{"id":"50ab4592-9b6f-5813-8976-94a418300b06","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-ccs-mouse-sod1","predicate":"loss_reduces_copper_loading_of","statement":"Ccs-null mice retained normal SOD1 protein abundance but had markedly reduced SOD1 copper incorporation and activity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7c9187c3-15b7-5abe-9d4c-be2544f89828","mechanism_event_label":"Counting enzyme molecules alone misses whether the enzyme has its working metal.","subject":{"id":"9dce69fb-cc03-54d0-8cd9-4f801c00bf42","slug":"mouse-ccs","display_name":"Mouse copper chaperone for SOD1 / Ccs","entity_type_key":"protein"},"object":{"id":"b752d8f4-066e-58d2-8322-ec0817437069","slug":"mouse-sod1","display_name":"Mouse copper-zinc superoxide dismutase Sod1","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"7c9187c3-15b7-5abe-9d4c-be2544f89828","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-ccs-mouse-sod1-event","event_type":"biochemical_relationship","label":"Counting enzyme molecules alone misses whether the enzyme has its working metal.","description":"Ccs-null mice retained normal SOD1 protein abundance but had markedly reduced SOD1 copper incorporation and activity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9dce69fb-cc03-54d0-8cd9-4f801c00bf42","slug":"mouse-ccs","display_name":"Mouse copper chaperone for SOD1 / Ccs","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"b752d8f4-066e-58d2-8322-ec0817437069","slug":"mouse-sod1","display_name":"Mouse copper-zinc superoxide dismutase Sod1","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/10694572.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad\", \"start_char\": 0, \"end_char\": 1205, \"text_sha256\": \"a8c8eb387b7e9d62e19f8de4ab12db826bbda965d5e673391bff49cb7ffe99ad\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Ccs knockout mice and radiocopper labeling","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Ccs deletion","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Normal protein abundance can coexist with low activity; the phenotype does not establish a general dietary copper deficiency.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Copper research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Mouse","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Counting enzyme molecules alone misses whether the enzyme has its working metal.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p10694572] Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. 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