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(2019). https://pubmed.ncbi.nlm.nih.gov/30660387/ DOI: 10.1016/j.ymgme.2018.12.012","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Lymphoblastoid and CD34-positive cells","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"08713b7d-7e0e-52cd-8370-2466a9c919d3","evidence_kind":"source_excerpt","locator":"Lines 1083-1094","start_line":1083,"end_line":1094,"excerpt":"### iron-glrx5-alas2\nALAS2 activity was altered in the GLRX5-deficient cells; a problem in succinyl-CoA supply was proposed as a contributor.\nCondition category: machinery_impairment\nnutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A mitochondrial assembly defect may also limit the starting materials used early in heme synthesis.\norganism: Human GLRX5-deficient patient\ntissue_or_cell_type: Lymphoblastoid and CD34-positive cells\nexperimental_model: Patient-derived cell biochemistry and variant structural analysis\nlimitations: One patient; reduced succinyl-CoA contribution to ALAS2 dysfunction was proposed, not definitively isolated.\nexposure: Compound-heterozygous GLRX5 variants\nevidence_span: {\"source_cache\": \"artifacts/iron-research/30660387.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e\", \"start_char\": 0, \"end_char\": 1625, \"text_sha256\": \"ea84d16e2c32450b285c269acb4a5343a8af27b49d8d1827afd3ad1961b8a61e\"}\n[iron-p30660387] GLRX5 mutations impair heme biosynthetic enzymes ALA synthase 2 and ferrochelatase in Human congenital sideroblastic anemia. 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