Relevant bibliographies by topics / Cytochrome P45Os

Academic literature on the topic 'Cytochrome P45Os'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Cytochrome P45Os"

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BRASH, ALAN R., MIN S. CHANG, COLIN D. FUNK, and WENCHAO SONG. "Novel Transformations of HPETEs by Cytochrome P45Os." Annals of the New York Academy of Sciences 744, no. 1 Cellular Gene (November 1994): 25–30. http://dx.doi.org/10.1111/j.1749-6632.1994.tb52720.x.

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Kim, Hyun-Mi, and Kwang-Hyeon Liu. "Screening for inhibitory effect on nine CYP isoforms by 20 herbal medications." Journal of Life Science 17, no. 3 (March 30, 2007): 334–39. http://dx.doi.org/10.5352/jls.2007.17.3.334.

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Godbole, Rucha C., Anupama A. Pable, and Vitthal T. Barvkar. "Transcriptome-wide identification, characterization, and phylogenomic analysis of cytochrome P450s from Nothapodytes nimmoniana reveal candidate genes involved in the camptothecin biosynthetic pathway." Genome 64, no. 1 (January 2021): 1–14. http://dx.doi.org/10.1139/gen-2020-0067.

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The plant Nothapodytes nimmoniana is an important source of camptothecin (CPT), an anticancer compound widely used in the treatment of colorectal, lung, and ovarian cancers. CPT is biosynthesized by the combination of the seco-iridoid and indole pathways in plants. The majority of the biosynthetic steps and associated genes still remain unknown. Certain reactions in the seco-iridoid pathway are catalyzed by cytochrome P450 enzymes. Hence, identifying transcriptionally active cytochrome P450 genes becomes essential in the elucidation of the CPT biosynthetic pathway. Here, we report the identification of 94 cytochrome P450s from the assembled transcriptomic data from leaf and root tissues of N. nimmoniana. The identified cytochrome P450 genes were full length and possessed all four conserved characteristic signature motifs of cytochrome P450 genes. Phylogenetic analysis of the protein sequences revealed their evolution and diversification and further categorized them into A-type (52.12%) and non-A-type (47.87%) cytochrome P450s. These 94 sequences represent 38 families and 63 subfamilies of cytochrome P450s. We also compared the transcriptional activity of identified cytochrome P450s with the expression of their homologs in the CPT-producing plant Ophiorrhiza pumila. Based on expression profiles and quantitative PCR validation, we propose NnCYP81CB1 and NnCYP89R1 as candidate cytochrome P450 genes involved in camptothecin biosynthesis in N. nimmoniana.
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Henderson, C. J., A. Sahraouei, and C. R. Wolf. "Cytochrome P450s and chemoprevention." Biochemical Society Transactions 28, no. 2 (February 1, 2000): 42–46. http://dx.doi.org/10.1042/bst0280042.

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The cytochrome P450 mono-oxygenase system represents a major defence against chemical challenge from the environment, constituting part of an adaptive response mounted by an organism following exposure to harmful agents. Cytochrome P450s are also able to catalyse the activation of compounds to toxic products, and participate in a variety of essential ‘housekeeping’ functions, such as biosynthesis of steroid hormones and fatty acid oxidation. It is clear that the modulation of expression of these enzymes can have a significant effect on chemical toxicity, carcinogenicity and mutagenicity. The concept of cancer chemoprevention, i.e. the administration of a (non-toxic) chemical or dietary component in order to prevent neoplastic disease or to inhibit its progression, is an attractive one. Despite this, relatively little work has been done to characterize the ability of putative chemopreventive agents to modulate P450 expression, or to understand the interaction between P450s and chemopreventive agents. Before chemopreventive treatment can become a reality, it is essential that this complex issue is addressed; for instance, it is likely that any single chemopreventive agent will induce more than one P450 isoenzyme, and while altered expression of a particular P450 may attenuate the effects of one toxic agent, the effects of others might well be potentiated. Our laboratory has created a transgenic mouse line in which the rat CYP1A1 promoter drives expression of the β-galactosidase gene. These mice can be used to define which compounds act via the Ah receptor, in which tissues, and at which stage of development. We are currently developing another mouse line in which β-galactosidase expression is controlled by the mouse GstA1 promoter, allowing us to define the role of the antioxidant responsive element in the action of chemopreventive agents. Finally, using cre-1oxP transgenic technology, we have generated a mouse line in which P450 reductase can be deleted in a conditional, i.e. tissue-specific, manner, permitting us to investigate the role of P450s in chemoprevention in a more defined manner.
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Sahraouei, A., C. J. Henderson, and C. R. Wolf. "Cytochrome P450s and Chemoprevention." Biochemical Society Transactions 28, no. 1 (February 1, 2000): A6. http://dx.doi.org/10.1042/bst028a006.

