EC Number   |
General Information |
Reference |
|---|
   1.14.11.16 | drug target |
a small molecule inhibitor (MO-I-1100) of beta-hydroxylase activity is developed and found to reduce pancreatic cancer growth by downregulating the Notch signaling pathway |
743377 |
| 1.14.11.16 | drug target |
downregulation of prolyl hydroxylase domain 3 and asparaginyl hydroxylase factor inhibiting (FIH) in hepatocellular carcinoma is associated with more aggressive tumor behavior and a poor prognosis. Both enzymes may be potential therapeutic targets for treatment of hepatocellular carcinoma |
743379 |
| 1.14.11.16 | drug target |
the enzyme (ASPH) may be a potential therapeutic target in CCA patients having the IDH1/2 wild-type genotype |
764397 |
| 1.14.11.16 | drug target |
the enzyme can be a potential therapeutic target and a 2nd generation beta-hydroxylase inhibitor is an effective anti-tumor agent against intrahepatic hepatocellular carcinoma growth and progression partially through the induction of cellular senescence |
742626 |
| 1.14.11.16 | drug target |
the enzyme is a potential biomarker for cancer diagnosis |
742226 |
| 1.14.11.16 | drug target |
the enzyme is a potential medicinal chemistry target for anticancer therapy |
764503 |
| 1.14.11.16 | drug target |
the overexpressed tumor-associated cell surface protein, is considered as a promising biomarker and therapeutic target for hepatocellular carcinoma. Gateway recombinant cloning technology is a powerful method of constructing adenovirus vector, and the product Ad-AAHIRES2-EGFP may present as a potential candidate for dendritic cells-based immunotherapy of hepatocellular carcinoma |
765190 |
| 1.14.11.16 | malfunction |
inhibition by fetal alcohol spectrum disorder, decrease leads to impairment in neuronal migration |
695432 |
| 1.14.11.16 | malfunction |
knockdown of enzyme (ASPH) expression inhibits cholangiocarcinoma development and growth by reducing retinoblastoma protein (RB1) inhibition |
764397 |
| 1.14.11.16 | metabolism |
hypoxia-inducible factors (HIFs) are key regulators in oxygen homeostasis. Their stabilization and activity are regulated by prolyl hydroxylase domain (PHD)-1, -2, -3 and asparaginyl hydroxylase factor inhibiting HIF-1 factor inhibiting HIF (FIH) |
743379 |
