PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3435455-5 1987 At higher concentrations of alcohol (25-30 mM), rates of ethanol uptake were about 80 mumol/h per g, whereas rates of butanol uptake were only about 9 mumol/h per g. Because rates of butanol metabolism via cytochrome P-450 in deermice were more than an order of magnitude lower than rates of ethanol uptake in livers from ADH-negative deermice, it is concluded that ethanol uptake by perfused livers from ADH-negative deermice is catalysed predominantly via catalase-H2O2. Ethanol 292-299 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 206-222 3435455-5 1987 At higher concentrations of alcohol (25-30 mM), rates of ethanol uptake were about 80 mumol/h per g, whereas rates of butanol uptake were only about 9 mumol/h per g. Because rates of butanol metabolism via cytochrome P-450 in deermice were more than an order of magnitude lower than rates of ethanol uptake in livers from ADH-negative deermice, it is concluded that ethanol uptake by perfused livers from ADH-negative deermice is catalysed predominantly via catalase-H2O2. Ethanol 292-299 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 206-222 3675576-1 1987 Cytochrome P-450-ALC, an ethanol-oxidizing form of microsomal cytochrome P-450 (P-450), has been purified from human liver. Ethanol 25-32 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 62-78 3632717-1 1987 Immunoblot analysis of liver microsomes from nine patients demonstrated that each contained a cytochrome P-450 that reacted with an antibody directed against the ethanol-inducible rabbit liver cytochrome, P-450 3a. Ethanol 162-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 94-110 3632717-6 1987 However, we conclude that there is a cytochrome P-450 present in human liver which is immunochemically and catalytically similar to the ethanol-inducible P-450 of rabbit liver. Ethanol 136-143 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 37-53 3307484-2 1987 The ADH-independent pathway of ethanol metabolism by neural cells appeared to be dependent on one or more isoenzymes of cytochrome P-450. Ethanol 31-38 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 120-136 3790167-9 1986 Under these conditions, the peroxidatic activity of catalase measured in vitro and the ethanol-dependent decrease in catalase-H2O2 in perfused livers also returned to near basal levels; however, the oxidation of ethanol by cytochrome P-450 was inhibited completely. Ethanol 87-94 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 223-239 3790167-9 1986 Under these conditions, the peroxidatic activity of catalase measured in vitro and the ethanol-dependent decrease in catalase-H2O2 in perfused livers also returned to near basal levels; however, the oxidation of ethanol by cytochrome P-450 was inhibited completely. Ethanol 212-219 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 223-239 3022748-0 1986 Differential effects of the cytochrome P-450/reductase ratio on the oxidation of ethanol and the hydroxyl radical scavenging agent 2-keto-4-thiomethylbutyric acid (KMBA). Ethanol 81-88 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 28-54 3782137-2 1986 The cDNAs encoding ethanol-inducible forms of rat and human cytochrome P-450s have been isolated, sequenced, and used to study the expression of this cytochrome P-450 during development and by various inducing agents. Ethanol 19-26 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 60-76 3022748-2 1986 The effect of various ratios of cytochrome P-450 (phenobarbital-inducible isozyme)/reductase on the oxidation of ethanol and KMBA was determined: There was essentially no increase in KMBA oxidation over the range of ratios from 0.5 to 5 as compared to the reductase-catalyzed rate. Ethanol 113-120 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 32-48 3954830-3 1986 The data suggest that most of the ethanol metabolism by blood-monocyte-derived macrophages is mediated via the cytochrome-P-450-dependent microsomal ethanol-oxidising system. Ethanol 34-41 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-127 3954830-3 1986 The data suggest that most of the ethanol metabolism by blood-monocyte-derived macrophages is mediated via the cytochrome-P-450-dependent microsomal ethanol-oxidising system. Ethanol 149-156 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 111-127 2865858-3 1985 Since ethanol is metabolized via a cytochrome P-450 dependent biotransformation system (MEOS) in hepatic microsomes, the microsomal enzyme induction in the smooth endoplasmic reticulum has to be considered as an adaptive response. Ethanol 6-13 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 35-51 2983957-0 1985 Inhibition of cytochrome P-450-dependent mixed function oxidation by ethanol. Ethanol 69-76 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 14-30 2983957-1 1985 The mechanism of inhibition of cytochrome P-450-dependent mixed function oxidation by ethanol was studied. Ethanol 86-93 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 31-47 2983957-2 1985 Ethanol competitively inhibited the binding of hexobarbital to liver microsomes, and increased the low spin signal of cytochrome P-450 in the electron spin resonance spectra. