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(1992). https://pubmed.ncbi.nlm.nih.gov/1378832/ DOI: 10.1016/s0021-9258(18)42066-2","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Arginine conversion and NO-dependent reporter guanylate cyclase activity","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a167d99f-f4aa-57ff-9a68-a5f360235bfa","evidence_kind":"source_excerpt","locator":"Lines 463-474","start_line":463,"end_line":474,"excerpt":"### citrulline-nos-no\nCells expressing human endothelial NOS produced bioactive NO that increased guanylate cyclase activity in cocultured reporter cells.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Arginine feeds an enzyme that makes the signal NO while also producing citrulline.\norganism: Human NOS3 expressed in NIH3T3 cells; rat reporter fibroblasts\ntissue_or_cell_type: Arginine conversion and NO-dependent reporter guanylate cyclase activity\nexperimental_model: Functional expression and reporter-cell coculture\nlimitations: Heterologous expression; reporter activation supports bioactive NO production, not a clinical calcium supplementation effect.\nexposure: NOS3 transfection and calcium ionophore A23187\nevidence_span: {\"source_cache\": \"artifacts/citrulline-research/1378832.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"265be186f6d8172b272e7b1e75b4fbae12a6df78c7396cad499bce2b195b1206\", \"start_char\": 0, \"end_char\": 1652, \"text_sha256\": \"265be186f6d8172b272e7b1e75b4fbae12a6df78c7396cad499bce2b195b1206\"}\n[citrulline-p1378832] Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. 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