Academic literature on the topic 'Nelfinavir'
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Journal articles on the topic "Nelfinavir"
Bergshoeff, Alina S., Tom FW Wolfs, Sibyl PM Geelen, and David M. Burger. "Ritonavir-Enhanced Pharmacokinetics of Nelfinavir/M8 during Rifampin Use." Annals of Pharmacotherapy 37, no. 4 (April 2003): 521–25. http://dx.doi.org/10.1345/aph.1c335.
Full text&NA;. "Nelfinavir." Reactions Weekly &NA;, no. 1200 (May 2008): 25. http://dx.doi.org/10.2165/00128415-200812000-00070.
Full textJarvis, Blair, and Diana Faulds. "Nelfinavir." Drugs 56, no. 1 (1998): 147–67. http://dx.doi.org/10.2165/00003495-199856010-00013.
Full textBardsley-Elliot, Anne, and Greg L. Plosker. "Nelfinavir." Drugs 59, no. 3 (March 2000): 581–620. http://dx.doi.org/10.2165/00003495-200059030-00014.
Full textPerry, Caroline M., James E. Frampton, Paul L. McCormack, M. Asif A. Siddiqui, and Risto S. Cvetkovi?? "Nelfinavir." Drugs 65, no. 15 (2005): 2209–44. http://dx.doi.org/10.2165/00003495-200565150-00015.
Full text&NA;. "Nelfinavir." Reactions Weekly &NA;, no. 788 (February 2000): 9. http://dx.doi.org/10.2165/00128415-200007880-00028.
Full text&NA;. "Nelfinavir." Reactions Weekly &NA;, no. 804 (June 2000): 10. http://dx.doi.org/10.2165/00128415-200008040-00026.
Full text&NA;. "Nelfinavir." Reactions Weekly &NA;, no. 814 (August 2000): 10. http://dx.doi.org/10.2165/00128415-200008140-00027.
Full text&NA;. "Nelfinavir." Drugs & Therapy Perspectives 10, no. 12 (December 1997): 7–9. http://dx.doi.org/10.2165/00042310-199710120-00003.
Full text&NA;. "Nelfinavir." Reactions Weekly &NA;, no. 733 (January 1999): 10–11. http://dx.doi.org/10.2165/00128415-199907330-00026.
Full textDissertations / Theses on the topic "Nelfinavir"
Hirt, Déborah. "Pharmacocinétique de population du nelfinavir." Paris 5, 2006. http://www.theses.fr/2006PA05P636.
Full textNelfinavir is a protease inhibitor used for AIDS treatment. This drug is metabolized by CYP2C19 to an active metabolite, M8. There is a high interindividual variability in nelfinavir and M8 plasma concentrations, with consequences on therapeutic efficacy. In four different publications, we analyzed variability factors of these concentrations thanks to population pharmacokinetics method: in pregnant women and women at delivery, in children and fetus and in adults with genetic polymorphism for the CYP2C19. Then, from the estimated individual pharmacokinetic parameters, we calculated minimal dose necessary to reach an effective concentration. When data concerning efficacy and toxicity were available, pharmacokinetic – pharmacodynamic relationships were studied. The results obtained permitted to give adapted doses recommendations
Hones, Stefanie. "Identifizierung und Regulation Nelfinavir-induzierter Peptidhormone." Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-160475.
Full textPortolan, Frédérique. "Recherche sur les antiviraux anti-VIH : synthèse des immunogènes de l'indinavir et du nelfinavir, mise au point des dosages radio-immunologiques de ces anti-protéases." Nice, 2001. http://www.theses.fr/2001NICE5624.
Full textHones, Stefanie [Verfasser], and Ioannis [Akademischer Betreuer] Mylonas. "Identifizierung und Regulation Nelfinavir-induzierter Peptidhormone / Stefanie Hones. Betreuer: Ioannis Mylonas." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2013. http://d-nb.info/1042147329/34.
Full textCristina, da Silva Monteiro Vandessa. "Tecnologia de obtenção de anti-retroviral à base de Mesilato de Nelfinavir." Universidade Federal de Pernambuco, 2005. https://repositorio.ufpe.br/handle/123456789/3507.