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 118-134 2983957-3 1985 Therefore, ethanol decreased the substrates bound to ferric cytochrome P-450 in the first step of mixed function oxidation. Ethanol 11-18 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 60-76 2983957-6 1985 Ethanol decreased the rate constants of the fast and slow phases of microsomal cytochrome P-450 reduction. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 79-95 2983957-7 1985 Thus, it is concluded that the inhibition of drug oxidation by ethanol may be due to the displacement of substrates from cytochrome P-450 and to the inhibition of reduction of cytochrome P-450 by NADPH-cytochrome P-450 reductase. Ethanol 63-70 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 2983957-7 1985 Thus, it is concluded that the inhibition of drug oxidation by ethanol may be due to the displacement of substrates from cytochrome P-450 and to the inhibition of reduction of cytochrome P-450 by NADPH-cytochrome P-450 reductase. Ethanol 63-70 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 176-192 6370262-7 1984 When microsomal proteins were separated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, ethanol-fed animals had a distinct band which reflected the increase in microsomal cytochrome P-450 content and seemed to reflect a unique form of cytochrome P-450 induced by ethanol. Ethanol 108-115 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 191-207 6091674-0 1984 Increased microsomal oxidation of ethanol by cytochrome P-450 and hydroxyl radical-dependent pathways after chronic ethanol consumption. Ethanol 34-41 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 45-61 6091674-0 1984 Increased microsomal oxidation of ethanol by cytochrome P-450 and hydroxyl radical-dependent pathways after chronic ethanol consumption. Ethanol 116-123 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 45-61 6725272-2 1984 This laboratory has recently reported that, in a reconstituted enzyme system containing alcohol-induced isozyme 3a of liver microsomal cytochrome P-450, the sum of acetaldehyde generated by the monooxygenation of ethanol and of hydrogen peroxide produced by the NADPH oxidase activity is inadequate to account for the O2 and NADPH consumed. Ethanol 213-220 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 135-151 6370262-7 1984 When microsomal proteins were separated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, ethanol-fed animals had a distinct band which reflected the increase in microsomal cytochrome P-450 content and seemed to reflect a unique form of cytochrome P-450 induced by ethanol. Ethanol 108-115 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 255-271 6370262-8 1984 Thus, despite the absence of the ADH pathway, a large amount of ethanol was metabolized by MEOS in ADH-negative deermice; this was associated with increased blood ethanol elimination rates, enhanced MEOS activity, and quantitative and qualitative changes of cytochrome P-450. Ethanol 64-71 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 258-274 6772704-1 1980 The first step in ethanol metabolism is carried out by two enzyme systems: Alcohol dehydrogenase and cytochrome P-450. Ethanol 18-25 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 101-117 6356158-10 1983 Thus despite absence of ADH, ADH- deermice can consume large amounts of ethanol: this is associated with increased BEC, SER proliferation, enhanced MEOS activity and quantitative and qualitative changes of cytochrome P-450. Ethanol 72-79 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 206-222 16661486-0 1980 Time Course of Induction of Cytochrome P-450, NADPH-Cytochrome c Reductase, and Cinnamic Acid Hydroxylase by Phenobarbital, Ethanol, Herbicides, and Manganese in Higher Plant Microsomes. Ethanol 124-131 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 28-44 7117257-0 1982 The D(V/K) isotope effect of the cytochrome P-450-mediated oxidation of ethanol and its biological applications. Ethanol 72-79 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 33-49 6797432-0 1981 Ethanol-mediated increase in cytochrome P-450 in cultured hepatocytes. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 29-45 7256785-6 1981 The data suggest that chronic ethanol administration may effect the biotransformation enzyme activities by changing the structural properties of the membranes as well as increasing the cytochrome P-450 concentration. Ethanol 30-37 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 185-201 507813-0 1979 Induction by manganese, ethanol, phenobarbital, and herbicides of microsomal cytochrome P-450 in higher plant tissues. Ethanol 24-31 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 77-93 6775511-6 1980 The possible effect of ethanol on these interactions should be considered in evaluating the reported inhibition by high concentrations of ethanol of reactions catalyzed by liver microsomal cytochrome P-450. Ethanol 23-30 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 189-205 6775511-6 1980 The possible effect of ethanol on these interactions should be considered in evaluating the reported inhibition by high concentrations of ethanol of reactions catalyzed by liver microsomal cytochrome P-450. Ethanol 138-145 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 189-205 25763-7 1977 Fluroxene metabolism and toxicity are modified by drugs metabolized by or affecting the activity of the microsomal cytochrome P-450-system or enzymes involved in ethanol metabolism. Ethanol 162-169 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 115-131 552352-8 1979 Ethanol inhibition of drug metabolism in vitro appears to result from a modification of the lipophilic milieu that surrounds the cytochrome P-450 in the microsomal membrane. