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1. Full Text Structures of human cytochrome P-450 2E1: Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates
by Porubsky, Patrick R and Meneely, Kathleen M and Scott, Emily E
Journal of Biological Chemistry, ISSN 0021-9258, 11/2008, Volume 283, Issue 48, pp. 33698 - 33707
Human microsomal cytochrome P-450 2E1 (CYP2E1) monooxygenates > 70 low molecular weight xenobiotic compounds, as well as much larger endogenous fatty acid... 
OBESE OVERFED RAT | MACROMOLECULAR STRUCTURES | BACULOVIRUS EXPRESSION | CATALYTIC-PROPERTIES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACETAMINOPHEN ACTIVATION | ESCHERICHIA-COLI | P450 2E1 | LIVER-MICROSOMES | SITE-DIRECTED MUTAGENESIS | HALOTHANE HEPATITIS | Acetaminophen - adverse effects | Arachidonic Acid - metabolism | Heme - metabolism | Cytochrome P-450 CYP2E1 Inhibitors | Enzyme Inhibitors - metabolism | Nitrosamines - metabolism | Humans | Imidazoles - chemistry | Models, Molecular | Cytochrome P-450 CYP2E1 - metabolism | Hydroxylation - physiology | Carcinogens - metabolism | Smoking - metabolism | Heme - chemistry | Hydrogen Bonding | Analgesics, Non-Narcotic - adverse effects | Enzyme Inhibitors - chemistry | Hydrophobic and Hydrophilic Interactions | Protein Structure, Secondary - physiology | Xenobiotics - metabolism | Cytochrome P-450 CYP2E1 - chemistry | Imidazoles - metabolism | Index Medicus
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2. Full Text Hepatic Cytochrome P450 Enzyme Alterations in Humans with Progressive Stages of Nonalcoholic Fatty Liver Disease
by Craig D. Fisher and Andrew J. Lickteig and Lisa M. Augustine and James Ranger-Moore and Jonathan P. Jackson and Stephen S. Ferguson and Nathan J. Cherrington
Drug Metabolism and Disposition, ISSN 0090-9556, 10/2009, Volume 37, Issue 10, pp. 2087 - 2094
Members of the cytochrome P450 (P450) enzyme families CYP1, CYP2, and CYP3 are responsible for the metabolism of approximately 75% of all clinically relevant... 
NOMENCLATURE | CIRRHOSIS | GENE-EXPRESSION | CAFFEINE | SUPERFAMILY | PHARMACOLOGY & PHARMACY | STEATOHEPATITIS | PREVALENCE | INDUCTION | HYPOXIA | DRUG-METABOLISM | Cytochrome P-450 CYP2C9 | Fatty Liver - genetics | Cytochrome P-450 CYP2D6 - genetics | Oxidoreductases, N-Demethylating - genetics | Fatty Liver - metabolism | Fatty Liver - pathology | Humans | Aryl Hydrocarbon Hydroxylases - genetics | Cytochrome P-450 Enzyme System - metabolism | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | RNA, Messenger - metabolism | Cytochrome P-450 CYP1A2 - metabolism | Disease Progression | Aryl Hydrocarbon Hydroxylases - metabolism | Cytochrome P-450 CYP3A - genetics | Cytochrome P-450 CYP2C19 | Cytochrome P-450 CYP1A2 - genetics | Fatty Liver - enzymology | Cytochrome P-450 CYP2D6 - metabolism | Cytochrome P-450 Enzyme System - genetics | Microsomes, Liver - enzymology | Oxidoreductases, N-Demethylating - metabolism | Cytochrome P-450 CYP2B6
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3. Full Text Differences in the epigenetic regulation of cytochrome P450 genes between human embryonic stem cell-derived hepatocytes and primary hepatocytes
by Park, Han-Jin and Choi, Young-Jun and Kim, Ji Woo and Chun, Hang-Suk and Im, Ilkyun and Yoon, Seokjoo and Han, Yong-Mahn and Song, Chang-Woo and Kim, Hyemin
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, pp. e0132992 - e0132992
Human pluripotent stem cell-derived hepatocytes have the potential to provide in vitro model systems for drug discovery and hepatotoxicity testing. However,... 
