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1. Full Text Contributions of ionic interactions and protein dynamics to cytochrome P450 2D6 (CYP2D6) substrate and inhibitor binding
by Wang, An and Stout, C. David and Zhang, Qinghai and Johnson, Eric F
Journal of Biological Chemistry, ISSN 0021-9258, 02/2015, Volume 290, Issue 8, pp. 5092 - 5104
P450 2D6 contributes significantly to the metabolism of > 15% of the 200 most marketed drugs. Open and closed crystal structures of P450 2D6 thioridazine... 
METABOLISM | PLASMA-LEVELS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTALLOGRAPHY | PHARMACOPHORE | P4502B4 | CONFORMATION | MODEL | HUMAN-LIVER | THIORIDAZINE | Cytochrome P-450 CYP2D6 - genetics | Catalytic Domain | Cytochrome P-450 CYP2D6 Inhibitors - chemistry | Secologanin Tryptamine Alkaloids - chemistry | Hydrogen Bonding | Humans | Cytochrome P-450 CYP2D6 - chemistry | Organic Chemicals - chemistry | Crystallography, X-Ray | Molecular Dynamics Simulation | Index Medicus | Protein Structure and Folding | Crystal Structure | Thioridazine | Cytochrome P450 | Quinidine | Drug Metabolism | Protein Structure | Cytochrome P450 2D6 (CYP2D6) | Quinine | Ajmalicine | Enzyme Inhibitor
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2. Full Text Transcriptional regulation of chicken cytochrome P450 2D49 basal expression by CCAAT/enhancer‐binding protein α and hepatocyte nuclear factor 4α
by Yang, Qi and Tang, Shulin and Dong, Linfeng and Chen, Qingmei and Liu, Xin and Jiang, Jun and Deng, Yiqun
FEBS Journal, ISSN 1742-464X, 03/2014, Volume 281, Issue 5, pp. 1379 - 1392
Chicken cytochrome P450 ( CYP )2D49 is structurally and functionally related to human CYP 2D6, which is an important drug‐metabolizing enzyme. To date, little... 
2D49 | HNF | EBP | chicken | transcriptional regulation | CCAAT | CYP | hepatocyte nuclear factor 4α | 4α | enhancer‐binding protein α (C | cytochrome P450 | CCAAT/enhancer-binding protein α (C/EBPα) | hepatocyte nuclear factor 4α (HNF4α) | cytochrome P450 (CYP) 2D49 | BIOCHEMISTRY & MOLECULAR BIOLOGY | hepatocyte nuclear factor4 (HNF4) | enhancer-binding protein (C | IDENTIFICATION | cytochromeP450 (CYP) 2D49 | AVIAN CYTOCHROME-P450 | C/EBP-ALPHA | XENOBIOTICS | CYP2D6 | CONSTITUTIVE ANDROSTANE RECEPTOR | GENES | HEPG2 CELLS | P450 | HNF4-ALPHA | Cytochrome P-450 CYP2D6 - genetics | Hepatocyte Nuclear Factor 4 - metabolism | Promoter Regions, Genetic | Sequence Deletion | Avian Proteins - metabolism | CCAAT-Enhancer-Binding Protein-alpha - metabolism | Humans | Liver - metabolism | Transcriptional Activation | Cytochrome P-450 Enzyme System - metabolism | Molecular Sequence Data | Binding Sites - genetics | DNA - genetics | Gene Expression Regulation, Enzymologic | Animals | Regulatory Elements, Transcriptional | Base Sequence | Chickens | Cytochrome P-450 CYP2D6 - metabolism | Cytochrome P-450 Enzyme System - genetics | Mutation | Avian Proteins - genetics | Index Medicus
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3. Full Text Oliceridine (TRV130), a Novel G Protein–Biased Ligand at the μ‐Opioid Receptor, Demonstrates a Predictable Relationship Between Plasma Concentrations and Pain Relief. I: Development of a Pharmacokinetic/Pharmacodynamic Model
by Fossler, Michael J and Sadler, Brian M and Farrell, Colm and Burt, David A and Pitsiu, Maria and Skobieranda, Franck and Soergel, David G
The Journal of Clinical Pharmacology, ISSN 0091-2700, 06/2018, Volume 58, Issue 6, pp. 750 - 761
Conventional opioids bind to μ‐opioid receptors and activate 2 downstream signaling pathways: G‐protein coupling, linked to analgesia, and β‐arrestin... 
