PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28803208-6 2017 In addition, UGT1A4 and UGT2B10 were primarily responsible for N-glucuronidation of many tertiary amines, including asenapine, loxapine, clozapine, chlorpromazine, dothiepin, doxepin, mirtazapine, mianserin, chlorcyclizine, cyclizine, promethazine, cyclobenzaprine, imatinib, retrorsine, strychnine and brucine. Nitrogen 63-64 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 13-19 35636643-4 2022 More importantly N-glucuronidation adduct was exclusively identified in all the hUGT1A4 mice, liver microsomes, and cultured primary hepatocytes, yet absent in the wide-type controls. Nitrogen 17-18 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 80-87 29572863-7 2018 N-glucuronidation of norketamine was studied in vitro with liver microsomes of different species and the single human enzyme UGT1A4. Nitrogen 0-1 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 125-131 28803208-0 2017 N-glucuronidation catalyzed by UGT1A4 and UGT2B10 in human liver microsomes: Assay optimization and substrate identification. Nitrogen 0-1 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 31-37 28803208-3 2017 However, the metabolic patterns of UGT1A4- and UGT2B10-mediated N-glucuronidation are not fully clear. Nitrogen 64-65 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 35-41 28803208-4 2017 In this study, we first optimized in vitro reaction conditions for N-glucuronidation by using specific substrates (i.e., trifluoperazine for UGT1A4, cotinine and amitriptyline for UGT2B10). Nitrogen 67-68 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 141-147 28803208-8 2017 Also, UGT1A4- and UGT2B10-mediated N-glucuronidation might play significant roles in metabolism and detoxification of tertiary amines in humans. Nitrogen 35-36 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 6-12 19372226-8 2009 Incubations with recombinant human UDP-glucuronosyltransferases (UGTs) and inhibition by the UGT1A4 and UGT1A1 substrates/inhibitors imipramine and bilirubin suggested that UGT1A4 is the major UGT isozyme catalyzing the N-glucuronidation of motesanib, with a minor contribution from UGT1A1. Nitrogen 220-221 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 93-99 20056725-5 2010 Finally, this isozyme was demonstrated to be UDP-glucuronosyltransferase (UGT) 1A4, with the direct evidence that recombinant UGT1A4 exhibited predominant and exclusive activity on SEN N-glucuronidation. Nitrogen 183-184 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 45-82 20056725-5 2010 Finally, this isozyme was demonstrated to be UDP-glucuronosyltransferase (UGT) 1A4, with the direct evidence that recombinant UGT1A4 exhibited predominant and exclusive activity on SEN N-glucuronidation. Nitrogen 183-184 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 126-132 20056725-7 2010 The exclusive role of UGT1A4 on SEN N-glucuronidation was strengthened additionally by its inhibitory kinetic study in which the selective inhibitor of UGT1A4 showed a similar inhibition pattern and K(i) values in both HLM and recombinant UGT1A4 systems. Nitrogen 34-35 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 22-28 20056725-7 2010 The exclusive role of UGT1A4 on SEN N-glucuronidation was strengthened additionally by its inhibitory kinetic study in which the selective inhibitor of UGT1A4 showed a similar inhibition pattern and K(i) values in both HLM and recombinant UGT1A4 systems. Nitrogen 34-35 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 152-158 20056725-7 2010 The exclusive role of UGT1A4 on SEN N-glucuronidation was strengthened additionally by its inhibitory kinetic study in which the selective inhibitor of UGT1A4 showed a similar inhibition pattern and K(i) values in both HLM and recombinant UGT1A4 systems. Nitrogen 34-35 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 152-158 23371966-4 2013 It also, however, is subject to direct N-glucuronidation by UDP-glucuronosyltransferase 1A4 (UGT1A4). Nitrogen 39-40 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 60-91 23371966-4 2013 It also, however, is subject to direct N-glucuronidation by UDP-glucuronosyltransferase 