Full textOs Inibidores de protease (PI) constituem uma potente classe de drogas anti-retrovirais que mudou o tratamento e a evolução da infecção pelo HIV. Em março de 1997, um novo medicamento desta classe, o mesilato de nelfinavir foi aprovado pela Food and Drug Administration (FDA), sendo desde então, extensamente utilizado isoladamente ou em associação a Inibidores da Transcriptase Reversa (RTIs), obtendo-se considerável eficácia clínica no tratamento da AIDS. O mesilato de nelfinavir tem como produto de referência no mercado o Viracept®, fabricado pela indústria Roche. Esta medicação faz parte do coquetel anti-AIDS distribuído no Brasil, sendo usada por 25% dos pacientes. O presente trabalho tem como objetivo apresentar o desenvolvimento farmacotécnico-industrial de comprimidos revestidos de mesilato de nelfinavir 250 mg, baseado em uma planificação qualitativa e quantitativa dos excipientes, além da realização de testes de bancada visando à obtenção de uma forma farmacêutica com qualidade e baixo custo. Para tanto, realizou-se a caracterização da matéria-prima com vistas à qualificação de fornecedores, e executou-se o desenvolvimento da metodologia de dissolução para os comprimidos obtidos, além de estudo comparativo do seu perfil de dissolução frente ao medicamento de referência. O trabalho também contemplou o desenvolvimento e a validação da metodologia para doseamento da matéria-prima e produto acabado, por Cromatografia Líquida de Alta Eficiência (CLAE), obedecendo aos parâmetros estabelecidos na Resolução-RE n° 899, publicada em 02 de junho de 2003 pela Agência Nacional de Vigilância Sanitária (ANVISA). Também foi realizado um estudo comparativo entre o produto de referência Viracept® e o produto desenvolvido mesilato de nelfinavir LAFEPE®. Os comprimidos revestidos de mesilato de nelfinavir desenvolvidos apresentaram boa qualidade e as comparações efetuadas entre estes e o Viracept® não apresentaram diferenças significativas. Encontra-se em curso o estudo de estabilidade nos modelos acelerado e longa duração. Este estudo foi realizado em parceria com o Núcleo de Controle de Qualidade de Medicamentos e Correlatos, o Laboratório de Tecnologia dos Medicamentos, ambos do Departamento de Ciências Farmacêuticas da UFPE e o Laboratório Farmacêutico do Estado de Pernambuco (LAFEPE)
Chaworth-Musters, Tessa. "Plasma concentrations of nelfinavir and viral suppression in HIV-1 infected pregnant women." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/965.
Full textBatista, Rui. "Pharmacocinétique du nelfinavir chez des patients atteints de complications neurologiques dues au VIH-1." Paris 5, 1999. http://www.theses.fr/1999PA05P159.
Full textHOLANDA, Luiz Henrique Campos. "Análise conformacional da enzima protease do HIV-1 relacionada à resistência ao inibidor Nelfinavir." Universidade Federal do Pará, 2017. http://repositorio.ufpa.br/jspui/handle/2011/9249.
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CNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
O Vírus da imunodeficiência humana (HIV), causador da síndrome da imunodeficiência adquirida (AIDS), é um retrovírus que possui glicoproteínas altamente virulentas que invadem o linfócito TCD4+ através de seus receptores CCR4 e CXCR5. O ciclo biológico do HIV é mediado pelas enzimas protease, transcriptase e integrase. A HIV-1 protease é uma enzima que está presente na fase final do ciclo biológico, onde ocorre a maturação do vírus e é um importante alvo farmacológico. O objetivo principal deste projeto é verificar os efeitos das mutações D30N, I84A e M46I na enzima protease HIV-1 e na formação do complexo com o inibidor nelfinavir através de técnicas de dinâmica molecular e bioinformática. Os resultados baseados nas análises estruturais mostraram diferenças estruturais entre os sistemas estudados. O sistema 1OHR apresentou uma conformação fechada, os sistemas D30N e D30N_I84A_M46I apresentaram conformação semi-aberta e o sistema D30N_I84A apresentou conformação aberta, em que o último apresentou menor valor de energia livre e maior instabilidade nas análises de RMSD, porém a maior flutuação de resíduos de aminoácidos. As análises teóricas mostraram a importância na resistência da dupla mutação D30N_I84A e a capacidade de reestruturação conformacional da mutação M46I e capacidade catalítica.
