 40 of about 21,311 (187)
Protein disulfide isomerase mediates integrin‐dependent adhesion [PDF]
FEBS Letters, 2000 Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear. Our earlier work implied a role for sulfhydryls in integrin response to ligand binding in the intact blood platelet.
Lahav, J. +4 more
openaire +2 more sources
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
Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase [PDF]
Journal of Biological Chemistry, 1999 Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic reticulum and is secreted by cells and associates with the cell surface. We examined the consequence of over- or underexpression of PDI in HT1080 fibrosarcoma cells for the redox state of cell-surface protein thiols/disulfides ...
X M, Jiang +3 more
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Haematologica, 2013 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
Cell Reports, 2018 Summary: Multiple sulfatase deficiency (MSD) is a fatal, inherited lysosomal storage disorder characterized by reduced activities of all sulfatases in patients.
Lars Schlotawa +6 more
doaj +1 more source
Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization. [PDF]
PLoS ONE, 2013 BACKGROUND: Tau protein is implicated in the pathogenesis of neurodegenerative disorders such as tauopathies including Alzheimer disease, and Tau fibrillization is thought to be related to neuronal toxicity. Physiological inhibitors of Tau fibrillization
Li-Rong Xu +3 more
doaj +1 more source
Roles of Protein Disulfide Isomerase in Breast Cancer [PDF]
Cancers, 2022 Protein disulfide isomerase (PDI) is the endoplasmic reticulum (ER)’s most abundant and essential enzyme and serves as the primary catalyst for protein folding. Due to its apparent role in supporting the rapid proliferation of cancer cells, the selective blockade of PDI results in apoptosis through sustained activation of UPR pathways. The functions of
Suhui Yang +8 more
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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
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Genes and Diseases, 2018 Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family.
Hedy A. Chawsheen +3 more
doaj +1 more source
A functionalized hydroxydopamine quinone links thiol modification to neuronal cell death
Redox Biology, 2020 Recent findings suggest that dopamine oxidation contributes to the development of Parkinson's disease (PD); however, the mechanistic details remain elusive.
Ali Farzam +6 more
doaj +1 more source