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 129-145 16661486-2 1980 Although the microsomal hydroxylating complex is already induced by the slicing and aging process, 25 millimolar MnCl(2), 4 millimolar phenobarbital, and 300 millimolar ethanol caused a marked increase of hydroxylase activity and cytochrome P-450 content and shifted their time course. Ethanol 169-176 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 230-246 409715-1 1977 Qualitative and quantitative changes of cytochrome P-450 after chronic ethanol consumption. Ethanol 71-78 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 40-56 32198084-1 2020 Cytochrome P450 (P450) 2E1 is the major P450 enzyme involved in ethanol metabolism. Ethanol 64-71 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-26 191295-5 1977 Based on recent evidence, we conclude that it is unnecessary to postulate that ethanol is oxidized directly via cytochrome P-450. Ethanol 79-86 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 112-128 337820-0 1977 Chronic ethanol administration induces a form of cytochrome P-450 with specific spectral and catalytic properties. Ethanol 8-15 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 49-65 30373287-0 2018 beta-Naphtoflavone and Ethanol Induce Cytochrome P450 and Protect towards MPP+ Toxicity in Human Neuroblastoma SH-SY5Y Cells. Ethanol 23-30 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 38-53 31576541-6 2019 We also review the updated roles of the ethanol-inducible cytochrome P450-2E1 (CYP2E1) and other cytochrome P450 isozymes in the metabolism of various potentially toxic substrates, and consequent toxicities, including carcinogenesis in different tissues. Ethanol 40-47 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 58-73 30373287-4 2018 We have studied the inducibility of CYP isozymes in human neuroblastoma SH-SY5Y cells, treated with beta-naphtoflavone (beta-NF) or ethanol (EtOH) as inducers, by qRT-PCR, Western blot (WB), and metabolic activity assays. Ethanol 132-139 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 36-39 30373287-4 2018 We have studied the inducibility of CYP isozymes in human neuroblastoma SH-SY5Y cells, treated with beta-naphtoflavone (beta-NF) or ethanol (EtOH) as inducers, by qRT-PCR, Western blot (WB), and metabolic activity assays. Ethanol 141-145 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 36-39 24760842-0 2014 Overexpression of the steroidogenic enzyme cytochrome P450 side chain cleavage in the ventral tegmental area increases 3alpha,5alpha-THP and reduces long-term operant ethanol self-administration. Ethanol 167-174 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 43-58 26727525-0 2016 Chronic Effects of Ethanol and/or Darunavir/Ritonavir on U937 Monocytic Cells: Regulation of Cytochrome P450 and Antioxidant Enzymes, Oxidative Stress, and Cytotoxicity. Ethanol 19-26 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 93-108 26727525-4 2016 METHODS: This study examined the chronic effects of EtOH and ART (darunavir/ritonavir), alone and in combination, on expression/levels of cytochrome P450 enzymes (CYPs), antioxidant enzymes (AOEs), reactive oxygen species (ROS), and cytotoxicity in U937 cells. Ethanol 52-56 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 138-153 11996890-9 2002 Since these cells lack the isoenzymatic form of cytochrome P(450) mainly involved in the ethanol metabolism (namely cytochrome P(450)2E1) and also are devoid of alcohol dehydrogenase activity, we propose that the toxic actions of ethanol on liver must be linked to the activity of one or both of these systems. Ethanol 89-96 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 48-65 20606811-2 2010 The cytochrome P(450) isoform (CYP2E1) specifically involved in ethanol oxidation is discussed. Ethanol 64-71 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 4-21 20606811-6 2010 The formation of carbon-centered (1-hydroxyethyl) and oxygen-centered (hydroxyl) radicals during the metabolism of ethanol is considered: the generation of hydroxyethyl radicals, which occurs likely during the process of univalent reduction of dioxygen, is highlighted and is carried out by ferric cytochrome P(450) oxy-complex (P(450)-Fe(3+)O(2) (.-)) formed during the reduction of heme-oxygen. Ethanol 115-122 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 298-315 17084997-0 2006 Ethanol oxidation into acetaldehyde by 16 recombinant human cytochrome P450 isoforms: role of CYP2C isoforms in human liver microsomes. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 60-75 22126492-2 2011 Many CYP enzymes function in the liver, but presence of CYP2E1 in the brain is demonstrating its role in both nicotine and ethanol metabolism. Ethanol 123-130 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 5-8 16713055-6 2006 These observations suggest that NOS2 can behave similarly to cytochrome P-450 in the catalysis of acetaldehyde formation from ethanol via the generation of alpha-hydroxyethyl radical when L-arginine is present. Ethanol 126-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 61-77 11996890-9 2002 Since these cells lack the isoenzymatic form of cytochrome P(450) mainly involved in the ethanol metabolism (namely cytochrome P(450)2E1) and also are devoid of alcohol dehydrogenase activity, we propose that the toxic actions of ethanol on liver must be linked to the activity of one or both of these systems. Ethanol 230-237 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 48-65 9591923-3 1998 Ethanol is consumed worldwide in tremendous amounts and is an effective inducer of hepatic drug metabolism, especially involving pathways accomplished by the CYP2E1 isoform of the cytochrome P-450 (CYP) superfamily. