PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28238899-3 2017 Montelukast and ketoconazole showed a potent and concentration-dependent inhibition of CYP2C8-mediated paclitaxel 6alpha-hydroxylation and CYP3A4-mediated triazolam alpha-hydroxylation, respectively, without dependence on the buffer condition. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 87-93 29870591-0 2018 Amenamevir: Studies of Potential CYP2C8- and CYP2B6-Mediated Pharmacokinetic Interactions With Montelukast and Bupropion in Healthy Volunteers. montelukast 95-106 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 33-39 29171020-0 2018 Clopidogrel but Not Prasugrel Significantly Inhibits the CYP2C8-Mediated Metabolism of Montelukast in Humans. montelukast 87-98 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 57-63 29171020-1 2018 The oxidation of montelukast is mainly mediated by cytochrome P450 (CYP) 2C8, but other mechanisms may contribute to its disposition. montelukast 17-28 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 51-76 28940478-5 2018 In addition, a candidate gene analysis suggested that CYP2C8 and ABCC9 SNVs also affect the AUC0- of montelukast. montelukast 102-113 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 54-60 30117405-7 2018 CYP2C8 was inhibited by montelukast, montelukast sulfoxide, montelukast sulfone, tribendazole, triclabendazole sulfoxide, and triclabendazole sulfone with IC50 of 0.08 microM, 0.05 microM, 0.02 microM, 3.31 microM, 8.95 microM, and 1.05 microM, respectively. montelukast 24-35 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 0-6 27648490-1 2017 Montelukast, a leukotriene receptor antagonist commonly prescribed for treatment of asthma, is primarily metabolized by cytochrome P450 (CYP)2C8, and has been suggested as a probe substrate for investigating CYP2C8 activity in vivo. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 120-144 27599706-4 2017 METHODS: This study predicted the magnitude of the DDI between efavirenz, an inducer of CYP3A4 and inhibitor of CYP2C8, and dual CYP3A4/CYP2C8 substrates (repaglinide, montelukast, pioglitazone, paclitaxel) using a physiologically based pharmacokinetic (PBPK) modeling approach integrating concurrent effects on CYPs. montelukast 168-179 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 136-142 27648490-1 2017 Montelukast, a leukotriene receptor antagonist commonly prescribed for treatment of asthma, is primarily metabolized by cytochrome P450 (CYP)2C8, and has been suggested as a probe substrate for investigating CYP2C8 activity in vivo. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 208-214 27648490-5 2017 Clinical DDIs of montelukast were evaluated using physiologically based pharmacokinetic modeling; and simulation of the interactions with gemfibrozil-CYP2C8 and OATP1B1/1B3 inhibitor, clarithromycin-CYP3A and OATP1B1/1B3 inhibitor, and itraconazole-CYP3A inhibitor, implicated OATPs-CYP2C8-CYP2C8 interplay as the primary determinant of montelukast pharmacokinetics. montelukast 17-28 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 283-289 27648490-5 2017 Clinical DDIs of montelukast were evaluated using physiologically based pharmacokinetic modeling; and simulation of the interactions with gemfibrozil-CYP2C8 and OATP1B1/1B3 inhibitor, clarithromycin-CYP3A and OATP1B1/1B3 inhibitor, and itraconazole-CYP3A inhibitor, implicated OATPs-CYP2C8-CYP2C8 interplay as the primary determinant of montelukast pharmacokinetics. montelukast 17-28 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 283-289 26374173-1 2015 Montelukast has been recommended as a selective in vitro and in vivo probe of cytochrome P450 (P450) CYP2C8 activity, but its selectivity toward this enzyme remains unclear. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 101-107 26721703-3 2016 CYP2C8 substrate drugs include amodiaquine, cerivastatin, dasabuvir, enzalutamide, imatinib, loperamide, montelukast, paclitaxel, pioglitazone, repaglinide, and rosiglitazone, and the number is increasing. montelukast 105-116 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 0-6 26581561-4 2016 Amodiaquine, montelukast, quercetin and rosiglitazone, known as substrates or competitive inhibitors of human CYP2C8, were metabolically depleted by recombinant monkey CYP2C8 at relatively high rates. montelukast 13-24 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 110-116 26581561-4 2016 Amodiaquine, montelukast, quercetin and rosiglitazone, known as substrates or competitive inhibitors of human CYP2C8, were metabolically depleted by recombinant monkey CYP2C8 at relatively high rates. montelukast 13-24 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 168-174 26581561-5 2016 Taken together with our reported findings of the slow eliminations of amodiaquine and montelukast by monkey CYP2C9, CYP2C19 and CYP2C76, the present results suggest that these at least four chemicals may be good marker substrates for monkey CYP2C8. montelukast 86-97 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 241-247 26374173-3 2015 Kinetic and inhibition experiments performed at therapeutically relevant concentrations reveal