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Volumn 18, Issue 7, 2011, Pages 1050-1066

The medicinal potential of influenza virus surface proteins: Hemagglutinin and neuraminidase

Author keywords

Antibody; Antigenic shift; Hemagglutinin; Influenza; Inhibitor; Membrane fusion; Neuraminidase; Receptor specificity

Indexed keywords

5,7,4' TRIHYDROXY 8 METHOXYFLAVONE; A 315675; ABT 675; ANTIVIRUS AGENT; ARBIDOL; AURINTRICARBOXYLIC ACID; CATECHIN; CURCUMIN; DAS 181; ENFUVIRTIDE; EPITOPE; FLAVANONE DERIVATIVE; FLAVONOID; FLAVONOL DERIVATIVE; HEMAGGLUTININ INHIBITOR; INFLUENZA VIRUS HEMAGGLUTININ; ISOFLAVONE DERIVATIVE; LANINAMIVIR OCTANOATE; MARAVIROC; OSELTAMIVIR; PERAMIVIR; PROTEIN ANTIBODY; PTEROCARPAN DERIVATIVE; RIBAVIRIN; SIALIDASE INHIBITOR; TERT BUTYL HYDROQUINONE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS SIALIDASE; XANTHONE DERIVATIVE; ZANAMIVIR;

EID: 79952801722     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711794940815     Document Type: Article
Times cited : (21)

References (185)
  • 1
    • 70349547208 scopus 로고    scopus 로고
    • Resurrected pandemic influenza viruses
    • Tumpey, T.M.; Belser, J.A. Resurrected pandemic influenza viruses. Annu. Rev. Microbiol., 2009, 63, 79-98.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 79-98
    • Tumpey, T.M.1    Belser, J.A.2
  • 2
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann, G.; Noda, T.; Kawaoka, Y. Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature, 2009, 459(7249), 931-939.
    • (2009) Nature , vol.459 , Issue.7249 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 3
    • 69449091677 scopus 로고    scopus 로고
    • Emergence of oseltamivir-resistant influenza A H1N1 virus during the 2007- 2008 winter season in Luxembourg: Clinical characteristics and epidemiology
    • Mossong, J.; Opp, M.; Gerloff, N.; Hau, P.; Kremer, J.; Lackenby, A.; Gregory, V.; Even, J.; Huberty-Krau, P.; Muller, C.P.; Schneider, F. Emergence of oseltamivir-resistant influenza A H1N1 virus during the 2007- 2008 winter season in Luxembourg: Clinical characteristics and epidemiology. Antiviral Res., 2009, 84(1), 91-94.
    • (2009) Antiviral Res. , vol.84 , Issue.1 , pp. 91-94
    • Mossong, J.1    Opp, M.2    Gerloff, N.3    Hau, P.4    Kremer, J.5    Lackenby, A.6    Gregory, V.7    Even, J.8    Huberty-Krau, P.9    Muller, C.P.10    Schneider, F.11
  • 4
    • 68649122631 scopus 로고    scopus 로고
    • Emerging antiviral targets for influenza A virus
    • Krug, R.M.; Aramini, J.M. Emerging antiviral targets for influenza A virus. Trends Pharmacol. Sci., 2009, 30(6), 269-277.
    • (2009) Trends Pharmacol. Sci. , vol.30 , Issue.6 , pp. 269-277
    • Krug, R.M.1    Aramini, J.M.2
  • 6
    • 0036953373 scopus 로고    scopus 로고
    • Genetics of influenza viruses
    • DOI 10.1146/annurev.genet.36.052402.152757
    • Steinhauer, D.A.; Skehel, J.J. Genetics of influenza viruses. Annu. Rev. Genet., 2002, 36, 305-332. (Pubitemid 36109192)
    • (2002) Annual Review of Genetics , vol.36 , pp. 305-332
    • Steinhauer, D.A.1    Skehel, J.J.2
  • 7
    • 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., 2000, 69, 531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 8
    • 3142574848 scopus 로고    scopus 로고
    • H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
    • DOI 10.1016/j.virol.2004.04.040, PII S004268220400282X
    • Russell, R.J.; Gamblin, S.J.; Haire, L.F.; Stevens, D.J.; Xiao, B.; Ha, Y.; Skehel, J.J. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology, 2004, 325(2), 287-296. (Pubitemid 38902794)
    • (2004) Virology , vol.325 , Issue.2 , pp. 287-296
    • Russell, R.J.1    Gamblin, S.J.2    Haire, L.F.3    Stevens, D.J.4    Xiao, B.5    Ha, Y.6    Skehel, J.J.7
  • 10
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A.; Skehel, J.J.; Wiley, D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 1981, 289(5796), 366-373.
    • (1981) Nature , vol.289 , Issue.5796 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 12
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens, J.; Blixt, O.; Tumpey, T.M.; Taubenberger, J.K.; Paulson, J.C.; Wilson, I.A. Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science, 2006, 312(5772), 404-410.
    • (2006) Science , vol.312 , Issue.5772 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5    Wilson, I.A.6
  • 15
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • DOI 10.1016/S0092-8674(00)81771-7
    • Chen, J.; Lee, K.H.; Steinhauer, D.A.; Stevens, D.J.; Skehel, J.J.; Wiley, D.C. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell, 1998, 95(3), 409-417. (Pubitemid 28507328)
    • (1998) Cell , vol.95 , Issue.3 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 16
    • 66149151445 scopus 로고    scopus 로고
    • Acquisition of a polybasic hemagglutinin cleavage site by a low-pathogenic avian influenza virus is not sufficient for immediate transformation into a highly pathogenic strain
    • Stech, O.; Veits, J.; Weber, S.; Deckers, D.; Schroer, D.; Vahlenkamp, T.W.; Breithaupt, A.; Teifke, J.; Mettenleiter, T.C.; Stech, J. Acquisition of a polybasic hemagglutinin cleavage site by a low-pathogenic avian influenza virus is not sufficient for immediate transformation into a highly pathogenic strain. J. Virol., 2009, 83(11), 5864-5868.
    • (2009) J. Virol. , vol.83 , Issue.11 , pp. 5864-5868
    • Stech, O.1    Veits, J.2    Weber, S.3    Deckers, D.4    Schroer, D.5    Vahlenkamp, T.W.6    Breithaupt, A.7    Teifke, J.8    Mettenleiter, T.C.9    Stech, J.10
  • 17
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • DOI 10.1038/nsmb.1456, PII NSMB1456
    • Harrison, S.C. Viral membrane fusion. Nat. Struct. Mol. Biol., 2008, 15(7), 690-698. (Pubitemid 351932011)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.7 , pp. 690-698
    • Harrison, S.C.1
  • 20
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • DOI 10.1016/0092-8674(93)90260-W
    • Carr, C.M.; Kim, P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell, 1993, 73(4), 823-832. (Pubitemid 23159019)
    • (1993) Cell , vol.73 , Issue.4 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 21
    • 2442629758 scopus 로고    scopus 로고
    • 2 Refolds into the Trimeric Low-pH-Induced Conformation
    • DOI 10.1021/bi049807k
    • Swalley, S.E.; Baker, B.M.; Calder, L.J.; Harrison, S.C.; Skehel, J.J.; Wiley, D.C. Full-length influenza hemagglutinin HA2 refolds into the trimeric lowpH- induced conformation. Biochemistry, 2004, 43(19), 5902-5911. (Pubitemid 38623623)
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5902-5911
    • Swalley, S.E.1    Baker, B.M.2    Calder, L.J.3    Harrison, S.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 22
    • 33947661927 scopus 로고    scopus 로고
    • The relevance of salt bridges for the stability of the influenza virus hemagglutinin
    • DOI 10.1096/fj.06-7052hyp
    • Rachakonda, P.S.; Veit, M.; Korte, T.; Ludwig, K.; Bottcher, C.; Huang, Q.; Schmidt, M.F.; Herrmann, A. The relevance of salt bridges for the stability of the influenza virus hemagglutinin. FASEB J., 2007, 21(4), 995-1002. (Pubitemid 46495718)
    • (2007) FASEB Journal , vol.21 , Issue.4 , pp. 995-1002
    • Rachakonda, P.S.1    Veit, M.2    Korte, T.3    Ludwig, K.4    Bottcher, C.5    Huang, Q.6    Schmidt, M.F.G.7    Herrmann, A.8
  • 23
    • 0036151820 scopus 로고    scopus 로고
    • Protonation and stability of the globular domain of influenza virus hemagglutinin
    • Huang, Q.; Opitz, R.; Knapp, E.W.; Herrmann, A. Protonation and stability of the globular domain of influenza virus hemagglutinin. Biophys. J., 2002, 82(2), 1050-1058. (Pubitemid 34111241)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 1050-1058
    • Huang, Q.1    Opitz, R.2    Knapp, E.-W.3    Herrmann, A.4
  • 24
    • 0037811025 scopus 로고    scopus 로고
    • Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state: Stability and energetics of the hemagglutinin
    • DOI 10.1016/S0005-2736(03)00158-5
    • Huang, Q.; Sivaramakrishna, R.P.; Ludwig, K.; Korte, T.; Bottcher, C.; Herrmann, A. Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state: Stability and energetics of the hemagglutinin. Biochim. Biophys. Acta, 2003, 1614(1), 3-13. (Pubitemid 36851599)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1614 , Issue.1 , pp. 3-13
    • Huang, Q.1    Sivaramakrishna, R.P.2    Ludwig, K.3    Korte, T.4    Bottcher, C.5    Herrmann, A.6
  • 25
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • DOI 10.1016/j.virol.2007.08.035, PII S0042682207005636
    • Thoennes, S.; Li, Z.N.; Lee, B.J.; Langley, W.A.; Skehel, J.J.; Russell, R.J.; Steinhauer, D.A. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology, 2008, 370(2), 403-414. (Pubitemid 350199676)
    • (2008) Virology , vol.370 , Issue.2 , pp. 403-414
    • Thoennes, S.1    Li, Z.-N.2    Lee, B.-J.3    Langley, W.A.4    Skehel, J.J.5    Russell, R.J.6    Steinhauer, D.A.7
  • 26
    • 64049092310 scopus 로고    scopus 로고
    • Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein
    • Reed, M.L.; Yen, H.L.; DuBois, R.M.; Bridges, O.A.; Salomon, R.; Webster, R.G.; Russell, C.J. Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein. J. Virol., 2009, 83(8), 3568-3580.
