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Published in 2017 at "Archives of biochemistry and biophysics"
DOI: 10.1016/j.abb.2016.11.007
Abstract: Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in ER-related redox homeostasis and signaling are well-studied. PDIA1 exerts thiol oxidation/reduction and isomerization,…
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Keywords:
protein disulfide;
disulfide isomerases;
endoplasmic reticulum;
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Published in 2018 at "Scientific Reports"
DOI: 10.1038/s41598-018-19429-4
Abstract: A Disintegrin and Metalloprotease 17 (ADAM17) can cause the fast release of growth factors and inflammatory mediators from the cell surface. Its activity has to be turned on which occurs by various stimuli. The active…
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Keywords:
disintegrin metalloprotease;
disulfide switch;
switch;
disulfide isomerases ... See more keywords
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Published in 2023 at "Cancer Research"
DOI: 10.1158/1538-7445.am2023-6148
Abstract: Previous studies indicated that compounds termed Disulfide bond Disrupting Agents (DDAs) exhibit anti-cancer activity that is associated with downregulation of EGFR/HER1, HER2, and HER3, and activation of Death Receptors 4 and 5 (DR4/5). DDA-induced HER1-3…
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Keywords:
agr2 erp44;
erp44 pdia1;
auto;
disulfide isomerases ... See more keywords
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Published in 2025 at "Biomolecules"
DOI: 10.3390/biom15081146
Abstract: Protein Disulfide Isomerases (PDIs) are emerging targets in anticancer therapy, with several PDI inhibitors demonstrating anticancer efficacy in preclinical models. Research has largely focused on “canonical” PDIs, such as PDIA1, which contain CXXC active site…
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Keywords:
protein disulfide;
canonical pdis;
disulfide isomerases;
protein ... See more keywords