1A4 (UGT1A4). Nitrogen 39-40 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 93-99 21434773-9 2011 The N-glucuronidation rates in humans are typically much higher than in animals, largely due to the activity of two enzymes, the extensively studied UGT1A4, and the more recently identified as a main player in N-glucuronidation, UGT2B10. Nitrogen 4-5 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 149-155 21434773-9 2011 The N-glucuronidation rates in humans are typically much higher than in animals, largely due to the activity of two enzymes, the extensively studied UGT1A4, and the more recently identified as a main player in N-glucuronidation, UGT2B10. Nitrogen 210-211 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 149-155 20713656-5 2010 Consistent with these observations, the UGT1A4 inhibitor hecogenin and the UGT2B7 substrate diclofenac potently inhibited the N- and O-glucuronidation of 1"-hydroxymidazolam in HLMs, respectively. Nitrogen 126-127 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 40-46 19372226-8 2009 Incubations with recombinant human UDP-glucuronosyltransferases (UGTs) and inhibition by the UGT1A4 and UGT1A1 substrates/inhibitors imipramine and bilirubin suggested that UGT1A4 is the major UGT isozyme catalyzing the N-glucuronidation of motesanib, with a minor contribution from UGT1A1. Nitrogen 220-221 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 173-179 17576790-4 2007 UGT2B10 was also more active than UGT1A4 in N-glucuronidation of cotinine (oxidative nicotine metabolite), whereas UGT2B7 exhibited only low nicotine glucuronidation activity and was essentially inactive toward cotinine. Nitrogen 44-45 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 34-40 18256203-8 2008 Among the recombinant human UDP glucuronosyltransferase (UGT) isoforms tested, only isoform UGT1A4 catalyzed the N-glucuronidation of MDZ fitting a Michaelis-Menten model. Nitrogen 113-114 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 92-98 17998299-11 2008 Consistent with these observations, hecogenin, a selective inhibitor of UGT1A4, selectively inhibited the N-glucuronidation, whereas diclofenac, a potent inhibitor of UGT2B7, had a greater inhibitory effect on the O-glucuronidation than on the N-glucuronidation. Nitrogen 106-107 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 72-78 16713428-6 2006 At the 50 micromol/L uridine diphosphate glucoronic acid (UDPGA) concentration, UGT1A4 also catalyzed the N-glucuronidation of retigabine, the rates being approximately 5 and 6 pmol/(min.mg protein). Nitrogen 106-107 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 80-86 16480962-6 2006 Only UGT1A4 catalyzed the N-linked glucuronidation of 4-HO-TAM among recombinant human UGT isoforms (UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9, UGT1A10, UGT2B4, UGT2B7, UGT2B15, and UGT2B17) expressed in insect cells. Nitrogen 26-27 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 5-11 15475412-8 2005 The K(m) value of AFQ N-glucuronidation in recombinant UGT1A4 microsomes was very close to that in human liver microsomes. Nitrogen 22-23 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 55-61 15470160-6 2005 These results suggest that trans-3"-hydroxycotinine N-glucuronidation in human liver microsomes would be mainly catalyzed by UGT1A4. Nitrogen 52-53 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 125-131 15475412-9 2005 The formation of AFQ N-glucuronidation by human liver, jejunum, and recombinant UGT1A4 microsomes was effectively inhibited by trifluoperazine, a known specific substrate for UGT1A4. Nitrogen 21-22 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 80-86 15475412-9 2005 The formation of AFQ N-glucuronidation by human liver, jejunum, and recombinant UGT1A4 microsomes was effectively inhibited by trifluoperazine, a known specific substrate for UGT1A4. Nitrogen 21-22 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 175-181 15475412-12 2005 These results demonstrate that AFQ N-glucuronidation in human is mainly catalyzed by UGT1A4 in the liver and by UGT1A3, as well as UGT1A4 in the intestine. Nitrogen 35-36 