PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3442670-4 1987 We have accumulated evidence that autoimmune antibodies observed in sera of patients with tienilic acid induced hepatitis (anti-liver kidney microsome 2 or anti-LKM2 antibodies) specifically recognize the cytochrome P-450 involved in the mephenytoin hydroxylation polymorphism. Mephenytoin 238-249 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 205-221 2827463-3 1988 In the present paper we report the isolation and sequence of a cDNA clone for the human hepatic cytochrome P-450 responsible for mephenytoin (an anticonvulsant) oxidation. Mephenytoin 129-140 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 96-112 3442670-6 1987 The cytochrome P-450 recognized by anti-LKM2 antibodies was immunopurified from microsomes derived from livers of extensive (EM) or poor metabolizers (PM) of (S)-mephenytoin. Mephenytoin 158-173 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 4-20 3442670-9 1987 These data strongly suggest that the mephenytoin hydroxylation deficiency is caused by a minor structural change leading to a functionally altered cytochrome P-450 isozyme. Mephenytoin 37-48 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 147-163 30399481-2 2019 Although CYP2C19 isoform is a minor hepatic CYP, it metabolizes clinically important drugs such as omeprazole and S-mephenytoin. Mephenytoin 114-127 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 9-12 3096378-0 1986 Mephenytoin-type polymorphism of drug oxidation: purification and characterization of a human liver cytochrome P-450 isozyme catalyzing microsomal mephenytoin hydroxylation. Mephenytoin 0-11 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 100-116 3096378-0 1986 Mephenytoin-type polymorphism of drug oxidation: purification and characterization of a human liver cytochrome P-450 isozyme catalyzing microsomal mephenytoin hydroxylation. Mephenytoin 147-158 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 100-116 3096378-2 1986 By monitoring the activities of the two major oxidative pathways of mephenytoin metabolism in the column eluates, we have purified from human livers a cytochrome P-450 isozyme, P-450 meph, which exclusively and stereoselectively catalyzes the 4-hydroxylation of (S)-mephenytoin, the major pathway affected by the polymorphism, whereas P-450 meph was virtually devoid of catalytic activity for N-demethylation of mephenytoin, the pathway remaining unaffected by the genetic deficiency. Mephenytoin 68-79 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 151-167 3096378-2 1986 By monitoring the activities of the two major oxidative pathways of mephenytoin metabolism in the column eluates, we have purified from human livers a cytochrome P-450 isozyme, P-450 meph, which exclusively and stereoselectively catalyzes the 4-hydroxylation of (S)-mephenytoin, the major pathway affected by the polymorphism, whereas P-450 meph was virtually devoid of catalytic activity for N-demethylation of mephenytoin, the pathway remaining unaffected by the genetic deficiency. Mephenytoin 262-277 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 151-167 3096378-2 1986 By monitoring the activities of the two major oxidative pathways of mephenytoin metabolism in the column eluates, we have purified from human livers a cytochrome P-450 isozyme, P-450 meph, which exclusively and stereoselectively catalyzes the 4-hydroxylation of (S)-mephenytoin, the major pathway affected by the polymorphism, whereas P-450 meph was virtually devoid of catalytic activity for N-demethylation of mephenytoin, the pathway remaining unaffected by the genetic deficiency. Mephenytoin 266-277 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 151-167 3709029-10 1986 Moreover, this ratio may be used to detect drug interactions that involve the cytochrome P-450 isozyme(s) responsible for the polymorphic 4-hydroxylation of mephenytoin. Mephenytoin 157-168 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 78-94 2874666-13 1986 A cytochrome P-450 with high activity for mephenytoin 4-hydroxylation was purified from human liver. Mephenytoin 42-53 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 2-18 6697650-2 1984 We used human liver preparations to test whether mephenytoin competes with sparteine for binding to the genetically variable cytochrome P-450, which mediates metabolism of both sparteine and debrisoquine. Mephenytoin 49-60 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 125-141 3598900-1 1987 In vitro investigations suggest the same human liver cytochrome P-450 that catalyzes S-mephenytoin 4-hydroxylation, P-450MP, is responsible for methyl hydroxylation of the oral hypoglycemic agent tolbutamide. Mephenytoin 85-98 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 53-69 3032244-1 1987 A cDNA sequence related to the human cytochrome P-450 responsible for S-mephenytoin 4-hydroxylation (P-450MP) has been isolated from a human liver bacteriophage lambda gt11 library with antibodies specific for P-450MP. Mephenytoin 70-83 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 37-53 2874666-0 1986 The molecular mechanisms of two common polymorphisms of drug oxidation--evidence for functional changes in cytochrome P-450 isozymes catalysing bufuralol and mephenytoin oxidation. Mephenytoin 158-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 107-123 4053486-5 1985 These results support our hypothesis that the mephenytoin polymorphism is caused by a partial or complete absence or inactivity of a cytochrome P-450 isozyme with high affinity for S-mephenytoin. Mephenytoin 46-57 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 133-149 4053486-5 1985 These results support our hypothesis that the mephenytoin polymorphism is caused by a partial or complete absence or inactivity of a cytochrome P-450 isozyme with high affinity for S-mephenytoin. Mephenytoin 181-194 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 133-149 1021219-1 1976 Mephenytoin, diphenylhydantoin, pheneturide, and phenobarbital produced a concentration-dependent inhibition in the binding of hexobarbital to cytochrome P-450 at the type 1 