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KARLGREN, M., S. MIURA, and M. INGELMANSUNDBERG. "Novel extrahepatic cytochrome P450s." Toxicology and Applied Pharmacology 207, no. 2 (September 1, 2005): 57–61. http://dx.doi.org/10.1016/j.taap.2004.12.022.

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Blackbourn, H. "Gibberellins and cytochrome P450s." Trends in Plant Science 3, no. 9 (September 1998): 334. http://dx.doi.org/10.1016/s1360-1385(98)01309-0.

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Alzahrani, Abdullah M., and Peramaiyan Rajendran. "The Multifarious Link between Cytochrome P450s and Cancer." Oxidative Medicine and Cellular Longevity 2020 (January 4, 2020): 1–18. http://dx.doi.org/10.1155/2020/3028387.

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Cancer is a leading cause of death worldwide. Cytochrome P450s (P450s) play an important role in the metabolism of endogenous as well as exogenous substances, especially drugs. Moreover, many P450s can serve as targets for disease therapy. Increasing reports of epidemiological, diagnostic, and clinical research indicate that P450s are enzymes that play a major part in the formation of cancer, prevention, and metastasis. The purposes of this review are to shed light on the current state of knowledge about the cancer molecular mechanism involving P450s and to summarize the link between the cancer effects and the participation of P450s.
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Munro, A. W., K. J. McLean, K. R. Marshall, A. J. Warman, G. Lewis, O. Roitel, M. J. Sutcliffe, et al. "Cytochromes P450: novel drug targets in the war against multidrug-resistant Mycobacterium tuberculosis." Biochemical Society Transactions 31, no. 3 (June 1, 2003): 625–30. http://dx.doi.org/10.1042/bst0310625.

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Novel drug strategies are desperately needed to combat the global threat posed by multidrug-resistant strains of Mycobacterium tuberculosis (Mtb). The genome sequence of Mtb has revealed an unprecedented number of cytochrome P450 enzymes in a prokaryote, suggesting fundamental physiological roles for many of these enzymes. Several azole drugs (known inhibitors of cytochromes P450) have been shown to have potent anti-mycobacterial activity, and the most effective azoles have extremely tight binding constants for one of the Mtb P450s (CYP121). The structure of CYP121 has been determined at atomic resolution, revealing novel features of P450 structure, including mixed haem conformations and putative proton-relay pathways from protein surface to haem iron. The structure provides both a platform for investigation of structure/mechanism of cytochrome P450, and for design of inhibitor molecules as novel anti-tubercular agents.
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Unterweger, Birgit, Dieter M. Bulach, Judith Scoble, David J. Midgley, Paul Greenfield, Dena Lyras, Priscilla Johanesen, and Geoffrey J. Dumsday. "CYP101J2, CYP101J3, and CYP101J4, 1,8-Cineole-Hydroxylating Cytochrome P450 Monooxygenases from Sphingobium yanoikuyae Strain B2." Applied and Environmental Microbiology 82, no. 22 (September 2, 2016): 6507–17. http://dx.doi.org/10.1128/aem.02067-16.

