메뉴 건너뛰기




Volumn 95, Issue PART 2, 2014, Pages 263-277

Entry of influenza A virus: Host factors and antiviral targets

Author keywords

[No Author keywords available]

Indexed keywords

ADAMANTANE; AMANTADINE; ANTIBODY; BAFILOMYCIN A1; HOST FACTOR; RIBONUCLEOPROTEIN; RIMANTADINE; SIALIC ACID; VIRUS RECEPTOR;

EID: 84892608409     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.059477-0     Document Type: Review
Times cited : (177)

References (178)
  • 1
    • 0025620241 scopus 로고
    • Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity
    • Baum, L. G. & Paulson, J. C. (1990). Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40, 35-38.
    • (1990) Acta Histochem Suppl , vol.40 , pp. 35-38
    • Baum, L.G.1    Paulson, J.C.2
  • 2
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian, D. L., Yamasaki, R. B., Buswell, R. L., Stearns, J. F., White, J. M. & Kuntz, I. D. (1993). Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32, 2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1    Yamasaki, R.B.2    Buswell, R.L.3    Stearns, J.F.4    White, J.M.5    Kuntz, I.D.6
  • 3
    • 0037370304 scopus 로고    scopus 로고
    • Reverse genetics studies on the filamentous morphology of influenza A virus
    • Bourmakina, S. V. & García-Sastre, A. (2003). Reverse genetics studies on the filamentous morphology of influenza A virus. J Gen Virol 84, 517-527.
    • (2003) J Gen Virol , vol.84 , pp. 517-527
    • Bourmakina, S.V.1    García-Sastre, A.2
  • 4
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., Siebers, A. & Altendorf, K. (1988). Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc Natl Acad Sci U S A 85, 7972-7976.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 5
    • 25844438380 scopus 로고    scopus 로고
    • Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: A cause for concern
    • Bright, R. A., Medina, M. J., Xu, X., Perez-Oronoz, G., Wallis, T. R., Davis, X. M., Povinelli, L., Cox, N. J. & Klimov, A. I. (2005). Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern. Lancet 366, 1175-1181.
    • (2005) Lancet , vol.366 , pp. 1175-1181
    • Bright, R.A.1    Medina, M.J.2    Xu, X.3    Perez-Oronoz, G.4    Wallis, T.R.5    Davis, X.M.6    Povinelli, L.7    Cox, N.J.8    Klimov, A.I.9
  • 6
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C., Parton, R. G., Mather, I. H., Stunnenberg, H., Simons, K., Hoflack, B. & Zerial, M. (1992). The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 7
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui, M., Whittaker, G. & Helenius, A. (1996). Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J Virol 70, 8391-8401.
    • (1996) J Virol , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 9
    • 0343049028 scopus 로고    scopus 로고
    • Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein
    • Bullido, R., Gómez-Puertas, P., Albo, C. & Portela, A. (2000). Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein. J Gen Virol 81, 135-142.
    • (2000) J Gen Virol , vol.81 , pp. 135-142
    • Bullido, R.1    Gómez-Puertas, P.2    Albo, C.3    Portela, A.4
  • 10
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 12
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M. & Kim, P. S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 13
    • 0021932393 scopus 로고
    • Differential infection of receptormodified host cells by receptor-specific influenza viruses
    • Carroll, S. M. & Paulson, J. C. (1985). Differential infection of receptormodified host cells by receptor-specific influenza viruses. Virus Res 3, 165-179.
    • (1985) Virus Res , vol.3 , pp. 165-179
    • Carroll, S.M.1    Paulson, J.C.2
  • 15
    • 50149096579 scopus 로고    scopus 로고
    • Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
    • Chen, C. & Zhuang, X. (2008). Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus. Proc Natl Acad Sci U S A 105, 11790-11795.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11790-11795
    • Chen, C.1    Zhuang, X.2
  • 16
    • 0033529752 scopus 로고    scopus 로고
    • 2 subunit to form an N cap that terminates the triple-stranded coiled coil
    • 2 subunit to form an N cap that terminates the triple-stranded coiled coil. Proc Natl Acad Sci U S A 96, 8967-8972.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 17
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik, L. V., Frolov, V. A., Leikina, E., Bronk, P. & Zimmerberg, J. (1998). The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J Cell Biol 140, 1369-1382.
    • (1998) J Cell Biol , vol.140 , pp. 1369-1382
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 18
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov, I. V., Geraghty, F. M., Ogden, D. C., Hayhurst, A., Antoniou, M. & Hay, A. J. (1996). Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J Physiol 494, 329-336.
    • (1996) J Physiol , vol.494 , pp. 329-336
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 19
    • 84878522822 scopus 로고    scopus 로고
    • Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis
    • Chou, Y. Y., Heaton, N. S., Gao, Q., Palese, P., Singer, R. & Lionnet, T. (2013). Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis. PLoS Pathog 9, e1003358.
    • (2013) PLoS Pathog , vol.9
    • Chou, Y.Y.1    Heaton, N.S.2    Gao, Q.3    Palese, P.4    Singer, R.5    Lionnet, T.6
  • 20
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis, S., McBride, H. M., Burgoyne, R. D. & Zerial, M. (1999a). The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621-625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 22
    • 11144239774 scopus 로고    scopus 로고
    • Influenza virus entry and infection require host cell N-linked glycoprotein
    • Chu, V. C. & Whittaker, G. R. (2004). Influenza virus entry and infection require host cell N-linked glycoprotein. Proc Natl Acad Sci U S A 101, 18153-18158.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 18153-18158
    • Chu, V.C.1    Whittaker, G.R.2
  • 23
    • 84870588311 scopus 로고    scopus 로고
    • Influenza B-cells protective epitope characterization: A passkey for the rational design of new broad-range antiinfluenza vaccines
    • Clementi, N., Criscuolo, E., Castelli, M., Mancini, N., Clementi, M. & Burioni, R. (2012). Influenza B-cells protective epitope characterization: a passkey for the rational design of new broad-range antiinfluenza vaccines. Viruses 4, 3090-3108.
    • (2012) Viruses , vol.4 , pp. 3090-3108
    • Clementi, N.1    Criscuolo, E.2    Castelli, M.3    Mancini, N.4    Clementi, M.5    Burioni, R.6
  • 24
    • 84864634144 scopus 로고    scopus 로고
    • The first five seconds in the life of a clathrin-coated pit
    • Cocucci, E., Aguet, F., Boulant, S. & Kirchhausen, T. (2012). The first five seconds in the life of a clathrin-coated pit. Cell 150, 495-507.