Pain perception | Narcotics | Opioid receptors | Body weight | Cytochrome P450 | Arrestin | Pharmacology | Recruitment | Proteins | Analgesia | Receptors | Pain | Ligands | Mathematical models | Coupling | Pharmacokinetics | CYP2D6 protein | Index Medicus
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4. Full Text Oliceridine, a Novel G Protein–Biased Ligand at the μ‐Opioid Receptor, Demonstrates a Predictable Relationship Between Plasma Concentrations and Pain Relief. II: Simulation of Potential Phase 3 Study Designs Using a Pharmacokinetic/Pharmacodynamic Model
by Fossler, Michael J and Sadler, Brian M and Farrell, Colm and Burt, David A and Pitsiu, Maria and Skobieranda, Franck and Soergel, David G
The Journal of Clinical Pharmacology, ISSN 0091-2700, 06/2018, Volume 58, Issue 6, pp. 762 - 770
Oliceridine is a novel G protein–biased ligand at the μ‐opioid receptor that differentially activates G protein coupling while mitigating β‐arrestin... 
Dosing | Pain perception | Computer simulation | Narcotics | Opioid receptors | Cytochrome P450 | Morphine | Arrestin | Pharmacology | Patients | Proteins | Analgesia | Pain | Metabolites | Simulation | Ligands | Mathematical models | Genotypes | CYP2D6 protein | Index Medicus
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5. Full Text The global spectrum of protein-coding pharmacogenomic diversity
by Wright, G.E.B and Carleton, B and Hayden, M.R and Ross, C.J.D
Pharmacogenomics Journal, ISSN 1470-269X, 01/2018, Volume 18, Issue 1, pp. 187 - 195
Differences in response to medications have a strong genetic component. By leveraging publically available data, the spectrum of such genomic variation can be... 
IMPLEMENTATION CONSORTIUM GUIDELINES | GENETIC-VARIATION | VARIANTS | CYP2D6 | GENOTYPE | GENETICS & HEREDITY | POPULATIONS | PHARMACOLOGY & PHARMACY | ADVERSE-REACTIONS | TACROLIMUS | ASSOCIATION | ANCESTRY | Proteins - genetics | Pharmacogenetics - methods | Gene Frequency - genetics | Ethnic Groups - genetics | Genetics, Population - methods | Humans | Alleles | Genetic Variation - genetics | Physiological aspects | Pharmacogenetics | Research | Genetic variation | Genetic variance | Populations | Gene frequency | Genomes | Genetic diversity | Pharmacology | Variation | Gene sequencing | Index Medicus | Original
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6. Full Text CYP2D6-CYP2C9 Protein-Protein Interactions and Isoform-Selective Effects on Substrate Binding and Catalysis
by Murali Subramanian and Michael Low and Charles W. Locuson and Timothy S. Tracy
Drug Metabolism and Disposition, ISSN 0090-9556, 08/2009, Volume 37, Issue 8, pp. 1682 - 1689
Cytochrome P450 (P450) protein-protein interactions have been observed with various in vitro systems. It is interesting to note that these interactions seem to... 
