PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28951593-0 2017 MicroRNA regulation of CYP 1A2, CYP3A4 and CYP2E1 expression in acetaminophen toxicity. Acetaminophen 64-77 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 23-30 28963035-0 2017 miRNA-122 Protects Mice and Human Hepatocytes from Acetaminophen Toxicity by Regulating Cytochrome P450 Family 1 Subfamily A Member 2 and Family 2 Subfamily E Member 1 Expression. Acetaminophen 51-64 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 88-133 28951593-7 2017 Collectively, the data suggest that miRNA elevations in APAP toxicity represent a regulatory response to modify CYP1A2, CYP3A4 and CYP2E1 translation due to cellular stress and injury. Acetaminophen 56-60 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 112-118 24119207-7 2014 In this study, uremic serum was found to inhibit the CYP1A2-mediated metabolism of phenacetin to acetaminophen in a concentration-dependent and competitive manner. Acetaminophen 97-110 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 53-59 24732412-4 2014 Of the drugs screened, only the potent CYP1A2 inhibitor 5-methoxypsoralen impaired the 6-melatonin hydroxylation at pharmacologically relevant concentrations, and is likely to lead to clinical interactions; diazepam, tamoxifen and acetaminophen (paracetamol) did not impair the metabolic conversion of melatonin to 6-sulphatoxymelatonin at concentrations attained following therapeutic administration. Acetaminophen 231-244 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 39-45 24732412-4 2014 Of the drugs screened, only the potent CYP1A2 inhibitor 5-methoxypsoralen impaired the 6-melatonin hydroxylation at pharmacologically relevant concentrations, and is likely to lead to clinical interactions; diazepam, tamoxifen and acetaminophen (paracetamol) did not impair the metabolic conversion of melatonin to 6-sulphatoxymelatonin at concentrations attained following therapeutic administration. Acetaminophen 246-257 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 39-45 24498291-6 2014 The calculated binding equilibrium of APAP within the compact active site of CYP2A6 is able to predict the experimentally documented product ratios and is also applied to explain APAP regioselectivity in CYP1A2 and CYP2C9. Acetaminophen 38-42 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 204-210 11130219-4 2000 Because R-warfarin is a weak inhibitor of vitamin K epoxide reductase and is metabolized by cytochrome P450 (CYP) 1A2 and 3A4, it is hypothesized that simultaneous competition with R-warfarin for CYP1A2 and 3A4 is required for drug interactions to be clinically significant with compounds exclusively affecting the R enantiomer, such as acetaminophen. Acetaminophen 337-350 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 92-117 22949628-5 2012 Moreover, despite higher H2O2 production, the coupling efficiency of reducing equivalents to acetaminophen formation in CYP1A2 was tighter than that in CYP1A1. Acetaminophen 93-106 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 120-126 21825116-2 2011 Phenacetin O-deethylation is the preferred probe reaction for CYP1A2, in which the metabolite, acetaminophen, is quantified using liquid chromatography-tandem mass spectrometry. Acetaminophen 95-108 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 62-68 19219744-4 2009 This method was used to determine the bioactivation of acetaminophen at two concentrations: 50 microM therapeutic and 1 mM toxic by using nine human recombinant CYP enzymes: CYP1A1, CYP1A2, CYP2A6, CYP2B6, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4; and with different microsomes from experimental animals. Acetaminophen 55-68 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 182-188 18588957-7 2008 When APAP and LEF were incubated with human recombinant P450 enzymes, CYP1A2 was found to be the isozyme responsible for the inhibition of APAP bioactivation. Acetaminophen 5-9 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 70-76 22305191-4 2012 PSP (1.25-20muM) dose-dependently decreased CYP1A2-mediated metabolism of phenacetin to paracetamol (IC(50) 19.7muM) and CYP3A4-mediated metabolism of testosterone to 6beta-hydroxytestosterone (IC(20) 7.06muM). Acetaminophen 88-99 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 44-50 21111054-6 2011 The assessment of CYP activity was performed with a rapid, sensitive liquid chromatography-tandem mass spectrometry method which simultaneously assessed activity of CYP3A4, CYP2B6, and CYP1A2 in a single 3-min method by examining the formation of the probe substrate metabolites, 1"-hydroxymidazolam, hydroxybupropion, and acetaminophen, respectively. Acetaminophen 323-336 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 185-191 23045133-5 2006 Acetaminophen formation in incubations of phenacetin with a CYP1A2 source is readily measured by HPLC with UV detection. Acetaminophen 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 60-66 11130219-4 2000 Because R-warfarin is a weak inhibitor of vitamin K epoxide reductase and is metabolized by cytochrome P450 (CYP) 1A2 and 3A4, it is hypothesized that simultaneous competition with R-warfarin for CYP1A2 and 3A4 is required for drug interactions to be clinically significant with compounds exclusively affecting the R enantiomer, such as acetaminophen. Acetaminophen 337-350 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 196-202 11130219-5 2000 The discrepant observations in the literature regarding the clinical significance of the acetaminophen-warfarin interaction may be resolved if the hepatic enzyme activity of CYP1A2 and 3A4 is enhanced relative to CYP2E1 and the nonoxidative pathways of glucuronidation and sulfation responsible for acetaminophen metabolism. Acetaminophen 89-102 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 