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(2015). https://pubmed.ncbi.nlm.nih.gov/25845827/ DOI: 10.1124/dmd.114.061804","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Liver cytosol","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"66ea43c1-fc6f-56e9-a8d6-fa5db009fc9b","evidence_kind":"source_excerpt","locator":"Lines 924-935","start_line":924,"end_line":935,"excerpt":"### mo-aox-amide\nInhibitor and fractionation experiments implicated AO and carboxylesterase, but not XOR, in GDC-0834 amide hydrolysis.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: AOX1 can participate in drug breakdown beyond simple aldehyde oxidation.\norganism: Homo sapiens\ntissue_or_cell_type: Liver cytosol\nexperimental_model: Human liver cytosolic fractionation, proteomics, inhibitors and docking\nlimitations: AO and carboxylesterase both implicated; docking proposes a mechanism but does not prove every catalytic step.\nexposure: GDC-0834 amide-hydrolysis assays\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/25845827.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40\", \"start_char\": 0, \"end_char\": 1619, \"text_sha256\": \"8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40\"}\n[mo-p25845827] A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834. 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