CYP2C9 | ENZYMES | CYP1A2 | OXIDOREDUCTASE | FUNCTIONAL INTERACTIONS | SYSTEMS | PHARMACOLOGY & PHARMACY | LIVER-MICROSOMES | CYTOCHROME P450 REDUCTASE | RECONSTITUTION | DRUG-METABOLISM | Cytochrome P-450 CYP2C9 | Catalytic Domain | Biocatalysis | NADPH-Ferrihemoprotein Reductase - metabolism | Hydroxylation | Dealkylation | Humans | Substrate Specificity | Dextromethorphan - metabolism | Aryl Hydrocarbon Hydroxylases - metabolism | Dextrorphan - metabolism | Models, Biological | Cytochrome P-450 CYP2D6 - metabolism | Kinetics | Spectrum Analysis | Binding Sites | Flurbiprofen - metabolism | Flurbiprofen - analogs & derivatives | Index Medicus
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7. Full Text Time-dependent interaction between differentiated embryo chondrocyte-2 and CCAAT/enhancer-binding protein α underlies the circadian expression of CYP2D6 in serum- shocked HepG2 cells
by Matsunaga, Naoya and Inoue, Miki and Kusunose, Naoki and Kakimoto, Keisuke and Hamamura, Kengo and Hanada, Yuichi and Toi, Ayumi and Yoshiyama, Yuji and Sato, Fuyuki and Fujimoto, Katsumi and Koyanagi, Satoru and Ohdo, Shigehiro
Molecular Pharmacology, ISSN 0026-895X, 05/2012, Volume 81, Issue 5, pp. 739 - 747
Differentiated embryo chondrocyte-2 (DEC2), also known as bHLHE41 or Sharp1, is a pleiotropic transcription repressor that controls the expression of genes... 
RHYTHMIC EXPRESSION | HUMAN HEPATOCYTES | GENE-EXPRESSION | MOUSE-LIVER | RECEPTOR | PHARMACOLOGY & PHARMACY | PERIPHERAL-TISSUES | MOLECULAR CLOCK | CYTOCHROME-P450 2D6 | REPRESSES TRANSCRIPTION | DEC2 | Cytochrome P-450 CYP2D6 - genetics | Basic Helix-Loop-Helix Transcription Factors - physiology | CLOCK Proteins - physiology | Time Factors | CCAAT-Enhancer-Binding Protein-alpha - physiology | Humans | RNA, Messenger - analysis | Serum | Circadian Rhythm | Hepatocyte Nuclear Factor 4 - physiology | Hep G2 Cells | Index Medicus
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8. Full Text G Protein–Coupled Receptor Kinase 5 Gene Polymorphisms Are Associated With Postoperative Atrial Fibrillation After Coronary Artery Bypass Grafting in Patients Receiving β-Blockers
by Kertai, Miklos D and Li, Yen-Wei and Li, Yi-Ju and Shah, Svati H and Kraus, William E and Fontes, Manuel L and Stafford-Smith, Mark and Newman, Mark F and Podgoreanu, Mihai V and Mathew, Joseph P and Duke Perioperative Genetics Safety and Duke Perioperative Genetics and Safety Outcomes (PEGASUS) Investigative Team
Circulation: Cardiovascular Genetics, ISSN 1942-325X, 10/2014, Volume 7, Issue 5, pp. 625 - 633
BACKGROUND—We hypothesized that genetic variations in the adrenergic signaling pathway and cytochrome P450 2D6 enzyme are associated with new-onset atrial... 
Coronary artery bypass | Single nucleotide | Atrial fibrillation | Polymorphism | CARDIAC & CARDIOVASCULAR SYSTEMS | MANAGEMENT | HEART-FAILURE | polymorphism | METOPROLOL | coronary artery bypass | CYTOCHROME-P450 2D6 | atrial fibrillation | IN-VITRO | CARDIAC-SURGERY | PHARMACOGENOMICS | GENETICS & HEREDITY | single nucleotide | CYP2D6 GENOTYPE | NF-KAPPA-B | BETA-ADRENERGIC RECEPTOR | Haplotypes | Signal Transduction | Humans | Middle Aged | Male | Atrial Fibrillation - genetics | Case-Control Studies | Linkage Disequilibrium | Genetic Variation | Adrenergic beta-Antagonists - pharmacology | Coronary Artery Bypass | Female | Aged | Polymorphism, Single Nucleotide | Odds Ratio | G-Protein-Coupled Receptor Kinase 5 - genetics | Postoperative Complications | Cohort Studies | Index Medicus
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9. Full Text Crystal Structure of Human Cytochrome P450 2D6
by Paul Rowland and Frank E. Blaney and Martin G. Smyth and Jo J. Jones and Vaughan R. Leydon and Amanda K. Oxbrow and Ceri J. Lewis and Mike G. Tennant and Sandeep Modi and Drake S. Eggleston and Richard J. Chenery and Angela M. Bridges
Journal of Biological Chemistry, ISSN 0021-9258, 03/2006, Volume 281, Issue 11, pp. 7614 - 7622
Cytochrome P450 2D6 is a heme-containing enzyme that is responsible for the metabolism of at least 20% of known drugs. Substrates of 2D6 typically contain a... 