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ABSTRACTWe report the isolation and characterization of three new cytochrome P450 monooxygenases: CYP101J2, CYP101J3, and CYP101J4. These P450s were derived fromSphingobium yanoikuyaeB2, a strain that was isolated from activated sludge based on its ability to fully mineralize 1,8-cineole. Genome sequencing of this strain in combination with purification of native 1,8-cineole-binding proteins enabled identification of 1,8-cineole-binding P450s. The P450 enzymes were cloned, heterologously expressed (N-terminally His6tagged) inEscherichia coliBL21(DE3), purified, and spectroscopically characterized. Recombinant whole-cell biotransformation inE. colidemonstrated that all three P450s hydroxylate 1,8-cineole using electron transport partners fromE. colito yield a product putatively identified as (1S)-2α-hydroxy-1,8-cineole or (1R)-6α-hydroxy-1,8-cineole. The new P450s belong to the CYP101 family and share 47% and 44% identity with other 1,8-cineole-hydroxylating members found inNovosphingobium aromaticivoransandPseudomonas putida. Compared to P450cin(CYP176A1), a 1,8-cineole-hydroxylating P450 fromCitrobacter braakii, these enzymes share less than 30% amino acid sequence identity and hydroxylate 1,8-cineole in a different orientation. Expansion of the enzyme toolbox for modification of 1,8-cineole creates a starting point for use of hydroxylated derivatives in a range of industrial applications.IMPORTANCECYP101J2, CYP101J3, and CYP101J4 are cytochrome P450 monooxygenases fromS. yanoikuyaeB2 that hydroxylate the monoterpenoid 1,8-cineole. These enzymes not only play an important role in microbial degradation of this plant-based chemical but also provide an interesting route to synthesize oxygenated 1,8-cineole derivatives for applications as natural flavor and fragrance precursors or incorporation into polymers. The P450 cytochromes also provide an interesting basis from which to compare other enzymes with a similar function and expand the CYP101 family. This could eventually provide enough bacterial parental enzymes with similar amino acid sequences to enablein vitroevolution via DNA shuffling.
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Dissertations / Theses on the topic "Cytochrome P45Os"

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Stok, Jeanette Elizabeth. "Biosynthetic cytochrome P450s /." [St. Lucia, Qld.], 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16210.pdf.

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Orr, Catherine. "Characterisation of equine cytochrome P450s." Thesis, University of Nottingham, 2016. http://eprints.nottingham.ac.uk/33315/.

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Cytochrome P450s (CYPs) are a superfamily of enzymes involved in the phase I metabolism of endogenous and exogenous substances. They are present in almost all forms of life and have been studied extensively, particularly in relation to human medicine, where knowledge of their activities is essential for predicting drug-drug interactions. In the horse, little is currently known about CYP-specific drug metabolism, which holds importance for animal welfare and for doping control within the horseracing industry where drug-specific metabolites are tested for on race days. Recently the first recombinant equine CYPs have been produced, allowing specific data on equine P450 activity to be gathered for the first time. During the current study,46 full-length P450 sequences were identified from the equine genome. RT-PCR analysis was then carried out on equine liver in order to detect hepatic expression of P450s across various families. After this, cold-induction (pCold) E. coli were used for production of recombinant P450 proteins for subsquent functional testing. Four recombinant equine P450s were successfully expressed (CYP1A1, CYP2A13, CYP2C92 and CYP2D50). Due to being the isoforms most likely to be involved in drug metabolism, rCYP2D50 and rCYP2C92 were selected to be screened against ten of the most commonly used horse drugs to identify potential substrates. rCYP2C92 appeared to metabolise all four NSAIDs tested (flunixin, ketoprofen, phenylbutazone and diclofenac), however presence of the known hydroxylated metabolites of diclofenac and phenylbutazone (4-hydroxydiclofenac and oxyphenbutazone, respectively) could not be confirmed despite being present within equine liver microsome and human recombinant CYP2C9 samples. In spite of the apparant acivity displayed by rCYP2C92 towards all four NSAIDs, no conclussions can be made about this enzyme’s role in NSAID metabolism due to a lack of known hydroxylated metabolite production.
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Rylander, Rudqvist Tove. "Extrahepatic cytochrome P450s : relation to cancer susceptibility /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-601-4/.

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Kusimo, Michael Olugbenga. "Characterisation of cytochrome P450s in Anopheles gambiae." Thesis, University of Sheffield, 2014. http://etheses.whiterose.ac.uk/9313/.