    • (2009) J. Virol. , vol.83 , Issue.8 , pp. 3568-3580
    • Reed, M.L.1    Yen, H.L.2    DuBois, R.M.3    Bridges, O.A.4    Salomon, R.5    Webster, R.G.6    Russell, C.J.7
  • 27
    • 44649118051 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the hinge peptide from the hemagglutinin protein: Enhancement of the pH-responsive conformational change
    • DOI 10.1093/protein/gzn018
    • Casali, M.; Banta, S.; Zambonelli, C.; Megeed, Z.; Yarmush, M.L. Sitedirected mutagenesis of the hinge peptide from the hemagglutinin protein: Enhancement of the pH-responsive conformational change. Protein Eng. Des. Sel., 2008, 21(6), 395-404. (Pubitemid 351786658)
    • (2008) Protein Engineering, Design and Selection , vol.21 , Issue.6 , pp. 395-404
    • Casali, M.1    Banta, S.2    Zambonelli, C.3    Megeed, Z.4    Yarmush, M.L.5
  • 28
    • 59449104515 scopus 로고    scopus 로고
    • Energetics of the loop-to-helix transition leading to the coiled-coil structure of influenza virus hemagglutinin HA2 subunits
    • Huang, Q.; Korte, T.; Rachakonda, P.S.; Knapp, E.W.; Herrmann, A. Energetics of the loop-to-helix transition leading to the coiled-coil structure of influenza virus hemagglutinin HA2 subunits. Proteins, 2009, 74(2), 291-303.
    • (2009) Proteins , vol.74 , Issue.2 , pp. 291-303
    • Huang, Q.1    Korte, T.2    Rachakonda, P.S.3    Knapp, E.W.4    Herrmann, A.5
  • 29
    • 0036846370 scopus 로고    scopus 로고
    • Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin
    • DOI 10.1093/emboj/cdf559
    • Leikina, E.; Ramos, C.; Markovic, I.; Zimmerberg, J.; Chernomordik, L.V. Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin. EMBO J., 2002, 21(21), 5701-5710. (Pubitemid 35315270)
    • (2002) EMBO Journal , vol.21 , Issue.21 , pp. 5701-5710
    • Leikina, E.1    Ramos, C.2    Markovic, I.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 30
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz, J. Membrane fusion mediated by coiled coils: A hypothesis. Biophys. J., 2000, 78(2), 886-900. (Pubitemid 30211846)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 886-900
    • Bentz, J.1
  • 31
    • 0242708788 scopus 로고    scopus 로고
    • Fluorescence evidence for a loose self-assembly of the fusion peptide of influenza virus HA2 in the lipid bilayer
    • DOI 10.1080/0968708031000138046
    • Cheng, S.F.; Kantchev, A.B.; Chang, D.K. Fluorescence evidence for a loose self-assembly of the fusion peptide of influenza virus HA2 in the lipid bilayer. Mol. Membr. Biol., 2003, 20(4), 345-351. (Pubitemid 37392090)
    • (2003) Molecular Membrane Biology , vol.20 , Issue.4 , pp. 345-351
    • Cheng, S.-F.1    Kantchev, A.B.2    Chang, D.-K.3
  • 32
    • 0034671359 scopus 로고    scopus 로고
    • pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers
    • DOI 10.1006/jmbi.2000.4251
    • Han, X.; Tamm, L.K. pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers. J. Mol. Biol., 2000, 304(5), 953-965. (Pubitemid 32047093)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.5 , pp. 953-965
    • Han, X.1    Tamm, L.K.2
  • 33
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • DOI 10.1083/jcb.133.3.559
    • Danieli, T.; Pelletier, S.L.; Henis, Y.I.; White, J.M. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell. Biol., 1996, 133(3), 559-569. (Pubitemid 26160968)
    • (1996) Journal of Cell Biology , vol.133 , Issue.3 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 34
    • 33744958558 scopus 로고    scopus 로고
    • Membrane fusion by single influenza hemagglutinin trimers: Kinetic evidence from image analysis of hemagglutinin-reconstituted vesicles
    • DOI 10.1074/jbc.M600902200
    • Imai, M.; Mizuno, T.; Kawasaki, K. Membrane fusion by single influenza hemagglutinin trimers. Kinetic evidence from image analysis of hemagglutinin-reconstituted vesicles. J. Biol. Chem., 2006, 281(18), 12729-12735. (Pubitemid 43855363)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12729-12735
    • Imai, M.1    Mizuno, T.2    Kawasaki, K.3
  • 35
    • 33744983345 scopus 로고    scopus 로고
    • PH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide
    • Chang, D.K.; Cheng, S.F. pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide. Biochem. J., 2006, 396(3), 557-563.
    • (2006) Biochem. J. , vol.396 , Issue.3 , pp. 557-563
    • Chang, D.K.1    Cheng, S.F.2
  • 36
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian, S.A.; Hinterdorfer, P.; Baber, G.; Tamm, L.K. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J., 1995, 14(22), 5514-5523.
    • (1995) EMBO J. , vol.14 , Issue.22 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 37
    • 33646831343 scopus 로고    scopus 로고
    • Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity
    • DOI 10.1074/jbc.M512280200
    • Lai, A.L.; Park, H.; White, J.M.; Tamm, L.K. Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity. J. Biol. Chem., 2006, 281(9), 5760-5770. (Pubitemid 43847675)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5760-5770
    • Lai, A.L.1    Park, H.2    White, J.M.3    Tamm, L.K.4
  • 38
    • 34548212404 scopus 로고    scopus 로고
    • Locking the kink in the influenza hemagglutinin fusion domain structure
    • DOI 10.1074/jbc.M704008200
    • Lai, A.L.; Tamm, L.K. Locking the kink in the influenza hemagglutinin fusion domain structure. J. Biol. Chem., 2007, 282(33), 23946-23956. (Pubitemid 47328033)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.33 , pp. 23946-23956
    • Lai, A.L.1    Tamm, L.K.2
  • 39
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • DOI 10.1038/90434
    • Han, X.; Bushweller, J.H.; Cafiso, D.S.; Tamm, L.K. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol., 2001, 8(8), 715-720. (Pubitemid 32757933)
    • (2001) Nature Structural Biology , vol.8 , Issue.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 40
    • 44949233215 scopus 로고    scopus 로고
    • How to lose a kink and gain a helix: PH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers
    • DOI 10.1002/prot.21925
    • Jang, H.; Michaud-Agrawal, N.; Johnston, J.M.; Woolf, T.B. How to lose a kink and gain a helix: PH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers. Proteins, 2008, 72(1), 299-312. (Pubitemid 351809168)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 299-312
    • Jang, H.1    Michaud-Agrawal, N.2    Johnston, J.M.3    Woolf, T.B.4
  • 41
    • 68949109991 scopus 로고    scopus 로고
    • Fusion peptide from influenza hemagglutinin increases membrane surface order: An electron-spin resonance study
    • Ge, M.; Freed, J.H. Fusion peptide from influenza hemagglutinin increases membrane surface order: An electron-spin resonance study. Biophys. J., 2009, 96(12), 4925-4934.