    • (2012) Cell , vol.150 , pp. 495-507
    • Cocucci, E.1    Aguet, F.2    Boulant, S.3    Kirchhausen, T.4
  • 25
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor, R. J., Kawaoka, Y., Webster, R. G. & Paulson, J. C. (1994). Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205, 17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 26
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti, D. & Lanzavecchia, A. (2013). Broadly neutralizing antiviral antibodies. Annu Rev Immunol 31, 705-742.
    • (2013) Annu Rev Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 27
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • other authors
    • Corti, D., Voss, J., Gamblin, S. J., Codoni, G., Macagno, A., Jarrossay, D., Vachieri, S. G., Pinna, D., Minola, A. & other authors (2011). A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856.
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1    Voss, J.2    Gamblin, S.J.3    Codoni, G.4    McAgno, A.5    Jarrossay, D.6    Vachieri, S.G.7    Pinna, D.8    Minola, A.9
  • 28
    • 0142091712 scopus 로고    scopus 로고
    • Trafficking of viral genomic RNA into and out of the nucleus: Influenza, Thogoto and Borna disease viruses
    • Cros, J. F. & Palese, P. (2003). Trafficking of viral genomic RNA into and out of the nucleus: influenza, Thogoto and Borna disease viruses. Virus Res 95, 3-12.
    • (2003) Virus Res , vol.95 , pp. 3-12
    • Cros, J.F.1    Palese, P.2
  • 31
    • 78650533541 scopus 로고    scopus 로고
    • Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells
    • De Conto, F., Covan, S., Arcangeletti, M. C., Orlandini, G., Gatti, R., Dettori, G. & Chezzi, C. (2011). Differential infectious entry of human influenza A/NWS/33 virus (H1N1) in mammalian kidney cells. Virus Res 155, 221-230.
    • (2011) Virus Res , vol.155 , pp. 221-230
    • De Conto, F.1    Covan, S.2    Arcangeletti, M.C.3    Orlandini, G.4    Gatti, R.5    Dettori, G.6    Chezzi, C.7
  • 32
    • 84864111699 scopus 로고    scopus 로고
    • Highly dynamic microtubules improve the effectiveness of early stages of human influenza A/NWS/33 virus infection in LLC-MK2 cells
    • De Conto, F., Di Lonardo, E., Arcangeletti, M. C., Chezzi, C., Medici, M. C. & Calderaro, A. (2012). Highly dynamic microtubules improve the effectiveness of early stages of human influenza A/NWS/33 virus infection in LLC-MK2 cells. PLoS ONE 7, e41207.
    • (2012) PLoS ONE , vol.7
    • De Conto, F.1    Di Lonardo, E.2    Arcangeletti, M.C.3    Chezzi, C.4    Medici, M.C.5    Calderaro, A.6
  • 35
    • 0030010945 scopus 로고    scopus 로고
    • H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
    • Durrer, P., Galli, C., Hoenke, S., Corti, C., Glück, R., Vorherr, T. & Brunner, J. (1996). H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region. J Biol Chem 271, 13417-13421.
    • (1996) J Biol Chem , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Glück, R.5    Vorherr, T.6    Brunner, J.7
  • 36
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff, T., Hrincius, E. R., Rescher, U., Ludwig, S. & Ehrhardt, C. (2010). The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog 6, e1001099.
    • (2010) PLoS Pathog , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 37
    • 84859510667 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza virus and prospects for universal therapies
    • Ekiert, D. C. & Wilson, I. A. (2012). Broadly neutralizing antibodies against influenza virus and prospects for universal therapies. Curr Opin Virol 2, 134-141.
    • (2012) Curr Opin Virol , vol.2 , pp. 134-141
    • Ekiert, D.C.1    Wilson, I.A.2
  • 40
    • 1642274781 scopus 로고    scopus 로고
    • The M1 matrix protein controls the filamentous phenotype of influenza A virus
    • Elleman, C. J. & Barclay, W. S. (2004). The M1 matrix protein controls the filamentous phenotype of influenza A virus. Virology 321, 144-153.
    • (2004) Virology , vol.321 , pp. 144-153
    • Elleman, C.J.1    Barclay, W.S.2
  • 41
    • 0028082049 scopus 로고
    • A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction
    • Elster, C., Fourest, E., Baudin, F., Larsen, K., Cusack, S. & Ruigrok, R. W. (1994). A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction. J Gen Virol 75, 37-42.
    • (1994) J Gen Virol , vol.75 , pp. 37-42
    • Elster, C.1    Fourest, E.2    Baudin, F.3    Larsen, K.4    Cusack, S.5    Ruigrok, R.W.6
  • 42
    • 84877324091 scopus 로고    scopus 로고
    • At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane
    • Fontana, J. & Steven, A. C. (2013). At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane. J Virol 87, 5621-5628.
    • (2013) J Virol , vol.87 , pp. 5621-5628
    • Fontana, J.1    Steven, A.C.2
  • 43
    • 84857981961 scopus 로고    scopus 로고
    • Structural changes in Influenza virus at low pH characterized by cryo-electron tomography
    • Fontana, J., Cardone, G., Heymann, J. B., Winkler, D. C. & Steven, A. C. (2012). Structural changes in Influenza virus at low pH characterized by cryo-electron tomography. J Virol 86, 2919-2929.
    • (2012) J Virol , vol.86 , pp. 2919-2929
    • Fontana, J.1    Cardone, G.2    Heymann, J.B.3    Winkler, D.C.4    Steven, A.C.5
  • 44
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat Rev Mol Cell Biol 8, 917-929.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 917-929
    • Forgac, M.1
  • 45
    • 79251616335 scopus 로고    scopus 로고
    • The Ras-PI3K signaling pathway is involved in clathrin-independent endocytosis and the internalization of influenza viruses
    • Fujioka, Y., Tsuda, M., Hattori, T., Sasaki, J., Sasaki, T., Miyazaki, T. & Ohba, Y. (2011). The Ras-PI3K signaling pathway is involved in clathrin-independent endocytosis and the internalization of influenza viruses. PLoS ONE 6, e16324.
