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(2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Recombinant purified AOX1","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ca982ad4-2daf-5e2f-9f2f-82676f4f562d","evidence_kind":"source_excerpt","locator":"Lines 833-844","start_line":833,"end_line":844,"excerpt":"### mo-aox-phthalazine\nHuman AOX1 structures and kinetics characterize phthalazine binding and oxidation at its molybdenum active site.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: AOX1 processes certain nitrogen-containing compounds.\norganism: Homo sapiens protein\ntissue_or_cell_type: Recombinant purified AOX1\nexperimental_model: Human AOX1 structures and steady-state kinetics with substrate and inhibitor\nlimitations: Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements.\nexposure: Phthalazine and thioridazine\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/26322824.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188\", \"start_char\": 0, \"end_char\": 1067, \"text_sha256\": \"0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188\"}\n[mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. 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