{"id":"df7cb687-bb6f-5b31-965c-ce3f0ecca600","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-ttm-copper-transfer","predicate":"inhibits_copper_delivery_to","statement":"The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"3af43e2c-9404-5511-9883-b1924812908c","mechanism_event_label":"Trapping the copper interrupted its handoff to another protein.","subject":{"id":"f54dd59b-b06f-514e-8038-503661e6507b","slug":"moco-copper-atx1-drug-complex","display_name":"Tetrathiomolybdate-copper-yeast Atx1 cluster","entity_type_key":"protein_complex"},"object":{"id":"5d6a97f7-0115-5038-b54b-6a4a1abfa3d4","slug":"yeast-ccc2","display_name":"Saccharomyces cerevisiae copper-transporting ATPase / Ccc2","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"3af43e2c-9404-5511-9883-b1924812908c","stable_key":"dc8975b1-95ff-5d9b-be17-a1c04610cca7:mo-ttm-copper-transfer-event","event_type":"biochemical_relationship","label":"Trapping the copper interrupted its handoff to another protein.","description":"The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"9f0afdde-1ec1-5c8a-bb5e-f3b2b75f67f6","slug":"copper","display_name":"Copper","entity_type_key":"nutrient_element"},"role":"transported metal","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f54dd59b-b06f-514e-8038-503661e6507b","slug":"moco-copper-atx1-drug-complex","display_name":"Tetrathiomolybdate-copper-yeast Atx1 cluster","entity_type_key":"protein_complex"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5d6a97f7-0115-5038-b54b-6a4a1abfa3d4","slug":"yeast-ccc2","display_name":"Saccharomyces cerevisiae copper-transporting ATPase / Ccc2","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/molybdenum-research/19965379.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57\", \"start_char\": 0, \"end_char\": 950, \"text_sha256\": \"166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Tetrathiomolybdate exposure","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Molybdenum research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"molybdenum","display_name":"Molybdenum","entity_type_key":"nutrient_element"}},{"dimension":"organism","value_text":"Saccharomyces cerevisiae proteins; comparison with animal drug complexes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Trapping the copper interrupted its handoff to another protein.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified copper chaperones","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"32de51aa-637d-5a10-ae62-befe3e70668d","evidence_kind":"source_excerpt","locator":"Lines 1613-1624","start_line":1613,"end_line":1624,"excerpt":"### mo-ttm-copper-transfer\nThe drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system.\nCondition category: normal\nnutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Trapping the copper interrupted its handoff to another protein.\norganism: Saccharomyces cerevisiae proteins; comparison with animal drug complexes\ntissue_or_cell_type: Purified copper chaperones\nexperimental_model: Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments\nlimitations: Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.\nexposure: Tetrathiomolybdate exposure\nevidence_span: {\"source_cache\": \"artifacts/molybdenum-research/19965379.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57\", \"start_char\": 0, \"end_char\": 950, \"text_sha256\": \"166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57\"}\n[mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. 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