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Dissertations / Theses on the topic 'Cytochrome P450'

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Published: 4 June 2021

Last updated: 25 July 2025

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1

Skinner, Michael Stephen. "Olfactory cytochrome P450." Thesis, University of Warwick, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.307349.

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2

Farooq, Yassar. "Mechanisms of electron transfer from cytochrome P450 reductase to cytochrome P450 3A4." Thesis, University of Leicester, 2010. http://hdl.handle.net/2381/8597.

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The study demonstrates that CPR and P450 3A4 can be prepared to highly pure state by the use of detergent CHAPS. Optimisation of published methods led to pure flavoprotein, ~90% full-length with a small amount of truncated CPR. The reconstitution of CPR and P450 3A4 into liposomes using CHAPS and Superose 6 column purification has achieved a homogenous highly functional proteoliposomes with good catalytic activity and almost completely reducible P450 3A4 in a simple controllable system. The spectroscopic data has shown that reduction of P450 3A4 in proteoliposomes was at least 10 fold higher t

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3

Al-Anizy, Mohammed. "Studies on cytochrome P450 4X1." Thesis, University of Nottingham, 2005. http://eprints.nottingham.ac.uk/10404/.

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Antisera raised against recombinant human CYP4Z1 (4Z1), mouse Aryl hydrocarbon receptor (AhR), and C.elegans Latrophilin (LpH) proteins were titred over the course of several bleeds. The sensitivity of the antibodies shows an increase over the course of several immunizations, with the minimum amount detected being 1 ng of 4Z1, 0.3 ng of AhR, and 0.3 ng of LpH. Terminal bleeds were taken for the AhR and LpH antisera. The AhR antisera detects proteins in rat and mouse liver cytosol consistent with previous reports of the AhR. LpH is predicted to be localized in a membrane compartment on the basi

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4

Bell, Stephen Graham. "The use of active site mutants of cytochrome P450(cam) in chemical synthesis." Thesis, University of Oxford, 1999. http://ora.ox.ac.uk/objects/uuid:7f48cf79-37b0-45cd-a40e-e971af466cff.

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This thesis describes a study of the substrate selectivity of active site mutants of the monooxygenase cytochrome P450<sub>cam</sub>. A range of mutants was constructed which replaced the phenolic side-chain at the Tyr-96 position by various hydrophobic amino acid residues. These 'hydrophobic mutants' were then combined with other mutations around the active site (Val-247, Phe-87, Ile-395 and Phe-193) which altered the space available at different positions in the active site. These mutants were then tested with an in vitro reconstituted P450<sub>cam</sub> system with a range of substrates rel

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5

Sideri, Anastasia. "Directed evolution of cytochrome P450 BM3." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.435931.

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6

Marsh, Rachael. "Cytochrome P450 studies in Aspergillus fumigatus." Thesis, University of Sheffield, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364267.

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7

Maughan, Juanita Amanda. "Molecular investigations of plant cytochrome P450." Thesis, University College London (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388204.

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8

Papagiannidou, Eleni. "Cytochrome P450-mediated metabolism of melatonin." Thesis, University of Surrey, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422928.

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9

Tyzack, Jonathan David. "Prediction of cytochrome P450 xenobiotic metabolism." Thesis, University of Cambridge, 2014. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708289.

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10

Busi, Florent. "Pharmacogénétique du cytochrome P450 humain CYP3A5." Paris 5, 2005. http://www.theses.fr/2005PA05P621.

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Les CYP3A sont les P450 les plus abondants dans le foie où ils métabolisent plus de 50 % des médicaments. Le CYP3A5 n'est exprimé que dans 25 % de la population caucasienne. Une mutation (CYP3A5*3) entraînant un épissage alternatif a été associée à un faible niveau de CYP3A5. Un niveau d'ARNm CYP3A5 plus élevé chez les individus *1/*3 par rapport aux homozygotes *3/*3 nous a amené à rechercher les causes de cette variation. L'ARN *3 est plus instable et sa dégradation est réalisée par la NMD (nonsense mediated mRNA decay). Le génotype CYP3A5 a des conséquences en clinique. Nous avons mis au po

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11

Eiben, Sabine. "CYP102A P450 monooxygenases: comparative analysis and construction of cytochrome P450 chimera." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-33683.

