UDP-glucuronosyltransferase 1A7
Definition:
References:
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[1]. Hugo Girard, et al. Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity. Pharmacogenet Genomics. 2007 Dec;17(12):1077-89. [Content Brief]
[2]. Nicolas Picard, et al. Identification of the UDP-glucuronosyltransferase isoforms involved in mycophenolic acid phase II metabolism. Drug Metab Dispos. 2005 Jan;33(1):139-46. [Content Brief]
[3]. Mélanie Rouleau, et al. The relative protein abundance of UGT1A alternative splice variants as a key determinant of glucuronidation activity in vitro. Drug Metab Dispos. 2013 Apr;41(4):694-7. [Content Brief]
[4]. Jean-François Gagné, et al. Common human UGT1A polymorphisms and the altered metabolism of irinotecan active metabolite 7-ethyl-10-hydroxycamptothecin (SN-38). Mol Pharmacol. 2002 Sep;62(3):608-17. [Content Brief]
[5]. Anna Alonen, et al. The human UDP-glucuronosyltransferase UGT1A3 is highly selective towards N2 in the tetrazole ring of losartan, candesartan, and zolarsartan. Biochem Pharmacol. 2008 Sep 15;76(6):763-72. [Content Brief]
[6]. Judith Bellemare, et al. Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro. Drug Metab Dispos. 2010 Oct;38(10):1785-9. [Content Brief]
[7]. Tiby B Joseph, et al. Disposition of flavonoids via enteric recycling: enzyme stability affects characterization of prunetin glucuronidation across species, organs, and UGT isoforms. Mol Pharm. 2007 Nov-Dec;4(6):883-94. [Content Brief]
[8]. Katriina Itäaho, et al. The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases. Drug Metab Dispos. 2008 Nov;36(11):2307-15. [Content Brief]
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