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- W2093652475 endingPage "158" @default.
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- W2093652475 abstract "Drug oxidation and conjugation mediated by cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) have long been considered to take place separately. However, our recent studies have suggested that CYP3A4 specifically associates with UGT2B7 and alters the regioselectivity of morphine glucuronidation. This observation strongly supports the view that there is functional cooperation between P450 and UGT to facilitate multistep drug metabolism. In recent years, accumulating evidence has suggested an interaction between UGT isoforms or between P450 and UGTs and a change in UGT function by protein-protein association. In this review, we summarize these interactions and discuss their relevance to UGT function." @default.
- W2093652475 created "2016-06-24" @default.
- W2093652475 creator A5014577532 @default.
- W2093652475 creator A5044211060 @default.
- W2093652475 creator A5079992977 @default.
- W2093652475 date "2009-10-12" @default.
- W2093652475 modified "2023-10-12" @default.
- W2093652475 title "Modulation of UDP-glucuronosyltransferase activity by protein-protein association" @default.
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- W2093652475 doi "https://doi.org/10.3109/03602530903208579" @default.
- W2093652475 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19817679" @default.
- W2093652475 hasPublicationYear "2009" @default.
- W2093652475 type Work @default.