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Cytochrome P450s provide a natural mechanism by which insects defend themselves against the relatively small number of insecticides approved by WHO in fighting malaria vectors. Three dimensional structures of these enzymes are important to aid our understanding of the mechanism of their action in dissipating the harmful effects of such insecticides. However, to date no coordinates of any insect P450 structure have been deposited in the Protein Data Base. In this study a C-terminally, His-tagged, recombinant CYP6Z2, CYP for cytochrome P450, was constructed genetically and its expression and biochemical properties evaluated in an attempt to produce material suitable for crystallisation trials and ultimately X-ray structural analysis. The recombinant enzyme was purified in a soluble form through the introduction of a range of chemical agents including sodium cholate. A series of truncating mutants were constructed to determine the minimum set of primary structural elements that create a barrier to crystallisation. Genetically engineered truncations (11 amino acids and 22 amino acids) of the N-terminal hydrophobic region did not produce holoprotein. The N-terminal region appears to be essential to ensure the proper folding of insect P450 investigated, which may be the principal reason underpinning the lack of success in producing crystal structures for this group of enzymes. The homology model of CYP6Z2 used in this thesis, compared with those of the confirmed pyrethroid metabolisers; CYP6D1 and CYP6P3, revealed three key amino acid differences at their active sites. Single and double mutations of these three amino acids were constructed to explore their individual and joint roles in the metabolic activities of CYP6Z2. The single mutants, CYP6Z2 (Y102F) and CYP6Z2 (F212L) retained similar affinities as wild type for both benzyloxyresorufin (BR) and methoxyresorufin (MR) fluorescent probes. However, the turnover number of CYP6Z2 (Y102F) was 1.7-fold lower than the wild type for BR but shows improved activity with MR achieving 2-fold increase in turnover. CYP6Z2 (F212L) maintained the same turnover number with the wild type against BR but attained a 3.9-fold increase in activity against the methoxy derivative. Deletion of the positively charged arginine in CYP6Z2 (R210A) significantly improved the activity of the enzyme. The turnover number increased by 3-fold against BR and the enzyme effectiveness also increased by 2-fold. To further investigate the roles of these residues, the same mutations were introduced into CYP6P3. The addition of a hydroxyl group in CYP6P3 (F110Y) changed the kinetic behaviour of the enzyme drastically: the mutant lost activity with the resorufin probe and the affinity for the DEF probe was lowered by 7-fold. Conversely, introduction of benzyl ring in CYP6P3 (L216F) did not affect the affinity, but the enzyme’s activity increased by 15-fold with DEF. CYP6P3 (L216F) also improved the pyrethroid metabolising ability of the enzyme. These experiments clearly point to the important contribution of these amino acids in modulating the metabolic characteristics of these P450s. Similar studies were carried out to investigate the function of F115 in CYP6Z2 and CYP6Z3. This residue is frequently found close to the heam in P450s, where it is believed to play a key stabilising role in substrate recognition. A range of mutants were prepared and all produced holoproteins except F115H. The results presented in this thesis, point to a significant role in metabolic function for this residue, F115A, in CYP6Z3, and a rationalisation of the data is presented. Finally, the metabolic activities of CYP6Z2 and CYP6Z3 were compared in this study. Results presented here, suggest that both act independently in the presence of cytochrome b5 in their activities against the resorufin fluorescent probes but their activities with diethyl fluorescein (DEF) probe increased significantly when cytochrome b5 is present. CYP6Z3 has 2-fold turnover rate and 5-fold greater efficiency more than CYP6Z2 in dealkylation of BR and 8-fold and 10-fold in turnover and efficiency respectively for MR. These metabolic comparisons suggest strongly that CYP6Z3 is an improved “version” of CYP6Z2.
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Hodgkinson, Conrad Phillip. "Expression of cytochrome P450s in rat hepatocyte culture." Thesis, Queen Mary, University of London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244085.

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Gillett, Lorna. "Function of cytochrome P450s in the CYP4 family." Thesis, University of Nottingham, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408051.

