Literatura académica sobre el tema "CYP3A4"
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Artículos de revistas sobre el tema "CYP3A4"
Sun, Jie-Yu, Ze-Jun Xu, Fang Sun, Hui-Lei Guo, Xuan-Sheng Ding, Feng Chen y Jing Xu. "Individualized Tacrolimus Therapy for Pediatric Nephrotic Syndrome: Considerations for Ontogeny and Pharmacogenetics of CYP3A". Current Pharmaceutical Design 24, n.º 24 (8 de noviembre de 2018): 2765–73. http://dx.doi.org/10.2174/1381612824666180829101836.
Texto completoNiwa, Toshiro, Kanae Narita, Ayaka Okamoto, Norie Murayama y Hiroshi Yamazaki. "Comparison of Steroid Hormone Hydroxylations by and Docking to Human Cytochromes P450 3A4 and 3A5". Journal of Pharmacy & Pharmaceutical Sciences 22 (24 de julio de 2019): 332–39. http://dx.doi.org/10.18433/jpps30558.
Texto completoKamdem, Landry K., Frank Streit, Ulrich M. Zanger, Jürgen Brockmöller, Michael Oellerich, Victor W. Armstrong y Leszek Wojnowski. "Contribution of CYP3A5 to the in Vitro Hepatic Clearance of Tacrolimus". Clinical Chemistry 51, n.º 8 (1 de agosto de 2005): 1374–81. http://dx.doi.org/10.1373/clinchem.2005.050047.
Texto completoMaruf, AA, MU Ahmed, M. A. K. Azad, M. Ahmed y A. Hasnat. "CYP3A Genotypes in Bangladeshi Tuberculosis Patients". Bangladesh Medical Research Council Bulletin 38, n.º 1 (22 de abril de 2012): 1–5. http://dx.doi.org/10.3329/bmrcb.v38i1.6978.
Texto completoKlees, Theresa Mariero, Pamela Sheffels, Kenneth E. Thummel y Evan D. Kharasch. "Pharmacogenetic Determinants of Human Liver Microsomal Alfentanil Metabolism and the Role of Cytochrome P450 3A5". Anesthesiology 102, n.º 3 (1 de marzo de 2005): 550–56. http://dx.doi.org/10.1097/00000542-200503000-00012.
Texto completoLeskelä, S., E. Honrado, C. Montero-Conde, I. Landa, A. Cascón, R. Letón, P. Talavera et al. "Cytochrome P450 3A5 is highly expressed in normal prostate cells but absent in prostate cancer". Endocrine-Related Cancer 14, n.º 3 (septiembre de 2007): 645–54. http://dx.doi.org/10.1677/erc-07-0078.
Texto completoRaymond, Lendelle, Nikita Rayani, Grace Polson, Kylie Sikorski, Ailin Lian y Melissa A. VanAlstine-Parris. "Determining the IC50 Values for Vorozole and Letrozole, on a Series of Human Liver Cytochrome P450s, to Help Determine the Binding Site of Vorozole in the Liver". Enzyme Research 2015 (9 de noviembre de 2015): 1–4. http://dx.doi.org/10.1155/2015/321820.
Texto completoChang, Thomas KH y Rosita KY Yeung. "Effect of trans-resveratrol on 7-benzyloxy-4-trifluoromethylcoumarin O-dealkylation catalyzed by human recombinant CYP3A4 and CYP3A5". Canadian Journal of Physiology and Pharmacology 79, n.º 3 (1 de marzo de 2001): 220–26. http://dx.doi.org/10.1139/y00-130.
Texto completoBořek-Dohalská, Lucie y Marie Stiborová. "Cytochrome P450 3A activities and their modulation by α-naphthoflavone in vitro are dictated by the efficiencies of model experimental systems". Collection of Czechoslovak Chemical Communications 75, n.º 2 (2010): 201–20. http://dx.doi.org/10.1135/cccc2009525.