site, while sulthiame slightly potentiated, and ethosuximide did not affect the binding characteristic of hexobarbital. Mephenytoin 0-11 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 143-159 21198441-2 2011 The specific CYP substrates used in this cocktail assay included phenacetin (CYP1A2), bupropion (CYP2B6), amodiaquine (CYP2C8), tolbutamide (CYP2C9), S-mephenytoin (CYP2C19), dextromethorphan (CYP2D6), and midazolam (CYP3A4/5). Mephenytoin 150-163 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 13-16 22765278-3 2013 METHODS: Fourteen healthy, male volunteers aged 18 to 45 years were recruited into an open label, two period, single centre study in which CYP enzyme activity was measured by administration of the selectively metabolized probe drugs theophylline (CYP1A2), tolbutamide (CYP2C9), mephenytoin (CYP2C19), debrisoquine (CYP2D6) and dapsone (CYP3A4) on day 1 of the study. Mephenytoin 278-289 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 139-142 8861658-4 1996 Dextromethorphan, debrisoquine and sparteine are good substrates for CYP2D6, whereas the S-enantiomer of mephenytoin is a good substrate for CYP2C19, both being two isozymes of cytochrome P-450. Mephenytoin 105-116 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 177-193 11037108-5 2000 Human CYP probe substrates used for characterization of mouse CYP activities included bufuralol, testosterone, dextromethorphan, phenacetin, diclofenac and S-mephenytoin. Mephenytoin 156-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 6-9 11037108-5 2000 Human CYP probe substrates used for characterization of mouse CYP activities included bufuralol, testosterone, dextromethorphan, phenacetin, diclofenac and S-mephenytoin. Mephenytoin 156-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 62-65 9190854-0 1997 Reappraisal of human CYP isoforms involved in imipramine N-demethylation and 2-hydroxylation: a study using microsomes obtained from putative extensive and poor metabolizers of S-mephenytoin and eleven recombinant human CYPs. Mephenytoin 177-190 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 21-24 9190854-1 1997 Cytochrome P450 (CYP) involved in the two major pathways of imipramine (IMI) was reappraised using human liver microsomes phenotyped for S-mephenytoin 4"-hydroxylation in vitro and 11 recombinant human CYP isoforms. Mephenytoin 137-150 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-15 9190854-1 1997 Cytochrome P450 (CYP) involved in the two major pathways of imipramine (IMI) was reappraised using human liver microsomes phenotyped for S-mephenytoin 4"-hydroxylation in vitro and 11 recombinant human CYP isoforms. Mephenytoin 137-150 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-20 11956503-4 2002 CYP enzyme activities were measured by means of the metabolic ratios of sparteine (CYP2D6), endogenous cortisol metabolism (CYP3A4), and caffeine (CYP1A2), as well as by the S/R ratio of mephenytoin (CYP2C19) and antipyrine clearance. Mephenytoin 187-198 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-3 7704038-1 1994 Metabolism of diazepam was studied in vitro to identify the forms of cytochrome P450 (CYP) responsible for N-demethylation (nordazepam formation) and 3-hydroxylation (temazepam formation), using liver microsomes obtained from extensive (EM) and poor metabolizers (PM) for S-mephenytoin 4"-hydroxylation. Mephenytoin 272-285 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 69-84 7704038-1 1994 Metabolism of diazepam was studied in vitro to identify the forms of cytochrome P450 (CYP) responsible for N-demethylation (nordazepam formation) and 3-hydroxylation (temazepam formation), using liver microsomes obtained from extensive (EM) and poor metabolizers (PM) for S-mephenytoin 4"-hydroxylation. Mephenytoin 272-285 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 86-89 1857342-1 1991 Purification and immunoinhibition studies have suggested that the hydroxylations of (S)-mephenytoin and tolbutamide are catalyzed by rather similar forms of human liver cytochrome P-450 (P-450). Mephenytoin 84-99 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 169-185 8454228-2 1993 Debrisoquine/sparteine and mephenytoin polymorphisms are now known to be derived from defects in the human liver of specific forms of microsomal CYP (P450 or previously termed cytochrome P-450), CYP2D6 and CYP2C9 (2C18), respectively. Mephenytoin 27-38 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 145-148 8454228-2 1993 Debrisoquine/sparteine and mephenytoin polymorphisms are now known to be derived from defects in the human liver of specific forms of microsomal CYP (P450 or previously termed cytochrome P-450), CYP2D6 and CYP2C9 (2C18), respectively. Mephenytoin 27-38 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 176-192 1441599-0 1992 Polymorphism in stereoselective hydroxylations of mephenytoin and hexobarbital by Japanese liver samples in relation to cytochrome P-450 human-2 (IIC9). Mephenytoin 50-61 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 120-136 1441599-16 1992 These findings indicate that P-450 human-2 is the major cytochrome P-450 responsible for the polymorphisms in stereoselective hydroxylations of mephenytoin and hexobarbital. Mephenytoin 144-155 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-72 2910639-1 1989 The relative contributions of the debrisoquin and mephenytoin isozymes of hepatic cytochrome P-450 to the stereoselective metabolism of propranolol have been studied in a panel of volunteers of known oxidative phenotypes. Mephenytoin 50-61 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 82-98 2669966-1 1989 The human liver cytochrome P-450 (P-450) proteins responsible for catalyzing the oxidation of mephenytoin, tolbutamide, and hexobarbital are encoded by a multigene family (CYP2C). Mephenytoin 94-105 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 16-32 3196692-1 1988 A cytochrome P-450 (P-450) multigene family codes for several related human liver enzymes, including the P-450 responsible for (S)-mephenytoin 4"-hydroxylation. Mephenytoin 127-142 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 2-18