DNA METHYLATION | HUMAN LUNG | QUANTIFICATION | MULTIDISCIPLINARY SCIENCES | PLACENTA | HUMAN LIVER | HUMAN CYP1A1 | MECHANISMS | CYP2E1 | DIFFERENTIATION | EXPRESSION | Chromatin - metabolism | Cytochrome P-450 CYP1A1 - genetics | Cytochrome P-450 CYP1B1 - genetics | Epigenesis, Genetic | Human Embryonic Stem Cells - cytology | Humans | Cytochrome P-450 CYP1B1 - metabolism | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | Hepatocytes - metabolism | DNA Methylation | Hepatocytes - cytology | Cytochrome P-450 CYP1A2 - genetics | Transcription, Genetic | Cell Differentiation | Chromatin - ultrastructure | Cell Line | Cytochrome P-450 CYP2D6 - genetics | Human Embryonic Stem Cells - metabolism | DNA Modification Methylases - metabolism | Histone Deacetylases - genetics | Signal Transduction | Histone Deacetylases - metabolism | Cytochrome P-450 CYP1A1 - metabolism | Organ Specificity | Cytochrome P-450 CYP1A2 - metabolism | DNA Modification Methylases - genetics | Histones - genetics | CpG Islands | Cytochrome P-450 CYP2D6 - metabolism | Protein Processing, Post-Translational | Histones - metabolism | Primary Cell Culture | Epigenetic inheritance | Methylation | Embryonic stem cells | Genes | Cytochrome P-450 | Cytochrome | Chromatin | Transcription | Toxicity | Gene regulation | Liver | Science | Demethylation | Rodents | Toxicity testing | DNA methylation | Inhibition | Hepatotoxicity | CYP2D6 protein | Deoxyribonucleic acid--DNA | CpG islands | Enzymes | Cytochrome P450 | CYP1A2 protein | Gene expression | Hepatocytes | Stem cells | Pluripotency | Combinatorial analysis | Index Medicus | Deoxyribonucleic acid | DNA
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4. Full Text CYP2E1 potentiates binge alcohol-induced gut leakiness, steatohepatitis, and apoptosis
by Abdelmegeed, Mohamed A and Banerjee, Atrayee and Jang, Sehwan and Yoo, Seong-Ho and Yun, Jun-Won and Gonzalez, Frank J and Keshavarzian, Ali and Song, Byoung-Joon
Free Radical Biology and Medicine, ISSN 0891-5849, 12/2013, Volume 65, pp. 1238 - 1245
Ethanol-inducible cytochrome P450 2E1 (CYP2E1) contributes to increased oxidative stress and steatosis in chronic alcohol-exposure models. However, its role in... 
Oxidative stress | Binge ethanol | Free radicals | Liver | Steatohepatitis | Gut leakiness | CYP2E1 | Apoptosis | ACTIVATION | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYTOCHROME P4502E1 | INDUCED LIVER-INJURY | STEATOSIS | ENDOCRINOLOGY & METABOLISM | INDUCED FATTY LIVER | MITOCHONDRIAL DYSFUNCTION | ETHANOL | MICE | STRESS | Endotoxins - blood | Liver - pathology | Intestines - pathology | Signal Transduction | Apoptosis - drug effects | Fatty Liver - pathology | Liver - microbiology | Male | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | Binge Drinking - genetics | Mice, Knockout | Ethanol - pharmacology | Animals | Intestines - microbiology | Female | Mice | Oxidative Stress - drug effects | Endotoxemia | Lipid Metabolism - physiology | Cytokines - blood | Enterobacteriaceae | Alcoholism | Cytochrome P-450 | Acetylcysteine | Triglycerides | Superoxide | Glucose | Aldehydes | Dextrose | Proteins | Antioxidants | Glucose metabolism | Analysis | Physiological aspects | Nitric oxide | Liver cirrhosis | steatohepatitis | binge ethanol | gut leakiness | apoptosis | oxidative stress
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5. Full Text Interleukin-6 mediated upregulation of CYP1B1 and CYP2E1 in colorectal cancer involves DNA methylation, miR27b and STAT3
by Patel, S.A.A and Bhambra, U and Charalambous, M.P and David, R.M and Edwards, R.J and Lightfoot, T and Boobis, A.R and Gooderham, N.J
British Journal of Cancer, ISSN 0007-0920, 12/2014, Volume 111, Issue 12, pp. 2287 - 2296
Background: The pro-inflammatory cytokine interleukin-6 (IL6) promotes colorectal cancer (CRC) development. It is also known to regulate cytochrome P450... 
