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(2023). https://pubmed.ncbi.nlm.nih.gov/36888659/ DOI: 10.1073/pnas.2220677120","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified protein assay","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"1b969351-a737-56ac-ace0-c4aae2217b2d","evidence_kind":"source_excerpt","locator":"Lines 1412-1424","start_line":1412,"end_line":1424,"excerpt":"### adp-slows-mmut-cob-ii-offloading\nUnder anaerobic conditions, ADP reduced the rate of cob(II)alamin transfer from human MMUT to MMAB in the MMAA repair system.\nCondition category: normal\nnutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: When oxidation was excluded, ADP slowed transfer of inactive B12 between the purified human proteins.\norganism: Homo sapiens\ntissue_or_cell_type: Purified protein assay\nexperimental_model: Purified human proteins\nlimitations: Transfer rate differs from oxidation protection; methylmalonyl-CoA reversed ADP inhibition in this assay.\nexposure: Anaerobic cofactor-transfer assay with ADP\ncross_nutrient: false\nevidence_location: Full text Results; Figures 2-3, Table 3\n[gouda-2023-adp-repair] Bivalent molecular mimicry by ADP protects metal redox state and promotes coenzyme B12 repair. 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