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studies lead to a model for the developmental patterning of UGT1A8, UGT1A9, and UGT1A10 in hepatic and/or extrahepatic tissues involving discrete regulatory modules that may function (independently and cooperatively) in a context-dependent manner
Icaritin was subjected to significant glucuronidation, wherein UGT1A3, 1A7, 1A8, 1A9 and 2B7 were main contributing enzymes.
Inter-isoform Hetero-dimerization of Human UDP-Glucuronosyltransferases (UGTs) 1A1, 1A9, and 2B7 and Impacts on Glucuronidation Activity
The findings of the study highlighted correlation between UGT1A9 -440C/T gene polymorphisms and positive propofol efficacy in patients undergoing painless induced pregnancy termination procedures.
A significantly higher number of UGT1A9 polymorphisms was found in the group that did not respond to Mycophenolic acid treatment.
None of the patients with Regorafenib-induced severe toxic hepatitis had CYP3A4 gene mutations. Similar polymorphisms in UGT1A9 gene promoter region were found in both patients who presented acute hepatitis.
No association between the UGT1A9 c.98T>C polymorphism and mycophenolic acid plasma levels were found in renal transplant patients.
UGT1A1, UGT1A6, and UGT1A9 were the chief contributors to the regioselective glucuronidation of diosmetin and chrysoeriol in the liver.
polymorphisms c.98T>C in the UGT1A9 and c.1075A>C in the CYP2C9 genes did not affect the pharmacokinetic profile of propofol
Carriers of T-275A and C-2152T single-nucleotide polymorphisms of the UGT1A9 gene promoter region show a greater incidence of death from digestive system cancer after kidney transplantation.
demonstrated the effects of UGT1A9 genetic polymorphisms on MHD plasma concentrations and OXC therapeutic efficacy. Through MHD monitoring, we can predict OXC therapeutic efficacy, which may be useful for the personalization of OXC therapy in epileptic patients
Dimerization changed the chemical regioselectivity, substrate-binding affinity, and enzymatic activity of UGT1A1 and UGT1A9 in glucuronidation of quercetin.
UGT1A9 contributes to the in-vitro glucuronidation of arctigenin in liver microsomes.
the in vitro glucuronidation of raloxifene in humans and monkeys was examined using liver and intestinal microsomes and recombinant UGT enzymes (UGT1A1, UGT1A8 and UGT1A9).
Suggest that the enzymatic properties of UGT1A9 are considerably different between humans and cynomolgus monkeys, although humUGT1A9 and monUGT1A9 were highly conserved at the amino acid level.
We observed statistically significant associations between SNP and Drug-induced liver injury at both allele and genotype levels of of UGT1A9 promoter
UGT1A10 exhibited somewhat higher BPA glucuronidation activity than UGT1A9, but it was lower than UGT2A1 and UGT2B15. 4.
in tumor liver microsomes from HCC patients, either V(max) (maximum reaction rate, R(max) for UGT1A1) or clearance rates (V(max)/K(m), Clint) of UGT1A, UGT1A1, UGT1A4, UGT1A9 and UGT2B7 were lower than those in the adjacent normal liver microsomes
Significantly lower estimated glomerular filtration rate of the renal allograft in UGT1A9 c.98C carriers did not translate into decreased allograft survival.
Data shows that UGT1A9*22 allele was significantly less frequent in the Uzbek population compared to the Japanese.
Diabetes mellitus caused a decrease in the activity of Cyp3a11-mediated testosterone-6beta-hydroxylation, but no change in the activity of Cyp3a11-mediated midazolam 1-hydroxylation and an increase in the activity of UGT1a9-mediated propofol O-glucuronidation in db/db mice
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene is active on phenols.
UDP glycosyltransferase 1 family, polypeptide A9
, UDP-glucuronosyltransferase 1-9
, UDP-glucuronosyltransferase 1A9
, UDP glucuronosyltransferase 1 family, polypeptide A9
, UDP glycosyl transferase 1A9
, UDP-glucuronosyltransferase 1-I
, UDP glycosyltransferase 1 family polypeptide A12
, UDP-glucuronosyltransferase 1-7
, UDP glycosyltransferase 1 family polypeptide A10
, UDP glycosyltransferase 1 family polypeptide A11
, UDP glycosyltransferase 1 family, polypeptide A10