    • (2011) PLoS ONE , vol.6
    • Fujioka, Y.1    Tsuda, M.2    Hattori, T.3    Sasaki, J.4    Sasaki, T.5    Miyazaki, T.6    Ohba, Y.7
  • 47
    • 84874761652 scopus 로고    scopus 로고
    • Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: Implications for host range and adaptation
    • Galloway, S. E., Reed, M. L., Russell, C. J. & Steinhauer, D. A. (2013). Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation. PLoS Pathog 9, e1003151.
    • (2013) PLoS Pathog , vol.9
    • Galloway, S.E.1    Reed, M.L.2    Russell, C.J.3    Steinhauer, D.A.4
  • 48
    • 49649090449 scopus 로고    scopus 로고
    • 6-Sulfo sialyl Lewis X is the common receptor determinant recognized by H5, H6, H7 and H9 influenza viruses of terrestrial poultry
    • Gambaryan, A. S., Tuzikov, A. B., Pazynina, G. V., Desheva, J. A., Bovin, N. V., Matrosovich, M. N. & Klimov, A. I. (2008). 6-Sulfo sialyl Lewis X is the common receptor determinant recognized by H5, H6, H7 and H9 influenza viruses of terrestrial poultry. Virol J 5, 85.
    • (2008) Virol J , vol.5 , pp. 85
    • Gambaryan, A.S.1    Tuzikov, A.B.2    Pazynina, G.V.3    Desheva, J.A.4    Bovin, N.V.5    Matrosovich, M.N.6    Klimov, A.I.7
  • 50
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb, T. A., Ivanov, I. E., Adesnik, M. & Sabatini, D. D. (1993). Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J Cell Biol 120, 695-710.
    • (1993) J Cell Biol , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 51
    • 0027103930 scopus 로고
    • Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses
    • Grambas, S., Bennett, M. S. & Hay, A. J. (1992). Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses. Virology 191, 541-549.
    • (1992) Virology , vol.191 , pp. 541-549
    • Grambas, S.1    Bennett, M.S.2    Hay, A.J.3
  • 52
    • 0028930293 scopus 로고
    • Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells
    • Guinea, R. & Carrasco, L. (1995). Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells. J Virol 69, 2306-2312.
    • (1995) J Virol , vol.69 , pp. 2306-2312
    • Guinea, R.1    Carrasco, L.2
  • 53
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay, A. J., Wolstenholme, A. J., Skehel, J. J. & Smith, M. H. (1985). The molecular basis of the specific anti-influenza action of amantadine. EMBO J 4, 3021-3024.
    • (1985) EMBO J , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 56
  • 58
    • 0025923280 scopus 로고
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183, 32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 59
    • 0030593679 scopus 로고    scopus 로고
    • Involvement of annexin V in the entry of influenza viruses and role of phospholipids in infection
    • Huang, R. T., Lichtenberg, B. & Rick, O. (1996). Involvement of annexin V in the entry of influenza viruses and role of phospholipids in infection. FEBS Lett 392, 59-62.
    • (1996) FEBS Lett , vol.392 , pp. 59-62
    • Huang, R.T.1    Lichtenberg, B.2    Rick, O.3
  • 60
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari, J. & Helenius, A. (2011). Endosome maturation. EMBO J 30, 3481-3500.
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 62
    • 59149095897 scopus 로고    scopus 로고
    • Inhibitors of V-ATPases: Old and new players
    • Huss, M. & Wieczorek, H. (2009). Inhibitors of V-ATPases: old and new players. J Exp Biol 212, 341-346.
    • (2009) J Exp Biol , vol.212 , pp. 341-346
    • Huss, M.1    Wieczorek, H.2
  • 63
    • 84870250746 scopus 로고    scopus 로고
    • Nuclear import of the influenza A virus transcriptional machinery
    • Hutchinson, E. C. & Fodor, E. (2012). Nuclear import of the influenza A virus transcriptional machinery. Vaccine 30, 7353-7358.
    • (2012) Vaccine , vol.30 , pp. 7353-7358
    • Hutchinson, E.C.1    Fodor, E.2
  • 64
    • 84859497701 scopus 로고    scopus 로고
    • The role of receptor binding specificity in interspecies transmission of influenza viruses
    • Imai, M. & Kawaoka, Y. (2012). The role of receptor binding specificity in interspecies transmission of influenza viruses. Curr Opin Virol 2, 160-167.
    • (2012) Curr Opin Virol , vol.2 , pp. 160-167
    • Imai, M.1    Kawaoka, Y.2
  • 65
    • 0033798864 scopus 로고    scopus 로고
    • Recognition of Nglycolylneuraminic acid linked to galactose by the a 2, 3 linkage is associated with intestinal replication of influenza A virus in ducks
    • other authors
    • Ito, T., Suzuki, Y., Suzuki, T., Takada, A., Horimoto, T., Wells, K., Kida, H., Otsuki, K., Kiso, M. & other authors (2000). Recognition of Nglycolylneuraminic acid linked to galactose by the a 2, 3 linkage is associated with intestinal replication of influenza A virus in ducks. J Virol 74, 9300-9305.
    • (2000) J Virol , vol.74 , pp. 9300-9305
    • Ito, T.1    Suzuki, Y.2    Suzuki, T.3    Takada, A.4    Horimoto, T.5    Wells, K.6    Kida, H.7    Otsuki, K.8    Kiso, M.9
  • 66
    • 0028024644 scopus 로고
    • Nuclear import of microinjected influenza virus ribonucleoproteins
    • Kemler, I., Whittaker, G. & Helenius, A. (1994). Nuclear import of microinjected influenza virus ribonucleoproteins. Virology 202, 1028-1033.
    • (1994) Virology , vol.202 , pp. 1028-1033
    • Kemler, I.1    Whittaker, G.2    Helenius, A.3
  • 67
    • 67649365976 scopus 로고    scopus 로고
    • Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: A possible role in innate defense
    • Kesimer, M., Scull, M., Brighton, B., DeMaria, G., Burns, K., O'Neal, W., Pickles, R. J. & Sheehan, J. K. (2009). Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J 23, 1858-1868.
    • (2009) FASEB J , vol.23 , pp. 1858-1868
    • Kesimer, M.1    Scull, M.2    Brighton, B.3    DeMaria, G.4    Burns, K.5    O'Neal, W.6    Pickles, R.J.7    Sheehan, J.K.8
  • 68
    • 0033892730 scopus 로고    scopus 로고
    • Antiviral activity of NMSO3 against respiratory syncytial virus infection in vitro and in vivo
    • Kimura, K., Mori, S., Tomita, K., Ohno, K., Takahashi, K., Shigeta, S. & Terada, M. (2000). Antiviral activity of NMSO3 against respiratory syncytial virus infection in vitro and in vivo. Antiviral Res 47, 41-51.
