{"id":"d8ca1325-a0cd-5a0c-bb93-4d5eeb29a3e9","stable_key":"33bef151-bdc7-5892-aff6-0345ab149739:plasmin-does-not-degrade-those-fibrils","predicate":"does_not_proteolyze","statement":"Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"neutral","is_public":true,"mechanism_event_id":"72ea7712-ee5f-5253-9bef-f57863ad0e70","mechanism_event_label":"Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.","subject":{"id":"50bb8eb1-a684-5c21-b73a-1010e37aa336","slug":"plasmin","display_name":"Plasmin","entity_type_key":"protein"},"object":{"id":"f2b6bdc9-76e1-5cd8-b893-e18d774403a5","slug":"amyloid-beta-fibrils","display_name":"Amyloid-beta fibrils, sequence specified by study","entity_type_key":"protein_state"},"evidence_count":1,"mechanism_event":{"id":"72ea7712-ee5f-5253-9bef-f57863ad0e70","stable_key":"33bef151-bdc7-5892-aff6-0345ab149739:plasmin-does-not-degrade-those-fibrils-event","event_type":"biochemical_relationship","label":"Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.","description":"In vitro fibril proteolysis","status":"provisional","compartment":null,"participants":[{"entity":{"id":"50bb8eb1-a684-5c21-b73a-1010e37aa336","slug":"plasmin","display_name":"Plasmin","entity_type_key":"protein"},"role":"acting component","stoichiometry":null,"state_label":"","sequence_order":0,"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":"component the finding is about","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"duration","value_text":"Not stated here","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":"Purified fibril preparations","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Plasmin","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This measured null is the informative half of the comparison: the activity tracks the subtilisin family rather than proteolysis in general.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Purified fibril preparations","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. 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Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. 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