Influenza virus neuraminidase

Jedrzejas, M. J., Singh, S. Brouillette, W. J. Air, G. M. Luo, M. A. 1995. Strategy for theoretical binding constant, Ki calculation for neuraminidase aromatic inhibitors, designed on the basis of the active site structure of influenza virus neuraminidase. Proteins Struct. Funct. Genet. 23 (1995) 264-277... [Pg.147]

We have already discussed one envelope protein of influenza virus, neuraminidase, as an example of an up-and-down antiparallel p motif. In the second envelope protein, hemagglutinin, one domain of the polypeptide chain is folded into a jelly roll motif. We shall now look at some other features of hemagglutinin that are important for its biological function. [Pg.79]

Colman, P.M., Varghese, J.N., Laver, W.G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303 41-44, 1983. [Pg.87]

Colman, P.M., et al. Three-dimensional structure of a complex of antibody with influenza virus neuraminidase. Nature 326 358-363, 1987. [Pg.322]

Cinatl J Jr, Michaelis M, Doerr HW (2007b) The threat of avian influenza A (H5N1). IV. Development of vaccines. Med Microbiol Immunol 196 213-225 Colman PM (1994) Influenza virus neuraminidase structure, antibodies, and inhibitors. Protein Sd 3 1687-1696... [Pg.147]

Colman PM, Ward CW (1985) Structure and diversity of influenza virus neuraminidase. Curr Top Microbiol Immunol 114 177-255... [Pg.147]

Smith BJ, Colman PM, von Itzstein M, Danylec B, Varghese JN (2001) Analysis of inhibitor binding in influenza virus neuraminidase. Protein Sci 10 689-696... [Pg.152]

Smith BJ, McKimm-Breshkin JL, McDonald M, Fernley RT, Varghese JN, Colman PM (2002) Structural studies of the resistance of influenza virus neuraminidase to inhibitors. J Med Chem... [Pg.152]

Varghese IN, Colman PM (1991) Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. 1 Mol Biol 221 473 86 Varghese IN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303 35 0 Varghese IN, McKimm-Breschkin IL, Caldwell IB, Kortt AA, Colman PM (1992) The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14 327-332... [Pg.153]

Watson KG, Cameron R, Fenton RJ, Gower D, Hamilton S, Jin B, Krippner GY, Luttick A, McConnell D, MacDonald SJ, Mason AM, Nguyen V, Tucker SP, Wu WY (2004) Highly potent and long-acting trimeric and tetrameiic inhibitors of influenza virus neuraminidase. Bioorg Med Chem Lett 14 1589-1592... [Pg.154]

Yamashita M, Ohno A, TomozawaT, Yoshida S (2003) R-118958, a unique anti-influenza agenf. I. A prodrug form of R-125489, a novel inhibitor of influenza virus neuraminidase. In 43rd in-tersdence conference on antimicrobial agents and chemotherapy, Chicago, USA, Sept 14-17, Poster F-1829... [Pg.154]

Sivasubramanian, N. and Nayak, D. P. Mutational analysis of the signal-anchor domain of influenza virus neuraminidase. Proc. Natl. Acad. Sci. U.S.A. 84 1-5,1987. [Pg.32]

J. S. Oxford, R. Lambkin, Targeting Influenza Virus Neuraminidase-A New Strategy for Antiviral Therapy , Drug Discov. Today 1998, 3, 448-456. [Pg.536]

Pharmacology The proposed mechanism of action of zanamivir is via inhibition of influenza virus neuraminidase with the possibility of alteration of virus particle aggregation and release. [Pg.1787]

Gubareva LV, Kaiser L, and Hayden FG. Influenza virus neuraminidase inhibitors. Lancet 2000 355 827-835. [Pg.583]

Mechanism of Action A selective inhibitor of influenza virus neuraminidase, an enzyme essential for viral replication. Acts against both influenza A and B viruses. Therapeutic Effect Suppresses the spread of infect ion within the respiratory system and re-duces the duration of clinical symptoms. [Pg.909]

The Design of Anti-Influenza Virus Drugs from the X-ray Molecular Structure of Influenza Virus Neuraminidase... [Pg.459]

Stereo image of the active site of Tem/N9 showing the active-site residues surrounding 4-guanidino-Neu5Ac2en (black). Those residues that are conserved in both influenza and bacterial neuraminidase are shaded gray, and those that are conserved only in influenza virus neuraminidase are not shaded. [Pg.472]

Colman PM, Influenza virus neuraminidase Krug RM, ed. Enzyme and antigen. In The Influenza Viruses. New York Plenum, 1989 175-218. [Pg.481]

Colman PM. Influenza virus neuraminidase structure, antibodies, and inhibitors. Protein Science... [Pg.481]

Bucher DJ, Palase P. The biologically active proteins of influenza virus neuraminidase. In ... [Pg.482]

Luo M, Jedrzejas MJ, Singh S, White CL, Brouillette WJ, Air GM, Laver WG. Benzoic acid inhibitors of influenza virus neuraminidase. Acta Cryst 1995 ... [Pg.485]

Drzenick R, Frank H, Rott R. Electron microscopy of purified influenza virus neuraminidase. Virology 1968 36 703-707. [Pg.699]

Colman PM, Laver WG. The structure of influenza virus neuraminidase at 5A resolution. In Structural aspects of recognition and assembly in biological macromolecules. I.S.S. Rehovot, 1981 869-872. [Pg.699]

Colman PM. Zanamivir an influenza virus neuraminidase inhibitor. Expert Rev Anti Infect Ther. 2005 3 191-199. [Pg.542]

P. M. Colman Design and antiviral properties of influenza virus neuraminidase inhibitors... [Pg.56]

J. N. Varghese, J. L. McKimm-Breschkin, J. B. Caldwell, A. A. Kortt, and P. M. Colman, The structure of the complex between influenza virus neuraminidase and sialic acid, the viral... [Pg.345]

C. L. White, M. N. Janakiraman, W. G. Laver, C. Philippon, A. Vasella, G. M. Air, and M. Luo, A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies, J. Mol. Biol., 245 (1995) 623-634. [Pg.345]

W. M. Kati, D. Montgomery, R. Carrick, L. Gubareva, C. Maring, K. McDaniel, K. Steffy, A. Molla, F. Hayden, D. Kempf, and W. Kohlbrenner, In vitro characterization of A-315675, a highly potent inhibitor of A and B strain influenza virus neuraminidases and influenza virus replication, Antimicrob. Agents Chemother., 46 (2002) 1014-1021. [Pg.351]

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