    • (2000) Antiviral Res , vol.47 , pp. 41-51
    • Kimura, K.1    Mori, S.2    Tomita, K.3    Ohno, K.4    Takahashi, K.5    Shigeta, S.6    Terada, M.7
  • 71
    • 0033060915 scopus 로고    scopus 로고
    • Conformational intermediates and fusion activity of influenza virus hemagglutinin
    • Korte, T., Ludwig, K., Booy, F. P., Blumenthal, R. & Herrmann, A. (1999). Conformational intermediates and fusion activity of influenza virus hemagglutinin. J Virol 73, 4567-4574.
    • (1999) J Virol , vol.73 , pp. 4567-4574
    • Korte, T.1    Ludwig, K.2    Booy, F.P.3    Blumenthal, R.4    Herrmann, A.5
  • 73
    • 0019403963 scopus 로고
    • Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus
    • Lamb, R. A. & Choppin, P. W. (1981). Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus. Virology 112, 729-737.
    • (1981) Virology , vol.112 , pp. 729-737
    • Lamb, R.A.1    Choppin, P.W.2
  • 74
    • 0036846370 scopus 로고    scopus 로고
    • Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin
    • Leikina, E., Ramos, C., Markovic, I., Zimmerberg, J. & Chernomordik, L. V. (2002). Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin. EMBO J 21, 5701-5710.
    • (2002) EMBO J , vol.21 , pp. 5701-5710
    • Leikina, E.1    Ramos, C.2    Markovic, I.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 75
    • 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. (2009). Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol. Antiviral Res 81, 132-140.
    • (2009) Antiviral Res , vol.81 , pp. 132-140
    • Leneva, I.A.1    Russell, R.J.2    Boriskin, Y.S.3    Hay, A.J.4
  • 77
    • 79952410920 scopus 로고    scopus 로고
    • N-Linked glycosylation facilitates sialic acidindependent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN
    • Londrigan, S. L., Turville, S. G., Tate, M. D., Deng, Y. M., Brooks, A. G. & Reading, P. C. (2011). N-Linked glycosylation facilitates sialic acidindependent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN. J Virol 85, 2990-3000.
    • (2011) J Virol , vol.85 , pp. 2990-3000
    • Londrigan, S.L.1    Turville, S.G.2    Tate, M.D.3    Deng, Y.M.4    Brooks, A.G.5    Reading, P.C.6
  • 78
    • 0030894782 scopus 로고    scopus 로고
    • Molecular mechanism underlying the action of a novel fusion inhibitor of influenza A virus
    • other authors
    • Luo, G., Torri, A., Harte, W. E., Danetz, S., Cianci, C., Tiley, L., Day, S., Mullaney, D., Yu, K. L. & other authors (1997). Molecular mechanism underlying the action of a novel fusion inhibitor of influenza A virus. J Virol 71, 4062-4070.
    • (1997) J Virol , vol.71 , pp. 4062-4070
    • Luo, G.1    Torri, A.2    Harte, W.E.3    Danetz, S.4    Cianci, C.5    Tiley, L.6    Day, S.7    Mullaney, D.8    Yu, K.L.9
  • 80
    • 0019203091 scopus 로고
    • Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes
    • Maeda, T. & Ohnishi, S. (1980). Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes. FEBS Lett 122, 283-287.
    • (1980) FEBS Lett , vol.122 , pp. 283-287
    • Maeda, T.1    Ohnishi, S.2
  • 81
    • 0035956421 scopus 로고    scopus 로고
    • Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines
    • Markovic, I., Leikina, E., Zhukovsky, M., Zimmerberg, J. & Chernomordik, L. V. (2001). Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines. J Cell Biol 155, 833-844.
    • (2001) J Cell Biol , vol.155 , pp. 833-844
    • Markovic, I.1    Leikina, E.2    Zhukovsky, M.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 82
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin, K. & Helenius, A. (1991). Transport of incoming influenza virus nucleocapsids into the nucleus. J Virol 65, 232-244.
    • (1991) J Virol , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 83
    • 60849088256 scopus 로고    scopus 로고
    • Neutralizing antiinfluenza virus monoclonal antibodies: Therapeutics and tools for discovery
    • Martinez, O., Tsibane, T. & Basler, C. F. (2009). Neutralizing antiinfluenza virus monoclonal antibodies: therapeutics and tools for discovery. Int Rev Immunol 28, 69-92.
    • (2009) Int Rev Immunol , vol.28 , pp. 69-92
    • Martinez, O.1    Tsibane, T.2    Basler, C.F.3
  • 84
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin, K. S., Reggio, H., Helenius, A. & Simons, K. (1981). Infectious entry pathway of influenza virus in a canine kidney cell line. J Cell Biol 91, 601-613.
    • (1981) J Cell Biol , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 85
    • 68149168811 scopus 로고    scopus 로고
    • Influenza receptors, polymerase and host range
    • Matrosovich, M., Stech, J. & Klenk, H. D. (2009). Influenza receptors, polymerase and host range. Rev Sci Tech 28, 203-217.
    • (2009) Rev Sci Tech , vol.28 , pp. 203-217
    • Matrosovich, M.1    Stech, J.2    Klenk, H.D.3
  • 86
    • 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. (2009). Inhibition of influenza virus infections by sialylgalactose-binding peptides selected from a phage library. J Med Chem 52, 4247-4256.
    • (2009) J Med Chem , vol.52 , pp. 4247-4256
    • Matsubara, T.1    Sumi, M.2    Kubota, H.3    Taki, T.4    Okahata, Y.5    Sato, T.6
  • 88
    • 0023506243 scopus 로고
    • Endosome acidification and the pathways of receptor-mediated endocytosis
    • Maxfield, F. R. & Yamashiro, D. J. (1987). Endosome acidification and the pathways of receptor-mediated endocytosis. Adv Exp Med Biol 225, 189-198.
    • (1987) Adv Exp Med Biol , vol.225 , pp. 189-198
    • Maxfield, F.R.1    Yamashiro, D.J.2
  • 89
    • 0041344551 scopus 로고    scopus 로고
    • Importin a nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein
    • Melen, K., Fagerlund, R., Franke, J., Kohler, M., Kinnunen, L. & Julkunen, I. (2003). Importin a nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein. J Biol Chem 278, 28193-28200.