    • (2009) Biophys. J. , vol.96 , Issue.12 , pp. 4925-4934
    • Ge, M.1    Freed, J.H.2
  • 43
    • 0036231335 scopus 로고    scopus 로고
    • New insights into the spring-loaded conformational change of influenza virus hemagglutinin
    • DOI 10.1128/JVI.76.9.4456-4466.2002
    • Gruenke, J.A.; Armstrong, R.T.; Newcomb, W.W.; Brown, J.C.; White, J.M. New insights into the spring-loaded conformational change of influenza virus hemagglutinin. J. Virol., 2002, 76(9), 4456-4466. (Pubitemid 34309582)
    • (2002) Journal of Virology , vol.76 , Issue.9 , pp. 4456-4466
    • Gruenke, J.A.1    Armstrong, R.T.2    Newcomb, W.W.3    Brown, J.C.4    White, J.M.5
  • 44
    • 67649989357 scopus 로고    scopus 로고
    • A single bicontinuous cubic phase induced by fusion peptides
    • Fuhrmans, M.; Knecht, V.; Marrink, S.J. A single bicontinuous cubic phase induced by fusion peptides. J. Am. Chem. Soc., 2009, 131(26), 9166-9167.
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.26 , pp. 9166-9167
    • Fuhrmans, M.1    Knecht, V.2    Marrink, S.J.3
  • 46
    • 0344120220 scopus 로고    scopus 로고
    • Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement
    • DOI 10.1016/j.virol.2003.07.006
    • Borrego-Diaz, E.; Peeples, M.E.; Markosyan, R.M.; Melikyan, G.B.; Cohen, F.S. Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement. Virology, 2003, 316(2), 234-244. (Pubitemid 37468527)
    • (2003) Virology , vol.316 , Issue.2 , pp. 234-244
    • Borrego-Diaz, E.1    Peeples, M.E.2    Markosyan, R.M.3    Melikyan, G.B.4    Cohen, F.S.5
  • 47
    • 29144520288 scopus 로고    scopus 로고
    • Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion
    • DOI 10.1083/jcb.200510018
    • Reese, C.; Mayer, A. Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion. J. Cell. Biol., 2005, 171(6), 981-990. (Pubitemid 41815830)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 981-990
    • Reese, C.1    Mayer, A.2
  • 49
    • 0345059375 scopus 로고    scopus 로고
    • Leash in the groove mechanism of membrane fusion
    • DOI 10.1038/nsb1012
    • Park, H.E.; Gruenke, J.A.; White, J.M. Leash in the groove mechanism of membrane fusion. Nat. Struct. Biol., 2003, 10(12), 1048-1053. (Pubitemid 37500497)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 1048-1053
    • Park, H.E.1    Gruenke, J.A.2    White, J.M.3
  • 50
    • 40949146126 scopus 로고    scopus 로고
    • Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex
    • Chang, D.K.; Cheng, S.F.; Kantchev, E.A.; Lin, C.H.; Liu, Y.T. Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex. BMC Biol., 2008, 6, 2.
    • (2008) BMC Biol. , vol.6 , pp. 2
    • Chang, D.K.1    Cheng, S.F.2    Kantchev, E.A.3    Lin, C.H.4    Liu, Y.T.5
  • 51
    • 42949150297 scopus 로고    scopus 로고
    • Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin
    • DOI 10.1085/jgp.200709932
    • Biswas, S.; Yin, S.R.; Blank, P.S.; Zimmerberg, J. Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin. J. Gen. Physiol., 2008, 131(5), 503-513. (Pubitemid 351620106)
    • (2008) Journal of General Physiology , vol.131 , Issue.5 , pp. 503-513
    • Biswas, S.1    Yin, S.-R.2    Blank, P.S.3    Zimmerberg, J.4
  • 52
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • DOI 10.1038/nature05816, PII NATURE05816
    • Varki, A. Glycan-based interactions involving vertebrate sialic-acidrecognizing proteins. Nature., 2007, 446(7139), 1023-1029. (Pubitemid 46676064)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1023-1029
    • Varki, A.1
  • 54
    • 33645278326 scopus 로고    scopus 로고
    • Avian flu: Influenza virus receptors in the human airway
    • Shinya, K.; Ebina, M.; Yamada, S.; Ono, M.; Kasai, N.; Kawaoka, Y. Avian flu: Influenza virus receptors in the human airway. Nature, 2006, 440(7083), 435-436.
    • (2006) Nature , vol.440 , Issue.7083 , pp. 435-436
    • Shinya, K.1    Ebina, M.2    Yamada, S.3    Ono, M.4    Kasai, N.5    Kawaoka, Y.6
  • 55
    • 0033856695 scopus 로고    scopus 로고
    • Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals
    • DOI 10.1128/JVI.74.18.8502-8512.2000
    • Matrosovich, M.; Tuzikov, A.; Bovin, N.; Gambaryan, A.; Klimov, A.; Castrucci, M.R.; Donatelli, I.; Kawaoka, Y. Early alterations of the receptorbinding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals. J. Virol., 2000, 74(18), 8502-8512. (Pubitemid 30666701)
    • (2000) Journal of Virology , vol.74 , Issue.18 , pp. 8502-8512
    • Matrosovich, M.1    Tuzikov, A.2    Bovin, N.3    Gambaryan, A.4    Klimov, A.5    Castrucci, M.R.6    Donatelli, I.7    Kawaoka, Y.8
  • 56
    • 31344448218 scopus 로고    scopus 로고
    • Influenza pandemics of the 20th century
    • Kilbourne, E.D. Influenza pandemics of the 20th century. Emerg. Infect. Dis., 2006, 12(1), 9-14. (Pubitemid 43143528)
    • (2006) Emerging Infectious Diseases , vol.12 , Issue.1 , pp. 9-14
    • Kilbourne, E.D.1
  • 58
    • 70349117661 scopus 로고    scopus 로고
    • Glycan arrays: Recent advances and future challenges
    • Oyelaran, O.; Gildersleeve, J.C. Glycan arrays: Recent advances and future challenges. Curr. Opin. Chem. Biol., 2009, 13(4), 406-413.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , Issue.4 , pp. 406-413
    • Oyelaran, O.1    Gildersleeve, J.C.2
  • 59
    • 70350000599 scopus 로고    scopus 로고
    • Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands
    • Taylor, M.E.; Drickamer, K. Structural insights into what glycan arrays tell us about how glycan-binding proteins interact with their ligands. Glycobiology, 2009, 19(11), 1155-1162.
    • (2009) Glycobiology , vol.19 , Issue.11 , pp. 1155-1162
    • Taylor, M.E.1    Drickamer, K.2
  • 61
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus
    • DOI 10.1126/science.1093373
    • Stevens, J.; Corper, A.L.; Basler, C.F.; Taubenberger, J.K.; Palese, P.; Wilson, I.A. Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science, 2004, 303(5665), 1866-1870. (Pubitemid 38374878)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 63
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • DOI 10.1016/j.jmb.2005.11.002, PII S0022283605013707
    • Stevens, J.; Blixt, O.; Glaser, L.; Taubenberger, J.K.; Palese, P.; Paulson, J.C.; Wilson, I.A. Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J. Mol. Biol., 2006, 355(5), 1143-1155. (Pubitemid 43012153)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 1143-1155
    • Stevens, J.1    Blixt, O.2    Glaser, L.3    Taubenberger, J.K.4    Palese, P.5    Paulson, J.C.6    Wilson, I.A.7
  • 69
    • 64049108321 scopus 로고    scopus 로고
    • Role of sialic acid binding specificity of the 1918 influenza virus hemagglutinin protein in virulence and pathogenesis for mice
    • Qi, L.; Kash, J.C.; Dugan, V.G.; Wang, R.; Jin, G.; Cunningham, R.E.; Taubenberger, J.K. Role of sialic acid binding specificity of the 1918 influenza virus hemagglutinin protein in virulence and pathogenesis for mice. J. Virol., 2009, 83(8), 3754-3761.
    • (2009) J. Virol. , vol.83 , Issue.8 , pp. 3754-3761
    • Qi, L.1    Kash, J.C.2    Dugan, V.G.3    Wang, R.4    Jin, G.5    Cunningham, R.E.6    Taubenberger, J.K.7
  • 72
    • 67650892251 scopus 로고    scopus 로고
    • The persistent legacy of the 1918 influenza virus
    • Morens, D.M.; Taubenberger, J.K.; Fauci, A.S. The persistent legacy of the 1918 influenza virus. N. Engl. J. Med., 2009, 361(3), 225-229.
