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Volumn 61, Issue , 2007, Pages 293-352

Anti-Influenza Drug Discovery: Are We Ready for the Next Pandemic?

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VACCINE; OSELTAMIVIR; PERAMIVIR; SIALIDASE; ZANAMIVIR;

EID: 34948898078     PISSN: 00652318     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2318(07)61006-3     Document Type: Review
Times cited : (17)

References (151)
  • 1
    • 0034796387 scopus 로고    scopus 로고
    • A history of influenza
    • Potter C.W. A history of influenza. J. Appl. Microbiol. 91 (2001) 572-579
    • (2001) J. Appl. Microbiol. , vol.91 , pp. 572-579
    • Potter, C.W.1
  • 3
    • 0025707394 scopus 로고
    • Drug therapy, prophylaxis and treament of influenza
    • Douglas R.G.J. Drug therapy, prophylaxis and treament of influenza. N. Engl. J. Med. 322 (1990) 443-450
    • (1990) N. Engl. J. Med. , vol.322 , pp. 443-450
    • Douglas, R.G.J.1
  • 5
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto L.H., Holsinger L.J., and Lamb R.A. Influenza virus M2 protein has ion channel activity. Cell 69 (1992) 517-528
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 6
    • 0002988267 scopus 로고
    • The action of adamantanamines against influenza A viruses: Inhibition of the M2 ion channel protein
    • Hay A.J. The action of adamantanamines against influenza A viruses: Inhibition of the M2 ion channel protein. Semin. Virol. 3 (1992) 21-30
    • (1992) Semin. Virol. , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 8
    • 0036166775 scopus 로고    scopus 로고
    • Neuraminidase inhibitors for the treatment and prevention of influenza
    • McKimm-Breschkin J.L. Neuraminidase inhibitors for the treatment and prevention of influenza. Expert Opin. Pharmacother. 3 (2002) 103-112
    • (2002) Expert Opin. Pharmacother. , vol.3 , pp. 103-112
    • McKimm-Breschkin, J.L.1
  • 9
    • 0034603350 scopus 로고    scopus 로고
    • Influenza virus neuraminidase inhibitors
    • Gubareva L.V., Kaiser L., and Hayden F.G. Influenza virus neuraminidase inhibitors. Lancet 355 (2000) 827-835
    • (2000) Lancet , vol.355 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 10
    • 33646567090 scopus 로고    scopus 로고
    • Recent advances in anti-influenza agents with neuraminidase as target
    • Zhang J., and Xu W. Recent advances in anti-influenza agents with neuraminidase as target. Mini Rev. Med. Chem. 6 (2006) 429-448
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 429-448
    • Zhang, J.1    Xu, W.2
  • 12
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • Wagner R., Matrosovich M., and Klenk H.-D. Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev. Med. Virol. 12 (2002) 159-166
    • (2002) Rev. Med. Virol. , vol.12 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.-D.3
  • 13
    • 0034103270 scopus 로고    scopus 로고
    • Influenza A pandemics of the 20th century with special reference to 1918: Virology, pathology and epidemiology
    • Oxford J.S. Influenza A pandemics of the 20th century with special reference to 1918: Virology, pathology and epidemiology. Rev. Med. Virol. 10 (2000) 119-133
    • (2000) Rev. Med. Virol. , vol.10 , pp. 119-133
    • Oxford, J.S.1
  • 15
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley D.C., and Skehel J.J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56 (1987) 365-394
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 16
    • 0027302926 scopus 로고
    • Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity
    • Couceiro J.N., Paulson J.C., and Baum L.G. Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity. Virus Res. 29 (1993) 155-165
    • (1993) Virus Res. , vol.29 , pp. 155-165
    • Couceiro, J.N.1    Paulson, J.C.2    Baum, L.G.3
  • 18
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., and Wiley D.C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev. Biochem. 69 (2000) 531-569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 19
    • 0037341410 scopus 로고    scopus 로고
    • Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding
    • Matrosovich M., and Klenk H.-D. Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev. Med. Virol. 13 (2003) 85-97
    • (2003) Rev. Med. Virol. , vol.13 , pp. 85-97
    • Matrosovich, M.1    Klenk, H.-D.2
  • 20
    • 0344120220 scopus 로고    scopus 로고
    • Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement
    • Borrego-Diaz E., Peeples M.E., Markosyan R.M., Melikyan G.B., and Cohen F.S. Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement. Virology 316 (2003) 234-244
    • (2003) Virology , vol.316 , pp. 234-244
    • Borrego-Diaz, E.1    Peeples, M.E.2    Markosyan, R.M.3    Melikyan, G.B.4    Cohen, F.S.5
  • 21
    • 0024466223 scopus 로고
    • Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
    • Sauter N.K., Bednarski M.D., Wurzburg B.A., Hanson J.E., Whitesides G.M., Skehel J.J., and Wiley D.C. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study. Biochemistry 28 (1989) 8388-8396
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1    Bednarski, M.D.2    Wurzburg, B.A.3    Hanson, J.E.4    Whitesides, G.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 23
    • 0021953619 scopus 로고
    • Structure and diversity of influenza virus neuraminidase
    • Colman P.M., and Ward C.W. Structure and diversity of influenza virus neuraminidase. Curr. Top. Microbiol. Immunol. 114 (1985) 177-255
    • (1985) Curr. Top. Microbiol. Immunol. , vol.114 , pp. 177-255
    • Colman, P.M.1    Ward, C.W.2
  • 24
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • Varghese J.N., Laver W.G., and Colman P.M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303 (1983) 35-40