microRNA | colorectal cancer | cytochrome P450 | immunohistochemistry | inflammation | TRANSCRIPTION FACTORS | CYTOCHROME-P450 | DOWN-REGULATION | TUMOR | RISK | MECHANISMS | BETA-CATENIN | METABOLISM | ONCOLOGY | HUMAN HEPATOCYTES | EXPRESSION | Immunohistochemistry | Cytochrome P-450 CYP1B1 - genetics | Up-Regulation | Gene Expression | Interleukin-6 - genetics | HCT116 Cells | Humans | Middle Aged | Cytochrome P-450 CYP1B1 - metabolism | Male | MicroRNAs - metabolism | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | DNA Methylation | Female | Aged | MicroRNAs - genetics | Interleukin-6 - metabolism | STAT3 Transcription Factor - genetics | STAT3 Transcription Factor - metabolism | Index Medicus | Translational Therapeutics
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6. Full Text Human CYP2E1 is regulated by miR-378
by Mohri, Takuya and Nakajima, Miki and Fukami, Tatsuki and Takamiya, Masataka and Aoki, Yasuhiro and Yokoi, Tsuyoshi
Biochemical Pharmacology, ISSN 0006-2952, 2010, Volume 79, Issue 7, pp. 1045 - 1052
Human CYP2E1 is one of the pharmacologically and toxicologically important cytochrome P450 isoforms. Earlier studies have reported that the CYP2E1 expression... 
miRNA | Post-transcriptional regulation | Interindividual variability | Cytochrome P450 | Liver | MiRNA | POSTTRANSCRIPTIONAL REGULATION | PROTEIN STABILIZATION | RAT | CANCERS | RECEPTOR | MICRORNAS | MESSENGER-RNA LEVELS | CHEMICALS | PHARMACOLOGY & PHARMACY | HUMAN LIVER | EXPRESSION | Gene Expression Regulation, Enzymologic | Liver - enzymology | Luciferases - metabolism | Humans | Cells, Cultured | 3' Untranslated Regions - genetics | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - analysis | Cytochrome P-450 CYP2E1 - metabolism | MicroRNAs - physiology | Index Medicus
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7. Full Text Critical role of cytochrome P450 2E1 (CYP2E1) in the development of high fat-induced non-alcoholic steatohepatitis
by Abdelmegeed, Mohamed A and Banerjee, Atrayee and Yoo, Seong-Ho and Jang, Sehwan and Gonzalez, Frank J and Song, Byoung-Joon
Journal of Hepatology, ISSN 0168-8278, 2012, Volume 57, Issue 4, pp. 860 - 866
Background & Aims Ethanol-inducible cytochrome P450 2E1 (CYP2E1) activity contributes to oxidative stress. However, CYP2E1 may have an important role in the... 
Gastroenterology and Hepatology | Protein modifications | Oxidative stress | Null mice | NAFLD | Liver | High-fat diet | Insulin resistance | Inflammation | CYP2E1 | NASH | ACTIVATION | PROTEIN | INJURY | INDUCTION | LIVER-DISEASE | OVEREXPRESSION | NITRIC-OXIDE | MITOCHONDRIAL DYSFUNCTION | GASTROENTEROLOGY & HEPATOLOGY | EXPRESSION | Tumor Necrosis Factor-alpha - metabolism | Protein Carbonylation | Phosphorylation | Body Weight | Oxidative Stress | Fatty Liver - pathology | Diet, High-Fat - adverse effects | JNK Mitogen-Activated Protein Kinases - metabolism | Male | Cytochrome P-450 CYP2E1 - genetics | Osteopontin - metabolism | Cytochrome P-450 CYP2E1 - metabolism | Inflammation - complications | Inflammation - metabolism | Non-alcoholic Fatty Liver Disease | Antigens, Differentiation - metabolism | Chemokine CCL2 - metabolism | Receptor for Advanced Glycation End Products | Glucose Tolerance Test | Fatty Liver - metabolism | Insulin Resistance | Mice, Knockout | Animals | Glycation End Products, Advanced - metabolism | Mice | Lipid Peroxidation | Receptors, Immunologic - metabolism | Fatty Liver - etiology | Phosphates | Alcoholism | Oncology, Experimental | Cytochrome P-450 | Physiological aspects | Asparagine | Triglycerides | Glucose | Research | Dextrose | Cancer
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8. Full Text Understanding a substrate's product regioselectivity in a family of enzymes: A case study of acetaminophen binding in cytochrome P450s
by Yang, Yue and Wong, Sergio E and Lightstone, Felice C
PLoS ONE, ISSN 1932-6203, 02/2014, Volume 9, Issue 2, p. e87058
Product regioselectivity as influenced by molecular recognition is a key aspect of enzyme catalysis. We applied large-scale two-dimensional (2D) umbrella... 
