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Volumn 6, Issue 12, 2007, Pages 967-974

The war against influenza: Discovery and development of sialidase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; ANTIVIRUS AGENT; N ACETYL 2,3 DIDEHYDRO 2 DEOXYNEURAMINIC ACID; OSELTAMIVIR; PERAMIVIR; SIALIDASE; SIALIDASE INHIBITOR; UNCLASSIFIED DRUG; ZANAMIVIR;

EID: 36749056771     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd2400     Document Type: Article
Times cited : (627)

References (67)
  • 1
    • 20444436368 scopus 로고    scopus 로고
    • Human infection by avian influenza A H5N1
    • Yuen, K. Y. & Wong, S.S. Human infection by avian influenza A H5N1. Hong Kong Med. J. 11, 189-199 (2005).
    • (2005) Hong Kong Med. J , vol.11 , pp. 189-199
    • Yuen, K.Y.1    Wong, S.S.2
  • 2
    • 24644503497 scopus 로고    scopus 로고
    • Avian influenza (H5N1) viruses isolated from humans in Asia in 2004 exhibit increased virulence in mammals
    • Maines, T. R. et al. Avian influenza (H5N1) viruses isolated from humans in Asia in 2004 exhibit increased virulence in mammals. J. Virol. 79, 11788-11800 (2005).
    • (2005) J. Virol , vol.79 , pp. 11788-11800
    • Maines, T.R.1
  • 3
    • 34250617533 scopus 로고    scopus 로고
    • Influenza A/H5N1 virus infection in humans in Cambodia
    • Buchy, P. et al. Influenza A/H5N1 virus infection in humans in Cambodia. J. Clin. Virol. 39, 164-168 (2007).
    • (2007) J. Clin. Virol , vol.39 , pp. 164-168
    • Buchy, P.1
  • 4
    • 0025707394 scopus 로고
    • Prophylaxis and treatment of influenza
    • Douglas, R. G. Jr. Prophylaxis and treatment of influenza. N. Engl. J. Med. 322, 443-450 (1990).
    • (1990) N. Engl. J. Med , vol.322 , pp. 443-450
    • Douglas Jr., R.G.1
  • 5
    • 0028960915 scopus 로고
    • Rimantadine: A clinical perspective
    • Wintermeyer, S. M. & Nahata, M. C. Rimantadine: A clinical perspective. Ann. Pharmacother. 29, 299-310 (1995).
    • (1995) Ann. Pharmacother , vol.29 , pp. 299-310
    • Wintermeyer, S.M.1    Nahata, M.C.2
  • 6
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto, L. H., Holsinger, L. J. & Lamb, R. A. Influenza virus M2 protein has ion channel activity. Cell 69, 517-528 (1992).
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 8
    • 0037976526 scopus 로고
    • eds Mandell, G. L, Douglas, R. G. J. & Bennett, J. E, Churchill Livingston, New York
    • Hayden, F. G. in Principles and Practice of Infectious Disease (eds Mandell, G. L., Douglas, R. G. J. & Bennett, J. E.) 3-15 (Churchill Livingston, New York, 1993).
    • (1993) Principles and Practice of Infectious Disease , pp. 3-15
    • Hayden, F.G.1
  • 9
    • 0036850862 scopus 로고    scopus 로고
    • Pandemic influenza: Its origin and control
    • Laver, G. & Garman, E. Pandemic influenza: Its origin and control. Microbes Infect. 4, 1309-1316 (2002).
    • (2002) Microbes Infect , vol.4 , pp. 1309-1316
    • Laver, G.1    Garman, E.2
  • 10
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev Biochem. 69 531-569 (2000).
    • (2000) Annu. Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 13
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • Wagner, R., Matrosovich, M. & Klenk, H.-D. Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev. Med. Virol. 12, 159-166 (2002).
    • (2002) Rev. Med. Virol , vol.12 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.-D.3
  • 14
    • 0034103270 scopus 로고    scopus 로고
    • Oxford, J. S. Influenza A pandemics of the 20th century with special reference to 1918: Virology, pathology and epidemiology. Rev. Med. Virol. 10, 119-133 (2000).
    • Oxford, J. S. Influenza A pandemics of the 20th century with special reference to 1918: Virology, pathology and epidemiology. Rev. Med. Virol. 10, 119-133 (2000).
  • 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. & 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, 155-165 (1993).
    • (1993) Virus Res , vol.29 , pp. 155-165
    • Couceiro, J.N.1    Paulson, J.C.2    Baum, L.G.3
  • 17
    • 0034467921 scopus 로고    scopus 로고
    • Sialic acid species as a determinant of the host range of influenza A viruses
    • Suzuki, Y. et al. Sialic acid species as a determinant of the host range of influenza A viruses. J. Virol. 74, 11825-11831 (2000).