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12

Bertrand-Thiébault, Céline. "Cytochromes P450 et tonus vasculaire." Nancy 1, 2004. https://tel.archives-ouvertes.fr/tel-00120305.

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Les cytochromes P450 (CYP) sont des enzymes dont le rôle principalement connu est la détoxification. Cependant leur activité peut conduire à la formation de métabolites ayant des effets pharmacologiques, toxicologiques ou physiologiques. Depuis quelques années le rôle des cytochromes P450 dans le métabolisme de l'acide arachidonique est bien décrit. Parmi les métabolites produits lors de cette biotranformation, les acides epoxyeicosatriènoi͏̈ques (les EETs) et les acides hydroxyeicosatetraènoi͏̈ques (les HETEs ) occupent une place importante dans la régulation du tonus vasculaire. Ainsi les EE

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13

Vergères, Guy Vergeres Guy. "The membrane topoloy of microsomal cytochrome P450 /." [S.l.] : [s.n.], 1989. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=8866.

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14

Givens, Raymond Carlos Maeda Nobuyo. "Physiologic effects of cytochrome P450 3A activity." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2007. http://dc.lib.unc.edu/u?/etd,1371.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2007.<br>Title from electronic title page (viewed Apr. 25, 2008). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Nutrition, School of Public Health." Discipline: Nutrition; Department/School: Public Health.

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15

Rice, M. J. "Synthetic models of cytochrome P450 and photosynthesis." Thesis, University of Cambridge, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.233252.

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The work presented in this dissertation describes the prepartion and characterisation of various strapped porphyrin compounds which are designed to model cytochrome P450 and the charge separation in photosynthesis. The major part of this work is concerned with models of cytochrome P450. After a brief introduction to the philosophy of modelling, there follows a review of work on the enzyme and various compounds which are designed to reproduce the enzymic characteristics. The synthesis of two singly bridged porphyrins is reported. These incorporate a pendent methyl ester in the centre of the str

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16

Holmes, Victoria. "Structure activity relationships of cytochrome P450 4A1." Thesis, University of Nottingham, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.289361.

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17

Sabzevari, Omid. "Azole antifungal drugs and cytochrome P450 induction." Thesis, University of Surrey, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.359878.

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18

Singh, Subir. "Role of cytochrome P450 in breast carcinogenesis." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/role-of-cytochrome-p450-in-breast-carcinogenesis(ed2c5c1b-d2e9-458b-acc5-3c320cf22ee6).html.

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Cytochrome P450 enzymes (CYP) are key oxidative enzymes that are crucial in several biological processes, such as metabolism of exogenous and endogenous substances, the biological transformation of drugs and xenobiotics and biosynthesis of steroids and fatty acid. Several CYP have been identified in extra hepatic tissues implying that these enzymes exert other biological functions, which might explain their association with a number of diseases including diabetes, obesity and cancer. Understanding of these functions may provide the platform for the development of new therapeutic approaches and

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19

Dash, Hayley. "Studies of cytochrome P450 in biomimetic films." Thesis, University of Bath, 2007. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.512273.

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Cytochrome P450 enzymes are a super family of haem-containing mono-oxygenases which are found in all kingdoms of life. They show extraordinary diversity in their reaction chemistry and are involved in the biotransformation of a plethora of both exogenous and endogenous compounds. There has been a variety of approaches for the immobilisation of these biological redox systems and direct electrochemistry of these proteins can go towards providing biomimetic environments for fundamental studies together with a basis for designing devices without the need for electron transfer mediators. The incorp

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20

Smith, Gillian. "Xenobiotic regulation of cytochrome P450 gene expression." Thesis, University of Edinburgh, 1993. http://hdl.handle.net/1842/20797.

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Cytochromes P450 (P450) are a ubiquitous class of monooxygenases located in the endoplasmic reticulum of mammalian cells. These enzymes catalyse the Phase I oxidative metabolism of a wide range of structurally diverse chemicals resulting in increased hydrophilicity and excretion. Certain chemicals are, however, metabolically activated by cytochrome P450, leading to the formation of cytotoxic and/or carcinogenic metabolites. This has been exploited in the design of many prodrugs, including anti-tumour agents, which are inactive as administered but become active <i>in vivo</i> following metaboli

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21

Luciakova, Dominika. "Characterisation of novel cytochrome P450-fusion enzymes." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-of-novel-cytochrome-p450fusion-enzymes(08d9f0eb-666c-4f0f-b3ad-1fbf52555a0e).html.