    • (2009) N. Engl. J. Med. , vol.361 , Issue.3 , pp. 225-229
    • Morens, D.M.1    Taubenberger, J.K.2    Fauci, A.S.3
  • 77
    • 3142631790 scopus 로고    scopus 로고
    • Interregional transmission of the internal protein genes of H2 influenza virus in migratory ducks from North America to Eurasia
    • DOI 10.1023/B:VIRU.0000032791.26573.f1
    • Liu, J.H.; Okazaki, K.; Bai, G.R.; Shi, W.M.; Mweene, A.; Kida, H. Interregional transmission of the internal protein genes of H2 influenza virus in migratory ducks from North America to Eurasia. Virus Genes., 2004, 29(1), 81-86. (Pubitemid 38903594)
    • (2004) Virus Genes , vol.29 , Issue.1 , pp. 81-86
    • Liu, J.1    Okazaki, K.2    Bai, G.3    Shi, W.4    Mweene, A.5    Kida, H.6
  • 81
    • 34147098850 scopus 로고    scopus 로고
    • Avian-virus-like receptor specificity of the hemagglutinin impedes influenza virus replication in cultures of human airway epithelium
    • DOI 10.1016/j.virol.2006.11.030, PII S0042682206008798
    • Matrosovich, M.; Matrosovich, T.; Uhlendorff, J.; Garten, W.; Klenk, H.D. Avian-virus-like receptor specificity of the hemagglutinin impedes influenza virus replication in cultures of human airway epithelium. Virology, 2007, 361(2), 384-390. (Pubitemid 46574852)
    • (2007) Virology , vol.361 , Issue.2 , pp. 384-390
    • Matrosovich, M.1    Matrosovich, T.2    Uhlendorff, J.3    Garten, W.4    Klenk, H.-D.5
  • 84
    • 0034532059 scopus 로고    scopus 로고
    • Change in receptor-binding specificity of recent human influenza A viruses (H3N2): A single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides
    • DOI 10.1006/viro.2000.0679
    • Nobusawa, E.; Ishihara, H.; Morishita, T.; Sato, K.; Nakajima, K. Change in receptor-binding specificity of recent human influenza A viruses (H3N2): A single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides. Virology, 2000, 278(2), 587-596. (Pubitemid 32012792)
    • (2000) Virology , vol.278 , Issue.2 , pp. 587-596
    • Nobusawa, E.1    Ishihara, H.2    Morishita, T.3    Sato, K.4    Nakajima, K.5
  • 85
    • 0035840797 scopus 로고    scopus 로고
    • Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes
    • DOI 10.1006/viro.2001.1121
    • Medeiros, R.; Escriou, N.; Naffakh, N.; Manuguerra, J.C.; van der Werf, S. Hemagglutinin residues of recent human A(H3N2) influenza viruses that contribute to the inability to agglutinate chicken erythrocytes. Virology, 2001, 289(1), 74-85. (Pubitemid 33016239)
    • (2001) Virology , vol.289 , Issue.1 , pp. 74-85
    • Medeiros, R.1    Escriou, N.2    Naffakh, N.3    Manuguerra, J.-C.4    Van Der Werf, S.5
  • 86
    • 35148875043 scopus 로고    scopus 로고
    • Alterations in receptor binding properties of recent human influenza H3N2 viruses are associated with reduced natural killer cell lysis of infected cells
    • DOI 10.1128/JVI.01217-07
    • Owen, R.E.; Yamada, E.; Thompson, C.I.; Phillipson, L.J.; Thompson, C.; Taylor, E.; Zambon, M.; Osborn, H.M.; Barclay, W.S.; Borrow, P. Alterations in receptor binding properties of recent human influenza H3N2 viruses are associated with reduced natural killer cell lysis of infected cells. J. Virol., 2007, 81(20), 11170-11178. (Pubitemid 47536089)
    • (2007) Journal of Virology , vol.81 , Issue.20 , pp. 11170-11178
    • Owen, R.E.1    Yamada, E.2    Thompson, C.I.3    Phillipson, L.J.4    Thompson, C.5    Taylor, E.6    Zambon, M.7    Osborn, H.M.I.8    Barclay, W.S.9    Borrow, P.10
  • 87
    • 4444376554 scopus 로고    scopus 로고
    • Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin
    • DOI 10.1128/JVI.78.18.9605-9611.2004
    • Abe, Y.; Takashita, E.; Sugawara, K.; Matsuzaki, Y.; Muraki, Y.; Hongo, S. Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. J. Virol., 2004, 78(18), 9605-9611. (Pubitemid 39187078)
    • (2004) Journal of Virology , vol.78 , Issue.18 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 89
    • 61649123517 scopus 로고    scopus 로고
    • Sialic acid recognition is a key determinant of influenza A virus tropism in murine trachea epithelial cell cultures
    • Pekosz, A.; Newby, C.; Bose, P.S.; Lutz, A. Sialic acid recognition is a key determinant of influenza A virus tropism in murine trachea epithelial cell cultures. Virology, 2009, 386(1), 61-67.
    • (2009) Virology , vol.386 , Issue.1 , pp. 61-67
    • Pekosz, A.1    Newby, C.2    Bose, P.S.3    Lutz, A.4
  • 91
    • 48749093648 scopus 로고    scopus 로고
    • Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity
    • Stevens, J.; Blixt, O.; Chen, L.M.; Donis, R.O.; Paulson, J.C.; Wilson, I.A. Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity. J. Mol. Biol., 2008, 381(5), 1382-1394.
    • (2008) J. Mol. Biol. , vol.381 , Issue.5 , pp. 1382-1394
    • Stevens, J.1    Blixt, O.2    Chen, L.M.3    Donis, R.O.4    Paulson, J.C.5    Wilson, I.A.6
  • 92
    • 50549103325 scopus 로고    scopus 로고
    • Positive selection at the receptor-binding site of haemagglutinin H5 in viral sequences derived from human tissues
    • Kongchanagul, A.; Suptawiwat, O.; Kanrai, P.; Uiprasertkul, M.; Puthavathana, P.; Auewarakul, P. Positive selection at the receptor-binding site of haemagglutinin H5 in viral sequences derived from human tissues. J. Gen. Virol., 2008, 89(Pt 8), 1805-1810.
    • (2008) J. Gen. Virol. , vol.89 , Issue.PART 8 , pp. 1805-1810
    • Kongchanagul, A.1    Suptawiwat, O.2    Kanrai, P.3    Uiprasertkul, M.4    Puthavathana, P.5    Auewarakul, P.6
  • 95
    • 66149130765 scopus 로고    scopus 로고
    • Minimal molecular constraints for respiratory droplet transmission of an avian-human H9N2 influenza A virus
    • Sorrell, E.M.; Wan, H.; Araya, Y.; Song, H.; Perez, D.R. Minimal molecular constraints for respiratory droplet transmission of an avian-human H9N2 influenza A virus. Proc. Natl. Acad. Sci. U. S. A., 2009, 106(18), 7565-7570.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.18 , pp. 7565-7570
    • Sorrell, E.M.1    Wan, H.2    Araya, Y.3    Song, H.4    Perez, D.R.5
  • 97
    • 70350342281 scopus 로고    scopus 로고
    • Swine flu vaccines: Reaching the finish line
    • Davies, J. Swine flu vaccines: Reaching the finish line. Cell, 2009, 139(3), 449-451.
    • (2009) Cell , vol.139 , Issue.3 , pp. 449-451
    • Davies, J.1
  • 98
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton, A.J.; Brownlee, G.G.; Yewdell, J.W.; Gerhard, W. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell, 1982, 31(2 Pt 1), 417-427. (Pubitemid 13178866)
    • (1982) Cell , vol.31 , Issue.2 II , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 100
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • DOI 10.1038/289373a0
    • Wiley, D.C.; Wilson, I.A.; Skehel, J.J. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature, 1981, 289(5796), 373-378. (Pubitemid 11135143)
    • (1981) Nature , vol.289 , Issue.5796 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2
  • 102
    • 0036441307 scopus 로고    scopus 로고
    • Mechanism of neutralization of influenza virus infectivity by antibodies
    • DOI 10.1006/viro.2002.1625
    • Knossow, M.; Gaudier, M.; Douglas, A.; Barrere, B.; Bizebard, T.; Barbey, C.; Gigant, B.; Skehel, J.J. Mechanism of neutralization of influenza virus infectivity by antibodies. Virology, 2002, 302(2), 294-298. (Pubitemid 35373857)
    • (2002) Virology , vol.302 , Issue.2 , pp. 294-298
    • Knossow, M.1    Gaudier, M.2    Douglas, A.3    Barrere, B.4    Bizebard, T.5    Barbey, C.6    Gigant, B.7    Skehel, J.J.8
  • 103
    • 66649100756 scopus 로고    scopus 로고
    • Differential neutralization efficiency of hemagglutinin epitopes, antibody interference, and the design of influenza vaccines
    • Ndifon, W.; Wingreen, N.S.; Levin, S.A. Differential neutralization efficiency of hemagglutinin epitopes, antibody interference, and the design of influenza vaccines. Proc. Natl. Acad. Sci. U. S. A., 2009, 106(21), 8701-8706.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.21 , pp. 8701-8706
    • Ndifon, W.1    Wingreen, N.S.2    Levin, S.A.3
  • 104
    • 33847623088 scopus 로고    scopus 로고
    • Antibodies specific to the HA2 glycopolypeptide of influenza A virus haemagglutinin with fusion-inhibition activity contribute to the protection of mice against lethal infection
    • DOI 10.1099/vir.0.82563-0
    • Gocnik, M.; Fislova, T.; Sladkova, T.; Mucha, V.; Kostolansky, F.; Vareckova, E. Antibodies specific to the HA2 glycopolypeptide of influenza A virus haemagglutinin with fusion-inhibition activity contribute to the protection of mice against lethal infection. J. Gen. Virol., 2007, 88(Pt 3), 951-955. (Pubitemid 46359566)
    • (2007) Journal of General Virology , vol.88 , Issue.3 , pp. 951-955
    • Gocnik, M.1    Fislova, T.2    Sladkova, T.3    Mucha, V.4    Kostolansky, F.5    Vareckova, E.6
  • 109
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • DOI 10.1002/rmv.352
    • Wagner, R.; Matrosovich, M.; Klenk, H.D. Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev. Med. Virol., 2002, 12(3), 159-166. (Pubitemid 34516947)
    • (2002) Reviews in Medical Virology , vol.12 , Issue.3 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.-D.3
  • 110
    • 0001147595 scopus 로고
    • Epidemiologic and immunologic significance of age distribution of antibody to antigenic variants of influenza virus
    • Davenport, F.M.; Hennessy, A.V.; Francis, T. Jr. Epidemiologic and immunologic significance of age distribution of antibody to antigenic variants of influenza virus. J. Exp. Med., 1953, 98(6), 641-656.