    • (2000) J. Virol , vol.74 , pp. 11825-11831
    • Suzuki, Y.1
  • 18
    • 0037341410 scopus 로고    scopus 로고
    • Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding
    • Matrosovich, M. & Klenk, H.-D. Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev. Med. Virol. 13, 85-97 (2003).
    • (2003) Rev. Med. Virol , vol.13 , pp. 85-97
    • Matrosovich, M.1    Klenk, H.-D.2
  • 19
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-373 (1981).
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 20
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W. et al. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426-431 (1988).
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1
  • 21
    • 0026580332 scopus 로고
    • Crystallographic detection of a second ligand binding site in influenza virus hemagglutinin
    • Sauter, N. K. et al. Crystallographic detection of a second ligand binding site in influenza virus hemagglutinin. Proc. Natl. Acad. Sci. USA 89, 324-328 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 324-328
    • Sauter, N.K.1
  • 22
    • 0028774043 scopus 로고
    • Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
    • Watowich, S. J., Skehel, J. J. & Wiley, D. C. Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure 2, 719-731 (1994).
    • (1994) Structure , vol.2 , pp. 719-731
    • Watowich, S.J.1    Skehel, J.J.2    Wiley, D.C.3
  • 23
    • 0021953619 scopus 로고
    • Structure and diversity of influenza virus neuraminidase
    • Colman, P. M. & Ward, C. W. Structure and diversity of influenza virus neuraminidase. Curr. Top. Microbiol. Immunol. 114, 177-255 (1985).
    • (1985) Curr. Top. Microbiol. Immunol , vol.114 , pp. 177-255
    • Colman, P.M.1    Ward, C.W.2
  • 24
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., Tobita, K., Ueda, M. & Compans, R. W. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61, 397-410 (1974).
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 25
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C., Eichelberger, M. C., Compans, R. W. & Air, G. M. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69, 1099-1106 (1995).
    • (1995) J. Virol , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 26
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J. N., Laver, W. G. & Colman P. M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303, 35-40 (1983).
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 27
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • 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).
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 28
    • 0037161611 scopus 로고    scopus 로고
    • Structural studies of the resistance of influenza virus neuraminidase to inhibitors
    • Smith, B. J. et al. Structural studies of the resistance of influenza virus neuraminidase to inhibitors. J. Med. Chem. 45 2207-2212 (2002).
    • (2002) J. Med. Chem , vol.45 , pp. 2207-2212
    • Smith, B.J.1
  • 29
    • 0037095563 scopus 로고    scopus 로고
    • Neuraminidase inhibitors as antivirals
    • Colman, P. M. Neuraminidase inhibitors as antivirals. Vaccine 20, S55-S58 (2002).
    • (2002) Vaccine , vol.20
    • Colman, P.M.1
  • 30
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, M. et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418-423 (1993).
    • (1993) Nature , vol.363 , pp. 418-423
    • von Itzstein, M.1
  • 31
    • 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. et al. 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, 681-690 (1997).
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 681-690
    • Kim, C.U.1
  • 32
    • 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. & Air, G. M. Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism. Biochemistry 26, 5351-5358 (1987).
    • (1987) Biochemistry , vol.26 , pp. 5351-5358
    • Lentz, M.R.1    Webster, R.G.2    Air, G.M.3
  • 33
    • 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. & von Itzstein, M. Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus. Eur. J. Biochem. 207, 335-343 (1992).
    • (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
  • 34
    • 0029149686 scopus 로고
    • Effect of substrate aglycon on enzyme mechanism in the reaction of sialidase from influenza virus
    • Tiralongo, J., Pegg, M. S. & von Itzstein, M. Effect of substrate aglycon on enzyme mechanism in the reaction of sialidase from influenza virus. FEBS Lett. 372, 148-150 (1995).
    • (1995) FEBS Lett , vol.372 , pp. 148-150
    • Tiralongo, J.1    Pegg, M.S.2    von Itzstein, M.3
  • 35
    • 0015452389 scopus 로고
    • Viral and bacterial neuraminidases
    • Drzeniek, R. Viral and bacterial neuraminidases. Curr. Top. Microbiol. Immunol. 59, 35-74 (1972).
    • (1972) Curr. Top. Microbiol. Immunol , vol.59 , pp. 35-74
    • Drzeniek, R.1
  • 36
    • 0020607871 scopus 로고
    • The interaction of substrate-related ketals with bacterial and viral neuraminidases
    • Flashner, M., Kessler, J. & Tanenbaum, S. W. The interaction of substrate-related ketals with bacterial and viral neuraminidases. Arch. Biochem. Biophys. 221, 188-196 (1983).