Texto completoFang, Jim y Jiuxue Song. "In vitro Characterization of the Oxidation of a Pyridinium Metabolite of Haloperidol by Human Placenta: The Effect of Smoking". Journal of Pharmacy & Pharmaceutical Sciences 15, n.º 4 (4 de octubre de 2012): 538. http://dx.doi.org/10.18433/j31w20.
Texto completoTesis sobre el tema "CYP3A4"
Sethabouppha, Benjabhorn. "Inter-Individual Variation in CYP3A4 and CYP3A5- Mediated Drug Metabolism". Thesis, University of Manchester, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.492887.
Texto completoWillrich, Maria Alice Vieira. "Efeitos de hipolipemiantes sobre a expressão de CYP3A4 e CYP3A5 in vitro e in vivo". Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-12092012-150610/.
Texto completoBackground: CYP3A4 and CYP3A5 are enzymes from the cytochrome P450 resposible for the biotransformation of endogenous steroids and several drugs, e.g. statins. Polymorphisms in CYP3A4 and CYP3A5 (CYP3A4*1B, CYP3A5*3C and CYP3A5*1D) have been associated with variation of lipid-lowering response in individuals treated with atorvastatin and simvastatin. In this study we evaluated the effect of hypolipemiants on expression and activity of CYP3A4 and CYP3A5, in HepG2 and Caco-2 cell lines as well as peripheral blood mononuclear cells (PBMC) in hypercholesterolemic individuals, and their relationship with CYP3A4 and CYP3A5 variants. Methods: We analyzed 99 normolipidemic individuals (NL) and 139 hypercholesterolemic (HC). HC subjects were treated with atorvastatin (HC, 10 mg/day/4 weeks). Analysis of CYP3A4*1B, CYP3A5*3C e CYP3A5*1D variants was performed with PCR-RFLP or sequencing assays and mRNA expression of CYP3A4 and CYP3A5 with Quantitative Real-time PCR (qRT-PCR) was performed . Total protein content was extracted from HepG2 for Western Blotting experiments. Activity of CYP3A4 and CYP3A5 in vivo was evaluated by 6βOH-cortisol and cortisol ratio in urine samples, by HPLC-UV method. Results: Baseline mRNA expression is different for HepG2 and Caco-2. Caco-2 expresses 31 times more CYP3A4 and 122 times more CYP3A5 than HepG2. In HepG2 cells treated for 12h, atorvastatin 20 µM increased CYP3A4 expression in 10 times, when compared to the control (p=0.006). After 24h treatment, atorvastatin (1-20 µM) increased CYP3A4 mRNA expression in 5 to 8 times, in HepG2 (p< 0.001). To CYP3A5, exposure for 12h to atorvastatin 20 µM increased expression in 4 times when compared to the control (p<0.001). Exposure to simvastatin 1.0 µM for 24 h increased CYP3A4 expression in 2 times, (p<0.01), in HepG2. With the 24h treatment,simvastatin (0.1 µM - 10 µM) CYP3A5 showed increased mRNA expression in 2 to 4 times (p<0.05). HepG2 cell line carries homozygous functional alleles (CYP3A4*1A e CYP3A5*1A). Caco-2 carries heterozygous CYP3A5*3C and CYP3A5*1D. We evaluated the protein expression of CYP3A4 and CYP3A5 with Western Blotting in HepG2 cells, after atorvastatin (0.1 - 20 µM) and simvastatin (0.01 - 10 µM) for 12 and 24 h. The proteins profile did not change with statins treatment. In PBMC, baseline mRNA expression of CYP3A4 is approximately 2.6 to 9.5 times higher than CYP3A5 (p< 0.05). There was a correlation in expression between CYP3A4 and CYP3A5, before (r2 = 0.22; p< 0.0001) and after treatment (r2 = 0.58; p<0.0001) with atorvastatin. Baseline mRNA expression of CYP3A4 and CYP3A5 is higher in (NL) than in (HC) (p<0.05). Atorvastatin treatment did not increase CYP3A4 and CYP3A5 mRNA in PBMC (p>0.05). CYP3A4/5 activity was higher in NL subjects than in HC (p<0.0001). Atorvastatin treatment did not affect CYP3A4/5 activity in HC (p>0.05). The studied variants CYP3A4*1B, CYP3A5*3C e CYP3A5*1D analyzed as a haplotype block did not affect response to treatment, mRNA expression or activity of CYP3A4 and CYP3A5. However, AGT haplotype showed lower CYP3A5 mRNA expression levels when compared to GAC and GAT haplotypes at baseline (p<0.05). Conclusion: The results of this study allow us to conclude that atorvastatin and simvastatin, but not ezetimibe, influence the expression of CYP3A4 and CYP3A5 mRNA in vitro in HepG2 cell line, but this effect was not reproduced in Caco-2 cell line or PBMC. CYP3A4 and CYP3A5 present great interindividual variability, despite the individual´s haplotype and is not influenced by atorvastatin.
