PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11124226-6 2001 Potent inhibitors of CYP1A2 were artemisinin, dihydroartemisinin, thiabendazole, primaquine, and niclosamide (K(i) = 0.43, 3.67, 1.54, 0.22, and 2.70 microM, respectively). Thiabendazole 66-79 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 21-27 11124226-9 2001 In addition, our results suggest CYP1A2 inhibition as the mechanism behind the observed thiabendazole/theophylline and primaquine/antipyrine interactions in vivo. Thiabendazole 88-101 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 33-39 10936227-0 2000 Evidence for cytochrome P4501A2-mediated protein covalent binding of thiabendazole and for its passive intestinal transport: use of human and rabbit derived cells. Thiabendazole 69-82 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 13-31 10936227-1 2000 Thiabendazole (TBZ), an anthelmintic and fungicide benzimidazole, was recently demonstrated to be extensively metabolized by cytochrome P450 (CYP) 1A2 in man and rabbit, yielding 5-hydroxythiabendazole (5OH-TBZ), the major metabolite furtherly conjugated, and two minor unidentified metabolites (M1 and M2). Thiabendazole 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 125-150 10936227-1 2000 Thiabendazole (TBZ), an anthelmintic and fungicide benzimidazole, was recently demonstrated to be extensively metabolized by cytochrome P450 (CYP) 1A2 in man and rabbit, yielding 5-hydroxythiabendazole (5OH-TBZ), the major metabolite furtherly conjugated, and two minor unidentified metabolites (M1 and M2). Thiabendazole 15-18 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 125-150 10936227-5 2000 Thus, CYP1A2 is a major isoenzyme involved in the formation of TBZ-derived residues bound to protein. Thiabendazole 63-66 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 6-12 10936227-10 2000 Nevertheless, caution is necessary in the use of TBZ concurrently with other drugs able to regulate CYP1A2, particularly in respect to liver and lung tissues, recognised as sites of covalent-binding. Thiabendazole 49-52 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 100-106 9565779-6 1998 Thus, CYP1A2 is a major isoenzyme involved in thiabendazole 5-hydroxylation. Thiabendazole 46-59 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 6-12 19299526-0 2009 In vitro and in silico identification and characterization of thiabendazole as a mechanism-based inhibitor of CYP1A2 and simulation of possible pharmacokinetic drug-drug interactions. Thiabendazole 62-75 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 110-116 19299526-1 2009 Thiabendazole (TBZ) and its major metabolite 5-hydroxythiabendazole (5OH-TBZ) were screened for potential time-dependent inhibition (TDI) against CYP1A2. Thiabendazole 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 146-152 19299526-1 2009 Thiabendazole (TBZ) and its major metabolite 5-hydroxythiabendazole (5OH-TBZ) were screened for potential time-dependent inhibition (TDI) against CYP1A2. Thiabendazole 15-18 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 146-152 19299526-8 2009 IC(50) shift studies also demonstrated that TBZ was a TDI of CYP1A2. Thiabendazole 44-47 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 61-67 19754423-9 2009 In particular, several therapeutic drugs including antofloxacin, carbamazepine, dihydralazine, furafylline, isoniazid, rofecoxib, clorgyline, thiabendazole, and zileuton are mechanism-based inhibitors of CYP1A2. Thiabendazole 142-155 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 204-210 18570159-4 2008 Treatment of human hepatocytes for 72 h with 2-200 microM TB produced concentration-dependent increases in CYP1A2, CYP2B6 and CYP3A4 mRNA levels, whereas treatment with BHT increased CYP2B6 and CYP3A4 mRNA levels. Thiabendazole 58-60 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 107-113 18570159-5 2008 CYP1A2, CYP2B6 and CYP3A4 mRNA levels were induced around 48-, 21- and 9-fold, respectively, by 200 microM TB, with CYP2B6 and CYP 3A4 mRNA levels being induced around 12- and 7-fold, respectively, by 200 microM BHT. Thiabendazole 107-109 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 0-6 16261361-0 2005 Artemisinin and thiabendazole are potent inhibitors of cytochrome P450 1A2 (CYP1A2) activity in humans. Thiabendazole 16-29 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 55-74 16261361-0 2005 Artemisinin and thiabendazole are potent inhibitors of cytochrome P450 1A2 (CYP1A2) activity in humans. Thiabendazole 16-29 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 76-82 16261361-1 2005 OBJECTIVE: To investigate the likelihood of artemisinin and thiabendazole causing pharmacokinetic interactions involving cytochrome P450 (CYP1A2) in humans given their potent inhibitory effects on the isoform in vitro. Thiabendazole 60-73 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 138-144 16261361-6 2005 RESULTS: Using the ratio of paraxanthine to caffeine after 4 h as an indicator of CYP1A2 activity, thiabendazole and artemisinin inhibited 92 and 66%, respectively, of the enzyme activity in vivo. Thiabendazole 99-112 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 82-88 16261361-10 2005 CONCLUSIONS: Co-administration of thiabendazole or artemisinin with CYP1A2 substrates could result in clinically significant effects. Thiabendazole 34-47 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 68-74