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 85-91 15475412-12 2005 These results demonstrate that AFQ N-glucuronidation in human is mainly catalyzed by UGT1A4 in the liver and by UGT1A3, as well as UGT1A4 in the intestine. Nitrogen 35-36 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 131-137 15135306-5 2004 A strong correlation (r(2) =0.92 ) was observed between N-glucuronidating activities toward TAM and trifluoperazine, a probe substrate for human UDP-glucuronosyltransferase (UGT) 1A4, in human liver microsomes from eight donors (five females, three males). Nitrogen 56-57 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 145-182 15135306-7 2004 Only UGT1A4 catalyzed the N-linked glucuronidation of TAM among recombinant UGTs (UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A9, UGT2B4, UGT2B7, UGT2B15, and UGT2B17) expressed in insect cells. Nitrogen 26-27 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 5-11 15135306-8 2004 Apparent K(m) values for TAM N-glucuronidation by human liver microsomes and recombinant UGT1A4 were 35.8 and 32.4 microM, respectively. Nitrogen 29-30 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 89-95 14709623-8 2004 Overexpressed UDP-glucuronosyltransferase (UGT) 1A4 exhibited significant levels of N-glucuronidating activity (V(max)/K(m) = 3.11 microl. Nitrogen 84-85 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 14-51 10901693-3 2000 Two UDP-glucuronosyltransferases (UGTs) present in human liver, UGT1A4 and UGT1A3, were previously shown to catalyze tertiary amine N-glucuronidation when expressed in HK293 cells. Nitrogen 132-133 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 64-70 12167564-7 2002 None of the UGTs examined catalyzed the N-glucuronidation of S(-)-nicotine, R(+)-nicotine, and S(-)-cotinine, including UGT1A3 and UGT1A4, the only isoforms known to catalyze many substrates at a tertiary amine. Nitrogen 0-1 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 131-137 12433823-10 2002 In conclusion, the involvement of UGT1A1 and UGT1A9 as well as UGT1A4 in nicotine and cotinine N-glucuronidations in human liver microsomes was suggested, although the contributions of each UGT isoform could not be determined conclusively. Nitrogen 95-96 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 63-69 10901693-5 2000 When homogenates of HK293 cells expressing UGT1A4 were incubated without detergent, N-glucuronidation kinetics were monophasic with K(M) values of 59 +/- 5 microM for (R)- and 86 +/- 26 microM for (S)-ketotifen. Nitrogen 84-85 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 43-49 10901693-8 2000 With amitriptyline as the substrate, N-glucuronidation kinetics in the absence of detergent were biphasic in human liver microsomes and monophasic with a high K(M) value in cell homogenates containing UGT1A4. Nitrogen 37-38 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 201-207 10901693-9 2000 The results suggest that UGT1A4 and UGT1A3 catalyze high-K(M) N-glucuronidation of tertiary amine drugs, whereas the low-K(M) reaction requires either an alternative enzyme or a special conformation of UGT1A4 or UGT1A3 that can be attained in liver microsomes, but not in HK293 cell membranes. Nitrogen 62-63 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 25-31 10901693-9 2000 The results suggest that UGT1A4 and UGT1A3 catalyze high-K(M) N-glucuronidation of tertiary amine drugs, whereas the low-K(M) reaction requires either an alternative enzyme or a special conformation of UGT1A4 or UGT1A3 that can be attained in liver microsomes, but not in HK293 cell membranes. Nitrogen 62-63 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 202-208 10506112-7 1999 UGT1A4 N-glucuronidated N"-hydroxy- N-acetylbenzidine at the highest relative rate compared with the other transferases. Nitrogen 7-8 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 0-6 8820428-2 1996 In this study, we show that human UDP-glucuronosyltransferase 1.4 protein, stably expressed in human embryonic kidney 293 cells, catalyzes the N-glucuronidation of primary, secondary, and tertiary amine substrates. Nitrogen 143-144 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 34-65