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This study focuses on the characterisation of three novel cytochrome P450-partner (P450-fusion) enzymes of unknown structure and function. Despite several well-established P450 functions, new structures of P450s are published frequently, with the P450-redox partner fusion systems being among the most discussed, due to their enhanced activity and biotechnological potential. Other, more intriguing, P450-fusions involve partners with functions distinct from electron transfer. Understanding why evolution drove the ‘partner’ proteins to evolve into a single unit is often unclear, but provides an im

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22

Robinson, Jacob. "Characterisation of novel cytochrome P450 fusion systems." Thesis, University of Manchester, 2010. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-of-novel-cytochrome-p450-fusion-systems(5b0847b2-8a5d-427d-9434-11a50f24311c).html.

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The biophysical and spectroscopic characterisation of two novel P450 fusion enzymes is reported. The first of these is CYP102A3, which is a fusion of P450 haem and cytochrome P450 reductase (CPR)-like domains and functions as a catalytically self-sufficient fatty acid hydroxylase in its host organism Bacillus subtilis. The elucidation of structural aspects of the isolated haem domain of CYP102A3 (HDCYP102A3) is described. This reveals a strong homology between HDCYP102A3 and the haem domain of the related, well studied enzyme CYP102A1 (known as BM3). Examination of the substrate binding and re

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23

Cirino, Patrick Carmen Arnold Frances Hamilton. "Laboratory evolution of cytochrome P450 peroxygenase activity /." Diss., Pasadena, Calif. : California Institute of Technology, 2004. http://resolver.caltech.edu/CaltechETD:etd-06062003-164310.

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24

Fraser, David John 1968. "Isolation and characterization of cytochrome P450 3A26." Diss., The University of Arizona, 1998. http://hdl.handle.net/10150/288850.

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The objective of these studies was to isolate and characterize novel members of the 3A subfamily of canine cytochromes P450. This subfamily is of interest due to the wide range of endogenous and exogenous compounds metabolized. Previous studies led to the identification, isolation, and heterologous expression of 3A12, the major P450 form in canine liver. This enzyme demonstrated the ability to metabolize steroidal compounds and macrolide antibiotics in reconstituted systems. However, several lines of evidence suggested the presence of additional 3A enzymes with different substrate specificitie

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25

Koenigs, Luke L. "Mechanism-based inactivation of P450 /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/8150.

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26

Perrin, Rachel. "Caractérisation de deux sous-familles d'isoenzymes du cytochrome p450 impliquées dans le métabolisme des xénobiotiques dans le cerveau." Nancy 1, 1991. http://www.theses.fr/1991NAN10462.

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27

Porro, Cristina Shino. "Quantum mechanical/molecular mechanics studies of Cytochrome P450BM3." Thesis, University of Manchester, 2011. https://www.research.manchester.ac.uk/portal/en/theses/quantum-mechanical--molecular-mechanics-studies-of-cytochrome-p450bm3(ad4255e7-b779-47a2-a2c5-8dbf6b603ca5).html.

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Cytochrome P450 (P450) enzymes are found in all kingdoms of life, catalysing a wide range of biosynthetic and metabolic processes. They are, in fact, of particular interest in a variety of applications such as the design of agents for the inhibition of a particular P450 to combat pathogens or the engineering of enzymes to produce a particular activity. Bacterial P450BM3 is of particular interest as it is a self-sufficient multi-domain protein with high reaction rates and a primary structure and function similar to mammalian isoforms. It is an attractive enzyme to study due to its potential for

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28

Liu, Kang-Cheng. "Influence of lipid membrane environment on the kinetics of the cytochrome P450 reductase- cytochrome P450 3A4 enzyme system in nanodiscs." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/influence-of-lipid-membrane-environment-on-the-kinetics-of-the-cytochrome-p450-reductase-cytochrome-p450-3a4-enzyme-system-in-nanodiscs(b8ee4e84-1230-40cf-9b98-b5d6f457f54c).html.

