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Pharmacology and toxicology of cytochrome P450 -- 60th anniversary /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Yamazaki, Hiroshi
Formato: eBook
Idioma:Inglés
Publicado: Cambridge, MA : Academic Press, 2022.
Colección:Advances in Pharmacology ; v. 95.
Temas:
Acceso en línea:Texto completo

MARC

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245 0 0 |a Pharmacology and toxicology of cytochrome P450 -- 60th anniversary /  |c Edited by Hiroshi Yamazaki. 
260 |a Cambridge, MA :  |b Academic Press,  |c 2022. 
300 |a 1 online resource 
490 1 |a Advances in Pharmacology ;  |v v. 95 
588 0 |a Print version record. 
505 0 |a Intro -- Pharmacology and Toxicology of Cytochrome P450 -- 60th Anniversary -- Copyright -- Contents -- Contributors -- Preface -- Reference -- In Memoriam-Tsuneo Omura -- Chapter One: Roles of cytochrome P450 enzymes in pharmacology and toxicology: Past, present, and future -- 1. Introduction -- 2. Where is the P450 field today and what do we know? -- 2.1. Roles of individual human P450s -- 2.2. Abundance of P450s -- 2.3. Regulation -- 2.4. Catalytic mechanism -- 2.5. Structures of P450s and binding of ligands -- 3. P450s and drug metabolism -- 3.1. P450s and pharmacokinetic issues -- 3.1.1. Changing molecules to attenuate metabolism -- 3.1.2. Variations in pharmacokinetics -- 3.2. Drug-drug interactions -- 3.2.1. Induction -- 3.2.2. Inhibition -- 3.2.2.1. Modes of inhibition -- 3.2.2.2. Time-dependent inhibition -- 3.2.2.3. Use of inhibitors to slow drug metabolism -- 3.2.2.4. Clinical issues -- 3.3. Toxicity issues -- 3.3.1. Slow metabolism -- 3.3.2. Bioactivation -- 3.3.3. Human specific metabolites -- 3.3.4. Human differences in regulation -- 4. P450s as drug targets -- 4.1. Current P450 inhibitors in use -- 4.2. Future prospects for P450 inhibition -- 4.3. Pest control -- 4.4. Targeting accessory enzymes -- 5. The future of P450 research -- 5.1. Recent developments -- 5.2. Questions regarding basic research -- 5.3. Practical questions to be addressed -- 6. Conclusion -- Acknowledgments -- Conflict of interest statement -- References -- Chapter Two: Pharmacogenetics of the cytochromes P450: Selected pharmacological and toxicological aspects -- 1. Introduction -- 2. Relevance of cytochrome P450 polymorphisms to warfarin dosing and bleeding risk -- 2.1. Historic aspects of warfarin metabolism in relation to the cytochromes P450 -- 2.2. Warfarin dosing and relevance of P450 and other genotypes -- 2.3. CYP2C9 genotype relevance more broadly. 
