PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7628292-4 1995 However, expressed human UGT1.4 protein exhibited glucuronidation activity toward tertiary amine substrates, such as imipramine, cyproheptadine, tripelennamine, and chlorpromazine, which form quaternary ammonium-linked glucuronides. Imipramine 117-127 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 25-31 8820428-11 1996 The results show that detergents (such as Lubrol PX, Emulgen 911, and Triton X-100) are inhibitory for the quaternary ammonium-linked glucuronidation of chlorpromazine and imipramine catalyzed by expressed human UDP-glucuronosyltransferase 1.4. Imipramine 172-182 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 212-243 21726413-10 2011 Substrate inhibition was observed in lamotrigine, cyproheptadine and imipramine glucuronidation by wild-type UGT1A4 but vanished for p.P364L. Imipramine 69-79 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 109-115 35370268-6 2022 Imipramine N-glucuronidation, which is formed mainly by UGT1A4, was also decreased by SWCNTs. Imipramine 0-10 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 56-62 25448279-6 2015 In addition, finasteride strongly inhibited UGT1A4-catalyzed imipramine-N-beta-D-glucuronidation. Imipramine 61-71 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 44-50 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. Imipramine 133-143 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 93-99 20133892-2 2010 The apparent K(m) (S(50)) values for the formation of quaternary N-glucuronides of amitriptyline, imipramine, clomipramine, and trimipramine were 2.60, 16.8, 14.4, and 11.2 microM in UGT2B10 and 448, 262, 112, and 258 microM in UGT1A4, respectively. Imipramine 98-108 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 228-234 20133892-3 2010 The kinetics of amitriptyline and imipramine glucuronidation in human liver microsomes exhibited a biphasic character, where the high- and low-affinity components were in good agreement with our results in expressed UGT2B10 and UGT1A4, respectively. Imipramine 34-44 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 228-234 20133892-5 2010 The in vitro clearances (CL(int) or CL(max)) were comparable between UGT2B10 and UGT1A4 for glucuronidation of imipramine, clomipramine, and trimipramine, whereas CL(int) of amitriptyline glucuronidation by UGT2B10 was more than 10-fold higher than that by UGT1A4. Imipramine 111-121 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 81-87 16626519-0 2006 Biosynthesis of imipramine glucuronide and characterization of imipramine glucuronidation catalyzed by recombinant UGT1A4. Imipramine 16-26 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 115-121 17620344-2 2007 The substrates specific for UGT1A1 (estradiol and bilirubin), UGT1A4 (imipramine and trifluoperazine), and UGT1A6 (serotonin and diclofenac) were used to determine the effects of the coexpression of the other UGT1A isoforms on the enzymatic activity. Imipramine 70-80 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 62-68 16626519-3 2006 Imipramine N(+)-glucuronide was biosynthesized by incubating imipramine with recombinant UGT1A4 and then purified with solid-phase cartridges. Imipramine 61-71 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 89-95 16626519-7 2006 The values of apparent K(m), K(i), and V(max) for imipramine glucuronidation via UGT1A4 were 1.39+/-0.09 mmol/L, 6.24+/-0.45 mmol/L and 453.81+/-32.12 pmol/min per mg cell homogenate (n=3), respectively. Imipramine 50-60 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 81-87 16626519-8 2006 CONCLUSION: As a specific substrate of UGT1A4, imipramine was used as a convenient method to characterize the activity of recombinant UGT1A4 by using HPLC. Imipramine 47-57 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 39-45 16626519-8 2006 CONCLUSION: As a specific substrate of UGT1A4, imipramine was used as a convenient method to characterize the activity of recombinant UGT1A4 by using HPLC. Imipramine 47-57 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 134-140 16626519-9 2006 Furthermore, the profile of imipramine glucuronidation was evaluated by using recombinant UGT1A4 in vitro. Imipramine 28-38 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 90-96 15470160-13 2005 Trans-3"-hydroxycotinine O-glucuronosyltransferase activity in human liver microsomes was inhibited by imipramine (a substrate of UGT1A4, IC(50) = 55 microM), androstanediol (a substrate of UGT2B15, IC(50) = 169 microM), and propofol (a substrate of UGT1A9, IC(50) = 296 microM). Imipramine 103-113 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 130-136 14570768-15 2003 Both propofol, a UGT1A9 substrate, and imipramine, a UGT1A4 substrate, inhibited the glucuronidation of nicotine and cotinine by human liver microsomes. Imipramine 39-49 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 53-59 12019188-8 2002 The activity in UGT1A4 Supersomes was higher than that in recombinant UGT1A4 expressed in human B-lymphoblastoid cells at all imipramine concentration tested. Imipramine 126-136 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 16-22 12019188-8 2002 The activity in UGT1A4 Supersomes was higher than that in recombinant UGT1A4 expressed in human B-lymphoblastoid cells at all imipramine concentration tested. Imipramine 126-136 UDP glucuronosyltransferase family 1 member A4 Homo sapiens 70-76