    • (2003) J Biol Chem , vol.278 , pp. 28193-28200
    • Melen, K.1    Fagerlund, R.2    Franke, J.3    Kohler, M.4    Kinnunen, L.5    Julkunen, I.6
  • 90
    • 0027740001 scopus 로고
    • Influenza virus hemagglutinin-induced cell-planar bilayer fusion: Quantitative dissection of fusion pore kinetics into stages
    • Melikyan, G. B., Niles, W. D. & Cohen, F. S. (1993a). Influenza virus hemagglutinin-induced cell-planar bilayer fusion: quantitative dissection of fusion pore kinetics into stages. J Gen Physiol 102, 1151-1170.
    • (1993) J Gen Physiol , vol.102 , pp. 1151-1170
    • Melikyan, G.B.1    Niles, W.D.2    Cohen, F.S.3
  • 91
    • 0027715108 scopus 로고
    • Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: Flickering to final expansion
    • Melikyan, G. B., Niles, W. D., Peeples, M. E. & Cohen, F. S. (1993b). Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: flickering to final expansion. J Gen Physiol 102, 1131-1149.
    • (1993) J Gen Physiol , vol.102 , pp. 1131-1149
    • Melikyan, G.B.1    Niles, W.D.2    Peeples, M.E.3    Cohen, F.S.4
  • 92
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. (1996). Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 12, 575-625.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 93
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved a-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif
    • Mu, F. T., Callaghan, J. M., Steele-Mortimer, O., Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J. P., Tock, E. P. & Toh, B. H. (1995). EEA1, an early endosome-associated protein. EEA1 is a conserved a-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. J Biol Chem 270, 13503-13511.
    • (1995) J Biol Chem , vol.270 , pp. 13503-13511
    • Mu, F.T.1    Callaghan, J.M.2    Steele-Mortimer, O.3    Stenmark, H.4    Parton, R.G.5    Campbell, P.L.6    McCluskey, J.7    Yeo, J.P.8    Tock, E.P.9    Toh, B.H.10
  • 94
    • 80051966225 scopus 로고    scopus 로고
    • The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections
    • Müller, K. H., Kainov, D. E., El Bakkouri, K., Saelens, X., De Brabander, J. K., Kittel, C., Samm, E. & Muller, C. P. (2011). The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections. Br J Pharmacol 164, 344-357.
    • (2011) Br J Pharmacol , vol.164 , pp. 344-357
    • Müller, K.H.1    Kainov, D.E.2    El Bakkouri, K.3    Saelens, X.4    De Brabander, J.K.5    Kittel, C.6    Samm, E.7    Muller, C.P.8
  • 95
    • 84877097783 scopus 로고    scopus 로고
    • The use of sialidase therapy for respiratory viral infections
    • Nicholls, J. M., Moss, R. B. & Haslam, S. M. (2013). The use of sialidase therapy for respiratory viral infections. Antiviral Res 98, 401-409.
    • (2013) Antiviral Res , vol.98 , pp. 401-409
    • Nicholls, J.M.1    Moss, R.B.2    Haslam, S.M.3
  • 96
    • 84859837805 scopus 로고    scopus 로고
    • A novel family of peptides with potent activity against influenza A viruses
    • Nicol, M. Q., Ligertwood, Y., Bacon, M. N., Dutia, B. M. & Nash, A. A. (2012). A novel family of peptides with potent activity against influenza A viruses. J Gen Virol 93, 980-986.
    • (2012) J Gen Virol , vol.93 , pp. 980-986
    • Nicol, M.Q.1    Ligertwood, Y.2    Bacon, M.N.3    Dutia, B.M.4    Nash, A.A.5
  • 98
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton, S. L., Medcalf, E., Fisher, D., Mullin, A. E., Elton, D. & Digard, P. (2007). Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J Gen Virol 88, 2280-2290.
    • (2007) J Gen Virol , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5    Digard, P.6
  • 99
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill, R. E., Jaskunas, R., Blobel, G., Palese, P. & Moroianu, J. (1995). Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J Biol Chem 270, 22701-22704.
    • (1995) J Biol Chem , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 100
    • 0029115399 scopus 로고
    • Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolar-type proton pump, on the growth of influenza A and B viruses in MDCK cells
    • Ochiai, H., Sakai, S., Hirabayashi, T., Shimizu, Y. & Terasawa, K. (1995). Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolar-type proton pump, on the growth of influenza A and B viruses in MDCK cells. Antiviral Res 27, 425-430.
    • (1995) Antiviral Res , vol.27 , pp. 425-430
    • Ochiai, H.1    Sakai, S.2    Hirabayashi, T.3    Shimizu, Y.4    Terasawa, K.5
  • 101
    • 0037465545 scopus 로고    scopus 로고
    • Zinc-and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1
    • Okada, A., Miura, T. & Takeuchi, H. (2003). Zinc-and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1. Biochemistry 42, 1978-1984.
    • (2003) Biochemistry , vol.42 , pp. 1978-1984
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 102
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno, Y., Isegawa, Y., Sasao, F. & Ueda, S. (1993). A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J Virol 67, 2552-2558.
    • (1993) J Virol , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 103
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • In, 5th edn, Edited by D. M. Knipe & P. M. Howley. Philadelphia, PA: Lippincott Williams and Wilkins
    • Palese, P. & Shaw, M. L. (2007). Orthomyxoviridae: the viruses and their replication. In Fields Virology, 5th edn, pp. 1647-1689. Edited by D. M. Knipe & P. M. Howley. Philadelphia, PA: Lippincott Williams and Wilkins.
    • (2007) Fields Virology , pp. 1647-1689
    • Palese, P.1    Shaw, M.L.2
  • 104
    • 0018406085 scopus 로고
    • Studies on the mechanism of influenza virus entry into cells
    • Patterson, S., Oxford, J. S. & Dourmashkin, R. R. (1979). Studies on the mechanism of influenza virus entry into cells. J Gen Virol 43, 223-229.
    • (1979) J Gen Virol , vol.43 , pp. 223-229
    • Patterson, S.1    Oxford, J.S.2    Dourmashkin, R.R.3
  • 105
  • 106
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto, L. H., Holsinger, L. J. & Lamb, R. A. (1992). Influenza virus M2 protein has ion channel activity. Cell 69, 517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 107
    • 17344371121 scopus 로고    scopus 로고
    • Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutinin
    • other authors
    • Plotch, S. J., O'Hara, B., Morin, J., Palant, O., LaRocque, J., Bloom, J. D., Lang, S. A., Jr, DiGrandi, M. J., Bradley, M. & other authors (1999). Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutinin. J Virol 73, 140-151.