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 25
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman P.M., Varghese J.N., and Laver W.G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303 (1983) 41-44
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 26
    • 0024827395 scopus 로고
    • The neuraminidase of influenza virus
    • Air G.M., and Laver W.G. The neuraminidase of influenza virus. Proteins 6 (1989) 341-356
    • (1989) Proteins , vol.6 , pp. 341-356
    • Air, G.M.1    Laver, W.G.2
  • 27
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibodies, and inhibitors
    • Colman P.M. Influenza virus neuraminidase: Structure, antibodies, and inhibitors. Protein Sci. 3 (1994) 1687-1696
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 28
    • 34948875426 scopus 로고
    • The structure of the prosthetic group of bovine submaxillary gland mucoprotein
    • Gottschalk A. The structure of the prosthetic group of bovine submaxillary gland mucoprotein. Biochim. Biophys. Acta 24 (1957) 649-650
    • (1957) Biochim. Biophys. Acta , vol.24 , pp. 649-650
    • Gottschalk, A.1
  • 29
    • 0005918784 scopus 로고
    • Neuraminidase: its substrate and mode of action
    • Gottschalk A. Neuraminidase: its substrate and mode of action. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 135-146
    • (1958) Adv. Enzymol. Relat. Subj. Biochem. , vol.20 , pp. 135-146
    • Gottschalk, A.1
  • 30
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese P., Tobita K., Ueda M., and Compans R.W. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61 (1974) 397-410
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 31
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action
    • Palese P., and Compans R.W. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action. J. Gen. Virol. 33 (1976) 159-163
    • (1976) J. Gen. Virol. , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 33
    • 25444501243 scopus 로고    scopus 로고
    • Neuraminidase inhibitors for influenza
    • Moscona A. Neuraminidase inhibitors for influenza. N. Engl. J. Med. 353 (2005) 1363-1373
    • (2005) N. Engl. J. Med. , vol.353 , pp. 1363-1373
    • Moscona, A.1
  • 34
    • 27744503583 scopus 로고    scopus 로고
    • Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms
    • Watson J.N., Newstead S., Narine A.A., Taylor G., and Bennet A.J. Two nucleophilic mutants of the Micromonospora viridifaciens sialidase operate with retention of configuration by two different mechanisms. Chembiochem 6 (2005) 1999-2004
    • (2005) Chembiochem , vol.6 , pp. 1999-2004
    • Watson, J.N.1    Newstead, S.2    Narine, A.A.3    Taylor, G.4    Bennet, A.J.5
  • 35
    • 7544222677 scopus 로고    scopus 로고
    • Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens
    • Watson J.N., Newstead S., Dookhun V., Taylor G., and Bennet A.J. Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens. FEBS Lett. 577 (2004) 265-269
    • (2004) FEBS Lett. , vol.577 , pp. 265-269
    • Watson, J.N.1    Newstead, S.2    Dookhun, V.3    Taylor, G.4    Bennet, A.J.5
  • 36
    • 0242318374 scopus 로고    scopus 로고
    • Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase
    • Watson J.N., Dookhun V., Borgford T.J., and Bennet A.J. Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase. Biochemistry 42 (2003) 12682-12690
    • (2003) Biochemistry , vol.42 , pp. 12682-12690
    • Watson, J.N.1    Dookhun, V.2    Borgford, T.J.3    Bennet, A.J.4
  • 37
    • 0018167605 scopus 로고
    • Mechanism of Arthrobacter sialophilus neuraminidase: The binding of substrates and transition-state analogs
    • Miller C.A., Wang P., and Flashner M. Mechanism of Arthrobacter sialophilus neuraminidase: The binding of substrates and transition-state analogs. Biochem. Biophys. Res. Commun. 83 (1978) 1479-1487
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 1479-1487
    • Miller, C.A.1    Wang, P.2    Flashner, M.3
  • 38
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghese J.N., McKimm-Breschkin J.L., Caldwell J.B., Kortt A.A., and Colman P.M. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14 (1992) 327-332
    • (1992) Proteins , vol.14 , pp. 327-332
    • Varghese, J.N.1    McKimm-Breschkin, J.L.2    Caldwell, J.B.3    Kortt, A.A.4    Colman, P.M.5
  • 40
    • 0026755388 scopus 로고
    • Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus
    • Chong A.K., Pegg M.S., Taylor N.R., and von Itzstein M. Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus. Eur. J. Biochem. 207 (1992) 335-343
    • (1992) Eur. J. Biochem. , vol.207 , pp. 335-343
    • Chong, A.K.1    Pegg, M.S.2    Taylor, N.R.3    von Itzstein, M.4
  • 41
    • 0028325249 scopus 로고
    • Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis
    • Taylor N.R., and von Itzstein M. Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis. J. Med. Chem. 37 (1994) 616-624
    • (1994) J. Med. Chem. , vol.37 , pp. 616-624
    • Taylor, N.R.1    von Itzstein, M.2
  • 43
  • 44
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • Zechel D.L., and Withers S.G. Dissection of nucleophilic and acid-base catalysis in glycosidases. Curr. Opin. Chem. Biol. 5 (2001) 643-649
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2
  • 45
    • 0025895628 scopus 로고
    • Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution
    • Varghese J.N., and Colman P.M. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution. J. Mol. Biol. 221 (1991) 473-486
    • (1991) J. Mol. Biol. , vol.221 , pp. 473-486
    • Varghese, J.N.1    Colman, P.M.2
  • 46
    • 0023475950 scopus 로고
    • Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus
    • Baker A.T., Varghese J.N., Laver W.G., Air G.M., and Colman P.M. Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 2 (1987) 111-117
    • (1987) Proteins , vol.2 , pp. 111-117
    • Baker, A.T.1    Varghese, J.N.2    Laver, W.G.3    Air, G.M.4    Colman, P.M.5
  • 47
    • 0027292125 scopus 로고
    • Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid
    • Bossart-Whitaker P., Carson M., Babu Y.S., Smith C.D., Laver W.G., and Air G.M. Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid. J. Mol. Biol. 232 (1993) 1069-1083
    • (1993) J. Mol. Biol. , vol.232 , pp. 1069-1083
    • Bossart-Whitaker, P.1    Carson, M.2    Babu, Y.S.3    Smith, C.D.4    Laver, W.G.5    Air, G.M.6
  • 48
    • 0026508847 scopus 로고
    • The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • Burmeister W.P., Ruigrok R.W., and Cusack S. The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J. 11 (1992) 49-56
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 50
    • 0030050255 scopus 로고
    • Neuraminidase inhibitors as potential anti-influenza drugs
    • Bamford M.J. Neuraminidase inhibitors as potential anti-influenza drugs. J. Enzyme Inhib. 10 (1995) 1-16
    • (1995) J. Enzyme Inhib. , vol.10 , pp. 1-16
    • Bamford, M.J.1
  • 53
    • 0025145409 scopus 로고
    • New ganglioside analogs that inhibit influenza virus sialidase
    • Suzuki Y., Sato K., Kiso M., and Hasegawa A. New ganglioside analogs that inhibit influenza virus sialidase. Glycoconj. J. 7 (1990) 349-354
    • (1990) Glycoconj. J. , vol.7 , pp. 349-354
    • Suzuki, Y.1    Sato, K.2    Kiso, M.3    Hasegawa, A.4
  • 54
    • 0028763159 scopus 로고
    • Inhibition of bacterial and viral sialidases by 3-fluoro-N-acetylneuraminic acid
    • Hagiwara T., Kijima-Suda I., Ido T., Ohrui H., and Tomita K. Inhibition of bacterial and viral sialidases by 3-fluoro-N-acetylneuraminic acid. Carbohydr. Res. 263 (1994) 167-172
    • (1994) Carbohydr. Res. , vol.263 , pp. 167-172
    • Hagiwara, T.1    Kijima-Suda, I.2    Ido, T.3    Ohrui, H.4    Tomita, K.5
  • 55
    • 0028925854 scopus 로고
    • A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies
    • White C.L., Janakiraman M.N., Laver W.G., Philippon C., Vasella A., Air G.M., and Luo M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 245 (1995) 623-634
    • (1995) J. Mol. Biol. , vol.245 , pp. 623-634
    • White, C.L.1    Janakiraman, M.N.2    Laver, W.G.3    Philippon, C.4    Vasella, A.5    Air, G.M.6    Luo, M.7
  • 56
    • 84945736084 scopus 로고
    • 2-Deoxy-2,3-dehydrosialic acids. II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3-dehydro-N-acylneuraminic acids
    • Meindl P., and Tuppy H. 2-Deoxy-2,3-dehydrosialic acids. II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3-dehydro-N-acylneuraminic acids. Hoppe Seylers Z Physiol. Chem. 350 (1969) 1088-1092
    • (1969) Hoppe Seylers Z Physiol. Chem. , vol.350 , pp. 1088-1092
    • Meindl, P.1    Tuppy, H.2
  • 57
    • 0027287318 scopus 로고
    • Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position
    • Holzer C.T., von Itzstein M., Jin B., Pegg M.S., Stewart W.P., and Wu W.Y. Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position. Glycoconj. J. 10 (1993) 40-44
    • (1993) Glycoconj. J. , vol.10 , pp. 40-44
    • Holzer, C.T.1    von Itzstein, M.2    Jin, B.3    Pegg, M.S.4    Stewart, W.P.5    Wu, W.Y.6
  • 58
    • 0015959249 scopus 로고
    • Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid
    • Meindl P., Bodo G., Palese P., Schulman J., and Tuppy H. Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. Virology 58 (1974) 457-463
    • (1974) Virology , vol.58 , pp. 457-463
    • Meindl, P.1    Bodo, G.2    Palese, P.3    Schulman, J.4    Tuppy, H.5
  • 59
    • 0020380927 scopus 로고
    • Uptake, metabolism and excretion of orally and intravenously administered, double-labeled N-glycoloylneuraminic acid and single-labeled 2-deoxy-2,3-dehydro-N-acetylneuraminic acid in mouse and rat
    • Nohle U., Beau J.M., and Schauer R. Uptake, metabolism and excretion of orally and intravenously administered, double-labeled N-glycoloylneuraminic acid and single-labeled 2-deoxy-2,3-dehydro-N-acetylneuraminic acid in mouse and rat. Eur. J. Biochem. 126 (1982) 543-548
    • (1982) Eur. J. Biochem. , vol.126 , pp. 543-548
    • Nohle, U.1    Beau, J.M.2    Schauer, R.3
  • 60
    • 0016244226 scopus 로고
    • Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA)
    • Palese P., Schulman J.L., Bodo G., and Meindl P. Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA). Virology 59 (1974) 490-498
    • (1974) Virology , vol.59 , pp. 490-498
    • Palese, P.1    Schulman, J.L.2    Bodo, G.3    Meindl, P.4
  • 63
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford P.J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28 (1985) 849-857
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 64
    • 0030044141 scopus 로고    scopus 로고
    • A study of the active site of influenza virus sialidase: An approach to the rational design of novel anti-influenza drugs
    • von Itzstein M., Dyason J.C., Oliver S.W., White H.F., Wu W.Y., Kok G.B., and Pegg M.S. A study of the active site of influenza virus sialidase: An approach to the rational design of novel anti-influenza drugs. J. Med. Chem. 39 (1996) 388-391
    • (1996) J. Med. Chem. , vol.39 , pp. 388-391
    • von Itzstein, M.1    Dyason, J.C.2    Oliver, S.W.3    White, H.F.4    Wu, W.Y.5    Kok, G.B.6    Pegg, M.S.7
  • 65
    • 34948872196 scopus 로고    scopus 로고
    • L.M. von Itzstein, W.Y. Wu, V. Phan Tho, B. Danylec, and B. Jin, Preparation of Derivatives and Analogs of 2-Deoxy-2,3-Didehydro-N-Acetylneuraminic Acid as Antiviral Agents, Biota Scientific Management Pty. Ltd., Australia, 1991, WO 9116320.