that CYP2C8 and CYP2C9 are the principal enzymes responsible for montelukast 36-hydroxylation to 1,2-diol. montelukast 160-171 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 100-106 26374173-10 2015 The utility of montelukast as a probe of CYP2C8 activity may be compromised owing to involvement of multiple P450s and UGT1A3 in its metabolism. montelukast 15-26 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 41-47 21838784-9 2012 CONCLUSIONS: CYP2C8 is the dominant enzyme in the biotransformation of montelukast in humans, accounting for about 80% of its metabolism. montelukast 71-82 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 13-19 25595597-6 2015 Other inhibitors of CYP2C8 (gemfibrozil, montelukast, clopidogrel glucuronide, repaglinide, and cerivastatin) also caused extensive inhibition of 3-hydroxydesloratadine formation (73%-100%). montelukast 41-52 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 20-26 24523125-1 2014 Predicting the drug interaction potential for inhibition of CYP2C8 by montelukast. montelukast 70-81 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 60-66 21838784-0 2012 CYP2C8 but not CYP3A4 is important in the pharmacokinetics of montelukast. montelukast 62-73 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 0-6 21838784-3 2012 Our aim was to study the effects of selective CYP2C8 and CYP3A4 inhibitors on the pharmacokinetics of montelukast. montelukast 102-113 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 46-52 21838784-5 2012 Plasma concentrations of montelukast, gemfibrozil, itraconazole and their metabolites were measured up to 72 h. RESULTS: The CYP2C8 inhibitor gemfibrozil increased the AUC(0, ) of montelukast 4.3-fold and its t(1/2) 2.1-fold (P < 0.001). montelukast 25-36 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 125-131 21838784-5 2012 Plasma concentrations of montelukast, gemfibrozil, itraconazole and their metabolites were measured up to 72 h. RESULTS: The CYP2C8 inhibitor gemfibrozil increased the AUC(0, ) of montelukast 4.3-fold and its t(1/2) 2.1-fold (P < 0.001). montelukast 180-191 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 125-131 21838784-11 2012 Montelukast may serve as a safe and useful CYP2C8 probe drug. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 43-49 21289076-6 2011 The CYP2C8 inhibitors gemfibrozil 1-O-beta glucuronide and trimethoprim inhibited the depletion of 0.02 muM montelukast and formation of M6 from 0.05 muM montelukast more potently than did the CYP2C9 inhibitor sulfaphenazole. montelukast 108-119 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 4-10 21289076-0 2011 Reevaluation of the microsomal metabolism of montelukast: major contribution by CYP2C8 at clinically relevant concentrations. montelukast 45-56 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 80-86 21289076-2 2011 However, montelukast is a selective competitive CYP2C8 inhibitor, and our recent in vivo studies suggest that CYP2C8 is involved in its metabolism. montelukast 9-20 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 48-54 21289076-2 2011 However, montelukast is a selective competitive CYP2C8 inhibitor, and our recent in vivo studies suggest that CYP2C8 is involved in its metabolism. montelukast 9-20 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 110-116 21289076-6 2011 The CYP2C8 inhibitors gemfibrozil 1-O-beta glucuronide and trimethoprim inhibited the depletion of 0.02 muM montelukast and formation of M6 from 0.05 muM montelukast more potently than did the CYP2C9 inhibitor sulfaphenazole. montelukast 154-165 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 4-10 21289076-7 2011 Likewise, recombinant CYP2C8 catalyzed montelukast depletion and M6 formation at a 6 times higher intrinsic clearance than did CYP2C9, whereas other P450 isoforms produced no M6. montelukast 39-50 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 22-28 21289076-8 2011 On the basis of depletion of 0.02 muM montelukast, CYP2C8 was estimated to account for 72% of the oxidative metabolism of montelukast in vivo, with a 16% contribution for CYP3A4 and 12% for CYP2C9. montelukast 38-49 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 51-57 21289076-8 2011 On the basis of depletion of 0.02 muM montelukast, CYP2C8 was estimated to account for 72% of the oxidative metabolism of montelukast in vivo, with a 16% contribution for CYP3A4 and 12% for CYP2C9. montelukast 122-133 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 51-57 21289076-10 2011 In conclusion, CYP2C8 plays a major role in the main metabolic pathway of montelukast at clinically relevant montelukast concentrations in vitro. montelukast 74-85 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 15-21 21289076-10 2011 In conclusion, CYP2C8 plays a major role in the main metabolic pathway of montelukast at clinically relevant montelukast concentrations in vitro. montelukast 109-120 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 15-21 20931329-1 2011 PURPOSE: Gemfibrozil, a strong inhibitor of cytochrome P450 (CYP) 2C8 in vivo, was recently found to markedly increase the plasma concentrations of