MICROSOMAL P450S | MACROMOLECULAR STRUCTURES | SUBSTRATE-SPECIFICITY | GENETIC-POLYMORPHISM | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | ENZYMATIC-ACTIVITY | COMBINED PROTEIN | PHARMACOPHORE MODEL | DRUG-METABOLISM | Protein Structure, Tertiary | Amino Acid Sequence | Mutagenesis, Site-Directed | Protein Structure, Secondary | Humans | Cytochrome P-450 CYP2D6 - chemistry | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Carbon Monoxide - chemistry | Protein Folding | Sequence Homology, Amino Acid | Heme - chemistry | Protein Conformation | Software | Aspartic Acid - chemistry | Kinetics | Mutation | Subcellular Fractions | Binding Sites | Glutamic Acid - chemistry | Index Medicus
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10. Full Text Substituted imidazole of 5-fluoro-2-[4-[(2-phenyl-1H-imidazol-5-yl)methyl]- 1-piperazinyl]pyrimidine inactivates cytochrome P450 2D6 by protein adduction
by Nagy, Leslie D and Mocny, Catherine S and Diffenderfer, Laura E and Hsi, David J and Butler, Brendan F and Arthur, Evan J and Fletke, Kyle J and Palamanda, Jairam R and Nomeir, Amin A and Furge, Laura Lowe
Drug Metabolism and Disposition, ISSN 0090-9556, 06/2011, Volume 39, Issue 6, pp. 974 - 983
5-Fluoro-2-[4-[(2-phenyl-1H-imidazol-5-yl)methyl]-1-piperazinyl]pyrimidine (SCH 66712) is a potent mechanism-based inactivator of human cytochrome P450 2D6... 
OXIDATION | MECHANISM-BASED INACTIVATION | INHIBITION | ACTIVE-SITE | ENZYMES | PHARMACOLOGY & PHARMACY | LIVER-MICROSOMES | BINDING | RECEPTOR ANTAGONIST | HEME ALKYLATION | DRUG-METABOLISM | Cytochrome P-450 CYP2D6 Inhibitors | Cytochrome P-450 CYP2D6 - genetics | Recombinant Proteins - antagonists & inhibitors | Humans | Cytochrome P-450 CYP2D6 - chemistry | Enzyme Inhibitors - pharmacology | Imidazoles - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Imidazoles - pharmacology | Recombinant Proteins - genetics | Chromatography, High Pressure Liquid | Pyrimidines - pharmacology | Pyrimidines - chemistry | Heme - chemistry | Escherichia coli - genetics | Enzyme Inhibitors - chemistry | Protein Binding | Index Medicus
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11. Full Text Cis‐Nerolidol Induces Endoplasmic Reticulum Stress and Cell Death in Human Hepatocellular Carcinoma Cells through Extensive CYP2C19 and CYP1A2 Oxidation
by Biazi, Bruna Isabela and Zanetti, Thalita Alves and Baranoski, Adrivanio and Corveloni, Amanda Cristina and Mantovani, Mário Sérgio
Basic & Clinical Pharmacology & Toxicology, ISSN 1742-7835, 10/2017, Volume 121, Issue 4, pp. 334 - 341
Of late, many studies are attempting to find new molecules with anticancer properties, especially those with the capability to inhibit cell growth. The aim of... 