    • (1999) J Virol , vol.73 , pp. 140-151
    • Plotch, S.J.1    O'Hara, B.2    Morin, J.3    Palant, O.4    LaRocque, J.5    Bloom, J.D.6    Lang Jr., S.A.7    DiGrandi, M.J.8    Bradley, M.9
  • 108
    • 0014515393 scopus 로고
    • Treatment of influenza. The therapeutic efficacy of rimantadine HC1 in a naturally occurring influenza A2 outbreak
    • Rabinovich, S., Baldini, J. T. & Bannister, R. (1969). Treatment of influenza. The therapeutic efficacy of rimantadine HC1 in a naturally occurring influenza A2 outbreak. Am J Med Sci 257, 328-335.
    • (1969) Am J Med Sci , vol.257 , pp. 328-335
    • Rabinovich, S.1    Baldini, J.T.2    Bannister, R.3
  • 109
    • 0034063448 scopus 로고    scopus 로고
    • Involvement of the mannose receptor in infection of macrophages by influenza virus
    • Reading, P. C., Miller, J. L. & Anders, E. M. (2000). Involvement of the mannose receptor in infection of macrophages by influenza virus. J Virol 74, 5190-5197.
    • (2000) J Virol , vol.74 , pp. 5190-5197
    • Reading, P.C.1    Miller, J.L.2    Anders, E.M.3
  • 110
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J., Ghigo, E., Kalaidzidis, Y. & Zerial, M. (2005). Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 111
    • 0027238117 scopus 로고
    • Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin
    • Roberts, P. C., Garten, W. & Klenk, H. D. (1993). Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin. J Virol 67, 3048-3060.
    • (1993) J Virol , vol.67 , pp. 3048-3060
    • Roberts, P.C.1    Garten, W.2    Klenk, H.D.3
  • 112
    • 0032484479 scopus 로고    scopus 로고
    • The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation
    • Roberts, P. C., Lamb, R. A. & Compans, R. W. (1998). The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation. Virology 240, 127-137.
    • (1998) Virology , vol.240 , pp. 127-137
    • Roberts, P.C.1    Lamb, R.A.2    Compans, R.W.3
  • 113
    • 79960364334 scopus 로고    scopus 로고
    • Lack of transmission of a human influenza virus with avian receptor specificity between ferrets is not due to decreased virus shedding but rather a lower infectivity in vivo
    • Roberts, K. L., Shelton, H., Scull, M., Pickles, R. & Barclay, W. S. (2011). Lack of transmission of a human influenza virus with avian receptor specificity between ferrets is not due to decreased virus shedding but rather a lower infectivity in vivo. J Gen Virol 92, 1822-1831.
    • (2011) J Gen Virol , vol.92 , pp. 1822-1831
    • Roberts, K.L.1    Shelton, H.2    Scull, M.3    Pickles, R.4    Barclay, W.S.5
  • 114
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman, J. S. & Lamb, R. A. (2011). Influenza virus assembly and budding. Virology 411, 229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 115
    • 84869059389 scopus 로고    scopus 로고
    • Filamentous influenza virus enters cells via macropinocytosis
    • Rossman, J. S., Leser, G. P. & Lamb, R. A. (2012). Filamentous influenza virus enters cells via macropinocytosis. J Virol 86, 10950-10960.
    • (2012) J Virol , vol.86 , pp. 10950-10960
    • Rossman, J.S.1    Leser, G.P.2    Lamb, R.A.3
  • 116
    • 0034142287 scopus 로고    scopus 로고
    • Early stages of influenza virus entry into Mv-1 lung cells: Involvement of dynamin
    • Roy, A. M., Parker, J. S., Parrish, C. R. & Whittaker, G. R. (2000). Early stages of influenza virus entry into Mv-1 lung cells: involvement of dynamin. Virology 267, 17-28.
    • (2000) Virology , vol.267 , pp. 17-28
    • Roy, A.M.1    Parker, J.S.2    Parrish, C.R.3    Whittaker, G.R.4
  • 119
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust, M. J., Lakadamyali, M., Zhang, F. & Zhuang, X. (2004). Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat Struct Mol Biol 11, 567-573.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 120
    • 0024466223 scopus 로고
    • Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
    • Sauter, N. K., Bednarski, M. D., Wurzburg, B. A., Hanson, J. E., Whitesides, G. M., Skehel, J. J. & Wiley, D. C. (1989). Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. Biochemistry 28, 8388-8396.
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1    Bednarski, M.D.2    Wurzburg, B.A.3    Hanson, J.E.4    Whitesides, G.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 121
    • 26944491901 scopus 로고    scopus 로고
    • Influenza virus assembly and budding at the viral budozone
    • Schmitt, A. P. & Lamb, R. A. (2005). Influenza virus assembly and budding at the viral budozone. Adv Virus Res 64, 383-416.
    • (2005) Adv Virus Res , vol.64 , pp. 383-416
    • Schmitt, A.P.1    Lamb, R.A.2
  • 122
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski, S. B. & Whittaker, G. R. (2002). Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J Virol 76, 10455-10464.
    • (2002) J Virol , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 123
    • 0037690744 scopus 로고    scopus 로고
    • Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses
    • Sieczkarski, S. B. & Whittaker, G. R. (2003). Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Traffic 4, 333-343.
    • (2003) Traffic , vol.4 , pp. 333-343
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 124
    • 23844500631 scopus 로고    scopus 로고
    • Characterization of the host cell entry of filamentous influenza virus
    • Sieczkarski, S. B. & Whittaker, G. R. (2005). Characterization of the host cell entry of filamentous influenza virus. Arch Virol 150, 1783-1796.
    • (2005) Arch Virol , vol.150 , pp. 1783-1796
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 125
    • 0037213578 scopus 로고    scopus 로고
    • Role of protein kinase C betaII in influenza virus entry via late endosomes
    • Sieczkarski, S. B., Brown, H. A. & Whittaker, G. R. (2003). Role of protein kinase C betaII in influenza virus entry via late endosomes. J Virol 77, 460-469.
    • (2003) J Virol , vol.77 , pp. 460-469
    • Sieczkarski, S.B.1    Brown, H.A.2    Whittaker, G.R.3
  • 127
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. (2000). Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69, 531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 128
    • 0017924141 scopus 로고
    • On the mechanism of inhibition of influenza virus replication by amantadine hydrochloride
    • Skehel, J. J., Hay, A. J. & Armstrong, J. A. (1978). On the mechanism of inhibition of influenza virus replication by amantadine hydrochloride. J Gen Virol 38, 97-110.
