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(2025). https://pubmed.ncbi.nlm.nih.gov/40128258/ DOI: 10.1038/s41467-025-58200-y","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"XPR1-KIDINS220 transport complex","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"596df2f5-4dab-542e-afa5-ca20d28ad90a","evidence_kind":"source_excerpt","locator":"Lines 938-949","start_line":938,"end_line":949,"excerpt":"### ino-kidins-xpr1\nXPR1 alone remained closed even with InsP6 and phosphate in the tested structures, whereas the KIDINS220-containing complex could open.\nCondition category: normal\nnutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A partner protein mattered as well as the chemical signal.\norganism: Human proteins\ntissue_or_cell_type: XPR1-KIDINS220 transport complex\nexperimental_model: Cryo-EM and functional mutagenesis\nlimitations: This paper tests InsP6 despite pyrophosphate wording in its title. It does not establish that dietary phytate reaches this intracellular site or overrides InsP8 selectivity in other assays.\nexposure: InsP6 and phosphate binding\nevidence_span: {\"source_cache\": \"artifacts/inositol-research/40128258.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00\", \"start_char\": 0, \"end_char\": 1071, \"text_sha256\": \"4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00\"}\n[ino-p40128258] Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate. (2025). https://pubmed.ncbi.nlm.nih.gov/40128258/ DOI: 10.1038/s41467-025-58200-y","model_system":"Cryo-EM and functional mutagenesis","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. 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