  • 66
    • 0028454967 scopus 로고
    • The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: A potent influenza virus sialidase inhibitor
    • von Itzstein M., Wu W.Y., and Jin B. The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: A potent influenza virus sialidase inhibitor. Carbohydr. Res. 259 (1994) 301-305
    • (1994) Carbohydr. Res. , vol.259 , pp. 301-305
    • von Itzstein, M.1    Wu, W.Y.2    Jin, B.3
  • 67
    • 0027316217 scopus 로고
    • A convenient method for the introduction of nitrogen and sulfur at C-4 on a sialic acid analog
    • von Itzstein M., Jin B., Wu W.Y., and Chandler M. A convenient method for the introduction of nitrogen and sulfur at C-4 on a sialic acid analog. Carbohydr. Res. 244 (1993) 181-185
    • (1993) Carbohydr. Res. , vol.244 , pp. 181-185
    • von Itzstein, M.1    Jin, B.2    Wu, W.Y.3    Chandler, M.4
  • 68
    • 37049084551 scopus 로고
    • Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino Neu5Ac2en. X-ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-d-erythro-l-gluco-nonioni c acid
    • Chandler M., Bamford M.J., Conroy R., Lamont B., Patel B., Patel V.K., Steeples I.P., Storer R., Weir N.G., Wright M., and Williamson C. Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino Neu5Ac2en. X-ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-d-erythro-l-gluco-nonioni c acid. J. Chem. Soc. Perkin Trans. 1 (1995) 1173-1180
    • (1995) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1173-1180
    • Chandler, M.1    Bamford, M.J.2    Conroy, R.3    Lamont, B.4    Patel, B.5    Patel, V.K.6    Steeples, I.P.7    Storer, R.8    Weir, N.G.9    Wright, M.10    Williamson, C.11
  • 69
    • 0027162942 scopus 로고
    • 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro
    • Woods J.M., Bethell R.C., Coates J.A., Healy N., Hiscox S.A., Pearson B.A., Ryan D.M., Ticehurst J., Tilling J., Walcott S.M., et al. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro. Antimicrob. Agents Chemother. 37 (1993) 1473-1479
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1473-1479
    • Woods, J.M.1    Bethell, R.C.2    Coates, J.A.3    Healy, N.4    Hiscox, S.A.5    Pearson, B.A.6    Ryan, D.M.7    Ticehurst, J.8    Tilling, J.9    Walcott, S.M.10
  • 70
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 71
    • 0033730244 scopus 로고    scopus 로고
    • In vitro and in vivo assay systems for study of influenza virus inhibitors
    • Sidwell R.W., and Smee D.F. In vitro and in vivo assay systems for study of influenza virus inhibitors. Antiviral. Res. 48 (2000) 1-16
    • (2000) Antiviral. Res. , vol.48 , pp. 1-16
    • Sidwell, R.W.1    Smee, D.F.2
  • 72
    • 0020607871 scopus 로고
    • The interaction of substrate-related ketals with bacterial and viral neuraminidases
    • Flashner M., Kessler J., and Tanenbaum S.W. The interaction of substrate-related ketals with bacterial and viral neuraminidases. Arch. Biochem. Biophys. 221 (1983) 188-196
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 188-196
    • Flashner, M.1    Kessler, J.2    Tanenbaum, S.W.3
  • 73
    • 0028500713 scopus 로고
    • Synthesis of transition-state analogues as potential inhibitors of sialidase from influenza virus
    • Driguez P.-A., Barrere B., Quash G., and Doutheau A. Synthesis of transition-state analogues as potential inhibitors of sialidase from influenza virus. Carbohydr. Res. 262 (1994) 297-310
    • (1994) Carbohydr. Res. , vol.262 , pp. 297-310
    • Driguez, P.-A.1    Barrere, B.2    Quash, G.3    Doutheau, A.4
  • 74
    • 0035835014 scopus 로고    scopus 로고
    • Synthesis of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid analogues modified at the C-4 and C-9 positions and their behaviour towards sialidase from influenza virus and pig liver membrane
    • Ikeda K., Sano K., Ito M., Saito M., Hidari K., Suzuki T., Suzuki Y., and Tanaka K. Synthesis of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid analogues modified at the C-4 and C-9 positions and their behaviour towards sialidase from influenza virus and pig liver membrane. Carbohydr. Res. 330 (2001) 31-41
    • (2001) Carbohydr. Res. , vol.330 , pp. 31-41
    • Ikeda, K.1    Sano, K.2    Ito, M.3    Saito, M.4    Hidari, K.5    Suzuki, T.6    Suzuki, Y.7    Tanaka, K.8
  • 75
    • 0032213373 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of an N-acetylneuraminic acid analogue having a carbamoylmethyl group at C-4 as an inhibitor of sialidase from influenza virus
    • Ikeda K., Kimura F., Sano K., Suzuki Y., and Achiwa K. Chemoenzymatic synthesis of an N-acetylneuraminic acid analogue having a carbamoylmethyl group at C-4 as an inhibitor of sialidase from influenza virus. Carbohydr. Res. 312 (1998) 183-189
    • (1998) Carbohydr. Res. , vol.312 , pp. 183-189
    • Ikeda, K.1    Kimura, F.2    Sano, K.3    Suzuki, Y.4    Achiwa, K.5
  • 76
    • 33747624715 scopus 로고    scopus 로고
    • Syntheses of triazole-modified zanamivir analogues via click chemistry and anti-AIV activities