montelukast in humans. montelukast 148-159 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 44-69 20931329-2 2011 Like montelukast, zafirlukast is a substrate of CYP2C9 and CYP3A4 and a potent inhibitor of CYP2C8 in vitro. montelukast 5-16 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 92-98 18787056-6 2008 In contrast, less inhibition was observed with montelukast (CYP2C8 inhibitor, < or =35%) and anti-CYP2C8 mAbs (< or =24%) at all concentrations of IBU. montelukast 47-58 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 60-66 16981900-0 2007 Effect of multiple doses of montelukast on the pharmacokinetics of rosiglitazone, a CYP2C8 substrate, in humans. montelukast 28-39 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 84-90 16981900-1 2007 AIMS: To investigate the effect of multiple dosing with montelukast, a selective leukotriene-receptor antagonist, on the pharmacokinetics of rosiglitazone, a CYP2C8 substrate, in humans. montelukast 56-67 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 158-164 16981900-7 2007 CONCLUSIONS: Multiple doses of montelukast do not inhibit CYP2C8-mediated rosiglitazone metabolism in vivo despite in vitro findings indicating that montelukast is a selective CYP2C8 inhibitor. montelukast 149-160 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 176-182 16670899-2 2006 The leukotriene receptor antagonists montelukast and zafirlukast have potently inhibited CYP2C8 activity and the metabolism of pioglitazone in vitro. montelukast 37-48 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 89-95 16513447-3 2006 Montelukast, an antiasthmatic drug, is a potent inhibitor of CYP2C8 in vitro. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 61-67 20592724-0 2010 Gemfibrozil markedly increases the plasma concentrations of montelukast: a previously unrecognized role for CYP2C8 in the metabolism of montelukast. montelukast 60-71 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 108-114 20592724-0 2010 Gemfibrozil markedly increases the plasma concentrations of montelukast: a previously unrecognized role for CYP2C8 in the metabolism of montelukast. montelukast 136-147 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 108-114 20592724-2 2010 In order to study the significance of CYP2C8 in the pharmacokinetics of montelukast, 10 healthy subjects were administered gemfibrozil 600 mg or placebo twice daily for 3 days, and 10 mg montelukast on day 3, in a randomized, crossover study. montelukast 72-83 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 38-44 20592724-6 2010 In conclusion, gemfibrozil markedly increases the plasma concentrations of montelukast, indicating that CYP2C8 is crucial in the elimination of montelukast. montelukast 75-86 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 104-110 20592724-6 2010 In conclusion, gemfibrozil markedly increases the plasma concentrations of montelukast, indicating that CYP2C8 is crucial in the elimination of montelukast. montelukast 144-155 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 104-110 18413310-0 2008 Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cis-retinoic acid. montelukast 84-95 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 16-35 15608135-0 2005 Selective inhibition of human cytochrome P4502C8 by montelukast. montelukast 52-63 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 30-48 15608135-1 2005 The leukotriene receptor antagonist montelukast was examined for its inhibition of the human drug-metabolizing enzyme cytochrome P4502C8 (CYP2C8). montelukast 36-47 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 118-136 15608135-1 2005 The leukotriene receptor antagonist montelukast was examined for its inhibition of the human drug-metabolizing enzyme cytochrome P4502C8 (CYP2C8). montelukast 36-47 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 138-144 15608135-2 2005 Montelukast was demonstrated to be a potent inhibitor of CYP2C8-catalyzed amodiaquine N-deethylase, rosiglitazone N-demethylase, and paclitaxel 6alpha-hydroxylase in human liver microsomes. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 57-63 15608135-8 2005 Montelukast was a selective inhibitor for human CYP2C8; inhibition of other human cytochrome P450 enzymes was substantially less. montelukast 0-11 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 48-54 15608135-9 2005 These in vitro data support the use of montelukast as a selective CYP2C8 inhibitor that could be used to determine the contribution of this enzyme to drug metabolism reactions. montelukast 39-50 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 66-72 15608135-10 2005 These data also raise the possibility that montelukast could have an effect on the metabolic clearance of drugs possessing CYP2C8-catalyzed metabolism as a major clearance pathway, thereby eliciting pharmacokinetic drug-drug interactions. montelukast 43-54 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 123-129 34272712-0 2021 Case Study 5: Predicting the Drug Interaction Potential for Inhibition of CYP2C8 by Montelukast. montelukast 84-95 cytochrome P450 family 2 subfamily C member 8 Homo sapiens 74-80