Ciaccia, Antonio. "Investigation of the interindividual variability in hepatic cytochrome P450 CYP3A4, association with CYP3A4*1B". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape9/PQDD_0004/MQ46139.pdf.
Texto completoTomlinson, Emma Suzanne. "Dexamethasone as a probe for CYP3A4". Thesis, University of Liverpool, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337128.
Texto completoEl-Sankary, Wafaa Mahmoud. "Regulation of the human CYP3A4 gene". Thesis, University of Surrey, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326904.
Texto completoAl-Shakargi, Bilall. "Variationer i allelfrekvens hos cytokrom-generna;CYP3A4*1B, CYP3A5*3 och CYP2B6*6 mellan Uganda och Tanzania". Thesis, Uppsala universitet, Institutionen för farmaceutisk biovetenskap, 2019. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-388608.
Texto completoBombail, Vincent. "Transcriptional control of the human CYP3A4 gene". Thesis, University of Surrey, 2003. http://epubs.surrey.ac.uk/843500/.
Texto completoKluth, Dirk. "Vom Antioxidanz zum Genregulator : transkriptionelle Regulation von Phase I- und Phase II-Enzymen durch Vitamin E und antioxidative sekundäre Pflanzeninhaltsstoffe". Phd thesis, Universität Potsdam, 2006. http://opus.kobv.de/ubp/volltexte/2006/1006/.
Texto completoDer Einfluss von verschiedenen Vitamin E-Formen und antioxidativen Pflanzeninhaltsstoffen in Form von Reinsubstanzen (Curcumin, EGCG, Medox, Quercetin, Resveratrol und Sulforaphan) oder Pflanzenextrakten (aus Blaubeeren, Gewürznelken, Himbeeren, Nelkenpfeffer, Thymian oder Walnüssen) auf die Aktivierung von PXR und Nrf2 sowie des Promotors eines jeweiligen Zielgens (CYP3A4 bzw. GI-GPx) wurde in vitro mit Reportergenplasmiden untersucht. Es zeigte sich, dass sowohl Vitamin E-Formen als auch verschiedene sekundäre Pflanzeninhaltsstoffe PXR und/oder Nrf2 sowie die Promotoren der jeweiligen Zielgene CYP3A4 bzw. GI-GPx aktivieren. In einem Tierexperiment konnte diese genregulatorische Wirkung von Vitamin E auf die in vivo-Situation übertragen werden. In Lebern von Mäusen, deren Futter unterschiedliche Mengen von Vitamin E enthielt (Mangel-, Normal- und Überflussdiät), wurde eine direkte Korrelation zwischen der alpha-Tocopherol-Konzentration und der Cyp3a11 mRNA-Expression nachgewiesen (Cyp3a11 ist das murine Homolog zum humanen CYP3A4). Entgegen der in vitro-Situation hatte gamma-Tocotrienol in vivo einen nur kaum nachweisbaren Effekt auf die Expression der Cyp3a11 mRNA, induzierte aber die Expression der alpha-TTP mRNA. Es konnte gezeigt werden, dass Vitamin E und sekundäre Pflanzeninhaltsstoffe Phase I- und Phase II-Enzyme transkriptionell regulieren können.