505 8 |a 3. Idiosyncratic adverse drug reactions and cytochrome P450 polymorphisms -- 3.1. Idiosyncratic liver injury and cytochrome P450 polymorphisms -- 3.2. Idiosyncratic skin reactions and cytochrome P450 polymorphisms -- 4. Cytochrome P450 polymorphisms and disease susceptibility -- 4.1. Cancer -- 4.2. Other diseases -- 5. Conclusion -- Conflict of interest -- References -- Chapter Three: Cytochrome P450 enzymes and metabolism of drugs and neurotoxins within the mammalian brain -- 1. Introduction -- 1.1. Xenobiotic metabolizing CYPs in the brain -- 1.2. Studying CYPs in the brain -- 2. CYP expression in the brain -- 3. Factors influencing CYPs in the brain -- 3.1. Endogenous factors -- 3.1.1. Genetics -- 3.1.2. Hormones -- 3.2. Xenobiotics -- 3.2.1. Transcriptional regulation and induction -- 3.2.2. Post-transcriptional induction -- 3.2.3. Inhibition -- 4. Functional impact of brain CYP metabolism -- 4.1. Drugs -- 4.2. Neurotoxins -- 5. Conclusion -- Acknowledgments -- Conflict of interest -- References -- Chapter Four: Mammalian cytochrome P450 biodiversity: Physiological importance, function, and protein and genomic structu ... -- 1. Introduction -- 2. Results -- 2.1. Early work implicating CYP2B in dietary specialization -- 2.2. Functional assays implicating the role of P450s and of CYP2B in juniper ingestion by woodrats -- 2.3. Enormous diversity of CYP2B isoforms in woodrats -- 2.4. Background to biochemical and structural studies of woodrat CYP2B enzymes -- 2.5. Studies of woodrat CYP2B enzymes and of monoterpene binding to human CYP2B6 -- 2.6. Role of enzyme induction in species differences -- 3. Conclusion -- 3.1. Summary of main results -- 3.2. Reflections -- 3.3. Future directions -- Acknowledgments -- Conflict of interest statement -- References -- Chapter Five: Atypical kinetics of cytochrome P450 enzymes in pharmacology and toxicology. 
505 8 |a 1. Introduction -- 2. Atypical Michaelis-Menten kinetics and proposed mechanisms -- 2.1. Substrate inhibition kinetics in P450 -- 2.2. Drug inhibition of P450 in the presence of substrate inhibition -- 3. Atypicalities in mechanism-based inactivation of cytochrome P450 -- 3.1. Complexities in the mechanism-based inactivation of CYP3A -- 3.2. Probe substrate-dependent inactivation in CYP3A -- 3.3. Isoform-dependent inactivation in CYP3A -- 3.4. In vivo implications of atypicalities and complexities in mechanism-based inactivation -- 4. Conclusion -- Acknowledgments -- Conflict of interest -- References -- Chapter Six: Biosynthesis using cytochrome P450 enzymes: Focus on synthesis of drug metabolites -- 1. Introduction -- 2. Utility of metabolite biosynthesis -- 2.1. Discovery applications: Chemical diversity -- 2.2. Early development: Meeting MIST requirements -- 2.3. Late development -- 3. Directed metabolite biosynthesis -- 3.1. Metabolite isolation from incubation with expressed enzymes, microsomes, hepatocytes or in vivo -- 3.2. Biosynthesis of metabolites using bioreactors -- 3.3. Bioreactors with expressed mammalian CYPs -- 3.4. Microbial bioreactors -- 3.4.1. Examples of microbial-based bioreactors -- 4. Conclusion -- Conflict of interest statement -- References -- Chapter Seven: Use of engineered cytochromes P450 for accelerating drug discovery and development -- 1. Introduction -- 2. Lead candidate synthesis and late-stage functionalization of pharmaceutical compounds -- 3. Production of drug metabolites -- 4. Limitations of P450s as biocatalysts for the pharmaceutical industry -- 5. Progress in changing properties of P450 systems -- 6. Engineering of substrate specificity -- 7. Engineering catalytic efficiency via the redox system -- 8. Engineering the ability to use oxygen surrogates -- 9. Progress in engineering thermostability. 