CANCER-CELLS | APOPTOSIS | COMET ASSAY | C-MYC | PHARMACOLOGY & PHARMACY | ANTICANCER DRUGS | KINASE INHIBITORS | TOXICITY | TOXICOLOGY | MELANOMA-CELLS | INDUCTION | CYCLE | Activation, Metabolic | Sesquiterpenes - metabolism | Apoptosis - drug effects | Humans | Dose-Response Relationship, Drug | Carcinoma, Hepatocellular - drug therapy | Time Factors | Carcinoma, Hepatocellular - genetics | Apoptosis Regulatory Proteins - genetics | Cell Cycle Proteins - genetics | Liver Neoplasms - pathology | Antineoplastic Agents, Phytogenic - metabolism | Liver Neoplasms - enzymology | Endoplasmic Reticulum Stress - drug effects | Liver Neoplasms - genetics | Oxidation-Reduction | Cell Cycle Proteins - metabolism | Liver Neoplasms - drug therapy | Carcinoma, Hepatocellular - enzymology | Cytochrome P-450 CYP1A2 - metabolism | Apoptosis Regulatory Proteins - metabolism | Hep G2 Cells | Carcinoma, Hepatocellular - pathology | Cytochrome P-450 CYP2C19 - metabolism | Cell Proliferation - drug effects | Sesquiterpenes - pharmacology | Antineoplastic Agents, Phytogenic - pharmacology | G1 Phase Cell Cycle Checkpoints - drug effects | Cell death | Cytochrome P-450 | Physiological aspects | Biochemistry | Stress (Physiology) | Hepatoma | Tumor proteins | Xenobiotics | Gene expression | Cell proliferation | Bax protein | Genotoxicity | Cytotoxicity | Hepatocellular carcinoma | Myc protein | Kinases | Phase transitions | Liver cancer | Mitochondria | Cell growth | Nerolidol | Cell cycle | Oxidation | Membrane potential | CYP2D6 protein | G1 phase | Enzymes | Cell survival | Cytochrome P450 | Caspase | CYP1A2 protein | Metabolism | Survival | Cyclins | Cyclin-dependent kinase 2 | Endoplasmic reticulum | Phase transition | Apoptosis | Index Medicus
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12. Full Text Evaluation of CYP2D6 Protein Expression and Activity in the Small Intestine to Determine Its Metabolic Capability in the Japanese Population
by Kawakami, Momoko and Takenoshita-Nakaya, Sachiko and Takeba, Yuko and Nishimura, Yuki and Oda, Masayuki and Watanabe, Minoru and Ohta, Yuki and Kobayashi, Shinjiro and Ohtsubo, Takehito and Kobayashi, Shinichi and Uchida, Naoki and Matsumoto, Naoki
Biological and Pharmaceutical Bulletin, ISSN 0918-6158, 2017, Volume 40, Issue 9, pp. 1344 - 1351
CYP2D6 plays an important role in the metabolism of many drugs such as opioids and antidepressants. Polymorphisms of the CYP2D6 gene are widely observed in the... 
CYP 2D6 | small intestine | polymorphism | bufuralol | Japanese | Bufuralol | Small intestine | Polymorphism | CYP2D6-ASTERISK-10 | CHINESE | LOCUS | GENOTYPES | IN-VITRO | POLYMORPHISMS | CYTOCHROME-P450 EXPRESSION | GENE | PHARMACOKINETICS | LIVER | PHARMACOLOGY & PHARMACY | Cytochrome P-450 CYP2D6 - genetics | Blotting, Western - methods | Humans | Japan | Middle Aged | Asian Continental Ancestry Group - genetics | Real-Time Polymerase Chain Reaction - methods | Genotype | Male | Chromatography, High Pressure Liquid | RNA, Messenger - metabolism | Jejunum - metabolism | Polymorphism, Genetic | Ethanolamines - metabolism | Aged, 80 and over | Cytochrome P-450 CYP2D6 - metabolism | Adult | Female | Aged | Drugs | Enzymes | Narcotics | Hydroxylation | Liver | Cytochrome P450 | Oral administration | mRNA | Liquid chromatography | Metabolism | Tissues | High-performance liquid chromatography | Western blotting | Polymerase chain reaction | Proteins | Antidepressants | Opioids | Drug metabolism | Population | CYP2D6 protein | Genotypes | Index Medicus
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13. Full Text Species differences in metabolism of EPZ015666, an oxetane-containing protein arginine methyltransferase-5 (PRMT5) inhibitor
by Rioux, Nathalie and Duncan, Kenneth W and Lantz, Ronald J and Miao, Xiusheng and Chan-Penebre, Elayne and Moyer, Mikel P and Munchhof, Michael J and Copeland, Robert A and Chesworth, Richard and Waters, Nigel J
Xenobiotica, ISSN 0049-8254, 03/2016, Volume 46, Issue 3, pp. 268 - 277
1. Metabolite profiling and identification studies were conducted to understand the cross-species differences in the metabolic clearance of EPZ015666, a... 