    • (1953) J. Exp. Med. , vol.98 , Issue.6 , pp. 641-656
    • Davenport, F.M.1    Hennessy, A.V.2    Francis, Jr.T.3
  • 112
    • 84960989501 scopus 로고
    • Influenza: The new acquaintance
    • Francis Jr, T. Influenza: The new acquaintance. Ann. Intern. Med., 1953, 39, 203-221.
    • (1953) Ann. Intern. Med. , vol.39 , pp. 203-221
    • Francis, Jr.T.1
  • 113
    • 0032581491 scopus 로고    scopus 로고
    • Original antigenic sin impairs cytotoxic T lymphocyte responses to viruses bearing variant epitopes
    • DOI 10.1038/28860
    • Klenerman, P.; Zinkernagel, R.M. Original antigenic sin impairs cytotoxic T lymphocyte responses to viruses bearing variant epitopes. Nature, 1998, 394(6692), 482-485. (Pubitemid 28373959)
    • (1998) Nature , vol.394 , Issue.6692 , pp. 482-485
    • Klenerman, P.1    Zinkernagel, R.M.2
  • 114
    • 70349237173 scopus 로고    scopus 로고
    • Original antigenic sin responses to influenza viruses
    • Kim, J.H.; Skountzou, I.; Compans, R.; Jacob, J. Original antigenic sin responses to influenza viruses. J. Immunol., 2009, 183(5), 3294-3301.
    • (2009) J. Immunol. , vol.183 , Issue.5 , pp. 3294-3301
    • Kim, J.H.1    Skountzou, I.2    Compans, R.3    Jacob, J.4
  • 116
    • 0037341410 scopus 로고    scopus 로고
    • Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding
    • DOI 10.1002/rmv.372
    • Matrosovich, M.; Klenk, H.D. Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev. Med. Virol., 2003, 13(2), 85-97. (Pubitemid 36323672)
    • (2003) Reviews in Medical Virology , vol.13 , Issue.2 , pp. 85-97
    • Matrosovich, M.1    Klenk, H.-D.2
  • 117
    • 35348868611 scopus 로고    scopus 로고
    • Recent anti-influenza strategies in multivalent sialyloligosaccharides and sialylmimetics approaches
    • Sun, X.L. Recent anti-influenza strategies in multivalent sialyloligosaccharides and sialylmimetics approaches. Curr. Med. Chem., 2007, 14(21), 2304-2313.
    • (2007) Curr. Med. Chem. , vol.14 , Issue.21 , pp. 2304-2313
    • Sun, X.L.1
  • 118
    • 33845946003 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of artificial glycopolypeptides containing multivalent sialyloligosaccharides with a γ-polyglutamic acid backbone and their effect on inhibition of infection by influenza viruses
    • DOI 10.1016/j.bmc.2006.11.006, PII S0968089606009357
    • Ogata, M.; Murata, T.; Murakami, K.; Suzuki, T.; Hidari, K.I.; Suzuki, Y.; Usui, T. Chemoenzymatic synthesis of artificial glycopolypeptides containing multivalent sialyloligosaccharides with a gamma-polyglutamic acid backbone and their effect on inhibition of infection by influenza viruses. Bioorg. Med. Chem., 2007, 15(3), 1383-1393. (Pubitemid 46038129)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.3 , pp. 1383-1393
    • Ogata, M.1    Murata, T.2    Murakami, K.3    Suzuki, T.4    Hidari, K.I.P.J.5    Suzuki, Y.6    Usui, T.7
  • 119
    • 49449114141 scopus 로고    scopus 로고
    • Design of a sialylglycopolymer with a chitosan backbone having efficient inhibitory activity against influenza virus infection
    • Umemura, M.; Itoh, M.; Makimura, Y.; Yamazaki, K.; Umekawa, M.; Masui, A.; Matahira, Y.; Shibata, M.; Ashida, H.; Yamamoto, K. Design of a sialylglycopolymer with a chitosan backbone having efficient inhibitory activity against influenza virus infection. J. Med. Chem., 2008, 51(15), 4496-4503.
    • (2008) J. Med. Chem. , vol.51 , Issue.15 , pp. 4496-4503
    • Umemura, M.1    Itoh, M.2    Makimura, Y.3    Yamazaki, K.4    Umekawa, M.5    Masui, A.6    Matahira, Y.7    Shibata, M.8    Ashida, H.9    Yamamoto, K.10
  • 120
    • 51849164204 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis, characterization, and application of glycopolymers carrying lactosamine repeats as entry inhibitors against influenza virus infection
    • Hidari, K.I.; Murata, T.; Yoshida, K.; Takahashi, Y.; Minamijima, Y.H.; Miwa, Y.; Adachi, S.; Ogata, M.; Usui, T.; Suzuki, Y.; Suzuki, T. Chemoenzymatic synthesis, characterization, and application of glycopolymers carrying lactosamine repeats as entry inhibitors against influenza virus infection. Glycobiology, 2008, 18(10), 779-788.
    • (2008) Glycobiology , vol.18 , Issue.10 , pp. 779-788
    • Hidari, K.I.1    Murata, T.2    Yoshida, K.3    Takahashi, Y.4    Minamijima, Y.H.5    Miwa, Y.6    Adachi, S.7    Ogata, M.8    Usui, T.9    Suzuki, Y.10    Suzuki, T.11
  • 122
    • 34548716936 scopus 로고    scopus 로고
    • Biological evaluation of anti-influenza viral activity of semi-synthetic catechin derivatives
    • DOI 10.1016/j.antiviral.2007.07.001, PII S0166354207003713
    • Song, J.M.; Park, K.D.; Lee, K.H.; Byun, Y.H.; Park, J.H.; Kim, S.H.; Kim, J.H.; Seong, B.L. Biological evaluation of anti-influenza viral activity of semi-synthetic catechin derivatives. Antiviral Res., 2007, 76(2), 178-185. (Pubitemid 47422312)
    • (2007) Antiviral Research , vol.76 , Issue.2 , pp. 178-185
    • Song, J.M.1    Park, K.D.2    Lee, K.H.3    Byun, Y.H.4    Park, J.H.5    Kim, S.H.6    Kim, J.H.7    Seong, B.L.8
  • 123
    • 0036812633 scopus 로고    scopus 로고
    • A double blind, placebo-controlled study of Andrographis paniculata fixed combination Kan Jang in the treatment of acute upper respiratory tract infections including sinusitis
    • Gabrielian, E.S.; Shukarian, A.K.; Goukasova, G.I.; Chandanian, G.L.; Panossian, A.G.; Wikman, G.; Wagner, H. A double blind, placebocontrolled study of Andrographis paniculata fixed combination Kan Jang in the treatment of acute upper respiratory tract infections including sinusitis. Phytomedicine, 2002, 9(7), 589-597. (Pubitemid 35397789)
    • (2002) Phytomedicine , vol.9 , Issue.7 , pp. 589-597
    • Gabrielian, E.S.1    Shukarian, A.K.2    Goukasova, G.I.3    Chandanian, G.L.4    Panossian, A.G.5    Wikman, G.6    Wagner, H.7
  • 124
    • 69149103489 scopus 로고    scopus 로고
    • Activity of andrographolide and its derivatives against influenza virus in vivo and in vitro
    • Chen, J.X.; Xue, H.J.; Ye, W.C.; Fang, B.H.; Liu, Y.H.; Yuan, S.H.; Yu, P.; Wang, Y.Q. Activity of andrographolide and its derivatives against influenza virus in vivo and in vitro. Biol. Pharm. Bull., 2009, 32(8), 1385-1391.