OXIDATION | IN-VITRO | ACTIVATION | ACCURATE DOCKING | MULTIDISCIPLINARY SCIENCES | TOXIC METABOLITE | HYDROXYLATION | DYNAMICS | LIVER-MICROSOMES | CYP2E1 | DRUG-DRUG INTERACTIONS | Acetaminophen - metabolism | Stereoisomerism | Cytochrome P-450 CYP2C9 - chemistry | Humans | Molecular Conformation | Cytochrome P-450 Enzyme System - metabolism | Substrate Specificity | Cytochrome P-450 CYP2E1 - metabolism | Thermodynamics | Cytochrome P-450 CYP3A - chemistry | Molecular Structure | Cytochrome P-450 CYP2C9 - metabolism | Cytochrome P-450 CYP2E1 - chemistry | Protein Structure, Tertiary | Catalytic Domain | Cytochrome P-450 CYP1A2 - chemistry | Acetaminophen - chemistry | Cytochrome P-450 CYP2A6 - metabolism | Cytochrome P-450 CYP1A2 - metabolism | Molecular Dynamics Simulation | Cytochrome P-450 Enzyme System - chemistry | Cytochrome P-450 CYP3A - metabolism | Protein Binding | Molecular Docking Simulation | Cytochrome P-450 CYP2A6 - chemistry | Case studies | Biological products | Metabolites | Acetaminophen | Cytochrome P-450 | Molecular dynamics | Catalysis | Comparative analysis
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9. Full Text Absence of receptor interacting protein kinase 3 prevents ethanol‐induced liver injury
by Roychowdhury, Sanjoy and McMullen, Megan R and Pisano, Sorana G and Liu, Xiuli and Nagy, Laura E
Hepatology, ISSN 0270-9139, 05/2013, Volume 57, Issue 5, pp. 1773 - 1783
Hepatocyte cell death via apoptosis and necrosis are major hallmarks of ethanol‐induced liver injury. However, inhibition of apoptosis is not sufficient to... 
INDUCED CELL-DEATH | APOPTOSIS | OXIDATIVE STRESS | NECROPTOSIS | INHIBITION | INDUCED FATTY LIVER | NECROSIS-FACTOR-ALPHA | NONALCOHOLIC STEATOHEPATITIS | MICE | TNF-ALPHA | GASTROENTEROLOGY & HEPATOLOGY | Receptor-Interacting Protein Serine-Threonine Kinases - metabolism | Liver - pathology | Humans | Middle Aged | Hepatocytes - pathology | Male | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | Liver - drug effects | Ethanol - adverse effects | Adult | Female | Indoles - pharmacology | Disease Models, Animal | Chemical and Drug Induced Liver Injury - prevention & control | Liver - metabolism | Mice, Inbred C57BL | Imidazoles - pharmacology | Liver Diseases, Alcoholic - metabolism | Mice, Knockout | Cytochrome P-450 CYP2E1 - deficiency | Receptor-Interacting Protein Serine-Threonine Kinases - genetics | Animals | Biopsy | Chemical and Drug Induced Liver Injury - metabolism | Mice | Receptor-Interacting Protein Serine-Threonine Kinases - deficiency | Apoptosis | Ethanol | Kinases | Liver | Hepatology | apoptosis | liver injury | receptor interacting protein kinase 3 | Cytochrome P450 2E1 | Alcoholic liver disease | necroptosis
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10. Full Text MicroRNA regulation of CYP 1A2, CYP3A4 and CYP2E1 expression in acetaminophen toxicity
by Gill, Pritmohinder and Bhattacharyya, Sudeepa and McCullough, Sandra and Letzig, Lynda and Mishra, Prasun J and Luo, Chunqiao and Dweep, Harsh and James, Laura
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 12331 - 11
MicroRNAs (miRNAs) that regulate the cytochrome P-450 isoforms involved in acetaminophen (APAP) toxicity were examined in HepaRG cells treated with APAP (20... 