Die Wirkungen des Vitamin E können sich allerdings nur entfalten, wenn die Vitamin E-Formen ausreichend vom Körper aufgenommen werden. Gegenstand der Dissertation waren daher auch Untersuchungen zur Bioverfügbarkeit (zelluläre Akkumulation und Metabolismus) verschiedener Vitamin E-Formen. Es konnte gezeigt werden, dass Unterschiede in der chemischen Struktur der Vitamin E-Formen deren zelluläre Akkumulation und Metabolisierung beeinflussen.
Unter Berücksichtigung der Ergebnisse der Dissertation lassen sich protektive Wirkungen von antioxidativen Nahrungsinhaltsstoffen auch unabhängig von ihren antioxidativen Eigenschaften über die Induktion zelleigener Schutzsysteme, einschließlich der Phase I- und Phase II-Enzyme, erklären. Die Induktion der zelleigenen Abwehr lässt sich auch als adaptive Antwort (sog. "adaptive response") des Organismus gegenüber zellschädigenden Ereignissen betrachten.
In the organism food compounds are involved in regulatory and metabolic processes although the mechanisms of their effects have not been completely elucidated yet. Like vitamin E, secondary plant compounds have diverse biological effects, both in cell systems as well as in vivo. However, the explanation thereof is often reduced to their antioxidative capacity. The aim of this thesis was to investigate the influence of vitamin E and other plant compounds (in form of plant extracts or isolated secondary plant compounds, e.g. polyphenols), which were up to now classified primarily as antioxidants, on the transcription of phase I- and phase II-enzymes. For this, the activation of central transcription factors of the phase I- or phase II enzymes, PXR (pregnane X receptor) and Nrf2 (NF-E2-related factor-2), was tested.
The influence of different vitamin E forms and antioxidative plant compounds in form of pure substances (curcumin, EGCG, Medox, quercetin, resveratrol, and sulforaphane) or plant extracts (from blueberries, clove, raspberries, allspice, thyme, or walnuts) on the activation of PXR and Nrf2 as well as on the promoter of a respective target gene (CYP3A4 or GI-GPx) was investigated in vitro by reporter gene assays. It appeared that vitamin E forms as well as different secondary plant compounds activate PXR and/or Nrf2 as well as the promoter of the respective target genes CYP3A4 and GI-GPx. The effects of vitamin E were confirmed in vivo by an animal experiment. In livers of mice whose diet contained different amounts of vitamin E (deficient, adequate and supra-nutritional), a direct correlation between alpha-tocopherol content and Cyp3a11 mRNA expression was shown (Cyp3a11 is the murine homolog to the human CYP3A4). In contrast to the in vitro observations, gamma-tocotrienol in vivo only had a small effect on the expression of Cyp3a11 mRNA. However, it induced the expression of alpha-TTP on mRNA level. It could be shown that vitamin E and secondary plant compounds can influence the transcriptional regulation of phase I- and/or phase II-enzymes.
However, these effects of vitamin E can only be seen if the vitamin E forms are taken up by the body sufficiently. Therefore, another aim of the thesis was to investigate the bioavailability of different vitamin E forms (i.e., cellular accumulation and metabolism). It could be shown that differences in the chemical structure of vitamin E forms influence their cellular accumulation and metabolism.
Regarding the results of this thesis, protective effects of antioxidative food compounds can be explained independent of their antioxidative properties by the induction of cellular protective systems, including phase I- and phase II-enzymes. The induction of cellular defence mechanism can also be considered as an adaptive response of the organism towards cell-damaging events.
Gratien-Debette, Marilyne. "Etude rétrospective de l'influence des polymorphismes génétiques de CYP3A4, CYP3A5 et ABCB1 des donneurs et des receveurs sur les effets des immunosuppresseurs en transplantation hépatique". Thesis, Limoges, 2015. http://www.theses.fr/2015LIMO0032/document.