CYP2D6 | metabolite identification | hepatocytes | CYP2D15 | interspecies scaling | CYTOCHROME-P450 | DESIGN | MOUSE | MODEL | SUBSTRATE | IN-VIVO | PHARMACOLOGY & PHARMACY | TOXICOLOGY | LIVER-MICROSOMES | DOG | Cytochrome P-450 CYP2D6 Inhibitors - pharmacokinetics | Isoquinolines - pharmacokinetics | Species Specificity | Humans | Microsomes, Liver - metabolism | Ethers, Cyclic - pharmacokinetics | Ketoconazole - pharmacokinetics | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Rats | Cytochrome P-450 CYP3A Inhibitors - pharmacokinetics | Male | Hepatocytes - metabolism | Rats, Sprague-Dawley | Animals | Enzyme Inhibitors - pharmacokinetics | Quinidine - pharmacokinetics | Dogs | Pyrimidines - pharmacokinetics | Mice | Index Medicus
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14. Full Text CYP 2D6 Binding Affinity Predictions Using Multiple Ligand and Protein Conformations
by Peric-Hassler, L and Stjernschantz, E.M and Oostenbrink, B.C and Geerke, D.P
International Journal of Molecular Sciences, ISSN 1422-0067, 2013, Volume 14, Issue 12, pp. 24514 - 24530
Because of the large flexibility and malleability of Cytochrome P450 enzymes (CYPs), in silico prediction of CYP binding affinities to drugs and other... 
CYP 2D6 | Binding free energies | Thiourea ligands | LIE method | thiourea ligands | CRYSTAL-STRUCTURE | DOCKING | COMPLEXES | HUMAN CYTOCHROME-P450 2D6 | CHEMISTRY, MULTIDISCIPLINARY | FREE-ENERGY CALCULATIONS | MODES | SCORING FUNCTIONS | MOLECULAR-DYNAMICS SIMULATIONS | binding free energies | PLASTICITY | WATER | Protein Structure, Tertiary | Thiourea - metabolism | Thermodynamics | Cytochrome P-450 CYP2D6 - chemistry | Cytochrome P-450 CYP2D6 - metabolism | Models, Molecular | Protein Binding | Ligands | Thiourea - chemistry | Molecular Dynamics Simulation | Index Medicus
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15. Full Text Molecular dynamics simulations to investigate the influences of amino acid mutations on protein three-dimensional structures of cytochrome P450 2D6.1, 2, 10, 14A, 51, and 62
by Fukuyoshi, Shuichi and Kometani, Masaharu and Watanabe, Yurie and Hiratsuka, Masahiro and Yamaotsu, Noriyuki and Hirono, Shuichi and Manabe, Noriyoshi and Takahashi, Ohgi and Oda, Akifumi
PLoS ONE, ISSN 1932-6203, 04/2016, Volume 11, Issue 4, pp. e0152946 - e0152946
Many natural mutants of the drug metabolizing enzyme cytochrome P450 (CYP) 2D6 have been reported. Because the enzymatic activities of many mutants are... 
WILD-TYPE | NATURAL VARIANT | SEQUENCES | GENETICS | ENZYMES | MULTIDISCIPLINARY SCIENCES | DRUGS | SUPERFAMILY | FUNCTIONAL-CHARACTERIZATION | P450S | CYP2D6 ALLELIC VARIANTS | Protein Conformation | Cytochrome P-450 Enzyme System - chemistry | Isoenzymes - chemistry | Mutation | Molecular Dynamics Simulation | Amino Acid Substitution | Molecular dynamics | Drug metabolism | Amino acids | Research | Analysis | Cytochrome P-450 | Cytochrome | Drugs | Enzymes | Cytochrome P450 | Metabolism | Gene polymorphism | Mutants | Proteins | Studies | Dynamic tests | Enzymatic activity | Simulation | Metabolites | Ligands | CYP2D6 protein | Polymorphism | Index Medicus
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