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 158-161 10498654-4 1999 Ethanol feeding increased the hepatic content of all CYP forms. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 53-56 10498654-7 1999 In the noncastrated ethanol-fed micropigs a low expression of each CYP form was associated with scant evidence of aldehyde-protein adducts. Ethanol 20-27 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 67-70 9844795-0 1998 Alcohol-associated rhabdomyolysis: ethanol induction of cytochrome P450 may potentiate myotoxicity. Ethanol 35-42 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 56-71 9844795-2 1998 Ethanol is a potent inducer of cytochrome P450. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 31-46 9844795-4 1998 Accordingly, some alcohol-associated myotoxicity could be related to skeletal muscle cytochrome P450 induction by ethanol leading to the production of toxic metabolites of other compounds that then injure muscle. Ethanol 114-121 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 85-100 9844795-5 1998 The recent identification and localization of cytochrome P450 on skeletal muscle sarcoplasmic reticulum provides supportive evidence for this potential role of ethanol in the pathogenesis of alcohol-associated rhabdomyolysis. Ethanol 160-167 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 46-61 11055180-4 2000 These are: microsomal ethanol oxidation system (MEOS) connected with cytochrome P-450 and peroxisome catalase system. Ethanol 22-29 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 69-85 9591923-3 1998 Ethanol is consumed worldwide in tremendous amounts and is an effective inducer of hepatic drug metabolism, especially involving pathways accomplished by the CYP2E1 isoform of the cytochrome P-450 (CYP) superfamily. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 180-196 9493761-17 1998 Examples of human teratogens that are substrates for CYP enzymes include thalidomide, phenytoin, ethanol, and several hormonal agents. Ethanol 97-104 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 53-56 1335218-3 1992 There is a strong positive correlation between the rates of ethanol metabolism and the total cytochrome P-450 levels in the hepatoma cells. Ethanol 60-67 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 93-109 1461639-13 1992 Chronic ethanol consumption results also in the microsomal induction of a specific ethanol-inducible form of cytochrome P--450, the cytochrome P--450IIE1 with high affinity not only to ethanol but also to some drugs (acetaminophen), procarcinogens (nitrosamines) and industrial agents (carbon tetrachloride). Ethanol 8-15 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 109-126 1461639-13 1992 Chronic ethanol consumption results also in the microsomal induction of a specific ethanol-inducible form of cytochrome P--450, the cytochrome P--450IIE1 with high affinity not only to ethanol but also to some drugs (acetaminophen), procarcinogens (nitrosamines) and industrial agents (carbon tetrachloride). Ethanol 83-90 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 109-126 1461639-13 1992 Chronic ethanol consumption results also in the microsomal induction of a specific ethanol-inducible form of cytochrome P--450, the cytochrome P--450IIE1 with high affinity not only to ethanol but also to some drugs (acetaminophen), procarcinogens (nitrosamines) and industrial agents (carbon tetrachloride). Ethanol 83-90 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 109-126 8307581-1 1993 Human CYP2E encodes an ethanol-inducible cytochrome P450 monooxygenase that metabolizes various carcinogens and may therefore play a role in cancer susceptibility. Ethanol 23-30 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 41-56 1335218-4 1992 The involvement of the cytochrome P-450 system was further supported by the induction of aniline p-hydroxylase activity after ethanol treatment. Ethanol 126-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 23-39 1488918-12 1992 Stabilization of cytochrome P-450 protein and/or mRNA are the main processes of induction by PCN/glucocorticoids and ethanol-type inducers. Ethanol 117-124 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-33 1669007-5 1991 These reactions are elevated after chronic ethanol consumption, due in part, to induction of a unique isozyme of cytochrome P-450. Ethanol 43-50 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 113-129 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 28-35 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 110-126 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 28-35 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 167-183 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 110-126 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 167-183 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 110-126 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 