174-180 11130219-5 2000 The discrepant observations in the literature regarding the clinical significance of the acetaminophen-warfarin interaction may be resolved if the hepatic enzyme activity of CYP1A2 and 3A4 is enhanced relative to CYP2E1 and the nonoxidative pathways of glucuronidation and sulfation responsible for acetaminophen metabolism. Acetaminophen 299-312 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 174-180 9110357-7 1997 Acetaminophen use (p = 0.05), coffee consumption (p = 0.05) and plasma lycopene (p = 0.06) were positively associated with CYP1A2 activity. Acetaminophen 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 123-129 10811468-1 2000 Acetaminophen is oxidized by human CYP1A2 to the cytotoxic metabolite N-acetylbenzoquinoneimine (NABQI). Acetaminophen 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 35-41 10811468-2 2000 Incubation of cells transfected with human CYP1A2 (H1A2 MZ cells) with 4-20 mM acetaminophen for 6 hours at 37 degrees C caused extensive cytotoxicity (cell viability <10%). Acetaminophen 79-92 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 43-49 9246016-3 1997 Acetaminophen (INN, paracetamol), a widely used and effective analgesic and antipyretic agent, causes serious hepatic and renal toxicity at high doses by conversion of acetaminophen to the toxic intermediate N-acetyl-p-benzoquinone imine (NAPQI) through CYP1A2, CYP2E1, and CYP3A4. Acetaminophen 20-31 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 254-260 9867310-3 1998 The main probe drugs include caffeine and theophylline, whose metabolism is catalysed by CYP1A2, tolbutamide, phenytoin and ibuprofen, catalysed by CYP2C9, amitriptyline and nortriptyline, catalysed by CYP2C19, acetaminophen, catalysed by CYP2E1 and lidocaine, midazolam and terfenadine, catalysed by 3A3/4. Acetaminophen 211-224 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 89-95 9246016-3 1997 Acetaminophen (INN, paracetamol), a widely used and effective analgesic and antipyretic agent, causes serious hepatic and renal toxicity at high doses by conversion of acetaminophen to the toxic intermediate N-acetyl-p-benzoquinone imine (NAPQI) through CYP1A2, CYP2E1, and CYP3A4. Acetaminophen 0-13 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 254-260 9110357-11 1997 This study confirms an enhancing effect of acetaminophen and coffee on CYP1A2 activity and suggests and inhibitory effect of estrogens, alcohol and food sources of lutein and alpha-tocopherol on this enzyme. Acetaminophen 43-56 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 71-77 8986010-1 1996 Biotransformation of phenacetin via O-deethylation to acetaminophen, an index reaction reflecting activity of Cytochrome P450-1A2, was studied in microsomal preparations from a series of human livers. Acetaminophen 54-67 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 110-129 8861779-0 1996 Paracetamol-induced spindle disturbances in V79 cells with and without expression of human CYP1A2. Acetaminophen 0-11 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 91-97 8861779-6 1996 At 5 mM paracetamol the c-mitosis frequency was 14.4 + or - 5.0% and 19.0 + or - 3.8% in the native and CYP1A2 expressing cell lines, respectively (P<0.05). Acetaminophen 8-19 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 104-110 8563766-2 1995 In addition, CYP1A2 contributes to the inactivation of several common drugs and dietary constituents, including acetaminophen and caffeine. Acetaminophen 112-125 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 13-19 7987405-16 1994 It was significantly correlated to paracetamol glucoronidation in male heavy smokers (r=0.85), suggesting an element of co-regulation of CYP1A2 and of paracetamol conjugating UDP-glucuronosyltransferase isozymes, including UGTI.6. Acetaminophen 35-46 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 137-143 8261468-2 1994 The inhibitory potential of furafylline in vivo was first assessed by determining its effect on clearance of phenacetin to paracetamol by the model CYP1A2-dependent O-deethylation pathway. Acetaminophen 123-134 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 148-154 2351129-2 1990 The data of the present study revealed the ability of various commonly used anti-inflammatory drugs to alter the activity of this enzyme system, where all the tested drugs, namely phenyl butazone, ketoprofen, piroxicam, and acetaminophen, caused an increase in both the activity of aryl hydrocarbon hydroxylase and the cytochrome P450 content whether administered as a single dose or as a repeated dose for 6 consecutive days. Acetaminophen 224-237 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 282-310 35500453-1 2022 BACKGROUND: Acetaminophen is metabolized through a non-toxic sulfation and glucuronidation pathway and toxic oxidation pathway (via CYP2E1 and CYP1A2). Acetaminophen 12-25 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 143-149 31706005-2 2020 We found similar and stable CYP1A2 transcript and protein levels in both cell clones leading to specific enzyme activities of about 370 pmol paracetamol x min-1 x mg-1 protein analyzed by phenacetin conversion. Acetaminophen 141-152 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 28-34 31393259-1 2020 BACKGROUND AND AIM: Hepatic phase I drug metabolizing enzymes CYP2E1, CYP1A2 and CYP3A4 catalyze the biotransformation of acetaminophen (APAP) and are important in the mediation of toxicity. Acetaminophen 122-135 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 70-76 31393259-1 2020 BACKGROUND AND AIM: Hepatic phase I drug metabolizing enzymes CYP2E1, CYP1A2 and CYP3A4 catalyze the biotransformation of acetaminophen (APAP) and are important in the mediation of toxicity. Acetaminophen 137-141 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 70-76