EC Number |
Application |
Reference |
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5.3.4.1 | analysis |
development of a method to determine quantitatively the redox state of active-site cysteines found in the Cys-Xaa-Xaa-Cys motif in living cells. Method is based on the alkylation of cysteines by methoxy polyethylene glycol 5000 maleimide. In vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized |
690471 |
5.3.4.1 | analysis |
PDIA3 and C/EBP? may be valuable markers in fish for exposure and effect to environmental stress |
703301 |
5.3.4.1 | analysis |
study on the critical influence of reference genes used for data normalization, shown for protein disulfide isomerase |
692475 |
5.3.4.1 | biotechnology |
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhance by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 3fold, production method evaluation |
662490 |
5.3.4.1 | biotechnology |
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhanced by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 clone 3fold, production method evaluation |
662490 |
5.3.4.1 | diagnostics |
lung cancer patients with high Srx levels have significantly shorter survival and those with high TXNDC5 levels have longer survival. Cellular levels of Srx and TXNDC5 may be useful as biomarkers to predict the survival of individuals with lung cancer |
765061 |
5.3.4.1 | diagnostics |
the absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer |
705216 |
5.3.4.1 | drug development |
PDI constitutes a potential target for the development of alternative therapy strategies based on the inhibition of folding and chaperoning of exported proteins |
704056 |
5.3.4.1 | industry |
PDI assists incorporation of cysteine-containing compounds (CCCs) into hair and wool substrates in order to generate milder methods to dye hair with longer lasting colour by creating new disulfide bonds between hair and peptide. PDI-assists promotion of the migration of CCCs (dyes), previously attached to keratin, along hair fibres, to avoid repetitive hair dyeing procedures. PDI induces controlled release of a CCC protein (e.g. reduced form of RNase A) from wool matrices |
713901 |
5.3.4.1 | medicine |
inhibition of isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit activity increases apoptosis in response to agents which induce ER-stress such as fenretinide and velcade |
691615 |