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Pineau, Emmanuelle. "Formation des acides gras poly-hydroxylés et incorporation dans la cutine chez Arabidopsis thaliana." Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAJ052/document.

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Les plantes sont des organismes sessiles qui ne peuvent fuir des conditions souvent défavorables et doivent par conséquent s’adapter à un environnement hostile pour survivre. La cutine partie intégrante de la cuticule qui joue un rôle de barrière pour la plante est un polymère lipidique constitué principalement d’acides gras en C16 et C18 hydroxylés et époxydés reliés entre eux par des liaisons ester mettant en jeu les fonctions carboxyl et ω-hydroxyl des acides gras. La cutine ne joue pas seulement un rôle de barrière physique mais joue un rôle de réservoir de molécules possédant des propriétés physiologiques fondamentales. Grâce à des approches biochimiques et génétiques, nos travaux ont permis de mettre en évidence AtEH1, une époxyde hydrolase responsable de la formation des diols incorporés dans la cutine d’Arabidopsis thaliana. Ces diols sont décrits dans la littérature comme intervenant dans les interactions plante-pathogène. Nous avons également montré que ces composés ainsi que d’autres dérivés d’acides gras sont perçus par la plante. Nous avons identifié et caractérisé CYP77B1, une époxygénase d’acide gras qui a un rôle potentiel à jouer dans la formation d’acides gras polyhydroxylés incorporés dans la cutine
Plants are sessile organisms that are not able to escape from difficult environmental conditions and therefore have to adapt to multiple abiotic and biotic stress to survive. Cutin is a part of the cuticle which plays a major role as a barrier for the plant. It’s a lipid polymer composed mainly by hydroxylated and epoxidized C16 and C18 fatty acids linked together by ester links involving the carboxyl and ω-hydroxyl functions of those fatty acids. Cutin plays also a role as a reservoir of molecules with fundamental physiological properties. With biochemical and genetic approaches, we characterized AtEH1, an epoxide hydrolase responsible for the formation of diols incorporated in Arabidopsis thaliana cutin. These diols are described as being involved in plant-pathogen interactions. We also showed that these compounds as well as others fatty acids derivatives are perceived by plants. We have also identified and characterized CYP77B1, an epoxidase that has a potential role in the formation of polyhydroxylated fatty acids incorporated in cutin
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Hunter, Arwen Leigh. "The role of peri-transplant ischemia and reperfusion injury in cardiac allograft vasculopathy." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/2503.

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Heart transplantation is often the only therapeutic option for patients with end stage heart disease. Allograft organs are in short supply. Thus, preserving the life of a grafted organ is extremely important. Cardiac allograft vasculopathy (CAV) is an expression of chronic rejection that accounts for the greatest loss of graft function in transplanted hearts. Peri-transplant ischemia/reperfusion (I/R)-injury occurs during transplantation when blood flow is stopped to remove the heart from the donor and then is reinstated upon implantation of the donor heart into the recipient. This oxidative injury contributes to vascular dysfunction and CAV. In this dissertation, I hypothesize that prevention and/or reduction of I/R during transplantation reduces post-transplant vascular dysfunction and CAV. In this regard, myself and my colleagues examined the roles of apoptosis repressor with caspase recruitment domain (ARC) and cytochrome p450 (CYP) 2C enzymes in UR-induced vascular dysfunction and CAV. ARC expression was detected in endothelial cells (ECs) and smooth muscle cells (SMCs); however, increased levels of ARC do not protect against oxidant injury. ARC overexpression did protect against oxidant-induced cell death in H9c2 rat embryonic myoblasts. We observed that ARC-overexpression prevented H9c2 differentiation into muscle cells. With our focus on vascular injury, we turned our attention to the CYP 2C enzymes. Both endothelium-dependent and independent vascular function was impaired following I/R. Pre-treatment with the CYP 2C inhibitor sulfaphenazole (SP) restored endothelial sensitivity to acetylcholine, but did not restore sensitivity to endothelium-independent vasodilators. Rat heterotopic heart transplants were performed with rats being treated with SP or vector control prior to surgery. Rats treated with SP showed significantly reduced luminal narrowing and had decreased SMC proliferation, oxidant and interferon-y levels. No differences were detected in immune infiltration or apoptosis. Complementary studies in cultured vascular cells revealed that CYP 2C9 expression decreased viability and increased ROS production following hypoxia and re-oxygenation in ECs but not in SMCs. In summary, we did not detect protection of vascular cells by ARC, but did discover a novel role for ARC in differentiation. CYP 2C contributes to post-ischemic vascular dysfunction and CAV through increased oxidative stress and endothelial dysfunction.
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Rosic, Nedeljka. "Molecular breeding of cytochrome P450s for indigoid pigment production /." [St. Lucia, Qld.], 2005. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18978.pdf.