    • Li J., Zheng M., Tang W., He P.L., Zhu W., Li T., Zuo J.P., Liu H., and Jiang H. Syntheses of triazole-modified zanamivir analogues via click chemistry and anti-AIV activities. Bioorg. Med. Chem. Lett. 16 (2006) 5009-5013
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 5009-5013
    • Li, J.1    Zheng, M.2    Tang, W.3    He, P.L.4    Zhu, W.5    Li, T.6    Zuo, J.P.7    Liu, H.8    Jiang, H.9
  • 78
    • 0028874138 scopus 로고
    • Synthesis and influenza virus sialidase inhibitory activity of the 5-desacetamido analog of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid (GG167)
    • Starkey I.D., Mahmoudian M., Noble D., Smith P.W., Cherry P., Howes P.D., and Sollis S.L. Synthesis and influenza virus sialidase inhibitory activity of the 5-desacetamido analog of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid (GG167). Tetrahedron Lett. 36 (1995) 299-302
    • (1995) Tetrahedron Lett. , vol.36 , pp. 299-302
    • Starkey, I.D.1    Mahmoudian, M.2    Noble, D.3    Smith, P.W.4    Cherry, P.5    Howes, P.D.6    Sollis, S.L.7
  • 79
    • 0026414045 scopus 로고
    • 2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae
    • Schreiner E., Zbiral E., Kleineidam R.G., and Schauer R. 2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae. Carbohydr. Res. 216 (1991) 61-66
    • (1991) Carbohydr. Res. , vol.216 , pp. 61-66
    • Schreiner, E.1    Zbiral, E.2    Kleineidam, R.G.3    Schauer, R.4
  • 81
    • 0037025440 scopus 로고    scopus 로고
    • Synthesis and anti-influenza virus activity of 4-guanidino-7-substituted Neu5Ac2en derivatives
    • Honda T., Masuda T., Yoshida S., Arai M., Kobayashi Y., and Yamashita M. Synthesis and anti-influenza virus activity of 4-guanidino-7-substituted Neu5Ac2en derivatives. Bioorg. Med. Chem. Lett. 12 (2002) 1921-1924
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1921-1924
    • Honda, T.1    Masuda, T.2    Yoshida, S.3    Arai, M.4    Kobayashi, Y.5    Yamashita, M.6
  • 82
    • 0037025439 scopus 로고    scopus 로고
    • Synthesis and anti-influenza virus activity of 7-O-alkylated derivatives related to zanamivir
    • Honda T., Masuda T., Yoshida S., Arai M., Kaneko S., and Yamashita M. Synthesis and anti-influenza virus activity of 7-O-alkylated derivatives related to zanamivir. Bioorg. Med. Chem. Lett. 12 (2002) 1925-1928
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1925-1928
    • Honda, T.1    Masuda, T.2    Yoshida, S.3    Arai, M.4    Kaneko, S.5    Yamashita, M.6
  • 83
    • 0032710063 scopus 로고    scopus 로고
    • Synthesis and influenza virus sialidase inhibitory activity of analogues of 4-guanidino-Neu5Ac2en (Zanamivir) modified in the glycerol side-chain
    • Andrews D.M., Cherry P.C., Humber D.C., Jones P.S., Keeling S.P., Martin P.F., Shaw C.D., and Swanson S. Synthesis and influenza virus sialidase inhibitory activity of analogues of 4-guanidino-Neu5Ac2en (Zanamivir) modified in the glycerol side-chain. Eur. J. Med. Chem. 34 (1999) 563-574
    • (1999) Eur. J. Med. Chem. , vol.34 , pp. 563-574
    • Andrews, D.M.1    Cherry, P.C.2    Humber, D.C.3    Jones, P.S.4    Keeling, S.P.5    Martin, P.F.6    Shaw, C.D.7    Swanson, S.8
  • 85
    • 0037025441 scopus 로고    scopus 로고
    • Synthesis and anti-influenza evaluation of polyvalent sialidase inhibitors bearing 4-guanidino-Neu5Ac2en derivatives
    • Honda T., Yoshida S., Arai M., Masuda T., and Yamashita M. Synthesis and anti-influenza evaluation of polyvalent sialidase inhibitors bearing 4-guanidino-Neu5Ac2en derivatives. Bioorg. Med. Chem. Lett. 12 (2002) 1929-1932
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1929-1932
    • Honda, T.1    Yoshida, S.2    Arai, M.3    Masuda, T.4    Yamashita, M.5
  • 86
    • 3142767850 scopus 로고    scopus 로고
    • Synthesis and anti-influenza evaluation of polyvalent sialidase inhibitors bearing 4-guanidino-Neu5Ac2en derivatives
    • Masuda T., Yoshida S., Arai M., Kaneko S., Yamashita M., and Honda T. Synthesis and anti-influenza evaluation of polyvalent sialidase inhibitors bearing 4-guanidino-Neu5Ac2en derivatives. Chem. Pharm. Bull. (Tokyo) 51 (2003) 1386-1398
    • (2003) Chem. Pharm. Bull. (Tokyo) , vol.51 , pp. 1386-1398
    • Masuda, T.1    Yoshida, S.2    Arai, M.3    Kaneko, S.4    Yamashita, M.5    Honda, T.6
  • 90
    • 33748980940 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of sulfur isosteres of the potent influenza virus sialidase inhibitors 4-amino-4-deoxy- and 4-deoxy-4-guanidino-Neu5Ac2en
    • Kok G.B., Campbell M., Mackey B., and von Itzstein M. Synthesis and biological evaluation of sulfur isosteres of the potent influenza virus sialidase inhibitors 4-amino-4-deoxy- and 4-deoxy-4-guanidino-Neu5Ac2en. J. Chem. Soc. Perkin Trans. 1 (1996) 2811-2815
    • (1996) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2811-2815
    • Kok, G.B.1    Campbell, M.2    Mackey, B.3    von Itzstein, M.4
  • 92
