Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Isolation and identification of L-dopa decarboxylase as a protein that binds to and enhances transcriptional activity of the androgen receptor using the repressed transactivator yeast two-hybrid system.
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DDC (L-DOPA decarboxylase) was identified as a novel androgen receptor (AR)-interacting protein that enhances ligand-dependent AR transcriptional activity in prostate cancer cells, suggesting a moonlighting coactivator role distinct from its enzymatic function.
"DDC (L-dopa decarboxylase) was detected multiple times as a novel AR-interacting"
The assays of activities and function of TH, AADC, and GCH1 and their potential use in ex vivo gene therapy of PD.
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Developed an assay for human AADC (aromatic amino acid decarboxylase) enzymatic activity used with TH and GCH1 for dopamine-synthesis gene therapy of Parkinson disease.
"assay the activities of TH and AADC"
Large-scale proteomics and phosphoproteomics of urinary exosomes.
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DDC was detected among the proteins profiled by LC-MS/MS in human urinary exosomes, a high-throughput localization observation.
"we used LC-MS/MS to profile the proteome of human urinary exosomes"
Oxidative status of DJ-1-dependent activation of dopamine synthesis through interaction of tyrosine hydroxylase and 4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase with DJ-1.
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DJ-1 (PARK7) directly binds DDC and tyrosine hydroxylase and positively regulates their activities in human dopaminergic cells; a ternary DJ-1/TH/ DDC complex was detected. Grounds the direct L-DOPA decarboxylase activity (IDA), dopamine biosynthesis (IDA), and enzyme-binding (TH) annotations.
"we found that DJ-1 directly bound to TH and DDC and positively regulated their activities in human dopaminergic cells"
Aromatic-L-amino-acid decarboxylase, a pyridoxal phosphate-dependent enzyme, is a beta-cell autoantigen.
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Identifies human AADC (EC 4.1.1.28) as a PLP-dependent enzyme and beta-cell autoantigen, restating its catalytic decarboxylation of 5-HTP to serotonin and L-DOPA to dopamine.
"serotonin and that of L-3,4-dihydroxyphenylalanine to dopamine"
Decarboxylation of 5-hydroxytryptophan forms serotonin
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AADC, functioning as a PLP-dependent homodimer, decarboxylates 5-hydroxytryptophan to serotonin in the cytosol.
"Aromatic L-amino acid decarboxylase (AADC) catalyzes the decarboxylation of both dopa and 5-hydroxytryptophan"
Dopa is decarboxylated to dopamine
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AADC (DOPA decarboxylase) decarboxylates dopa to form dopamine in the cytosol.
"Aromatic L-amino acid decarboxylase (AADC, dopa decarboxylase) decarboxylates dopa to form dopamine"