167-183 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 110-126 1770192-4 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving cytochrome P-450: the newly discovered ethanol-inducible cytochrome P-450 (P-450IIE1) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 167-183 1650691-3 1991 Most investigations on this topic have focused on two aspects: ethanol"s capacity to induce the cytochrome P-450-dependent microsomal biotransformation system and its interference with at least one DNA repair mechanism. Ethanol 63-70 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 96-112 1354126-2 1992 Cytochrome P-450 was induced in adult hen liver by administering 15% ethanol in drinking water and compared with other inducers such as phenobarbital and beta-naphthoflavone. Ethanol 69-76 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 0-16 1523868-11 1992 The increase in toxicity of heroin and methadone produced by ethanol is concomitant with a 40% increase in cytochrome P-450 levels of the pretreated hepatocytes. Ethanol 61-68 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 107-123 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 28-35 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 179-195 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 179-195 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 28-35 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 179-195 2043050-10 1991 Immunoblotting of the microsomal proteins showed that the protein band induced by acetone in hamster liver, kidney and lung was cross-reactive with antibody raised against ethanol-inducible human liver cytochrome P-450. Ethanol 172-179 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 202-218 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 121-137 16840049-2 1991 It was also determined that ethanol can be oxidized by a microsomal ethanol oxidizing system (MEOS) involving a specific cytochrome P-450; this newly discovered ethanol-inducible cytochrome P-450 (P-450 IIEi) contributes to ethanol metabolism, tolerance, energy wastage (with associated weight loss), and the selective hepatic perivenular toxicity of various xenobiotics. Ethanol 68-75 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 179-195 2375760-2 1990 The purpose of this study was to purify and characterize the forms of cytochrome P-450 induced in chicken liver by acetone or ethanol. Ethanol 126-133 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 70-86 2375760-10 1990 A fourth form of cytochrome P-450 was identified whose N-terminal amino acid sequence and enzymic activities do not correspond to any mammalian cytochromes P-450 reported to be induced by acetone or ethanol. Ethanol 199-206 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 17-33 2181486-2 1990 Ethanol is also oxidized in liver microsomes by an ethanol-inducible cytochrome P-450 (P-450IIE1) which contributes to ethanol metabolism and tolerance, and activates xenobiotics to toxic radicals thereby explaining increased vulnerability of the heavy drinker to industrial solvents, anesthetic agents, commonly prescribed drugs, over-the-counter analgesics, chemical carcinogens and even nutritional factors such as vitamin A. Ethanol 0-7 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 69-85 2181486-2 1990 Ethanol is also oxidized in liver microsomes by an ethanol-inducible cytochrome P-450 (P-450IIE1) which contributes to ethanol metabolism and tolerance, and activates xenobiotics to toxic radicals thereby explaining increased vulnerability of the heavy drinker to industrial solvents, anesthetic agents, commonly prescribed drugs, over-the-counter analgesics, chemical carcinogens and even nutritional factors such as vitamin A. Ethanol 51-58 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 69-85 2181486-2 1990 Ethanol is also oxidized in liver microsomes by an ethanol-inducible cytochrome P-450 (P-450IIE1) which contributes to ethanol metabolism and tolerance, and activates xenobiotics to toxic radicals thereby explaining increased vulnerability of the heavy drinker to industrial solvents, anesthetic agents, commonly prescribed drugs, over-the-counter analgesics, chemical carcinogens and even nutritional factors such as vitamin A. Ethanol 119-126 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 69-85 2703963-6 1989 Of the cytochrome P-450 inducers, 3-methylcholanthrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin, increased the biliary excretion of AA-GS (2.9- and 3.2-fold, respectively) whereas ethanol and isoniazid did not affect it, and pregnenolone-16 alpha-carbonitrile tended to decrease it (43%). Ethanol 179-186 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 7-23 3404442-7 1988 Imidazole was used because it is a potent inducer of cytochrome P-450 isozyme 3a which is also induced by ethanol. Ethanol 106-113 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 53-69 3181604-2 1988 In man and animals, there is an associated rise in microsomal cytochrome P-450, including a specific form (P-450IIEI) with high affinity for ethanol and for the activation of some drugs (i.e. acetaminophen), carcinogens (i.e. N-nitrosodimethylamine) and hepatotoxic agents (i.e. CCl4), thereby contributing to the susceptibility of alcoholics to xenobiotics, including industrial solvents. Ethanol 141-148 cytochrome P450 family 4 subfamily F member 3 Homo sapiens 62-78