    • 0030040371 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of neuraminic acid analogs structurally varied at C-5 and C-9 as potential inhibitors of the sialidase from influenza virus
    • Murakami M., Ikeda K., and Achiwa K. Chemoenzymatic synthesis of neuraminic acid analogs structurally varied at C-5 and C-9 as potential inhibitors of the sialidase from influenza virus. Carbohydr. Res. 280 (1996) 101-110
    • (1996) Carbohydr. Res. , vol.280 , pp. 101-110
    • Murakami, M.1    Ikeda, K.2    Achiwa, K.3
  • 93
    • 0023664836 scopus 로고
    • Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism
    • Lentz M.R., Webster R.G., and Air G.M. Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism. Biochemistry 26 (1987) 5351-5358
    • (1987) Biochemistry , vol.26 , pp. 5351-5358
    • Lentz, M.R.1    Webster, R.G.2    Air, G.M.3
  • 94
    • 37049080529 scopus 로고
    • Synthesis of 6-, 7- and 8-carbon sugar analogs of potent anti-influenza 2,3-didehydro-2,3-dideoxy-N-acetylneuraminic acid derivatives
    • Bamford M.J., Pichel J.C., Husman W., Patel B., Storer R., and Wier N.G. Synthesis of 6-, 7- and 8-carbon sugar analogs of potent anti-influenza 2,3-didehydro-2,3-dideoxy-N-acetylneuraminic acid derivatives. J. Chem. Soc. Perkin Trans. 1 (1995) 1181-1187
    • (1995) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1181-1187
    • Bamford, M.J.1    Pichel, J.C.2    Husman, W.3    Patel, B.4    Storer, R.5    Wier, N.G.6
  • 95
    • 0030572487 scopus 로고    scopus 로고
    • Novel inhibitors of influenza sialidase related to GG167. Synthesis of 4-amino and guanidino-4H-pyran-2-carboxylic acid-6-propylamides; selective inhibitors of influenza A virus sialidase
    • Sollis S.L., Smith P.W., Howes P.D., Cherry P.C., and Bethell R.C. Novel inhibitors of influenza sialidase related to GG167. Synthesis of 4-amino and guanidino-4H-pyran-2-carboxylic acid-6-propylamides; selective inhibitors of influenza A virus sialidase. Bioorg. Med. Chem. Lett. 6 (1996) 1805-1808
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 1805-1808
    • Sollis, S.L.1    Smith, P.W.2    Howes, P.D.3    Cherry, P.C.4    Bethell, R.C.5
  • 99
    • 0032510373 scopus 로고    scopus 로고
    • Dihydropyrancarboxamides related to zanamivir: A new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B
    • Taylor N.R., Cleasby A., Singh O., Skarzynski T., Wonacott A.J., Smith P.W., Sollis S.L., Howes P.D., Cherry P.C., Bethell R., Colman P., and Varghese J. Dihydropyrancarboxamides related to zanamivir: A new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B. J. Med. Chem. 41 (1998) 798-807
    • (1998) J. Med. Chem. , vol.41 , pp. 798-807
    • Taylor, N.R.1    Cleasby, A.2    Singh, O.3    Skarzynski, T.4    Wonacott, A.J.5    Smith, P.W.6    Sollis, S.L.7    Howes, P.D.8    Cherry, P.C.9    Bethell, R.10    Colman, P.11    Varghese, J.12
  • 101
    • 0030930825 scopus 로고    scopus 로고
    • Novel inhibitors of influenza sialidases related to zanamivir. Heterocyclic replacements of the glycerol sidechain
    • Smith P.W., and Whittington A.R. Novel inhibitors of influenza sialidases related to zanamivir. Heterocyclic replacements of the glycerol sidechain. Bioorg. Med. Chem. Lett. 7 (1997) 2239-2242
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2239-2242
    • Smith, P.W.1    Whittington, A.R.2
  • 102
    • 31044444908 scopus 로고    scopus 로고
    • Modelling, synthesis and biological evaluation of novel glucuronide-based probes of Vibrio cholerae sialidase
    • Mann M.C., Thomson R.J., Dyason J.C., McAtamney S., and von Itzstein M. Modelling, synthesis and biological evaluation of novel glucuronide-based probes of Vibrio cholerae sialidase. Bioorg. Med. Chem. 14 (2006) 1518-1537
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 1518-1537
    • Mann, M.C.1    Thomson, R.J.2    Dyason, J.C.3    McAtamney, S.4    von Itzstein, M.5
  • 104
    • 5144219966 scopus 로고    scopus 로고
    • An efficient approach to N-acetyl-d-glucosaminuronic acid-based sialylmimetics as potential sialidase inhibitors
    • Mann M.C., Thomson R.J., and von Itzstein M. An efficient approach to N-acetyl-d-glucosaminuronic acid-based sialylmimetics as potential sialidase inhibitors. Bioorg. Med. Chem. Lett. 14 (2004) 5555-5558
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 5555-5558
    • Mann, M.C.1    Thomson, R.J.2    von Itzstein, M.3
  • 105
    • 0033584065 scopus 로고    scopus 로고
    • Synthesis of δ 4-β-d-glucopyranosiduronic acids as mimetics of 2,3-unsaturated sialic acids for sialidase inhibition
    • Florio P., Thomson R.J., Alafaci A., Abo S., and von Itzstein M. Synthesis of δ 4-β-d-glucopyranosiduronic acids as mimetics of 2,3-unsaturated sialic acids for sialidase inhibition. Bioorg. Med. Chem. Lett. 9 (1999) 2065-2068
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2065-2068
    • Florio, P.1    Thomson, R.J.2    Alafaci, A.3    Abo, S.4    von Itzstein, M.5
  • 106
    • 34948843722 scopus 로고    scopus 로고
    • P. Florio, R.J. Thomson, B. Smith, P.M. Colman, and M. von Itzstein, unpublished data.