Texto completoLiver transplantation is now a well mastered surgery with standardized procedures, but the long-term clinical outcomes of the graft and the patient remain uncertain. The pharmacogenetic study of the calcineurin inhibitors (CNI) cyclosporine and tacrolimus should help to understand the variability of their pharmacokinetics and therapeutic or side effects. In the first part of this work, we reviewed the main pharmacogenetic studies of CNI in liver transplantation, focusing on the three polymorphisms mostly involved in CNI pharmacokinetics (CYP3A4*22, CYP3A5*3 et ABCB1 exons 12, 21, 26) and their possible associations with clinical outcomes. To date, the only pharmacogenetic test consensually recommended in organ transplantation is the CYP3A5*3 variant for a better selection of the initial tacrolimus dose in kidney transplantation. The second part of this work was a retrospective cohort study in liver transplantation to investigate the influence of the above mentioned donor’s and recipient’s genotypes, involved in the metabolism (CYP3A4*22, CYP3A5*3) and the membrane transport (ABCB1 exons 12, 21 and 26) of cyclosporine and tacrolimus. 170 patients were enrolled in this study with a mean follow-up of more than ten years. Our main results are that: the recipient CYP3A5*1 allele was associated with a higher risk of graft loss than the CYP3A5*3 allele; the recipient ABCB1 exon 12 TT genotype was associated with a lower risk of chronic rejection than the CC genotype; overexposure to CNI, initial renal function and recipient age were associated with a higher risk of post-transplantation renal dysfunction. No genetic factor was associated with patient survival, acute rejection, liver function tests, recurrence of viral or other initial liver disease, or nephrotoxicity. Prospective characterization of both recipient and donor CYP3A4, CYP3A5 and ABCB1 polymorphisms could help to optimize immunosuppressive therapy for each candidate to liver transplantation. Further studies (pharmacogenetics of calcineurin pathway, early biomarkers of graft dysfunction, ...), should help to define a personalized profile for each transplant patient in order to best adapt the immunosuppressive strategy on the long term
Nem, Dieudonné [Verfasser]. "In vivo and in vitro investigation of the tissue-specific activity of the human CYP3A4 and CYP3A5 promoters / Dieudonné Nem". Mainz : Universitätsbibliothek Mainz, 2012. http://d-nb.info/1019667125/34.
Texto completoLibros sobre el tema "CYP3A4"
Pastrakuljic, Aleksandra. In vitro activities associated with CYP1A1 and CYP1A2 in normal human liver specimens. Ottawa: National Library of Canada, 1996.
Buscar texto completoMerle, Olivier. A 13CO2 breath test for cytochrome P450 CYP3A based on tamoxifen N-demethylation. Leicester: De Montfort University, 1999.
Buscar texto completoZhou, Yang Thomas. Assessment of caffeine as a probe for CYP1A2 activity. Ottawa: National Library of Canada, 1995.
Buscar texto completoGoodz, Shari D. Investigating aspects of CYP2A6 in Caucasian and African American smokers. Ottawa: National Library of Canada, 2002.
Buscar texto completoZeman, Marilyn Vera. evaluation of coumarin as an in vivo measure of CYP2A6 activity. Ottawa: National Library of Canada, 1998.
Buscar texto completoAndreou, Efrosini Roseann. Analysis of CYP7A1 gene regulation in HepG2 cells by reverse-transcriptase polymerase chain reaction. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.
Buscar texto completoDortok, E. Desiree. Analysis of the possible therapeutic use of CYP2A6 inhibition with methoxsalen in smoking cessation. Ottawa: National Library of Canada, 2001.
Buscar texto completoNowak, Maciej P. Comparison of polymorphic CYP2D6, CYP2C19 and CYP2A6 in Canadian Native Indian, Caucasian and Chinese populations. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.
Buscar texto completoChart, Thomas E. Flow effects on humpback chub (Gila cypha) in Westwater Canyon / Thomas E. Chart and Leo Lentsch. Moab, Utah: Utah Divison of Wildlife Resources, Moab Native Fishes Field Office, 1999.
Buscar texto completoInvestigation of the interindividual variability in hepatic cytochrome P450 CYP3A4: Association with CYP3A4*1B. Ottawa: National Library of Canada, 1999.
