PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 158-165 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 2, subfamily e, polypeptide 1 Rattus norvegicus 290-296 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 2, subfamily a, polypeptide 1 Rattus norvegicus 299-305 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Diazinon 29-37 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 314-320 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 158-165 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 2, subfamily e, polypeptide 1 Rattus norvegicus 290-296 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 2, subfamily a, polypeptide 1 Rattus norvegicus 299-305 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 98-110 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 314-320 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 53-59 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 158-165 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 2, subfamily e, polypeptide 1 Rattus norvegicus 290-296 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 2, subfamily a, polypeptide 1 Rattus norvegicus 299-305 9890448-5 1999 Results indicate that, after diazinon preincubation, CYP3A2-catalyzed reactions (2beta- and 6beta-testosterone hydroxylation) are very efficiently inhibited; CYP2C11- and CYP2B1/2-catalyzed reactions (2alpha- and 16beta-testosterone hydroxylation, respectively) are weakly inhibited, while CYP2E1-, CYP2A1/2-, and CYP1A1/2-related activities were unaffected. Testosterone 220-232 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 314-320 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Diazinon 242-250 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 150-157 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Diazinon 242-250 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Diazinon 242-250 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Phenobarbital 301-314 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 150-157 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Phenobarbital 301-314 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Phenobarbital 301-314 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Dexamethasone 321-334 cytochrome P450, subfamily 2, polypeptide 11 Rattus norvegicus 150-157 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Dexamethasone 321-334 cytochrome P450, family 3, subfamily a, polypeptide 2 Rattus norvegicus 159-165 9890448-6 1999 Results obtained by using chemical inhibitors or antibodies selectively active against specific CYPs provide a direct evidence for the involvement of CYP2C11, CYP3A2, and CYP2B1/2, indicating that each of them contributed about 40-50% of the diazinon metabolism, in hepatic microsomes from untreated, phenobarbital-, and dexamethasone-treated rats, respectively. Dexamethasone 321-334 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 171-177 9890448-7 1999 The higher diazoxon/pyrimidinol ratio observed after phenobarbital-treatment together with the significantly more effective inhibition toward diazoxon production exerted by metyrapone in microsomes from phenobarbital-treated rats supports the conclusion that CYP2B1/2 catalyze preferentially the production of diazoxon. Metyrapone 173-183 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 259-265 9890448-7 1999 The higher diazoxon/pyrimidinol ratio observed after phenobarbital-treatment together with the significantly more effective inhibition toward diazoxon production exerted by metyrapone in microsomes from phenobarbital-treated rats supports the conclusion that CYP2B1/2 catalyze preferentially the production of diazoxon. Phenobarbital 203-216 cytochrome P450, family 2, subfamily b, polypeptide 1 Rattus norvegicus 259-265