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(2022). https://pubmed.ncbi.nlm.nih.gov/35343688/ DOI: 10.1021/jacs.1c13626","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"LIAS radical-SAM site","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"aa239fcb-36d8-5066-af2b-21a3fea8ff9a","evidence_kind":"source_excerpt","locator":"Lines 364-375","start_line":364,"end_line":375,"excerpt":"### ala-nfu1-isca1-radical-site\nAn NFU1-ISCA1 heterodimer delivers a [4Fe-4S] cluster to the radical-SAM site of LIAS.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A separate assembly route equips the radical-generating site.\norganism: Human proteins\ntissue_or_cell_type: LIAS radical-SAM site\nexperimental_model: Recombinant protein interaction and cluster-insertion analysis\nlimitations: Loading the radical-SAM site is distinct from recycling the auxiliary sulfur-donor site.\nexposure: NFU1-ISCA1 donor complex\nevidence_span: {\"source_cache\": \"artifacts/ala-research/35343688.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689\", \"start_char\": 0, \"end_char\": 670, \"text_sha256\": \"62b2b8ddcff12b7264515cd251238a0f0e4dbe086fa72830ebff6e88f5db0689\"}\n[ala-p35343688] Protein-Interaction Affinity Gradient Drives [4Fe-4S] Cluster Insertion in Human Lipoyl Synthase. 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