    • (1978) J Gen Virol , vol.38 , pp. 97-110
    • Skehel, J.J.1    Hay, A.J.2    Armstrong, J.A.3
  • 129
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
    • Spruce, A. E., Iwata, A., White, J. M. & Almers, W. (1989). Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature 342, 555-558.
    • (1989) Nature , vol.342 , pp. 555-558
    • Spruce, A.E.1    Iwata, A.2    White, J.M.3    Almers, W.4
  • 130
    • 84881155738 scopus 로고    scopus 로고
    • Influenza: Pathways to human adaptation
    • Steinhauer, D. A. (2013). Influenza: pathways to human adaptation. Nature 499, 412-413.
    • (2013) Nature , vol.499 , pp. 412-413
    • Steinhauer, D.A.1
  • 132
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • Stevens, J., Blixt, O., Glaser, L., Taubenberger, J. K., Palese, P., Paulson, J. C. & Wilson, I. A. (2006a). Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J Mol Biol 355, 1143-1155.
    • (2006) J Mol Biol , vol.355 , 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
  • 133
    • 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. (2006b). Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312, 404-410.
    • (2006) Science , vol.312 , 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
  • 135
    • 0033859822 scopus 로고    scopus 로고
    • Influenza virus infection of desialylated cells
    • Stray, S. J., Cummings, R. D. & Air, G. M. (2000). Influenza virus infection of desialylated cells. Glycobiology 10, 649-658.
    • (2000) Glycobiology , vol.10 , pp. 649-658
    • Stray, S.J.1    Cummings, R.D.2    Air, G.M.3
  • 136
    • 84886389616 scopus 로고    scopus 로고
    • Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry
    • Su, W. C., Chen, Y. C., Tseng, C. H., Hsu, P. W., Tung, K. F., Jeng, K. S. & Lai, M. M. (2013). Pooled RNAi screen identifies ubiquitin ligase Itch as crucial for influenza A virus release from the endosome during virus entry. Proc Natl Acad Sci U S A 110, 17516-17521.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17516-17521
    • Su, W.C.1    Chen, Y.C.2    Tseng, C.H.3    Hsu, P.W.4    Tung, K.F.5    Jeng, K.S.6    Lai, M.M.7
  • 137
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R. J. & Hay, A. J. (1991). Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 180, 617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 138
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • other authors
    • Sui, J., Hwang, W. C., Perez, S., Wei, G., Aird, D., Chen, L. M., Santelli, E., Stec, B., Cadwell, G. & other authors (2009). Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat Struct Mol Biol 16, 265-273.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 265-273
    • Sui, J.1    Hwang, W.C.2    Perez, S.3    Wei, G.4    Aird, D.5    Chen, L.M.6    Santelli, E.7    Stec, B.8    Cadwell, G.9
  • 139
    • 34250734642 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton during influenza virus internalization into polarized epithelial cells
    • Sun, X. & Whittaker, G. R. (2007). Role of the actin cytoskeleton during influenza virus internalization into polarized epithelial cells. Cell Microbiol 9, 1672-1682.
    • (2007) Cell Microbiol , vol.9 , pp. 1672-1682
    • Sun, X.1    Whittaker, G.R.2
  • 140
    • 84875807120 scopus 로고    scopus 로고
    • Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism
    • Sun, X., Shi, Y., Lu, X., He, J., Gao, F., Yan, J., Qi, J. & Gao, G. F. (2013). Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism. Cell Rep 3, 769-778.
    • (2013) Cell Rep , vol.3 , pp. 769-778
    • Sun, X.1    Shi, Y.2    Lu, X.3    He, J.4    Gao, F.5    Yan, J.6    Qi, J.7    Gao, G.F.8
  • 141
    • 0025983151 scopus 로고
    • Virulence of rimantadine-resistant human influenza A (H3N2) viruses in ferrets
    • Sweet, C., Hayden, F. G., Jakeman, K. J., Grambas, S. & Hay, A. J. (1991). Virulence of rimantadine-resistant human influenza A (H3N2) viruses in ferrets. J Infect Dis 164, 969-972.
    • (1991) J Infect Dis , vol.164 , pp. 969-972
    • Sweet, C.1    Hayden, F.G.2    Jakeman, K.J.3    Grambas, S.4    Hay, A.J.5
  • 142
    • 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. (1995). Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J 14, 5514-5523.
    • (1995) EMBO J , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 143
    • 33746210053 scopus 로고    scopus 로고
    • Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates
    • Terabayashi, T., Morita, M., Ueno, M., Nakamura, T. & Urashima, T. (2006). Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates. Carbohydr Res 341, 2246-2253.
    • (2006) Carbohydr Res , vol.341 , pp. 2246-2253
    • Terabayashi, T.1    Morita, M.2    Ueno, M.3    Nakamura, T.4    Urashima, T.5
  • 144
    • 33746808986 scopus 로고    scopus 로고
    • Infection of human airway epithelium by human and avian strains of influenza A virus
    • Thompson, C. I., Barclay, W. S., Zambon, M. C. & Pickles, R. J. (2006). Infection of human airway epithelium by human and avian strains of influenza A virus. J Virol 80, 8060-8068.
    • (2006) J Virol , vol.80 , pp. 8060-8068
    • Thompson, C.I.1    Barclay, W.S.2    Zambon, M.C.3    Pickles, R.J.4
  • 149
    • 77950479967 scopus 로고    scopus 로고
    • Macrophage receptors for influenza A virus: Role of the macrophage galactose-type lectin and mannose receptor in viral entry
    • Upham, J. P., Pickett, D., Irimura, T., Anders, E. M. & Reading, P. C. (2010). Macrophage receptors for influenza A virus: role of the macrophage galactose-type lectin and mannose receptor in viral entry. J Virol 84, 3730-3737.
    • (2010) J Virol , vol.84 , pp. 3730-3737
    • Upham, J.P.1    Pickett, D.2    Irimura, T.3    Anders, E.M.4    Reading, P.C.5
  • 150
    • 77950840696 scopus 로고    scopus 로고
    • Novel inhibitors of influenza virus fusion: Structure-activity relationship and interaction with the viral hemagglutinin
    • Vanderlinden, E., Göktas, F., Cesur, Z., Froeyen, M., Reed, M. L., Russell, C. J., Cesur, N. & Naesens, L. (2010). Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin. J Virol 84, 4277-4288.
