{"id":"e409307b-1f5c-5cee-a85d-ba81e0953373","stable_key":"96d9034a-2550-5f3c-b767-1767c982533c:lariciresinol-inhibits-alpha-glucosidase","predicate":"inhibits","statement":"Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"negative","is_public":true,"mechanism_event_id":"0cfbf7a9-289a-57fd-ae06-2fe79365d751","mechanism_event_label":"Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.","subject":{"id":"4fcf5405-bafb-54bf-89b8-2fc11e0d9822","slug":"lariciresinol","display_name":"Lariciresinol, enantiomer unresolved","entity_type_key":"small_molecule"},"object":{"id":"d40ae172-7698-5aaa-8917-aba671505cc9","slug":"yeast-alpha-glucosidase-ryr-assay","display_name":"Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay","entity_type_key":"protein_family"},"evidence_count":1,"mechanism_event":{"id":"0cfbf7a9-289a-57fd-ae06-2fe79365d751","stable_key":"96d9034a-2550-5f3c-b767-1767c982533c:lariciresinol-inhibits-alpha-glucosidase-event","event_type":"observed_relationship","label":"Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.","description":"Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"4fcf5405-bafb-54bf-89b8-2fc11e0d9822","slug":"lariciresinol","display_name":"Lariciresinol, enantiomer unresolved","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"d40ae172-7698-5aaa-8917-aba671505cc9","slug":"yeast-alpha-glucosidase-ryr-assay","display_name":"Saccharomyces cerevisiae alpha-glucosidase in the 2024 pigment assay","entity_type_key":"protein_family"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"duration","value_text":"Not applicable","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"evidence_access","value_text":"Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"α-Glucosidase inhibitory assay with molecular docking","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Lariciresinol","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"α-Glucosidase inhibitory assay with molecular docking","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Lariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"route","value_text":"In vitro","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue","value_text":"Carbohydrate-hydrolysing enzyme activity","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a27f6204-7c09-5efe-b8d6-4137f23f494d","evidence_kind":"source_excerpt","locator":"Lines 165-174","start_line":165,"end_line":174,"excerpt":"## lariciresinol-inhibits-alpha-glucosidase\nLariciresinol inhibited α-glucosidase with a half-maximal inhibitory concentration of 6.97 ± 0.37 µM, acting as a competitive inhibitor with an inhibition constant of 0.046 µM.\nModel/species: α-Glucosidase inhibitory assay with molecular docking\nTissue/system: Carbohydrate-hydrolysing enzyme activity\nExposure: Lariciresinol\nRoute: In vitro\nDuration: Not applicable\nLimits: The enantiomer is not stated. The inhibition constant is about 150-fold below the inhibitory concentration, which is a large gap for a competitive inhibitor and depends on the substrate concentration used.\nPrimary reference: Lariciresinol Displays Anti-Diabetic Activity through Inhibition of α-Glucosidase and Activation and Enhancement of Insulin Signaling. (2022). https://pubmed.ncbi.nlm.nih.gov/35490401/ DOI: 10.1002/mnfr.202100910\nAccess: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.","model_system":"","directness":"reported_statement","verification_status":"source_derived_draft","notes":"","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"48c58761-0291-5bad-a926-75e904b2d802","stable_key":"import-96d9034a-2550-5f3c-b767-1767c982533c","title":"Lariciresinol: five molecules under one name, and the mechanisms each one carries (2026-09-22)","document_type":"imported_text","citation_label":"Original AI-assisted curation of twelve primary studies, every abstract read and all DOIs cross-checked against live PubMed metadata. Mechanism edges only, with no conclusion or claim of benefit recorded. Three author clusters account for eight of the twelve and carry shared laboratory keys. Study-specific concentrations, negative findings and limitations retained. Not publisher full text.","file_path":"","sha256":"6bf0015b7ff727b7a80d693dd18ffdd227d0e16ae45d9e85a5f81fa733edd3a4","revision_id":"219d9b0c-1a71-5e27-8d6c-7b3e77a594c6","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}