{"id":"f5af8193-c4b1-57c3-90b3-0c9bb1fde11f","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-nfu1-affinity-gradient","predicate":"directs_cluster_transfer_to","statement":"The NFU1 C-domain guides cluster transfer along increasing interaction affinity from ISCA1 toward LIAS.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"914fb888-6713-58f5-ac93-23fd290983ff","mechanism_event_label":"Protein-to-protein recognition helps deliver the cluster to the correct destination.","subject":{"id":"eedbebc4-3413-53f9-9da3-5e98084c0a66","slug":"nfu1","display_name":"Human NFU1 iron-sulfur cluster carrier","entity_type_key":"protein"},"object":{"id":"f9fc9417-ca4f-5e0c-b01d-60b337493d34","slug":"lias","display_name":"Lipoic acid synthetase / LIAS","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"914fb888-6713-58f5-ac93-23fd290983ff","stable_key":"5d8e27d8-6a74-5560-827f-3f90908bbc34:ala-nfu1-affinity-gradient-event","event_type":"biochemical_relationship","label":"Protein-to-protein recognition helps deliver the cluster to the correct destination.","description":"The NFU1 C-domain guides cluster transfer along increasing interaction affinity from ISCA1 toward LIAS.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"4717bf5e-52fa-50b8-a665-0a7239bbfe66","slug":"isca1","display_name":"Human ISCA1","entity_type_key":"protein"},"role":"upstream_partner","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"eedbebc4-3413-53f9-9da3-5e98084c0a66","slug":"nfu1","display_name":"Human NFU1 iron-sulfur cluster carrier","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"f9fc9417-ca4f-5e0c-b01d-60b337493d34","slug":"lias","display_name":"Lipoic acid synthetase / LIAS","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"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\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Recombinant protein interaction and cluster-insertion analysis","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"NFU1-ISCA1 donor complex","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Loading the radical-SAM site is distinct from recycling the auxiliary sulfur-donor site.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"lipoic-acid","display_name":"Lipoic acid","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human proteins","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Protein-to-protein recognition helps deliver the cluster to the correct destination.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[ala-p35343688] Protein-Interaction Affinity Gradient Drives [4Fe-4S] Cluster Insertion in Human Lipoyl Synthase. (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":"cebf5ec1-2d43-5a7a-b06a-2a3a1f1172ee","evidence_kind":"source_excerpt","locator":"Lines 377-388","start_line":377,"end_line":388,"excerpt":"### ala-nfu1-affinity-gradient\nThe NFU1 C-domain guides cluster transfer along increasing interaction affinity from ISCA1 toward LIAS.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Protein-to-protein recognition helps deliver the cluster to the correct destination.\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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