    • (2009) Biol. Pharm. Bull. , vol.32 , Issue.8 , pp. 1385-1391
    • Chen, J.X.1    Xue, H.J.2    Ye, W.C.3    Fang, B.H.4    Liu, Y.H.5    Yuan, S.H.6    Yu, P.7    Wang, Y.Q.8
  • 127
    • 33845405207 scopus 로고    scopus 로고
    • Inhibition of influenza virus infection by a novel antiviral peptide that targets viral attachment to cells
    • DOI 10.1128/JVI.01678-06
    • Jones, J.C.; Turpin, E.A.; Bultmann, H.; Brandt, C.R.; Schultz-Cherry, S. Inhibition of influenza virus infection by a novel antiviral peptide that targets viral attachment to cells. J. Virol., 2006, 80(24), 11960-11967. (Pubitemid 44904345)
    • (2006) Journal of Virology , vol.80 , Issue.24 , pp. 11960-11967
    • Jones, J.C.1    Turpin, E.A.2    Bultmann, H.3    Brandt, C.R.4    Schultz-Cherry, S.5
  • 128
    • 70350439598 scopus 로고    scopus 로고
    • A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells
    • Rajik, M.; Omar, A.R.; Ideris, A.; Hassan, S.S.; Yusoff, K. A novel peptide inhibits the influenza virus replication by preventing the viral attachment to the host cells. Int. J. Biol. Sci., 2009, 5(6), 543-548.
    • (2009) Int. J. Biol. Sci. , vol.5 , Issue.6 , pp. 543-548
    • Rajik, M.1    Omar, A.R.2    Ideris, A.3    Hassan, S.S.4    Yusoff, K.5
  • 129
    • 67650739109 scopus 로고    scopus 로고
    • Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library
    • Matsubara, T.; Sumi, M.; Kubota, H.; Taki, T.; Okahata, Y.; Sato, T. Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library. J. Med. Chem., 2009, 52(14), 4247-4256.
    • (2009) J. Med. Chem. , vol.52 , Issue.14 , pp. 4247-4256
    • Matsubara, T.1    Sumi, M.2    Kubota, H.3    Taki, T.4    Okahata, Y.5    Sato, T.6
  • 130
    • 2942560767 scopus 로고    scopus 로고
    • Phage display-derived peptides as therapeutic alternatives to antibodies
    • DOI 10.1016/S1359-6446(04)03104-6, PII S1359644604031046
    • Ladner, R.C.; Sato, A.K.; Gorzelany, J.; de Souza, M. Phage display-derived peptides as therapeutic alternatives to antibodies. Drug Discov. Today, 2004, 9(12), 525-529. (Pubitemid 38739333)
    • (2004) Drug Discovery Today , vol.9 , Issue.12 , pp. 525-529
    • Ladner, R.C.1    Sato, A.K.2    Gorzelany, J.3    De Souza, M.4
  • 132
    • 0032766880 scopus 로고    scopus 로고
    • Safety and efficacy of the neuraminidase inhibitor zanamivir in treating influenza virus infection in adults: Results from Japan
    • Matsumoto, K.; Ogawa, N.; Nerome, K.; Numazaki, Y.; Kawakami, Y.; Shirato, K.; Arakawa, M.; Kudoh, S.; Shimokata, K.; Nakajima, S.; Yamakido, M.; Kashiwagi, S.; Nagatake, T. Safety and efficacy of the neuraminidase inhibitor zanamivir in treating influenza virus infection in adults: Results from Japan. GG167 Group. Antivir. Ther., 1999, 4(2), 61-68. (Pubitemid 29355843)
    • (1999) Antiviral Therapy , vol.4 , Issue.2 , pp. 61-68
    • Matsumoto, K.1
  • 134
    • 44349125733 scopus 로고    scopus 로고
    • Arbidol: A broad-spectrum antiviral compound that blocks viral fusion
    • DOI 10.2174/092986708784049658
    • Boriskin, Y.S.; Leneva, I.A.; Pecheur, E.I.; Polyak, S.J. Arbidol: A broadspectrum antiviral compound that blocks viral fusion. Curr. Med. Chem., 2008, 15(10), 997-1005. (Pubitemid 351736402)
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.10 , pp. 997-1005
    • Boriskin, Y.S.1    Leneva, I.A.2    Pecheur, E.-I.3    Polyak, S.J.4
  • 135
    • 58249083139 scopus 로고    scopus 로고
    • Characteristics of arbidol-resistant mutants of influenza virus: Implications for the mechanism of anti-influenza action of arbidol
    • Leneva, I.A.; Russell, R.J.; Boriskin, Y.S.; Hay, A.J. Characteristics of arbidol-resistant mutants of influenza virus: Implications for the mechanism of anti-influenza action of arbidol. Antiviral. Res., 2009, 81(2), 132-140.
    • (2009) Antiviral. Res. , vol.81 , Issue.2 , pp. 132-140
    • Leneva, I.A.1    Russell, R.J.2    Boriskin, Y.S.3    Hay, A.J.4
  • 136
    • 36949001617 scopus 로고    scopus 로고
    • Strategies of development of antiviral agents directed against influenza virus replication
    • DOI 10.2174/138161207782794248
    • Hsieh, H.P.; Hsu, J.T. Strategies of development of antiviral agents directed against influenza virus replication. Curr. Pharm. Des., 2007, 13(34), 3531-3542. (Pubitemid 350238942)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.34 , pp. 3531-3542
    • Hsieh, H.-P.1    Hsu, J.T.-A.2
  • 137
    • 0030753409 scopus 로고    scopus 로고
    • Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: Irreversible inhibition of infectivity
    • Hoffman, L.R.; Kuntz, I.D.; White, J.M. Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: Irreversible inhibition of infectivity. J. Virol., 1997, 71(11), 8808-8820. (Pubitemid 27446465)
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8808-8820
    • Hoffman, L.R.1    Kuntz, I.D.2    White, J.M.3
  • 139
    • 0022643192 scopus 로고
    • Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy
    • DOI 10.1016/0042-6822(86)90084-X
    • Murti, K.G.; Webster, R.G. Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy. Virology, 1986, 149(1), 36-43. (Pubitemid 16174976)
    • (1986) Virology , vol.149 , Issue.1 , pp. 36-43
    • Murti, K.G.1    Webster, R.G.2
  • 140
    • 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., 1995, 69(2), 1099-1106.
    • (1995) J. Virol. , vol.69 , Issue.2 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 141
    • 33845991182 scopus 로고    scopus 로고
    • Structure and functions of influenza virus neuraminidase
    • DOI 10.2174/092986707779313444
    • Gong, J.; Xu, W.; Zhang, J. Structure and functions of influenza virus neuraminidase. Curr. Med. Chem., 2007, 14(1), 113-122. (Pubitemid 46050308)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.1 , pp. 113-122
    • Gong, J.1    Xu, W.2    Zhang, J.3
  • 142
    • 0025895628 scopus 로고
    • Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution
    • Varghese, J.N.; Colman, P.M. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. J. Mol. Biol., 1991, 221(2), 473-486. (Pubitemid 121003395)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.2 , pp. 473-486
    • Varghese, J.N.1    Colman, P.M.2
  • 143
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: Discovery and development of sialidase inhibitors
    • von Itzstein, M. The war against influenza: Discovery and development of sialidase inhibitors. Nat. Rev. Drug Discov., 2007, 6(12), 967-974.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , Issue.12 , pp. 967-974
    • Von Itzstein, M.1
  • 144
    • 36749080401 scopus 로고    scopus 로고
    • Recent progress in rational drug design of neuraminidase inhibitors
    • DOI 10.2174/092986707782360024
    • Liu, Y.; Zhang, J.; Xu, W. Recent progress in rational drug design of neuraminidase inhibitors. Curr. Med. Chem., 2007, 14(27), 2872-2891. (Pubitemid 350201654)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.27 , pp. 2872-2891
    • Liu, Y.1    Zhang, J.2    Xu, W.3
  • 145
    • 27644439501 scopus 로고    scopus 로고
    • Susceptibilities of antiviral-resistant influenza viruses to novel neuraminidase inhibitors
    • DOI 10.1128/AAC.49.11.4515-4520.2005
    • Mishin, V.P.; Hayden, F.G.; Gubareva, L.V. Susceptibilities of antiviralresistant influenza viruses to novel neuraminidase inhibitors. Antimicrob. Agents Chemother., 2005, 49(11), 4515-4520. (Pubitemid 41552580)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.11 , pp. 4515-4520
    • Mishin, V.P.1    Hayden, F.G.2    Gubareva, L.V.3
  • 147
    • 59749085707 scopus 로고    scopus 로고
    • Activity of the oral neuraminidase inhibitor A-322278 against the oseltamivir-resistant H274Y (A/H1N1) influenza virus mutant in mice
    • Baz, M.; Abed, Y.; Nehme, B.; Boivin, G. Activity of the oral neuraminidase inhibitor A-322278 against the oseltamivir-resistant H274Y (A/H1N1) influenza virus mutant in mice. Antimicrob. Agents Chemother., 2009, 53(2), 791-793.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.2 , pp. 791-793
    • Baz, M.1    Abed, Y.2    Nehme, B.3    Boivin, G.4
  • 148
    • 73349121665 scopus 로고    scopus 로고
    • The emergency use authorization of peramivir for treatment of 2009 H1N1 influenza
    • Birnkrant, D.; Cox, E. The emergency use authorization of peramivir for treatment of 2009 H1N1 influenza. N. Engl. J. Med., 2009, 361(23), 2204.
