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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
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
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
drug target
the enzyme is a potential biomarker for cancer diagnosis
drug target
the enzyme (ASPH) may be a potential therapeutic target in CCA patients having the IDH1/2 wild-type genotype
drug target
the enzyme is a potential medicinal chemistry target for anticancer therapy
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
malfunction
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inhibition by fetal alcohol spectrum disorder, decrease leads to impairment in neuronal migration
malfunction
knockdown of enzyme (ASPH) expression inhibits cholangiocarcinoma development and growth by reducing retinoblastoma protein (RB1) inhibition
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)
metabolism
the enzyme catalyzes the hydroxylation of epidermal growth factor (EGF)-like repeats in Notch receptors and ligands. It is highly overexpressed in pancreatic cancer. The upregulation confers a malignant phenotype characterized by enhanced cell proliferation, migration, invasion and colony formation in vitro as well as pancreatic cancer tumor growth in vivo. The transforming properties of aspartate beta-hydroxylase depend on enzymatic activity. The enzyme links pancreatic cancer growth factor signaling cascades to Notch activation
metabolism
the enzyme catalyzes the hydroxylation of specific aspartyl and asparaginyl residues in epidermal growth factor-like domains of proteins
metabolism
the enzyme induces epitope-specific T cell responses in hepatocellular carcinoma
metabolism
the enzyme is involved in regulating tumor cell infiltration and metastasis in tumor patients with malignant neoplasms. One of the ways by which the enzyme actively promotes tumor formation and proliferation is by inhibiting natural killer cell-surveillance activity
metabolism
the enzyme may play an important role in different carcinomas and may be a potential hub in carcinogenesis. Expression in tumor cells is increased with the development and progression of carcinomas
physiological function
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mediates neuronal motility
physiological function
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stimulates cell migration
physiological function
aspartate beta-hydroxylase modulates cellular senescence through glycogen synthase kinase 3beta in hepatocellular carcinoma. shRNA-mediated knockdown and CRISPR/Cas9-mediated knockout of aspartate beta-hydroxylase as well as enzymatic inhibition of the enzyme guide human hepatocellular carcinoma cells to undergo cellular senescence. Inhibition of aspartate beta-hydroxylase activity induces senescence as mediated through phosphorylation of GSK3beta. In addition, aspartate beta-hydroxylase binding to GSK3beta inhibits its phosphorylation (inactivation) and thus blocks the signal transduction from its upstream kinases
physiological function
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 (FIH)
physiological function
the enzyme (ASPH) is involved in cholangiocarcinoma growth, progression and induction of cell senescence. The protein interaction between RB1 and the CDK complexes is modulated by ASPH expression
physiological function
the enzyme catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth factor-like domains
physiological function
the enzyme catalyses the hydroxylation of Asp/Asn-residues of epidermal growth factor-like domains
physiological function
the enzyme catalyzes the post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like domains
physiological function
the enzyme may be involved in the development of breast cancer. It is overexpressed in breast cancer and correlates with cancer type, lymph node involvement, and TNM stage. The enzyme levels does not correlate with patient age, invasive carcinoma types, or molecular subtypes