Mais la polymyxine n'est pas du tout absorbée dans le sang du système gastro-intestinal et n'a d'effet que dans l'intestin et est utile pour le traitement des infections intestinales amoxicilline prix Internet en y faisant des achats permettant d’économiser jusqu'à soixante-dix pour cent, tout en étant sûr de la qualité des produits pharmaceutiques.


1 Webster R G, Bean W J, Gorman O T, et al. Evolution and ecology of influenza A viruses. Microbiol Rev, 1992, 56: 152—179 2 Peiris J S, de J, Guan Y. Avian influenza virus (H5N1): a threat to human health. Clin Microbiol Rev, 2007, 20: 243—2673 Kumar S, Tamura K, Jakobsen I B, et al. MEGA2: Molecular evolutionary genetics analysis software. Bioinformatics, 2001, 17: 1244— 4 Thompson J D, Higgins D G, Gibson T J. Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res, 1994, 22: 4673— 5 Schwede T, Kopp J, Guex N, et al. SWISS MODEL: An automated protein homology-modeling server. Nucleic Acids Res, 2003, 31: 6 William H, Andrew D, Klaus S. VMD: Visual molecular dynamics. J Mol Grap, 1996, 14: 33—387 Gabriel G, Herwig A, Klenk H D. Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus. PLoS Pathog, 2008, 4 8 Qi X, Li X, Rider P, et al. Molecular characterization of highly pathogenic H5N1 avian influenza A viruses isolated from raccoon dogs 9 Obenauer J C, Denson J, Mehta P K, et al. Large-scale sequence analysis of avian influenza isolates. Science, 2006, 311: 1576— 10 Jackson D, Hossain M J, Hickman D, et al. A new influenza virus virulence determinant: The NS1 protein four C-terminal residues modulate pathogenicity. Proc Natl Acad Sci USA, 2008, 105: 4381—4386 11 Atsushi O, Takashi M, Hideo T. Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza A virus. Biochemistry, 2001, 40: 6053—6060 12 Suzuki H, Saito R, Masuda H, et al. Emergence of amantadine-resistant influenza A viruses: Epidemiological study. J Infect Chemother, 13 Scholtissek C, Quack G, Klenk H D, et al. How to overcome resistance of influenza A viruses against adamantane derivatives. Antiviral 14 Novel Swine-Origin Influenza A (H1N1) Virus Investigation Team. Emergence of a novel swine-origin influenza A(H1N1) virus in 15 Parrish C R, Kawaoka Y. The origins of new pandemic viruses: the acquisition of new host ranges by canine parvovirus and influenza A viruses. Annu Rev Microbiol, 2005, 59: 553—586 16 Skehel J J, Wiley D C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu Rev Biochem, 2000, 17 Weis W, Brown J H, Cusack S, et al. Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature, 18 Rogers G N, Paulson J C, Daniels R S, et al. Single amino acid substitutions in influenza hemagglutinin change receptor binding speci- 19 Monto A S. The role of antivirals in the control of influenza. Vaccine, 2003, 21: 1796—180020 Hay A J, Wolstenholm A J, Skehel J J, et al. The molecular basis of the specific anti-influenza action of amantadine. EMBO J, 1985, 4: 21 Pinto L H, Holsinger L J, Lamb L A. Influenza virus M2 protein has ion channel activity. Cell, 1992, 69: 517—528 22 Madren L K, Shipman C, Hayden F G. In vitro inhibitory effects of combinations of anti-influenza agents. Antivir Chem Chemother, 23 Varghese J H, McKimm-Breschkin J L, Caldwel J B, et al. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins, 1992, 14: 327— 24 Von Itzstein M, Wu W Y, Kok G K, et al. Rational design of potent sialidase based inhibitors of influenza virus protection. Nature, 25 Hayden F G. Amantadine and rimantadine—clinical aspects. In: Richman D D, ed. Antiviral Drug Resistance. New York: Wiley, 1996. 26 Ziegler T, Hemphill M L, Ziegler M L, et al. Low incidence of rimantadine resistance in field isolates of influenza A viruses. J Infect Dis, 27 Bright R A, Medina M, Xu X, et al. Incidence of adamantine resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: A cause for concern. Lancet, 2005, 366: 1175— 28 Ilyushina N A, Govorkova E A, Webster R G. Detection of amantadine-resistant variants among avian influenza viruses isolated in North America and Asia. Virology, 2005, 341: 102—106 29 Monto A S, Fleming D M, Henry D, et al. Efficacy and safety of the neuraminidase inhibitor zanamivir in the treatment of influenza A and B virus infections. J Infect Dis, 1999, 180: 254— 30 Lew W, Chen X, Kim C U. Discovery and development of GS4104 (oseltamivir): An orally active influenza neuraminidase inhibitor. 31 McKimm-Breschkin J L. Resistance of influenza viruses to neraminidase inhibitors —A review. Antivir Res, 2000, 47: 1—1732 McKimm-Breschkin J L. Management of influenza virus infections with neuraminidase inhibitors: Detection, incidence, and implications of drug resistance. Treat Respir Med, 2005, 4: 107—116 33 Kiso M, Mitamura K, Sakai-Tagawa Y, et al. Resistant influenza A viruses in children treated with oseltamivir: Descriptive study. Lancet, 34 Gubareva L V, Matrosovich M N, Brenner M K, et al. Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus. J Infect Dis, 1998, 178: 1257—1262 35 Robert M K, Wei M Y, Diana L N, et al. Intracel ular warfare between human influenza viruses and human cells: The roles of the viral 36 Stacey S C, Naomi D S, Gabriele N, et al. Influenza virus NS1 protein induces apoptosis in cultured cells. J Virol, 2001, 75: 7875 37 Adolfo G S, Andrej E, Demetrius M, et al. Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems. Virology, 38 Sang H S, Erich H, Robert G W. The NS1 gene of H5N1 influenza viruses circumvents the host anti-viral cytokine responses. Virus 39 Gary K G, Mirella S, Terrence M T, et al. Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: The role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. Proc Natl Acad Sci USA, 2002, 99: 10736— 40 Aleksandr S L, Samita A, Richard J W, et al. Pathogenesis of Hong Kong H5N1 influenza virus NS gene reassortants in mice: The role of cytokines and B- and T-cell responses. J Gen Virol, 2005, 86: 1121— 41 Morgan S, Carlo S. PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci, 2001, 24: 1—29


Microsoft word - metformin _6-03_.doc

Metformin WHAT IS METFORMIN? • Metformin is a medication used to treat type 2 diabetes, which is also known as non-insulin- dependent diabetes mellitus. It works by lowering or regulating the amount of sugar in your blood. WHAT IS THE MOST IMPORTANT INFORMATION I SHOULD KNOW ABOUT METFORMIN? • In rare cases, metformin can cause a serious side effect called lactic acidosis. Lactic

Lettre info janvier 2013

DELEGATION DU TARN & GARONNE Pierre BAFFALIE 3 Chemin du moulin de Robert 82220 VAZERAC Tél. : 05 63 67 79 57 E-mail : [email protected] Site internet MPF 82 : Vazerac le 16 janvier 2013 LETTRE D’INFORMATION JANVIER 2013 BONNE ANNEE, bien sûr ! Pour vos projets et vos chantiers… C’est bien avec p

Copyright © 2010-2014 Medical Science