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(1996). https://pubmed.ncbi.nlm.nih.gov/8951046/ DOI: 10.1006/abbi.1996.0543","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"NOS expression and catalytic function","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a6bebf21-ef9a-5b4a-bc12-0f9ac8ec3c3f","evidence_kind":"source_excerpt","locator":"Lines 593-604","start_line":593,"end_line":604,"excerpt":"### citrulline-calmodulin-nos\nCoexpressing human calmodulin stabilized eNOS and raised its specific activity; later calmodulin addition did not reproduce the gain.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: How the enzyme assembles with its regulatory protein mattered.\norganism: Human NOS3 and human calmodulin expressed in E. coli\ntissue_or_cell_type: NOS expression and catalytic function\nexperimental_model: Recombinant coexpression and enzyme activity comparison\nlimitations: Expression-system result; not a test of dietary calcium or calmodulin supplementation.\nexposure: Calmodulin coexpression versus adding calmodulin after expression\nevidence_span: {\"source_cache\": \"artifacts/citrulline-research/8951046.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb\", \"start_char\": 0, \"end_char\": 1362, \"text_sha256\": \"f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb\"}\n[citrulline-p8951046] Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. 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