{"id":"ce084bc7-a5a2-5da2-8853-875933d2ec36","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-nrf2-slc7a11","predicate":"supports","statement":"NRF2 knockdown suppressed copper-induced SLC7A11 expression.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"1808ae7a-3072-5b5c-aac6-ed039561b137","mechanism_event_label":"The stress-response regulator was part of the transporter-expression response.","subject":{"id":"dc472dd3-d383-567a-ab37-a9ec4e112df4","slug":"nfe2l2","display_name":"Human Nrf2 / NFE2L2","entity_type_key":"protein"},"object":{"id":"3dce013b-fd9f-5305-96da-7d928281d237","slug":"cu-induced-slc7a11-expression","display_name":"Copper-exposure-induced SLC7A11 expression in human MDA-MB-231 cells","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"1808ae7a-3072-5b5c-aac6-ed039561b137","stable_key":"0ad8610d-d575-5870-b7cd-763a9f750783:copper-nrf2-slc7a11-event","event_type":"biochemical_relationship","label":"The stress-response regulator was part of the transporter-expression response.","description":"NRF2 knockdown suppressed copper-induced SLC7A11 expression.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"aac19cc3-1b68-5ca3-a896-f61184f7320a","slug":"slc7a11","display_name":"SLC7A11","entity_type_key":"protein"},"role":"regulated transporter","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"dc472dd3-d383-567a-ab37-a9ec4e112df4","slug":"nfe2l2","display_name":"Human Nrf2 / NFE2L2","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"3dce013b-fd9f-5305-96da-7d928281d237","slug":"cu-induced-slc7a11-expression","display_name":"Copper-exposure-induced SLC7A11 expression in human MDA-MB-231 cells","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/copper-research/40944334.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89\", \"start_char\": 0, \"end_char\": 1634, \"text_sha256\": \"6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Copper and iron exposure with transcription-factor knockdown","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction.","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":"Human MDA-MB-231 breast cancer cells","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The stress-response regulator was part of the transporter-expression response.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cellular amino-acid transport machinery","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ec7bdc7e-2a01-5074-839b-3a8435745528","evidence_kind":"source_excerpt","locator":"Lines 1300-1311","start_line":1300,"end_line":1311,"excerpt":"### copper-nrf2-slc7a11\nNRF2 knockdown suppressed copper-induced SLC7A11 expression.\nCondition category: normal\nnutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The stress-response regulator was part of the transporter-expression response.\norganism: Human MDA-MB-231 breast cancer cells\ntissue_or_cell_type: Cellular amino-acid transport machinery\nexperimental_model: Copper and iron exposure with transcription-factor knockdown\nlimitations: One cancer-cell model. Expression changes do not prove increased glutathione synthesis, tumor progression, or a clinical nutrient interaction.\nexposure: CuCl2 or FeCl2 exposure; NFE2L2 or ATOX1 knockdown\nevidence_span: {\"source_cache\": \"artifacts/copper-research/40944334.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89\", \"start_char\": 0, \"end_char\": 1634, \"text_sha256\": \"6df1716e8998546d22a1d96116e1bc35b1f7e24c94868ec5e441ada6a2be3e89\"}\n[copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847","model_system":"Copper and iron exposure with transcription-factor knockdown","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [copper-p40944334] Copper induces cystine/glutamate antiporter SLC7A11 through the activation of Nrf2 and Atox1 pathways. (2025). https://pubmed.ncbi.nlm.nih.gov/40944334/ DOI: 10.1080/10715762.2025.2560847","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9afba495-cbdc-51aa-998e-70a930dba3be","stable_key":"import-0ad8610d-d575-5870-b7cd-763a9f750783","title":"Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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