{"id":"ad746137-a2b1-5aa3-b115-8be77db6ffa5","stable_key":"ff370329-68a3-573d-96ee-597de78a3967:api-direct-sirt1-null","predicate":"no_detected_change_in_recorded_comparison","statement":"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.","claim_class":"observational","status":"source_recorded","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"5c555fbd-a963-5626-b05c-bd8629467d23","mechanism_event_label":"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.","subject":{"id":"4425961f-4764-56d3-9887-87e47749379b","slug":"apigenin","display_name":"Apigenin","entity_type_key":"small_molecule"},"object":{"id":"b8e1bfa9-c412-5f35-97af-cfc722123d27","slug":"sirt1","display_name":"SIRT1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"5c555fbd-a963-5626-b05c-bd8629467d23","stable_key":"ff370329-68a3-573d-96ee-597de78a3967:api-direct-sirt1-null-event","event_type":"experimental_observation","label":"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.","description":"### api-direct-sirt1-null\n\nApigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.\nThe paper instead investigated NAD preservation upstream of cellular deacetylation.\nModel and exposure: Cell-free SIRT1 assay.\nLimitations: Limited to the recorded preparation, model, exposure and endpoint. Does not establish a human dietary deficiency, clinical benefit or unique molecular mediation.\nReference: Flavonoid apigenin is an inhibitor of the NAD+ ase CD38: implications for cellular NAD+ metabolism, protein acetylation, and treatment of metabolic syndrome. | 2013 | https://pubmed.ncbi.nlm.nih.gov/23172919/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC3609577/ | https://doi.org/10.2337/db12-1139 | Access: Primary full text: relevant Results/Methods and figure descriptions reviewed; supplements only where explicitly stated.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"4425961f-4764-56d3-9887-87e47749379b","slug":"apigenin","display_name":"Apigenin","entity_type_key":"small_molecule"},"role":"tested factor","stoichiometry":null,"state_label":"Apigenin concentration series","sequence_order":0,"notes":""},{"entity":{"id":"b8e1bfa9-c412-5f35-97af-cfc722123d27","slug":"sirt1","display_name":"SIRT1","entity_type_key":"protein"},"role":"measured outcome","stoichiometry":null,"state_label":"no_detected_change","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text: relevant Results/Methods and figure descriptions reviewed; supplements only where explicitly stated.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_contrast","value_text":"{\"intervention\": \"Apigenin concentration series\", \"comparator\": \"Assay without apigenin\", \"endpoint\": \"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.\", \"effect_direction\": \"no_detected_change\", \"combination\": \"single\", \"conditions\": []}","comparator":null,"unit":null,"notes":"Explicit extracted experimental comparison; recorded from source.","entity":null},{"dimension":"experimental_model","value_text":"Cell-free SIRT1 assay.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Recorded from source with stated access limits; ungraded, not independent replication.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Limited to the recorded preparation, model, exposure and endpoint. Does not establish a human dietary deficiency, clinical benefit or unique molecular mediation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Apigenin collection; exact intervention and molecular form govern interpretation.","comparator":null,"unit":null,"notes":"","entity":{"slug":"apigenin","display_name":"Apigenin","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Flavonoid apigenin is an inhibitor of the NAD+ ase CD38: implications for cellular NAD+ metabolism, protein acetylation, and treatment of metabolic syndrome. | https://pubmed.ncbi.nlm.nih.gov/23172919/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC3609577/ | https://doi.org/10.2337/db12-1139","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference api-direct-sirt1-null; The paper instead investigated NAD preservation upstream of cellular deacetylation.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5d9c73fb-0036-5723-a836-0307000dbcd3","evidence_kind":"source_excerpt","locator":"Lines 192-198","start_line":192,"end_line":198,"excerpt":"### api-direct-sirt1-null\n\nApigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.\nThe paper instead investigated NAD preservation upstream of cellular deacetylation.\nModel and exposure: Cell-free SIRT1 assay.\nLimitations: Limited to the recorded preparation, model, exposure and endpoint. Does not establish a human dietary deficiency, clinical benefit or unique molecular mediation.\nReference: Flavonoid apigenin is an inhibitor of the NAD+ ase CD38: implications for cellular NAD+ metabolism, protein acetylation, and treatment of metabolic syndrome. | 2013 | https://pubmed.ncbi.nlm.nih.gov/23172919/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC3609577/ | https://doi.org/10.2337/db12-1139 | Access: Primary full text: relevant Results/Methods and figure descriptions reviewed; supplements only where explicitly stated.","model_system":"Cell-free SIRT1 assay.","directness":"reported_statement","verification_status":"source_recorded","notes":"Original paraphrase in the retained reviewed reference, not a verbatim primary-paper quotation. Access level is explicit.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"54eac90b-add1-5f56-9036-d900307c5697","stable_key":"import-ff370329-68a3-573d-96ee-597de78a3967","title":"Apigenin: detailed mechanisms of action (reviewed 10 October 2026)","document_type":"imported_text","citation_label":"AI-assisted original curation of primary studies; claim-local access and experimental limitations stated. Includes original-draft correction history. No independent replication claimed.","file_path":"","sha256":"ede6e5c6b91d66b66844f2ff667a7f8303d9ac1281f15dc09db703f7de4da942","revision_id":"b41a39a2-0197-549c-97a5-1765e6696931","review_status":"source_recorded","notes":""}}],"relations":[{"id":"f3b662af-2a6d-5c98-b1fa-bbc679bc9753","relation_type":"limits_scope_of","notes":"Cellular deacetylation does not establish direct SIRT1 activation.","source_claim_id":"ad746137-a2b1-5aa3-b115-8be77db6ffa5","source_claim_key":"ff370329-68a3-573d-96ee-597de78a3967:api-direct-sirt1-null","source_statement":"Apigenin did not directly activate recombinant SIRT1 in the tested 0–100 micromolar series.","target_claim_id":"394cef21-efb6-5f59-9e6a-4b9193943e8a","target_claim_key":"ff370329-68a3-573d-96ee-597de78a3967:api-cell-deacetylation","target_statement":"Apigenin lowered protein acetylation in HepG2 cells, and EX-527 blocked this response."}],"conflicts":[],"corrections":[],"research":null}