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The cytochrome P450 enzyme system is a multicomponent electron-transfer chain composed of a haem-containing monooxygenase cytochrome P450 (CYP) and one or more redox partners. Eukaryotic CYPs and their redox partner NADPH-dependent cytochrome P450 oxidoreductase (CPR) are involved in many biological processes. Each protein has one N- terminal membrane anchor domain for location within the endoplasmic reticulum (ER). In mammals, CYPs and CPR are especially abundant in liver cells, where they play important roles in the metabolism of steroids, fatty acids, and xenobiotic compounds including nume

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29

Diaz, Dominique. "Induction des cytochromes P450 par l'omeprazole : étude en culture primaire d'hépatocytes humains et résultats in vivo." Montpellier 1, 1989. http://www.theses.fr/1989MON11078.

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30

Marques-Soares, Cristina. "Topologie des sites actifs des cytochromes P450 2C8 et 2C9 de foie humain : étude de leur spécificité de substrats et utilisation de la structure RX du CYP 2C5 comme référence." Paris 11, 2002. http://www.theses.fr/2002PA112285.

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Pour étudier la topologie des sites actifs des CYP 2C9 et 2C8 humains, nous sommes partis de la première structure RX résolue d'un cytochrome P450 membranaire, le CYP 2C5 de lapin, fortement homologue aux CYP 2C humains. Nous avons tout d'abord construit un modèle 3D du CYP 2C9 par mutagenèse virtuelle du CYP 2C5. Ce travail ainsi qu'une étude de mutants du CYP 2C9 nous ont permis de souligner l'importance de certains résidus du CYP 2C9 dans sa reconnaissance et son oxydation des substrats. Dans un deuxième temps, nous avons élaboré de même un modèle 3D du CYP 2C8, tout en construisant indépen

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31

Hukkanen, J. (Janne). "Xenobiotic-metabolizing cytochrome P450 enzymes in human lung." Doctoral thesis, University of Oulu, 2000. http://urn.fi/urn:isbn:9514258649.

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Abstract The cytochrome P450 (CYP) enzyme system in human lung is an essential component in the pulmonary carcinogenicity of several inhaled xenobiotic compounds. The aim of this study was to elucidate the expression and regulation of xenobiotic-metabolizing CYP enzymes in human lung. To evaluate which of the two is a better surrogate cell model for lung tissue, the expression patterns of CYP enzymes in alveolar macrophages and peripheral blood lymphocytes were clarified by reverse transcriptase-polymerase chain reaction (RT-PCR) and compared to the expression in lung tissue. The pat

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32

Westlind, Johnsson Anna. "Pharmacogenetics of human cytochrome P450 3A (CYP3A) enzymes /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-688-x.

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33

Hu, Yin. "Genetic polymorphism and regulation of cytochrome P450 2E1 /." Stockholm, 1999. http://diss.kib.ki.se/1999/91-628-3690-0.

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34

Dapkūnas, Justas. "Computational modeling of cytochrome P450-mediated drug metabolism." Doctoral thesis, Lithuanian Academic Libraries Network (LABT), 2011. http://vddb.laba.lt/obj/LT-eLABa-0001:E.02~2011~D_20111003_114651-54627.

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The main objective of this study was the development of QSAR models for drug metabolism-related properties. Novel GALAS (Global, Adjusted Locally According to Similarity) modeling method was used, which is a combination of baseline global QSAR model and local similarity based corrections. GALAS modeling method allows forecasting the reliability of prediction thus defining the model applicability domain. Models predicting CYP3A4 inhibition and regioselectivity of metabolism in human liver microsomes were developed and validated using external test sets. In all cases the baseline models already

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35

Harvey, Joanna Louise. "The induction of cytochrome P450 1A1 by metyrapone." Thesis, Queen Mary, University of London, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300578.

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36

Fairhead, Michael James. "Construction of human/bacterial cytochrome P450 fusion proteins." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408140.

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37

Fan, Ming Qi. "Studies of the structure of cytochrome P450 4A1." Thesis, University of Nottingham, 2002. http://eprints.nottingham.ac.uk/10400/.