    • (1983) Arch. Biochem. Biophys , vol.221 , pp. 188-196
    • Flashner, M.1    Kessler, J.2    Tanenbaum, S.W.3
  • 37
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibodies, and inhibitors
    • Colman, P. M. Influenza virus neuraminidase: Structure, antibodies, and inhibitors. Protein Sci. 3, 1687-1696 (1994).
    • (1994) Protein Sci , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 38
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese, J. N., Epa, V. C. & Colman, P. M. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 4, 1081-1087 (1995).
    • (1995) Protein Sci , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 39
    • 0028325249 scopus 로고
    • Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis
    • Taylor, N. R. & von Itzstein, M. Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis. J. Med. Chem. 37, 616-624 (1994).
    • (1994) J. Med. Chem , vol.37 , pp. 616-624
    • Taylor, N.R.1    von Itzstein, M.2
  • 40
    • 0037530340 scopus 로고    scopus 로고
    • Recent strategies in the search for new anti-influenza therapies
    • Wilson, J. C. & von Itzstein, M. Recent strategies in the search for new anti-influenza therapies. Curr. Drug Targets 4, 389-408 (2003).
    • (2003) Curr. Drug Targets , vol.4 , pp. 389-408
    • Wilson, J.C.1    von Itzstein, M.2
  • 41
    • 36749037325 scopus 로고    scopus 로고
    • Colman, P. M. et al. Preparation of 2-deoxy-N acetylneuraminic acid derivatives as antiviral compounds which bind the active site of influenza neuraminidase. Patent WO9206691 (1992).
    • Colman, P. M. et al. Preparation of 2-deoxy-N acetylneuraminic acid derivatives as antiviral compounds which bind the active site of influenza neuraminidase. Patent WO9206691 (1992).
  • 42
    • 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. & Meindl, P. Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA). Virology 59, 490-498 (1974).
    • (1974) Virology , vol.59 , pp. 490-498
    • Palese, P.1    Schulman, J.L.2    Bodo, G.3    Meindl, P.4
  • 43
    • 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. & 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, 159-163 (1976).
    • (1976) J. Gen. Virol , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 45
    • 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
    • Nöhle, U., Beau, J. M. & 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. 126 543-548 (1982).
    • (1982) Eur J. Biochem , vol.126 , pp. 543-548
    • Nöhle, U.1    Beau, J.M.2    Schauer, R.3
  • 46
    • 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. et al. 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, 388-391 (1996).
    • (1996) J. Med. Chem , vol.39 , pp. 388-391
    • von Itzstein, M.1
  • 47
    • 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, 849-857 (1985).
    • (1985) J. Med. Chem , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 48
    • 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. & Jin, B. The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: A potent influenza virus sialidase inhibitor. Carbohydr. Res. 259 301-305 (1994).
    • (1994) Carbohydr. Res , vol.259 , pp. 301-305
    • von Itzstein, M.1    Wu, W.-Y.2    Jin, B.3
  • 49
    • 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 et al. 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, 40-44 (1993).
    • (1993) Glycoconj. J , vol.10 , pp. 40-44
    • Holzer, C.T.1
  • 50
    • 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. 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, 1473-1479 (1993).
    • (1993) Antimicrob. Agents Chemother , vol.37 , pp. 1473-1479
    • Woods, J.M.1
  • 51
    • 34247352375 scopus 로고    scopus 로고
    • A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: Potential link with severe adverse reactions to oseltamivir
    • Li, C. Y. et al. A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir. Cell Res. 17, 357-362 (2007).
    • (2007) Cell Res , vol.17 , pp. 357-362
    • Li, C.Y.1
  • 52
    • 33645458687 scopus 로고    scopus 로고
    • Unsaturated N-acetyl-D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase
    • Mann, M. C. et al. Unsaturated N-acetyl-D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase. Glycoconj. J. 23, 127-133 (2006).
    • (2006) Glycoconj. J , vol.23 , pp. 127-133
    • Mann, M.C.1
  • 53
    • 0034699492 scopus 로고    scopus 로고
    • BCX-1812 (RWJ-270201): Discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design
    • Babu, Y. S. et al. BCX-1812 (RWJ-270201): Discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design. J. Med. Chem. 43 3482-3486 (2000).
    • (2000) J. Med. Chem , vol.43 , pp. 3482-3486
    • Babu, Y.S.1
  • 54
    • 0037047524 scopus 로고    scopus 로고
    • Enantioselective synthesis of antiinfluenza compound A-315675
    • DeGoey D. A. et al. Enantioselective synthesis of antiinfluenza compound A-315675. J. Org. Chem. 67, 5445-5453 (2002).