The Human Immunodeficiency Virus (HIV), which causes acquired immunodeficiency syndrome (AIDS), is a retrovirus that has highly virulent glycoproteins that invade the CD4 + T lymphocyte through its CCR4 and CXCR5 receptors. The biological cycle of HIV is mediated by the protease, transcriptase and integrase enzymes. HIV-1 protease is an enzyme that is present in the final phase of the biological cycle, where virus maturation occurs, and is an important pharmacological target. The main objective of this project is to verify the effects of the D30N, I84A and M46I mutations on the HIV-1 protease enzyme and the complex formation with the nelfinavir inhibitor through molecular dynamics and bioinformatics techniques. The results based on the structural analyzes showed structural differences between the studied systems. The 1OHR system presented a closed conformation, the systems D30N and D30N_I84A_M46I presented semi-open conformation and the D30N_I84A system presented open conformation, in which the latter presented lower free energy value and greater instability in the RMSD analyzes, however the greater flotation of residues Of amino acids. The theoretical analyzes showed the importance in the resistance of the double mutation D30N_I84A and the conformational restructuring capacity of the M46I mutation and catalytic capacity.
Lenzner, Luzie [Verfasser]. "Apoptoseinduktion in kolorektalen Zellen und Gewebe durch die HIV-Proteaseinhibitoren Saquinavir und Nelfinavir / Luzie Lenzner." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2013. http://d-nb.info/1032558938/34.
Full textPayen, Salomé. "Intérêt de la pharmacocinétique de population pour l'adaptation posologique et le suivi thérapeutique en pédiatrie." Montpellier 1, 2004. http://www.theses.fr/2004MON13502.
Full textBooks on the topic "Nelfinavir"
Blokdijk, G. J. Nelfinavir Mesylate; A Complete Guide. CreateSpace Independent Publishing Platform, 2018.
Find full textPatel, Manish. A pilot study of therapeutic drug monitoring of nelfinavir in HIV infected patients. 1999.
Find full textRaymond, Colette. Response to nelfinavir in patients previously exposed to protease inhibitors--an Expanded Access Program in Ottawa, Ontario. 1999.
Find full textBook chapters on the topic "Nelfinavir"
Raposo, L. M., M. B. Arruda, R. M. Brindeiro, and F. F. Nobre. "Logistic Regression Models for Predicting Resistance to HIV Protease Inhibitor Nelfinavir." In IFMBE Proceedings, 1237–40. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-00846-2_306.
Full textHengge, U. R., V. Exner, S. Esser, H. P. Rudel, K. Müller, and M. Goos. "Effektivität, Verträglichkeit und Sicherheit einer Kombinationstherapie mit Stavudin, Didanosin und Nelfinavir in naiven vs. vorbehandelten HIV-Patienten: 18 Monatsdaten." In HIV-Infekt, 235–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-59683-4_40.
Full textHoffmann, F., G. Notheis, U. Wintergerst, J. Eberle, L. Gürtler, and B. H. Belohradsky. "Antiretrovirale Salvage-Therapie mit zwei Proteaseinhibitoren bei HIV-infizierten Kindern: Vergleich von Kombinations-therapien mit Ritonavir/Saquinavir und Nelfinavir/Saquinavir." In HIV-Infekt, 301–7. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-59683-4_53.
Full text"Nelfinavir." In Meyler's Side Effects of Drugs, 44–47. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-444-53717-1.01135-5.
Full textFindlay, Victoria J. "Nelfinavir." In xPharm: The Comprehensive Pharmacology Reference, 1–6. Elsevier, 2007. http://dx.doi.org/10.1016/b978-008055232-3.62257-3.
Full text"NELFINAVIR." In Litt's Drug Eruptions and Reactions Manual, 304. CRC Press, 2014. http://dx.doi.org/10.1201/b15347-142.