  • 108
    • 0242493938 scopus 로고    scopus 로고
    • N-Acetyl-6-sulfo-d-glucosamine as a promising mimic of N-acetyl neuraminic acid
    • Sasaki K., Nishida Y., Uzawa H., and Kobayashi K. N-Acetyl-6-sulfo-d-glucosamine as a promising mimic of N-acetyl neuraminic acid. Bioorg. Med. Chem. Lett. 13 (2003) 2821-2823
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2821-2823
    • Sasaki, K.1    Nishida, Y.2    Uzawa, H.3    Kobayashi, K.4
  • 110
    • 0029099621 scopus 로고
    • Structure-based inhibitors of influenza virus sialidase: A benzoic acid lead with novel interaction
    • Singh S., Jedrzejas M.J., Air G.M., Luo M., Laver W.G., and Brouillette W.J. Structure-based inhibitors of influenza virus sialidase: A benzoic acid lead with novel interaction. J. Med. Chem. 38 (1995) 3217-3225
    • (1995) J. Med. Chem. , vol.38 , pp. 3217-3225
    • Singh, S.1    Jedrzejas, M.J.2    Air, G.M.3    Luo, M.4    Laver, W.G.5    Brouillette, W.J.6
  • 114
    • 0033571049 scopus 로고    scopus 로고
    • Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping. (Erratum to document cited in CA131:266560)
    • Brouillette W.J., Atigadda V.R., Duarte F., Luo M., Air G.M., Babu Y.S., and Bantia S. Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping. (Erratum to document cited in CA131:266560). Bioorg. Med. Chem. Lett. 9 (1999) 3259
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 3259
    • Brouillette, W.J.1    Atigadda, V.R.2    Duarte, F.3    Luo, M.4    Air, G.M.5    Babu, Y.S.6    Bantia, S.7
  • 115
    • 0033550314 scopus 로고    scopus 로고
    • Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site
    • Finley J.B., Atigadda V.R., Duarte F., Zhao J.J., Brouillette W.J., Air G.M., and Luo M. Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. J. Mol. Biol. 293 (1999) 1107-1119
    • (1999) J. Mol. Biol. , vol.293 , pp. 1107-1119
    • Finley, J.B.1    Atigadda, V.R.2    Duarte, F.3    Zhao, J.J.4    Brouillette, W.J.5    Air, G.M.6    Luo, M.7
  • 117
    • 0028856207 scopus 로고
    • Synthesis and influenza neuraminidase inhibitory activity of aromatic analogs of sialic acid
    • Williams M., Bischofberger N., Swaminathan S., and Kim C.U. Synthesis and influenza neuraminidase inhibitory activity of aromatic analogs of sialic acid. Bioorg. Med. Chem. Lett. 5 (1995) 2251-2254
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 2251-2254
    • Williams, M.1    Bischofberger, N.2    Swaminathan, S.3    Kim, C.U.4
  • 118
    • 14844318121 scopus 로고    scopus 로고
    • Synthesis and inhibitory activity of benzoic acid and pyridine derivatives on influenza neuraminidase
    • Chand P., Kotian P.L., Morris P.E., Bantia S., Walsh D.A., and Babu Y.S. Synthesis and inhibitory activity of benzoic acid and pyridine derivatives on influenza neuraminidase. Bioorg. Med. Chem. 13 (2005) 2665-2678
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 2665-2678
    • Chand, P.1    Kotian, P.L.2    Morris, P.E.3    Bantia, S.4    Walsh, D.A.5    Babu, Y.S.6
  • 119
    • 0033584149 scopus 로고    scopus 로고
    • Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping
    • Brouillette W.J., Atigadda V.R., Luo M., Air G.M., Babu Y.S., and Bantia S. Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping. Bioorg. Med. Chem. Lett. 9 (1999) 1901-1906
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 1901-1906
    • Brouillette, W.J.1    Atigadda, V.R.2    Luo, M.3    Air, G.M.4    Babu, Y.S.5    Bantia, S.6
  • 120
    • 0032479225 scopus 로고    scopus 로고
    • Carbocyclic analogs of N-acetyl-2,3-didehydro-2-deoxy-d-neuraminic acid (Neu5Ac2en, DANA): Synthesis and inhibition of viral and bacterial neuraminidases
    • Vorwerk S., and Vasella A. Carbocyclic analogs of N-acetyl-2,3-didehydro-2-deoxy-d-neuraminic acid (Neu5Ac2en, DANA): Synthesis and inhibition of viral and bacterial neuraminidases. Angew. Chem. Int. Ed. 37 (1998) 1732-1734
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1732-1734
    • Vorwerk, S.1    Vasella, A.2
  • 121
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim C.U., Lew W., Williams M.A., Liu H., Zhang L., Swaminathan S., Bischofberger N., Chen M.S., Mendel D.B., Tai C.Y., Laver W.G., and Stevens R.C. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 119 (1997) 681-690
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10    Laver, W.G.11    Stevens, R.C.12
  • 123
    • 0030739707 scopus 로고    scopus 로고
    • C3-Thia and C3-carba isosteres of a carbocyclic influenza neuraminidase inhibitor, (3R,4R,5R)-4-acetamido-5-amino-3-propoxy-1-cyclohexene-1-carboxylic acid
    • Lew W., Williams M.A., Mendel D.B., Escarpe P.A., and Kim C.U. C3-Thia and C3-carba isosteres of a carbocyclic influenza neuraminidase inhibitor, (3R,4R,5R)-4-acetamido-5-amino-3-propoxy-1-cyclohexene-1-carboxylic acid. Bioorg. Med. Chem. Lett. 7 (1997) 1843-1846
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 1843-1846
    • Lew, W.1    Williams, M.A.2    Mendel, D.B.3    Escarpe, P.A.4    Kim, C.U.5
  • 124
    • 0034084227 scopus 로고    scopus 로고
    • Discovery and development of GS 4104 (oseltamivir): An orally active influenza neuraminidase inhibitor
    • Lew W., Chen X., and Kim C.U. Discovery and development of GS 4104 (oseltamivir): An orally active influenza neuraminidase inhibitor. Curr. Med. Chem. 7 (2000) 663-672
    • (2000) Curr. Med. Chem. , vol.7 , pp. 663-672