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Cytochrome P450 4A1 (CYP4A1) is involved in omega-hydroxylation of fatty acids and eicosanoids. The resulting metabolites may have physiological activities such as regulation of blood pressure. In order to identify structural determinants of substrate binding, site-directed mutagenesis was used. According to a model of CYP4A1, the residues K93, R87 and N116 were predicted to respond to substrate binding. To test the hypothesis, we designed a series of mutants, K93E, R87E, R87E/K93E, R87W/K93E, N116E and N116E/K93E, which would change the substrate specificity of CYP4A1 from a fatty acid to a f

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38

Caprotti, Domenico. "Control of electron transfer in cytochrome p450 enzymes." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509901.

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39

Tan, Hoon Leong. "Selective inhibitors of the cytochrome p450 enzyme CYP1B1." Thesis, De Montfort University, 2006. http://hdl.handle.net/2086/4295.

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The cytochrome P450 CYP1 ezymes, CYP1A1, CYP1A2 and CYP1B1, are members of the cytochrome P450 superfamily which catalyse the oxidative metabolism of a wide range of endogenous and exogenous compounds. CYP1B1 is highly overexpressed in different malignancies but not in the corresponding normal tissues. This significant discovery has provided an opportunity to develop tumour specific intracellular activated anticancer prodrugs, using CYP1B1 as molecular target. As part of the continuing CYP1B1 activated anticancer prodrugs discovery programme at Leicester School of Pharmacy, this research was s

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40

Ridd, Thomas Ian. "Reactions and ligand binding properties of cytochrome P450." Thesis, University of Surrey, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308553.

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41

Corcionivoschi, Nicolae. "A novel cytochrome P450 from Campylobacter jejuni 11168." Thesis, University of Edinburgh, 2005. http://hdl.handle.net/1842/13463.

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<i>Campylobacter jejuni</i> is the most commonly recognized cause of bacterial gastroenteritis in man and also infects cattle, sheep and poultry. Publishing of the genome sequence of <i>Campylobacter jejuni 11168</i> (Parkhill, 2000) revealed the presence of only one cytochrome P450. Its coding sequence (Cj411c) is located in an operon involved in sugar and cell surface biosynthesis. The gene name is Cj1411c, is 1359 bp long and encodes 453 aa. The sequence is strictly conserved in <i>Campylobacter jejuni</i> RM221. Recombinant P450 was expressed in <i>E. coli</i> and showed the 450 nm peak in

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42

Joyce, Michael Gordon. "Structural studies of cytochrome P450 BM3 and CprK." Thesis, University of Leicester, 2005. http://hdl.handle.net/2381/29702.

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This work presents the crystal structure determination of the transcriptional regulator CprK and of individual domains of the multidomain cytochrome P450-BM3. The crystal structure of the A264E mutant heme domain was determined with and without substrate present. Surprisingly, the structures reveal the protein to exhibit a substrate bound conformation regardless of the presence of substrate. This has provided further evidence that substrate binding leads to a dramatic shift in the equilibrium of conformational states available to the protein. In addition, the crystal structure of the C773A mut

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43

Urata, Kouji. "Hydrogen-driven hydrocarbon oxidation by cytochrome P450 enzymes." Thesis, University of Oxford, 2017. https://ora.ox.ac.uk/objects/uuid:d5ec728a-2aa8-4040-92b0-56dad59e6dc4.

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P450<sub>BM3</sub> (CYP102A1) from Bacillus megaterium is a 119 kDa, 1,046-residue polypeptide with the FAD/FMN reductase domain fused to the C-terminus of the haem domain and, as such it is catalytically self-sufficient; only NADPH and oxygen are required for monooxygenase activity. P450<sub>BM3</sub> is a sub-terminal fatty acid hydroxylase, but generations of CYP102A1 engineering allowed them to be used in, e.g. drug metabolism and alkane oxidation. This thesis describes protein engineering of P450BM3 and altering reaction conditions to enhance C<sub>1</sub> â C<sub>8</sub> alkane oxidati

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44

Razalan, Maria Magdalena. "Mining the Arabidopsis genome for cytochrome P450 biocatalysts." Thesis, University of York, 2016. http://etheses.whiterose.ac.uk/16839/.