CIRCULATING MICRORNAS | BIOMARKERS | VARIABILITY | LIQUID-CHROMATOGRAPHY | CYTOCHROME-P450 ENZYMES | HUMAN HEPATOCYTES | HEPATOMA HEPARG CELLS | MULTIDISCIPLINARY SCIENCES | HEPATOTOXICITY | INDUCED LIVER-INJURY | PROTEIN ADDUCTS | Drug Overdose - metabolism | Up-Regulation | Drug Overdose - blood | Humans | 3' Untranslated Regions - genetics | Child, Preschool | Male | MicroRNAs - metabolism | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | Cytochrome P-450 CYP3A - genetics | Cytochrome P-450 CYP1A2 - genetics | Drug Overdose - etiology | Female | Protein Biosynthesis - genetics | Binding Sites | Child | Cell Line | Drug Overdose - genetics | Acetaminophen - toxicity | Cytochrome P-450 CYP1A2 - metabolism | Hepatocytes | Cytochrome P-450 CYP3A - metabolism | Adolescent | MicroRNAs - blood | Toxicity | Cytochrome P450 | MiRNA | mRNA | CYP1A2 protein | Protein adducts | Analgesics | 3' Untranslated regions | Acetaminophen | Isoforms | Overdose | Children | Binding sites
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11. Full Text Transgenic animal models in toxicology: Historical perspectives and future outlook
by Boverhof, Darrell R and Chamberlain, Mark P and Elcombe, Clifford R and Gonzalez, Frank J and Heflich, Robert H and Hernández, Lya G and Jacobs, Abigail C and Jacobson-Kram, David and Luijten, Mirjam and Maggi, Adriana and Manjanatha, Mugimane G and van Benthem, Jan and Gollapudi, B. Bhaskar
Toxicological Sciences, ISSN 1096-6080, 2011, Volume 121, Issue 2, pp. 207 - 233
Transgenic animal models are powerful tools for developing a more detailed understanding on the roles of specific genes in biological pathways and systems.... 
Transgenic models | Humanized models | Knock-out models | Risk assessment | risk assessment | CYP1B1 DETERMINES SUSCEPTIBILITY | humanized models | PREGNANE-X-RECEPTOR | ZINC-FINGER NUCLEASES | TARGETED DISRUPTION | ARYL-HYDROCARBON RECEPTOR | CONSTITUTIVE ANDROSTANE RECEPTOR | knock-out models | EMBRYONIC STEM-CELLS | IN-VIVO | TOXICOLOGY | DNA-POLYMERASE ETA | transgenic models | DRUG-METABOLISM | Cytochrome P-450 CYP1A1 - genetics | Risk Assessment - methods | Receptors, Steroid - metabolism | Humans | Cytochrome P-450 Enzyme System - metabolism | Cytochrome P-450 CYP2E1 - genetics | Cytochrome P-450 CYP2E1 - metabolism | Toxicity Tests - trends | Cytochrome P-450 CYP1A2 - genetics | Models, Animal | Toxicity Tests - methods | Xenobiotics - metabolism | Animals, Genetically Modified | Rats | PPAR alpha - genetics | Cytochrome P-450 CYP1A1 - metabolism | Cytochrome P-450 CYP1A2 - metabolism | Sequence Analysis, DNA | Mice, Knockout | Animals | Receptors, Steroid - genetics | Cytochrome P-450 Enzyme System - genetics | Mice | Mutation | PPAR alpha - metabolism | Index Medicus
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