Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum.
Sign Up to like & getrecommendations! 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,… read more here.
Keywords: protein disulfide; disulfide isomerases; endoplasmic reticulum;
Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17
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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… read more here.
Keywords: disintegrin metalloprotease; disulfide switch; switch; disulfide isomerases ... See more keywords
Abstract 6148: Disulfide isomerases AGR2, ERp44, and PDIA1 maintain death receptor 5 in an auto-inhibited, monomeric form
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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… read more here.
Keywords: agr2 erp44; erp44 pdia1; auto; disulfide isomerases ... See more keywords