505 8 |a 9.1. Thermostabilization of bacterial P450s -- 9.2. Thermostabilization of eukaryotic P450 forms -- 9.3. Engineering solvent tolerance -- 10. Novel chemistry -- 11. Conclusion -- Acknowledgments -- Author contributions -- Conflict of interest statement -- References -- Chapter Eight: Assessing cytochrome P450 function using genetically engineered mouse models -- 1. Introduction -- 2. Available mouse models -- 3. Assessing CYP function in the in vivo metabolism and toxicity of therapeutic drugs -- 4. Assessing the function of CYPs in the in vivo metabolism, bioactivation, and toxicity of known or suspected chemical c ... -- 5. Conclusion -- Acknowledgments -- Conflict of interest statement -- References -- Chapter Nine: Expression and functional activity of cytochrome P450 enzymes in human hepatocytes with sustainable reprodu ... -- 1. Introduction -- 2. Preparation of hepatocytes (from chimeric mice) -- 3. Expression and activity of human P450 enzymes -- 4. P450 enzyme-dependent drug metabolism -- 5. Human hepatocytes during 1- to 4-weeks of culture -- 6. Conclusion -- Acknowledgments -- Conflict of interest -- Author contributions -- References -- Chapter Ten: Cytochrome P450s in chimeric mice with humanized liver -- 1. Introduction -- 2. Characterization of humanized liver from chimeric mice -- 2.1. Zonal expression of human P450 in the repopulated humanized liver -- 2.2. Levels of gene expression of drug metabolizing enzymes and transporters -- 2.3. Content of human P450 protein in liver microsomes -- 2.4. Drug oxidation activity in liver microsomes -- 3. In vivo drug metabolism by humanized liver mouse -- 3.1. Tolbutamide -- 3.2. Desloratadine -- 3.3. Thalidomide -- 3.4. Diclofenac -- 4. Pharmacokinetic study using humanized liver mouse -- 5. Drug interaction study using humanized liver mouse. 
505 8 |a 6. Human P450-inactivated chimeric mouse model using mechanism-based inhibitor -- 7. Conclusion -- Conflict of interest -- Acknowledgments -- Author contributions -- References -- Chapter Eleven: Polymorphic cytochromes P450 in non-human primates -- 1. Introduction -- 2. Molecular characteristics of P450s -- 2.1. CYP1A subfamily -- 2.2. CYP1B subfamily -- 2.3. CYP1D subfamily -- 2.4. CYP2A subfamily -- 2.5. CYP2B subfamily -- 2.6. CYP2C subfamily -- 2.7. CYP2D subfamily -- 2.8. CYP2E subfamily -- 2.9. CYP2F subfamily -- 2.10. CYP2G subfamily -- 2.11. CYP2J subfamily -- 2.12. CYP3A subfamily -- 2.13. CYP4A subfamily -- 2.14. CYP4F subfamily -- 3. Genetic polymorphisms -- 3.1. Genetic variants identified -- 3.2. Characterization of polymorphic P450s in vitro -- 3.3. Drug elimination mediated by polymorphic P450s in vivo -- 4. Conclusion -- Acknowledgments -- Conflicts of interest -- References -- Chapter Twelve: Cytochrome P450 enzymes in the pediatric population: Connecting knowledge on P450 expression with pediatr ... -- 1. Introduction -- 2. Developmental changes in cytochrome P450 enzyme expression -- 2.1. CYP1A1 -- 2.2. CYP1A2 -- 2.3. CYP2A6 -- 2.4. CYP2B6 -- 2.5. CYP2C8 -- 2.6. CYP2C9 -- 2.7. CYP2C19 -- 2.8. CYP2D6 -- 2.9. CYP2E1 -- 2.10. CYP3A7, CYP3A5, and CYP3A4 -- 3. Utilization of P450 ontogeny for predicting pharmacokinetics of drugs in the pediatric population: Physiologically-bas ... -- 4. Future challenges -- 4.1. Performing more comprehensive basic science and clinical studies in children -- 4.2. Disease effects on pediatric P450 expression -- 4.3. Effects of pharmacogenetics and drug-drug interactions on pediatric P450 enzymes -- 4.4. Pediatric PK prediction in an individual -- 5. Conclusion -- Acknowledgments -- Conflict of interest -- References -- Chapter Thirteen: Cytochrome P450 polymorphism: From evolution to clinical use. 
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700 1 |a Yamazaki, Hiroshi. 
776 0 8 |c Original  |z 0323911099  |z 9780323911092  |w (OCoLC)1303080096 
776 0 8 |i Print version:  |t Pharmacology and toxicology of cytochrome P450  |z 9780323911092  |w (OCoLC)1332952982 
830 0 |a Advances in Pharmacology ;  |v v. 95. 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/bookseries/10543589/95  |z Texto completo