    • (2002) J. Org. Chem , vol.67 , pp. 5445-5453
    • DeGoey, D.A.1
  • 55
    • 15444353753 scopus 로고    scopus 로고
    • Structure-activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors
    • Kim, C. U. et al. Structure-activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors. J. Med. Chem. 41, 2451-2460 (1998).
    • (1998) J. Med. Chem , vol.41 , pp. 2451-2460
    • Kim, C.U.1
  • 56
    • 27144468290 scopus 로고    scopus 로고
    • Avian flu: Isolation of drug-resistant H5N1 virus
    • Le, O. M. et al. Avian flu: Isolation of drug-resistant H5N1 virus. Nature 437, 1108 (2005).
    • (2005) Nature , vol.437 , pp. 1108
    • Le, O.M.1
  • 57
    • 33744995759 scopus 로고    scopus 로고
    • Oseltamivir and delirious behavior in children with influenza
    • Okumura, A. et al. Oseltamivir and delirious behavior in children with influenza. Pediatr. Infect. Dis. J. 25, 572 (2006).
    • (2006) Pediatr. Infect. Dis. J , vol.25 , pp. 572
    • Okumura, A.1
  • 58
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • Russell, R. J., et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443, 45-49 (2006).
    • (2006) Nature , vol.443 , pp. 45-49
    • Russell, R.J.1
  • 59
    • 33744975880 scopus 로고    scopus 로고
    • Antiviral therapy targeting viral polymerase
    • Tsai, C. H., Lee, P. Y., Stollar, V., Li, M. L. Antiviral therapy targeting viral polymerase. Curr. Pharm. Des. 12, 1339-1355 (2006).
    • (2006) Curr. Pharm. Des , vol.12 , pp. 1339-1355
    • Tsai, C.H.1    Lee, P.Y.2    Stollar, V.3    Li, M.L.4
  • 60
    • 34249307213 scopus 로고    scopus 로고
    • Avian influenza A (H5N1) infection: Targets and strategies for chemotherapeutic intervention
    • De Clercq, E. & Neyts, J. Avian influenza A (H5N1) infection: Targets and strategies for chemotherapeutic intervention. Trends Pharmacol. Sci. 28, 280-285 (2007).
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 280-285
    • De Clercq, E.1    Neyts, J.2
  • 61
    • 33646784370 scopus 로고    scopus 로고
    • Combination chemotherapy, a potential strategy for reducing the emergence of drug-resistant influenza A variants
    • Ilyushina, N. A. Bovin, N. V., Webster, R. G. & Govorkova, E. A. Combination chemotherapy, a potential strategy for reducing the emergence of drug-resistant influenza A variants. Antiviral Res. 70, 121-131 (2006).
    • (2006) Antiviral Res , vol.70 , pp. 121-131
    • Ilyushina, N.A.1    Bovin, N.V.2    Webster, R.G.3    Govorkova, E.A.4
  • 62
    • 34247257358 scopus 로고    scopus 로고
    • Development of a mucosal vaccine for influenza viruses: Preparation for a potential influenza pandemic
    • Hasegawa, H. et al. Development of a mucosal vaccine for influenza viruses: Preparation for a potential influenza pandemic. Expert Rev Vaccines 6, 193-201 (2007).
    • (2007) Expert Rev Vaccines , vol.6 , pp. 193-201
    • Hasegawa, H.1
  • 63
    • 34548611066 scopus 로고    scopus 로고
    • Influenza vaccine: The challenge of antigenic drift
    • Carrat, F. & Flahault, A. Influenza vaccine: The challenge of antigenic drift. Vaccine 25, 6852-6862 (2007).
    • (2007) Vaccine , vol.25 , pp. 6852-6862
    • Carrat, F.1    Flahault, A.2
  • 64
    • 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. & Colman P. M. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14 327-332 (1992).
    • (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
  • 65
    • 0027917892 scopus 로고
    • Influenza B virus neuraminidase can synthesize its own inhibitor
    • Burmeister, W. P. et al. Influenza B virus neuraminidase can synthesize its own inhibitor. Structure 1, 19-26 (1993).
    • (1993) Structure , vol.1 , pp. 19-26
    • Burmeister, W.P.1
  • 66
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • Zechel, D. L. & Withers. S. G. Dissection of nucleophilic and acid-base catalysis in glycosidases. Curr. Opin. Chem. Biol. 5, 643-649 (2001).
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2
  • 67
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., Laskowski, R. A. & Thornton, J. M. LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134 (1995).
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.