    • Lew, W.1    Chen, X.2    Kim, C.U.3
  • 125
    • 0035833045 scopus 로고    scopus 로고
    • Synthesis of (4R*,5R*)-4-acetylamino-5-diethylcarbamoylcyclohex-1-ene-1-c arboxylic acid and (3R*,4R*)-4-acetylamino-3-diethylcarbamoylcyclohex-1-ene-1-c arboxylic acid: New inhibitors of influenza virus sialidases
    • Kerrigan S.A., Smith P.W., and Stoodley R.J. Synthesis of (4R*,5R*)-4-acetylamino-5-diethylcarbamoylcyclohex-1-ene-1-c arboxylic acid and (3R*,4R*)-4-acetylamino-3-diethylcarbamoylcyclohex-1-ene-1-c arboxylic acid: New inhibitors of influenza virus sialidases. Tetrahedron Lett. 42 (2001) 4709-4712
    • (2001) Tetrahedron Lett. , vol.42 , pp. 4709-4712
    • Kerrigan, S.A.1    Smith, P.W.2    Stoodley, R.J.3
  • 128
    • 0034758713 scopus 로고    scopus 로고
    • Oseltamivir: A clinical and pharmacological perspective
    • Doucette K.E., and Aoki F.Y. Oseltamivir: A clinical and pharmacological perspective. Expert Opin. Pharmacother. 2 (2001) 1671-1683
    • (2001) Expert Opin. Pharmacother. , vol.2 , pp. 1671-1683
    • Doucette, K.E.1    Aoki, F.Y.2
  • 130
    • 33646567839 scopus 로고    scopus 로고
    • A short enantioselective pathway for the synthesis of the anti-influenza neuramidase inhibitor oseltamivir from 1,3-butadiene and acrylic acid
    • Yeung Y.Y., Hong S., and Corey E.J. A short enantioselective pathway for the synthesis of the anti-influenza neuramidase inhibitor oseltamivir from 1,3-butadiene and acrylic acid. J. Am. Chem. Soc. 128 (2006) 6310-6311
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6310-6311
    • Yeung, Y.Y.1    Hong, S.2    Corey, E.J.3
  • 131
    • 0842306928 scopus 로고    scopus 로고
    • Research and development of a second-generation process for oseltamivir phosphate, prodrug for a neuraminidase inhibitor
    • Harrington P.J., Brown J.D., Foderaro T., and Hughes R.C. Research and development of a second-generation process for oseltamivir phosphate, prodrug for a neuraminidase inhibitor. Org. Process Res. Dev. 8 (2004) 86-91
    • (2004) Org. Process Res. Dev. , vol.8 , pp. 86-91
    • Harrington, P.J.1    Brown, J.D.2    Foderaro, T.3    Hughes, R.C.4
  • 132
    • 6444232887 scopus 로고    scopus 로고
    • The synthetic development of the anti-influenza neuraminidase inhibitor oseltamivir phosphate (Tamiflu): A challenge for synthesis & process research
    • Abrecht S., Harrington P., Iding H., Karpf M., Trussardi R., Wirz B., and Zutter U. The synthetic development of the anti-influenza neuraminidase inhibitor oseltamivir phosphate (Tamiflu): A challenge for synthesis & process research. Chimia 58 (2004) 621-929
    • (2004) Chimia , vol.58 , pp. 621-929
    • Abrecht, S.1    Harrington, P.2    Iding, H.3    Karpf, M.4    Trussardi, R.5    Wirz, B.6    Zutter, U.7
  • 134
    • 0026662131 scopus 로고
    • Syntheses of sialic acid isomers with inhibitory activity against neuraminidase
    • Yamamoto T., Kumazawa H., Inami K., Teshima T., and Shiba T. Syntheses of sialic acid isomers with inhibitory activity against neuraminidase. Tetrahedron Lett. 33 (1992) 5791-5794
    • (1992) Tetrahedron Lett. , vol.33 , pp. 5791-5794
    • Yamamoto, T.1    Kumazawa, H.2    Inami, K.3    Teshima, T.4    Shiba, T.5
  • 137
    • 0036016097 scopus 로고    scopus 로고
    • Peramivir (BCX-1812, RWJ-270201): Potential new therapy for influenza
    • Sidwell R.W., and Smee D.F. Peramivir (BCX-1812, RWJ-270201): Potential new therapy for influenza. Expert Opin. Investig. Drugs 11 (2002) 859-869
    • (2002) Expert Opin. Investig. Drugs , vol.11 , pp. 859-869
    • Sidwell, R.W.1    Smee, D.F.2
  • 138
    • 29044434743 scopus 로고    scopus 로고
    • Anti-influenza virus activity of peramivir in mice with single intramuscular injection
    • Bantia S., Arnold C.S., Parker C.D., Upshaw R., and Chand P. Anti-influenza virus activity of peramivir in mice with single intramuscular injection. Antiviral Res. 69 (2006) 39-45
    • (2006) Antiviral Res. , vol.69 , pp. 39-45
    • Bantia, S.1    Arnold, C.S.2    Parker, C.D.3    Upshaw, R.4    Chand, P.5
  • 146
    • 0036078407 scopus 로고    scopus 로고
    • Recent advances in the discovery and development of anti-influenza drugs
    • Wang G.T. Recent advances in the discovery and development of anti-influenza drugs. Expert Opin. Ther. Patents 12 (2002) 845-861
    • (2002) Expert Opin. Ther. Patents , vol.12 , pp. 845-861
    • Wang, G.T.1
  • 147
    • 9644260491 scopus 로고    scopus 로고
    • Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core
    • Wang G.T., Wang S., Gentles R., Sowin T., Maring C.J., Kempf D.J., Kati W.M., Stoll V., Stewart K.D., and Laver G. Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core. Bioorg. Med. Chem. Lett. 15 (2005) 125-128
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 125-128
    • Wang, G.T.1    Wang, S.2    Gentles, R.3    Sowin, T.4    Maring, C.J.5    Kempf, D.J.6    Kati, W.M.7    Stoll, V.8    Stewart, K.D.9    Laver, G.10
  • 150
    • 0036569586 scopus 로고    scopus 로고
    • Total synthesis of A-315675: A potent inhibitor of influenza neuraminidase
    • Hanessian S., Bayrakdarian M., and Luo X. Total synthesis of A-315675: A potent inhibitor of influenza neuraminidase. J. Am. Chem. Soc. 124 (2002) 4716-4721
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4716-4721
    • Hanessian, S.1    Bayrakdarian, M.2    Luo, X.3


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