Full text"Nelfinavir." In PharmacotherapyFirst Drug Information. 2215 Constitution Avenue, N.W. Washington, DC 20037-2985: The American Pharmacists Association, 2017. http://dx.doi.org/10.21019/druginformation.nelfinavir.
Full text"Nelfinavir." In Meyler's Side Effects of Drugs: The International Encyclopedia of Adverse Drug Reactions and Interactions, 2433–35. Elsevier, 2006. http://dx.doi.org/10.1016/b0-44-451005-2/00770-1.
Full textJensen-Fangei, Soren, Suzanne Crowe, and Lars Ostergaard. "Nelfinavir." In Kucers' The Use of Antibiotics Sixth Edition, 2788–96. CRC Press, 2010. http://dx.doi.org/10.1201/b13787-274.
Full text"Nelfinavir (NFV)." In Checkliste Arzneimittel A–Z, edited by Detlev Schneider and Frank Richling. Stuttgart: Georg Thieme Verlag, 2013. http://dx.doi.org/10.1055/b-0034-82615.
Full textConference papers on the topic "Nelfinavir"
Methaneethorn, Janthima, Patcharaporn Kunyamee, Warangkana Jindasri, Warunee Wattanasaovaluk, Anoot Kraiboot, and Manupat Lohitnavy. "Pharmacokinetic modeling of simvastatin, nelfinavir and their interaction in humans." In 2014 36th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2014. http://dx.doi.org/10.1109/embc.2014.6944925.
Full text"Probabilistic Neural Network for Predicting Resistance to HIV-Protease Inhibitor Nelfinavir." In International Conference on Bioinformatics Models, Methods and Algorithms. SCITEPRESS - Science and and Technology Publications, 2014. http://dx.doi.org/10.5220/0004735900170023.
Full textKushchayeva, Yevgeniya, Aneeta Patel, John Costello, Vasyl Vasko, Nancy Carroll, Rubie Sue Jackson, Kenneth Burman, and Lisa Boyle. "Abstract 2124: The HIV protease inhibitor Nelfinavir inhibits medullary thyroid cancer cell growth." In 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.am2013-2124.
Full textKalu, Nene, Sunetra Biswas, Courtney Shirley, Meir Shamay, and Richard F. Ambinder. "Abstract C19: Nelfinavir-induced autophagy and cell death as potential anticancer therapy for KSHV-associated lymphomas." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c19.
Full textSanchez, Cecilia G., Fuselier Taylor, Marguerite Changala, Fayong Luo, and Joseph A. Lasky. "Nelfinavir Inhibits Myofibroblasts Differentiation And Induces Autophagic Degradation Of Type I Collagen In Human Lung Myofibroblasts." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3505.
Full textSubeha, Mahbuba R., Alicia A. Goyeneche, and Carlos M. Telleria. "Abstract 1013: Mechanistic role of nelfinavir as drug-repurposing strategy against high-grade serous ovarian cancer." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1013.
Full textKawabata, Shigeru, Nick Connis, Chunyu Zhang, Joell J. Gills, Christine L. Hann, and Phillip A. Dennis. "Abstract 684: Nelfinavir inhibits the growth of small cell lung cancer cells and patient-derived xenograft tumors." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-684.
Full textMathur, Aditi, Mikhail L. Kostochka, Asim B. Abdel-Mageed, and Debasis Mondal. "Abstract B42: Nelfinavir potentiates the anti-cancer efficacy of curcumin by subverting endoplasmic reticulum stress toward apoptosis: A promising chemoprevention approach." In Abstracts: Thirteenth Annual AACR International Conference on Frontiers in Cancer Prevention Research; September 27 - October 1, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1940-6215.prev-14-b42.
Full textChang, Yoon Soo, Leah M. Meza, Masahiro Onozawa, Joell J. Gills, Peter D. Aplan, and Phillip A. Dennis. "Abstract 2603: Inhibition of Notch and mTOR by nelfinavir as a novel approach for T cell acute lymphoblastic leukemia (T-ALL)." In 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.am2011-2603.
Full textGuan, Min. "Abstract 2653: Nelfinavir induces apoptosis in hormone-resistant prostate cancer cells through inhibition of regulated intramembrane proteolysis of SREBP-1 and ATF6." In 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.am2011-2653.
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