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(2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Liver cDNA and patient genetics","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"b02b0fb8-8c1d-5ed1-89b8-2efcbaa01154","evidence_kind":"source_excerpt","locator":"Lines 521-532","start_line":521,"end_line":532,"excerpt":"### mo-mocos-sulfuration\nMOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Two molybdenum enzymes need an additional sulfur-activation step.\norganism: Homo sapiens\ntissue_or_cell_type: Liver cDNA and patient genetics\nexperimental_model: Gene identification in two type II xanthinuria patients and comparison subjects\nlimitations: Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis.\nexposure: MOCOS Arg419 stop mutation\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/11302742.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3\", \"start_char\": 0, \"end_char\": 1011, \"text_sha256\": \"8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3\"}\n[mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. 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