{"id":"8729572f-4cc5-518b-adbe-106c60c2d83d","stable_key":"ec987f3e-0b3c-55cc-b304-c703a738e35d:egcg-amyloid-initiation","predicate":"redirects","statement":"EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"fa4244a5-339a-5cdd-8fd0-7adedffc4085","mechanism_event_label":"EGCG changed how these proteins assembled.","subject":{"id":"22e1b8eb-f35f-5afa-be20-b0534df9f6be","slug":"egcg","display_name":"Epigallocatechin-3-gallate (EGCG)","entity_type_key":"small_molecule"},"object":{"id":"05d28f9f-6ac4-5e04-9ba9-db8d46944513","slug":"amyloid-fibril-formation","display_name":"Amyloid fibril formation in specified assays","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"fa4244a5-339a-5cdd-8fd0-7adedffc4085","stable_key":"ec987f3e-0b3c-55cc-b304-c703a738e35d:egcg-amyloid-initiation-event","event_type":"observed_relationship","label":"EGCG changed how these proteins assembled.","description":"EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"22e1b8eb-f35f-5afa-be20-b0534df9f6be","slug":"egcg","display_name":"Epigallocatechin-3-gallate (EGCG)","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"05d28f9f-6ac4-5e04-9ba9-db8d46944513","slug":"amyloid-fibril-formation","display_name":"Amyloid fibril formation in specified assays","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"f2b6bdc9-76e1-5cd8-b893-e18d774403a5","slug":"amyloid-beta-fibrils","display_name":"Amyloid-beta fibrils, sequence specified by study","entity_type_key":"protein_state"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"310ed26c-0027-5fc6-91f7-91182f559a19","slug":"alpha-synuclein-fibrils","display_name":"Alpha-synuclein fibrils","entity_type_key":"protein_state"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Biophysical and cell-based aggregation experiments.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Not evidence of preventing or treating human neurodegenerative disease.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"EGCG collection; comparator and shared-pathway records retain their actual intervention.","comparator":null,"unit":null,"notes":"","entity":{"slug":"egcg","display_name":"Epigallocatechin-3-gallate (EGCG)","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"EGCG changed how these proteins assembled.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"cdc0df87-de9c-543a-8d3a-003a63e7bccd","evidence_kind":"source_excerpt","locator":"Lines 348-354","start_line":348,"end_line":354,"excerpt":"## egcg-amyloid-initiation\nEGCG changed how these proteins assembled.\nEGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.\nModel: Biophysical and cell-based aggregation experiments.\nLimitations: Not evidence of preventing or treating human neurodegenerative disease.\nEvidence access: primary abstract.\nEGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437","model_system":"Biophysical and cell-based aggregation experiments.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Primary-abstract paraphrase; no full-text methods verification claimed.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"1f6d09e8-3aae-5c41-9ea7-15d0d1cab72d","stable_key":"import-ec987f3e-0b3c-55cc-b304-c703a738e35d","title":"EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary-abstract references and experimental limitations individually identified. 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