{"id":"26140f12-5bec-585f-a180-930418eaa479","stable_key":"475ea55a-65e9-51c3-a539-738a6a8f683f:mangiferin-complex-gsh","predicate":"protects_against","statement":"The ferric complex protected mitochondrial glutathione against oxidation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"7d5fe26e-24bd-554d-8f37-8fa31e8a63f7","mechanism_event_label":"Metal coordination altered protection of the redox buffer.","subject":{"id":"ac12b6f1-68ff-5a1a-a3dd-a10c18d96903","slug":"mangiferin-ferric-complex","display_name":"Mangiferin-ferric iron complex, assay-defined","entity_type_key":"chemical_species"},"object":{"id":"1971ea50-6457-56d5-b817-c39a93fcdba6","slug":"rat-mitochondrial-gsh-oxidation","display_name":"Rat liver mitochondrial glutathione oxidation or depletion","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"7d5fe26e-24bd-554d-8f37-8fa31e8a63f7","stable_key":"475ea55a-65e9-51c3-a539-738a6a8f683f:mangiferin-complex-gsh-event","event_type":"biochemical_relationship","label":"Metal coordination altered protection of the redox buffer.","description":"The ferric complex protected mitochondrial glutathione against oxidation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"affected_buffer","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ac12b6f1-68ff-5a1a-a3dd-a10c18d96903","slug":"mangiferin-ferric-complex","display_name":"Mangiferin-ferric iron complex, assay-defined","entity_type_key":"chemical_species"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"1971ea50-6457-56d5-b817-c39a93fcdba6","slug":"rat-mitochondrial-gsh-oxidation","display_name":"Rat liver mitochondrial glutathione oxidation or depletion","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/mangiferin-research/17068204.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64\", \"start_char\": 0, \"end_char\": 1172, \"text_sha256\": \"1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Iron-coordination spectroscopy and mitochondrial challenge","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Assay-defined ferric iron-mangiferin complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Mangiferin research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"mangiferin","display_name":"Mangiferin","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Rattus norvegicus and cell-free chemistry","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Metal coordination altered protection of the redox buffer.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. (2007). https://pubmed.ncbi.nlm.nih.gov/17068204/ DOI: 10.1124/jpet.106.112003","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Isolated mitochondria","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"c76ff8aa-1e13-5477-8077-281e34e9f5ba","evidence_kind":"source_excerpt","locator":"Lines 757-768","start_line":757,"end_line":768,"excerpt":"### mangiferin-complex-gsh\nThe ferric complex protected mitochondrial glutathione against oxidation.\nCondition category: normal\nnutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Metal coordination altered protection of the redox buffer.\norganism: Rattus norvegicus and cell-free chemistry\ntissue_or_cell_type: Isolated mitochondria\nexperimental_model: Iron-coordination spectroscopy and mitochondrial challenge\nlimitations: Defined chemical form and calcium context explain the different response; no clinical iron/mangiferin co-dosing recommendation.\nexposure: Assay-defined ferric iron-mangiferin complex\nevidence_span: {\"source_cache\": \"artifacts/mangiferin-research/17068204.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64\", \"start_char\": 0, \"end_char\": 1172, \"text_sha256\": \"1d0b364cee6629228fe7bc41446a0e2ddfe62b9274d77d4781ca7439aedfbb64\"}\n[mangiferin-p17068204] Fe(III) shifts the mitochondria permeability transition-eliciting capacity of mangiferin to protection of organelle. 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