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Dodhia, Vikash Rajnikant. "Engineering human cytochrome P450s for structural and biosensing studies." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429524.

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Books on the topic "Cytochrome P45Os"

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Ing, Rachael. Enzymology and induction of hepatic cytochrome P450s in the guinea pig. Leicester: De Montfort University, 2001.

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Xu, Haibo. Effects of human milk and formula on the expression of cytochrome P450S in cell lines. Ottawa: National Library of Canada, 2001.

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Cozza, Kelly L., C. M. D. Armstrong Scott, and R. M. D. Oesterheld Jessica. Concise Guide to Drug Interaction Principles for Medical Practice: Cytochrome P450s, Ugts, P-Glycoproteins (Concise Guides). 2nd ed. American Psychiatric Publishing, Inc., 2003.

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Book chapters on the topic "Cytochrome P45Os"

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Peterson, Julian A., and Sandra E. Graham-Lorence. "Bacterial P450s." In Cytochrome P450, 151–80. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_5.

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Kagawa, Norio, and Michael R. Waterman. "Regulation of Steroidogenic and Related P450s." In Cytochrome P450, 419–42. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_12.

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Schuler, Mary A. "P450s in Plants, Insects, and Their Fungal Pathogens." In Cytochrome P450, 409–49. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6_7.

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Nakajima, Miki. "Control of Xeno/Endobiotics-Metabolizing Cytochrome P450s by MicroRNAs." In Fifty Years of Cytochrome P450 Research, 327–44. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54992-5_19.

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Lee, Su-Jun, and Jae-Gook Shin. "The Pharmacogenomics of Cytochrome P450s: From Molecular to Clinical Application." In Fifty Years of Cytochrome P450 Research, 345–70. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54992-5_20.

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Leach, Andrew G. "Tactics to Avoid Inhibition of Cytochrome P450s." In Topics in Medicinal Chemistry, 107–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/7355_2013_25.

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Calla, B., and M. R. Berenbaum. "Cytochrome P450s in the era of transcriptomics." In Transcriptomics in entomological research, 99–112. Wallingford: CABI, 2020. http://dx.doi.org/10.1079/9781789243130.0099.

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Shoji, Osami, and Yoshihito Watanabe. "Oxygenation of Nonnative Substrates Using a Malfunction State of Cytochrome P450s." In Fifty Years of Cytochrome P450 Research, 107–24. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54992-5_6.

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Fukushima, Ery Odette, Hikaru Seki, and Toshiya Muranaka. "Plant Cytochrome P450s in Triterpenoid Biosynthesis: Diversity and Application to Combinatorial Biosynthesis." In Fifty Years of Cytochrome P450 Research, 125–33. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54992-5_7.

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Shoji, Osami, and Yoshihito Watanabe. "Monooxygenation of Small Hydrocarbons Catalyzed by Bacterial Cytochrome P450s." In Advances in Experimental Medicine and Biology, 189–208. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_7.

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Conference papers on the topic "Cytochrome P45Os"

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Gonzalez, Frank J., and Harry V. Gelboin. "Cytochrome P450s and molecular epidemiology." In Environmental Sensing '92, edited by Tuan Vo-Dinh and Karl Cammann. SPIE, 1993. http://dx.doi.org/10.1117/12.140241.

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Beadle, Katherine. "Cytochrome P450s are responsible for the metabolism of thiacloprid in a solitary bee pollinator." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.111910.

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