Buscar texto completoCapítulos de libros sobre el tema "CYP3A4"
DeCou, Jennifer, Nathaniel Birgenheier y Randal O. Dull. "CYP3A4: The Workhorse". En A Case Approach to Perioperative Drug-Drug Interactions, 37–40. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_7.
Texto completoChen, Yuan y Adrian J. Fretland. "Evaluation of Time-Dependent CYP3A4 Inhibition Using Human Hepatocytes". En Methods in Pharmacology and Toxicology, 269–79. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_16.
Texto completoSinz, Michael W. "Avoiding PXR and CAR Activation and CYP3A4 Enzyme Induction". En Topics in Medicinal Chemistry, 159–90. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/7355_2013_24.
Texto completoZhang, J. George y David M. Stresser. "Assessment of CYP3A4 Time-Dependent Inhibition in Plated and Suspended Human Hepatocytes". En Methods in Pharmacology and Toxicology, 255–68. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_15.
Texto completoTakahashi, Kyoko, Hideyasu Matsuda, Kayoko Kinoshita, Norikazu Matsunaga, Akihiko Sumita, Takahisa Matsuda, Koichi Takahashi y Junichi Azuma. "Modulation of Taurine on CYP3A4 Induction by Rifampicin in a HepG2 Cell Line". En Advances in Experimental Medicine and Biology, 237–44. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0077-3_30.
Texto completoErratico, Claudio A., Anand K. Deo y Stelvio M. Bandiera. "Regioselective Versatility of Monooxygenase Reactions Catalyzed by CYP2B6 and CYP3A4: Examples with Single Substrates". En Advances in Experimental Medicine and Biology, 131–49. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_5.
Texto completoLuu, Alice, Brian C. Foster, Kristina L. McIntyre, Teresa W. Tam y John T. Arnason. "Pharmacogenetics in Potential Herb–Drug Interactions: Effects of Ginseng on CYP3A4 and CYP2C9 Allelic Variants". En The Biological Activity of Phytochemicals, 59–65. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-7299-6_5.
Texto completoRoussel, Danielle, Emily Hagn y Randal O. Dull. "CYP1A2: The Switch-hitter". En A Case Approach to Perioperative Drug-Drug Interactions, 41–44. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-7495-1_8.
Texto completoMoorthy, Bhagavatula. "Chapter 3. The CYP1A Subfamily". En Issues in Toxicology, 97–135. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558428-00097.
Texto completoRaunio, Hannu, Jukka Hakkola y Olavi Pelkonen. "Chapter 5. The CYP2A Subfamily". En Issues in Toxicology, 150–77. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558428-00150.
Texto completoActas de conferencias sobre el tema "CYP3A4"
Georgiev, Kaloyan, Maya Radeva y Tamara Pajpanova. "Potent inhibition of CYP3A4 by the endomorphin-2analogues". En 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.283.
Texto completoPotter, David A., Zhijun Guo, Ranjana Mitra, Monica Milani, Mariangellys Rodriguez, Li Ding, Robin Bliss et al. "Abstract 357: CYP3A4 Activates Stat3 in ER + breast cancer". En Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-357.
Texto completoGeorgiev, Kaloyan, Maya Radeva, Anelia Balacheva, Sylvia Michaylova y Tamara Pajpanova. "Modulation of CYP3A4 by the RGD- and Neurotensin(8-13)-analogues". En 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.215.
Texto completoMooiman, Kim D., Roel F. M. Maas-Bakker, Jos H. Beijnen, Jan H. M. Schellens y Irma Meijerman. "Abstract 3791: Milk thistle as an inhibitor of PXR-mediated CYP3A4 induction". En Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3791.
Texto completoGorjala, Priyatham, Oscar Goodman Jr y Ranjana Mitra. "Abstract 1805: CYP3A4 regulation of androgen receptor signaling in ER+ breast cancer". En Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1805.
Texto completoGuo, Zhijun, Beverly Norris, Jonathan Henriksen, Monique Morgan, Michael Maher, Robert Schumacher, Robin Bliss et al. "Abstract 82: CYP3A4 promotes mammary carcinoma angiogenesis in a cell iIntrinsic fashion." En Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-82.