    • (2009) N. Engl. J. Med. , vol.361 , Issue.23 , pp. 2204
    • Birnkrant, D.1    Cox, E.2
  • 149
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • DOI 10.1038/nature05114, PII NATURE05114
    • Russell, R.J.; Haire, L.F.; Stevens, D.J.; Collins, P.J.; Lin, Y.P.; Blackburn, G.M.; Hay, A.J.; Gamblin, S.J.; Skehel, J.J. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature, 2006, 443(7107), 45-49. (Pubitemid 44344043)
    • (2006) Nature , vol.443 , Issue.7107 , pp. 45-49
    • Russell, R.J.1    Haire, L.F.2    Stevens, D.J.3    Collins, P.J.4    Lin, Y.P.5    Blackburn, G.M.6    Hay, A.J.7    Gamblin, S.J.8    Skehel, J.J.9
  • 152
    • 38549150173 scopus 로고    scopus 로고
    • Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble
    • DOI 10.1111/j.1747-0285.2007.00614.x
    • Landon, M.R.; Amaro, R.E.; Baron, R.; Ngan, C.H.; Ozonoff, D.; McCammon, J.A.; Vajda, S. Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble. Chem. Biol. Drug Des., 2008, 71(2), 106-116. (Pubitemid 351160979)
    • (2008) Chemical Biology and Drug Design , vol.71 , Issue.2 , pp. 106-116
    • Landon, M.R.1    Amaro, R.E.2    Baron, R.3    Ngan, C.H.4    Ozonoff, D.5    Andrew McCammon, J.6    Vajda, S.7
  • 153
    • 67949124553 scopus 로고    scopus 로고
    • Characterizing loop dynamics and ligand recognition in human- and avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations
    • Amaro, R.E.; Cheng, X.; Ivanov, I.; Xu, D.; McCammon, J.A. Characterizing loop dynamics and ligand recognition in human- and avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations. J. Am. Chem. Soc., 2009, 131(13), 4702-4709.
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.13 , pp. 4702-4709
    • Amaro, R.E.1    Cheng, X.2    Ivanov, I.3    Xu, D.4    McCammon, J.A.5
  • 154
    • 60249087300 scopus 로고    scopus 로고
    • Inhibition of viral group-1 and group-2 neuraminidases by oseltamivir: A comparative structural analysis by the ScrewFit algorithm
    • Calligari, P.A.; Kneller, G.R.; Giansanti, A.; Ascenzi, P.; Porrello, A.; Bocedi, A. Inhibition of viral group-1 and group-2 neuraminidases by oseltamivir: A comparative structural analysis by the ScrewFit algorithm. Biophys. Chem., 2009, 141(1), 117-123.
    • (2009) Biophys. Chem. , vol.141 , Issue.1 , pp. 117-123
    • Calligari, P.A.1    Kneller, G.R.2    Giansanti, A.3    Ascenzi, P.4    Porrello, A.5    Bocedi, A.6
  • 155
    • 37349007892 scopus 로고    scopus 로고
    • Mutations of neuraminidase implicated in neuraminidase inhibitors resistance
    • DOI 10.1016/j.jcv.2007.10.020, PII S1386653207003903
    • Ferraris, O.; Lina, B. Mutations of neuraminidase implicated in neuraminidase inhibitors resistance. J. Clin. Virol., 2008, 41(1), 13-19. (Pubitemid 350298978)
    • (2008) Journal of Clinical Virology , vol.41 , Issue.1 , pp. 13-19
    • Ferraris, O.1    Lina, B.2
  • 156
    • 34548261773 scopus 로고    scopus 로고
    • Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drugresistant H5N1 virus
    • Du, Q.S.; Wang, S.Q.; Chou, K.C. Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drugresistant H5N1 virus. Biochem. Biophys. Res. Commun., 2007, 362(2), 525-531.
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , Issue.2 , pp. 525-531
    • Du, Q.S.1    Wang, S.Q.2    Chou, K.C.3
  • 157
    • 58649090243 scopus 로고    scopus 로고
    • On the structure-based design of novel inhibitors of H5N1 influenza A virus neuraminidase (NA)
    • Mitrasinovic, P.M. On the structure-based design of novel inhibitors of H5N1 influenza A virus neuraminidase (NA). Biophys. Chem., 2009, 140(1- 3), 35-38.
    • (2009) Biophys. Chem. , vol.140 , Issue.1-3 , pp. 35-38
    • Mitrasinovic, P.M.1
  • 158
    • 62349104787 scopus 로고    scopus 로고
    • Design of oseltamivir analogs inhibiting neuraminidase of avian influenza virus H5N1
    • Rungrotmongkol, T.; Frecer, V.; De-Eknamkul, W.; Hannongbua, S.; Miertus, S. Design of oseltamivir analogs inhibiting neuraminidase of avian influenza virus H5N1. Antiviral. Res., 2009, 82(1), 51-58.
    • (2009) Antiviral. Res. , vol.82 , Issue.1 , pp. 51-58
    • Rungrotmongkol, T.1    Frecer, V.2    De-Eknamkul, W.3    Hannongbua, S.4    Miertus, S.5
  • 160
    • 70349484061 scopus 로고    scopus 로고
    • Rational design of Tamiflu derivatives targeting at the open conformation of neuraminidase subtype 1
    • Li, Y.; Zhou, B.; Wang, R. Rational design of Tamiflu derivatives targeting at the open conformation of neuraminidase subtype 1. J. Mol. Graph. Model., 2009, 28(3), 203-219.
    • (2009) J. Mol. Graph. Model. , vol.28 , Issue.3 , pp. 203-219
    • Li, Y.1    Zhou, B.2    Wang, R.3
  • 161
    • 46849105028 scopus 로고    scopus 로고
    • Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase
    • DOI 10.1021/jm8001197
    • Cheng, L.S.; Amaro, R.E.; Xu, D.; Li, W.W.; Arzberger, P.W.; McCammon, J.A. Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase. J. Med. Chem., 2008, 51(13), 3878-3894. (Pubitemid 351956517)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.13 , pp. 3878-3894
    • Cheng, L.S.1    Amaro, R.E.2    Xu, D.3    Li, W.W.4    Arzberger, P.W.5    McCammon, J.A.6
  • 162
    • 56449084239 scopus 로고    scopus 로고
    • Design of multi-binding-site inhibitors, ligand efficiency, and consensus screening of avian influenza H5N1 wild-type neuraminidase and of the oseltamivir-resistant H274Y variant
    • Garcia-Sosa, A.T.; Sild, S.; Maran, U. Design of multi-binding-site inhibitors, ligand efficiency, and consensus screening of avian influenza H5N1 wild-type neuraminidase and of the oseltamivir-resistant H274Y variant. J. Chem. Inf. Model., 2008, 48(10), 2074-2080.
    • (2008) J. Chem. Inf. Model. , vol.48 , Issue.10 , pp. 2074-2080
    • Garcia-Sosa, A.T.1    Sild, S.2    Maran, U.3
  • 163
    • 0025045072 scopus 로고
    • Inhibition of influenza virus sialidase and anti-influenza virus activity by plant flavonoids
    • Nagai, T.; Miyaichi, Y.; Tomimori, T.; Suzuki, Y.; Yamada, H. Inhibition of influenza virus sialidase and anti-influenza virus activity by plant flavonoids. Chem. Pharm. Bull. (Tokyo), 1990, 38(5), 1329-1332. (Pubitemid 20290829)
    • (1990) Chemical and Pharmaceutical Bulletin , vol.38 , Issue.5 , pp. 1329-1332
    • Nagai, T.1    Miyaichi, Y.2    Tomimori, T.3    Suzuki, Y.4    Yamada, H.5
  • 166
    • 0028842287 scopus 로고
    • Mode of action of the anti-influenza virus activity of plant flavonoid, 5,7,4'- trihydroxy-8-methoxyflavone, from the roots of Scutellaria baicalensis
    • Nagai, T.; Moriguchi, R.; Suzuki, Y.; Tomimori, T.; Yamada, H. Mode of action of the anti-influenza virus activity of plant flavonoid, 5,7,4'- trihydroxy-8-methoxyflavone, from the roots of Scutellaria baicalensis. Antiviral. Res., 1995, 26(1), 11-25.