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Cytochromes P450 (CYPs) constitute a wide group of NAD(P)H-dependent monooxygenases, found throughout all kingdoms of life. Among the most important functions of CYPs are the synthesis of bioactive compounds and the conversion of xenobiotics. These functions can be translated into biotechnological applications, such as the production of highly regio- and stereo-specific drug metabolites for the pharmaceutical industry, or to confer activity towards toxic compounds for agronomics and bioremediation purposes. Plants possess a large number of CYP sequences, but most still remain uncharacterised,

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45

Leishman, Amy G. "Cytochrome P450, CYP3 in the human fetal liver." Thesis, University of Aberdeen, 1991. http://digitool.abdn.ac.uk/R?func=search-advanced-go&find_code1=WSN&request1=AAIU045930.

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Previous work (Barnes et al, 1989) suggested that a different major im-munorelated form of CYP3 existed in adult and fetal human liver. Northern blot analysis was conducted, therefore, using an adult CYP3 cDNA probe, to determine how similar the fetal CYP3 messenger RNA species was to the adult. Two major messenger RNA species of similar length (2.1kb and 3.0kb) in both the adult and fetal liver were observed, indicating a high degree of homology between the two. A human fetal cDNA expression library in Agtll was prepared and screened using both an adult cDNA probe and monoclonal antibodies ra

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46

Kelly, Paul. "Engineering cytochrome P450-reductase fusion enzymes for biocatalysis." Thesis, University of Manchester, 2014. https://www.research.manchester.ac.uk/portal/en/theses/engineering-cytochrome-p450reductase-fusion-enzymes-for-biocatalysis(c4b3aa48-1c73-4980-b480-e3a881267ee5).html.

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Cytochromes P450 (P450s) are a superfamily of heme-thiolate monooxygenases. They catalyse a wide variety of reactions on a vast number of substrates and are of particular interest for biocatalyst development due to their ability to oxidise non-activated C-H bonds. Fusion of a P450 to a suitable redox partner protein produces a catalytically self-sufficient enzyme and removes the need to produce electron transfer proteins separately. The well-studied bacterial protein P450cam (Pseudomonas putida) has been fused to the reductase (RhFRed) from the natural fusion protein P450-RhF (Rhodococcus sp.)

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47

Aoyama, Ronald Gordon. "Probing the active site of cytochrome P450 CYP2C9 /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/8188.

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48

Quesnot, Nicolas. "Évaluation de la génotoxicité des contaminants environnementaux, production de lignées bio-senseurs et mesure de l'activité enzymatique du cytochrome P450 2E1 dans les cellules d'hépatome humain HepaRG." Thesis, Rennes 1, 2015. http://www.theses.fr/2015REN1B005/document.

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L'exposition humaine aux contaminants environnementaux est inévitable du fait de leur présence dans l'eau, l'air et l'alimentation. La plupart d'entre eux sont reconnus comme étant mutagènes et/ou carcinogènes chez l'animal mais ils sont souvent seulement suspectés de l'être chez l'Homme. Le manque de connaissance vis-à-vis des substances chimiques a conduit l'UE à lancer le programme REACH avec l'objectif d'évaluer la toxicité d'environ 30 000 molécules. Cette évaluation nécessiterait l'utilisation de plus de 4 millions d'animaux et la pertinence controversée de ces modèles pourrait aboutir à

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Zhao, Jin 1975. "Investigations of the biocatalytic activity of human P450 2D6." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111940.

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Abstract:

The cytochrome P450 enzymes (CYPs) are very attractive biocatalysts because of their ability to regio- and stereo-selectively catalyze the insertion of a single atom of molecular oxygen into inactivated C-H bonds. There are many drawbacks, however, limiting the use of these enzymes in organic synthesis, including the need for expensive cofactors, low stability, and low tolerance to organic solvents. The goal of this thesis was to overcome some of these drawbacks for human CYP2D6. This isoform was selected because of its broad substrate promiscuity and high importance in drug metabolism.<br>We

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Stahl, Gunther. "Entwicklung von Homologie-Modellen der Cytochrome P450 2A5 und 2A6." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964988984.

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