Texto completoAndrade, Carolina, Flávia Silva, Ekaterina Varlamova y Rodolpho Braga. "Development of QSAR models for identification of CYP3A4 substrates and inhibitors". En MOL2NET, International Conference on Multidisciplinary Sciences. Basel, Switzerland: MDPI, 2015. http://dx.doi.org/10.3390/mol2net-1-b034.
Texto completoAhmed, Atif, Hamid Zia, Graeme I. Murray, Carrie A. Vyhlidal, J. Steven Leeder y Marilyn M. Bui. "Abstract 415: Cytochrome CYP3A4 expression may predict metastasis in Ewing's sarcoma family of tumors." En Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-415.
Texto completoGuo, Zhijun, Ranjana Mitra, Monica Milani, Mariangellys Rodriguez, Douglas Yee, Deepali Sachdev y David A. Potter. "Abstract 2288: CYP3A4 monoxygenase regulates IGF-1 signaling in ER-positive breast cancer cells". En Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2288.
Texto completoChen, Yakun, Yong Tang, Gregory Thomas Robbins y Daotai Nie. "Abstract 2667: Inhibition of CYP3A4 expression by camptothecin via blocking activation of pregnane X receptor". En Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2667.
Texto completoInformes sobre el tema "CYP3A4"
Casabar, Richard C., Andrew D. Wallace, Ernest Hodgson y Randy L. Rose. Metabolism of Endosulfan-Alpha by Human Liver Microsomes and its Utility as a Simultaneous In Vitro Probe for CYP2B6 and CYP3A4. Fort Belvoir, VA: Defense Technical Information Center, marzo de 2006. http://dx.doi.org/10.21236/ada445178.
Texto completoDudley, A., M. M. Peden-Adams, J. E. Daly y D. E. Keil. JP-8 Jet Fuel Induces CYP2B1, CYP2BE1, and GSTPI but not CYP1A1 in Murine Liver. Fort Belvoir, VA: Defense Technical Information Center, marzo de 2001. http://dx.doi.org/10.21236/ada402064.
Texto completoLamb, Dolores J. Enhancement of Vitamin D Action in Prostate Cancer through Silencing of CYP24. Fort Belvoir, VA: Defense Technical Information Center, febrero de 2009. http://dx.doi.org/10.21236/ada502323.
Texto completoLamb, Dolores. Enhancement of Vitamin D Action in Prostate Cancer through Silencing of CYP24. Fort Belvoir, VA: Defense Technical Information Center, febrero de 2011. http://dx.doi.org/10.21236/ada550337.
Texto completoLamb, Dolores J. Enhancement of Vitamin D Action in Prostate Cancer through Silencing of CYP24. Fort Belvoir, VA: Defense Technical Information Center, febrero de 2010. http://dx.doi.org/10.21236/ada625333.
Texto completoLamb, Dolores J. Enhancement of Vitamin D Action in Prostate Cancer through Silencing of CYP24. Fort Belvoir, VA: Defense Technical Information Center, febrero de 2008. http://dx.doi.org/10.21236/ada482357.
Texto completoDraeger, E., B. Bennion, F. Gygi y F. Lightstone. Understanding the Mechanism of Human P450 CYP1A2 Using Coupled Quantum-Classical Simulations in a Dynamical Environment. Office of Scientific and Technical Information (OSTI), febrero de 2006. http://dx.doi.org/10.2172/899113.
Texto completoGoulet, C. T. y K. E. LaGory. Annotated bibliography for the humpback chub (Gila cypha) with emphasis on the Grand Canyon population. Office of Scientific and Technical Information (OSTI), octubre de 2009. http://dx.doi.org/10.2172/965762.
Texto completoCarlson, E. A., Y. Li y J. T. Zelikoff. Inhibition of CYP1A-Mediated Metabolism of Benzo(A)Pyrene (BAP): Effects Upon BAP-Induced Immunotoxicity in Japanese Medaka (Oryzias Latipes). Fort Belvoir, VA: Defense Technical Information Center, marzo de 2001. http://dx.doi.org/10.21236/ada402076.
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