    • (1995) Antiviral. Res. , vol.26 , Issue.1 , pp. 11-25
    • Nagai, T.1    Moriguchi, R.2    Suzuki, Y.3    Tomimori, T.4    Yamada, H.5
  • 167
    • 48449102581 scopus 로고    scopus 로고
    • Structure-activity relationship of flavonoids as influenza virus neuraminidase inhibitors and their in vitro anti-viral activities
    • Liu, A.L.; Wang, H.D.; Lee, S.M.; Wang, Y.T.; Du, G.H. Structure-activity relationship of flavonoids as influenza virus neuraminidase inhibitors and their in vitro anti-viral activities. Bioorg. Med. Chem., 2008, 16(15), 7141-7147.
    • (2008) Bioorg. Med. Chem. , vol.16 , Issue.15 , pp. 7141-7147
    • Liu, A.L.1    Wang, H.D.2    Lee, S.M.3    Wang, Y.T.4    Du, G.H.5
  • 168
    • 77949488035 scopus 로고    scopus 로고
    • QSAR study of flavonoids and biflavonoids as influenza H1N1 virus neuraminidase inhibitors
    • Mercader, A.G.; Pomilio, A.B. QSAR study of flavonoids and biflavonoids as influenza H1N1 virus neuraminidase inhibitors. Eur. J. Med. Chem., 2010, 45(5), 1724-1730.
    • (2010) Eur. J. Med. Chem. , vol.45 , Issue.5 , pp. 1724-1730
    • Mercader, A.G.1    Pomilio, A.B.2
  • 169
    • 68549110347 scopus 로고    scopus 로고
    • Structural characteristics of flavanones and flavones from Cudrania tricuspidata for neuraminidase inhibition
    • Ryu, Y.B.; Curtis-Long, M.J.; Lee, J.W.; Ryu, H.W.; Kim, J.Y.; Lee, W.S.; Park, K.H. Structural characteristics of flavanones and flavones from Cudrania tricuspidata for neuraminidase inhibition. Bioorg. Med. Chem. Lett., 2009, 19(17), 4912-4915.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.17 , pp. 4912-4915
    • Ryu, Y.B.1    Curtis-Long, M.J.2    Lee, J.W.3    Ryu, H.W.4    Kim, J.Y.5    Lee, W.S.6    Park, K.H.7
  • 170
    • 70249116086 scopus 로고    scopus 로고
    • Neuraminidase inhibitory activities of flavonols isolated from Rhodiola rosea roots and their in vitro anti-influenza viral activities
    • Jeong, H.J.; Ryu, Y.B.; Park, S.J.; Kim, J.H.; Kwon, H.J.; Park, K.H.; Rho, M.C.; Lee, W.S. Neuraminidase inhibitory activities of flavonols isolated from Rhodiola rosea roots and their in vitro anti-influenza viral activities. Bioorg. Med. Chem., 2009, 17(19), 6816-6823.
    • (2009) Bioorg. Med. Chem. , vol.17 , Issue.19 , pp. 6816-6823
    • Jeong, H.J.1    Ryu, Y.B.2    Park, S.J.3    Kim, J.H.4    Kwon, H.J.5    Park, K.H.6    Rho, M.C.7    Lee, W.S.8
  • 173
    • 74349130089 scopus 로고    scopus 로고
    • Inhibition of neuraminidase activity by polyphenol compounds isolated from the roots of Glycyrrhiza uralensis
    • Ryu, Y.B.; Kim, J.H.; Park, S.J.; Chang, J.S.; Rho, M.C.; Bae, K.H.; Park, K.H.; Lee, W.S. Inhibition of neuraminidase activity by polyphenol compounds isolated from the roots of Glycyrrhiza uralensis. Bioorg. Med. Chem. Lett., 2010, 20(3), 971-974.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.3 , pp. 971-974
    • Ryu, Y.B.1    Kim, J.H.2    Park, S.J.3    Chang, J.S.4    Rho, M.C.5    Bae, K.H.6    Park, K.H.7    Lee, W.S.8
  • 176
    • 0016422815 scopus 로고
    • Triphenylmethane dyes as inhibitors of reverse transcriptase, ribonucleic acid polymerase, and protein synthesis. Structure-activity relationships
    • Liao, L.L.; Horwitz, S.B.; Huang, M.T.; Grollman, A.P.; Steward, D.; Martin, J. Triphenylmethane dyes as inhibitors of reverse transcriptase, ribonucleic acid polymerase, and protein synthesis. Structure-activity relationships. J. Med. Chem., 1975, 18(1), 117-120.
    • (1975) J. Med. Chem. , vol.18 , Issue.1 , pp. 117-120
    • Liao, L.L.1    Horwitz, S.B.2    Huang, M.T.3    Grollman, A.P.4    Steward, D.5    Martin, J.6
  • 179
    • 33750532297 scopus 로고    scopus 로고
    • Synthesis and evaluation of a new series of substituted acyl(thio)urea and thiadiazolo [2,3-a] pyrimidine derivatives as potent inhibitors of influenza virus neuraminidase
    • DOI 10.1016/j.bmc.2006.08.034, PII S096808960600695X
    • Sun, C.; Zhang, X.; Huang, H.; Zhou, P. Synthesis and evaluation of a new series of substituted acyl(thio)urea and thiadiazolo [2,3-a] pyrimidine derivatives as potent inhibitors of influenza virus neuraminidase. Bioorg. Med. Chem., 2006, 14(24), 8574-8581. (Pubitemid 44667533)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.24 , pp. 8574-8581
    • Sun, C.1    Zhang, X.2    Huang, H.3    Zhou, P.4
  • 180
    • 38949167100 scopus 로고    scopus 로고
    • Quantitative structure activity relationship studies on thiourea analogues as influenza virus neuraminidase inhibitors
    • DOI 10.1016/j.ejmech.2007.03.020, PII S0223523407001559
    • Nair, P.C.; Sobhia, M.E. Quantitative structure activity relationship studies on thiourea analogues as influenza virus neuraminidase inhibitors. Eur. J. Med. Chem., 2008, 43(2), 293-299. (Pubitemid 351215598)
    • (2008) European Journal of Medicinal Chemistry , vol.43 , Issue.2 , pp. 293-299
    • Nair, P.C.1    Sobhia, M.E.2
  • 181
    • 33749999559 scopus 로고    scopus 로고
    • Structure-guided design of a novel class of benzyl-sulfonate inhibitors for influenza virus neuraminidase
    • DOI 10.1042/BJ20060447
    • Platis, D.; Smith, B.J.; Huyton, T.; Labrou, N.E. Structure-guided design of a novel class of benzyl-sulfonate inhibitors for influenza virus neuraminidase. Biochem. J., 2006, 399(2), 215-223. (Pubitemid 44570283)
    • (2006) Biochemical Journal , vol.399 , Issue.2 , pp. 215-223
    • Platis, D.1    Smith, B.J.2    Huyton, T.3    Labrou, N.E.4
  • 182
    • 65649103683 scopus 로고    scopus 로고
    • A novel small-molecule inhibitor of the avian influenza H5N1 virus determined through computational screening against the neuraminidase
    • An, J.; Lee, D.C.; Law, A.H.; Yang, C.L.; Poon, L.L.; Lau, A.S.; Jones, S.J. A novel small-molecule inhibitor of the avian influenza H5N1 virus determined through computational screening against the neuraminidase. J. Med. Chem., 2009, 52(9), 2667-2672.
    • (2009) J. Med. Chem. , vol.52 , Issue.9 , pp. 2667-2672
    • An, J.1    Lee, D.C.2    Law, A.H.3    Yang, C.L.4    Poon, L.L.5    Lau, A.S.6    Jones, S.J.7
  • 185
    • 59749091876 scopus 로고    scopus 로고
    • CS-8958, a prodrug of the new neuraminidase inhibitor R-125489, shows long-acting anti-influenza virus activity
    • Yamashita, M.; Tomozawa, T.; Kakuta, M.; Tokumitsu, A.; Nasu, H.; Kubo, S. CS-8958, a prodrug of the new neuraminidase inhibitor R-125489, shows long-acting anti-influenza virus activity. Antimicrob. Agents Chemother., 2009, 53(1), 186-192.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.1 , pp. 186-192
    • Yamashita, M.1    Tomozawa, T.2    Kakuta, M.3    Tokumitsu, A.4    Nasu, H.5    Kubo, S.6


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