    • (2010) J Virol , vol.84 , pp. 4277-4288
    • Vanderlinden, E.1    Göktas, F.2    Cesur, Z.3    Froeyen, M.4    Reed, M.L.5    Russell, C.J.6    Cesur, N.7    Naesens, L.8
  • 151
    • 84895064488 scopus 로고    scopus 로고
    • Emerging antiviral strategies to interfere with influenza virus entry
    • (in press)
    • Vanderlinden, E. & Naesens, L. (2013). Emerging antiviral strategies to interfere with influenza virus entry. Med Res Rev (in press).
    • (2013) Med Res Rev
    • Vanderlinden, E.1    Naesens, L.2
  • 153
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block
    • Wang, C., Takeuchi, K., Pinto, L. H. & Lamb, R. A. (1993). Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J Virol 67, 5585-5594.
    • (1993) J Virol , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 154
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin a) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., Palese, P. & O'Neill, R. E. (1997). The NPI-1/NPI-3 (karyopherin a) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J Virol 71, 1850-1856.
    • (1997) J Virol , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 156
    • 84876266002 scopus 로고    scopus 로고
    • Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus
    • Wang, J., Ma, C., Wang, J., Jo, H., Canturk, B., Fiorin, G., Pinto, L. H., Lamb, R. A., Klein, M. L. & DeGrado, W. F. (2013). Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus. J Med Chem 56, 2804-2812.
    • (2013) J Med Chem , vol.56 , pp. 2804-2812
    • Wang, J.1    Ma, C.2    Wang, J.3    Jo, H.4    Canturk, B.5    Fiorin, G.6    Pinto, L.H.7    Lamb, R.A.8    Klein, M.L.9    DeGrado, W.F.10
  • 158
    • 0032505542 scopus 로고    scopus 로고
    • A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins
    • Weber, F., Kochs, G., Gruber, S. & Haller, O. (1998). A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins. Virology 250, 9-18.
    • (1998) Virology , vol.250 , pp. 9-18
    • Weber, F.1    Kochs, G.2    Gruber, S.3    Haller, O.4
  • 159
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J. H., Cusack, S., Paulson, J. C., Skehel, J. J. & Wiley, D. C. (1988). Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 160
    • 0028300061 scopus 로고
    • Role of virion M2 protein in influenza virus uncoating: Specific reduction in the rate of membrane fusion between virus and liposomes by amantadine
    • Wharton, S. A., Belshe, R. B., Skehel, J. J. & Hay, A. J. (1994). Role of virion M2 protein in influenza virus uncoating: specific reduction in the rate of membrane fusion between virus and liposomes by amantadine. J Gen Virol 75, 945-948.
    • (1994) J Gen Virol , vol.75 , pp. 945-948
    • Wharton, S.A.1    Belshe, R.B.2    Skehel, J.J.3    Hay, A.J.4
  • 161
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White, J. M. & Wilson, I. A. (1987). Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J Cell Biol 105, 2887-2896.
    • (1987) J Cell Biol , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 163
    • 84861968318 scopus 로고    scopus 로고
    • A review of influenza haemagglutinin receptor binding as it relates to pandemic properties
    • Wilks, S., de Graaf, M., Smith, D. J. & Burke, D. F. (2012). A review of influenza haemagglutinin receptor binding as it relates to pandemic properties. Vaccine 30, 4369-4376.
    • (2012) Vaccine , vol.30 , pp. 4369-4376
    • Wilks, S.1    de Graaf, M.2    Smith, D.J.3    Burke, D.F.4
  • 167
    • 75449093578 scopus 로고    scopus 로고
    • Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic
    • Xu, R., McBride, R., Paulson, J. C., Basler, C. F. & Wilson, I. A. (2010). Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic. J Virol 84, 1715-1721.
    • (2010) J Virol , vol.84 , pp. 1715-1721
    • Xu, R.1    McBride, R.2    Paulson, J.C.3    Basler, C.F.4    Wilson, I.A.5
  • 169
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses
    • Yoshida, R., Igarashi, M., Ozaki, H., Kishida, N., Tomabechi, D., Kida, H., Ito, K. & Takada, A. (2009). Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog 5, e1000350.
    • (2009) PLoS Pathog , vol.5
    • Yoshida, R.1    Igarashi, M.2    Ozaki, H.3    Kishida, N.4    Tomabechi, D.5    Kida, H.6    Ito, K.7    Takada, A.8
  • 170
    • 0033027378 scopus 로고    scopus 로고
    • Identification of a novel HA conformational change inhibitor of human influenza virus
    • Yoshimoto, J., Kakui, M., Iwasaki, H., Fujiwara, T., Sugimoto, H. & Hattori, N. (1999). Identification of a novel HA conformational change inhibitor of human influenza virus. Arch Virol 144, 865-878.
    • (1999) Arch Virol , vol.144 , pp. 865-878
    • Yoshimoto, J.1    Kakui, M.2    Iwasaki, H.3    Fujiwara, T.4    Sugimoto, H.5    Hattori, N.6
  • 172
    • 0023820458 scopus 로고
    • Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions
    • Zebedee, S. L. & Lamb, R. A. (1988). Influenza A virus M2 protein: monoclonal antibody restriction of virus growth and detection of M2 in virions. J Virol 62, 2762-2772.
    • (1988) J Virol , vol.62 , pp. 2762-2772
    • Zebedee, S.L.1    Lamb, R.A.2
  • 173
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial, M. & McBride, H. (2001). Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2, 107-117.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 174
    • 0030588962 scopus 로고    scopus 로고
    • Characterization of the membrane association of the influenza virus matrix protein in living cells
    • Zhang, J. & Lamb, R. A. (1996). Characterization of the membrane association of the influenza virus matrix protein in living cells. Virology 225, 255-266.
    • (1996) Virology , vol.225 , pp. 255-266
    • Zhang, J.1    Lamb, R.A.2
  • 175
    • 0025266931 scopus 로고
    • Solubilization of matrix protein M1/M from virions occurs at different pH for orthomyxo-and paramyxoviruses
    • Zhirnov, O. P. (1990). Solubilization of matrix protein M1/M from virions occurs at different pH for orthomyxo-and paramyxoviruses. Virology 176, 274-279.
    • (1990) Virology , vol.176 , pp. 274-279
    • Zhirnov, O.P.1
  • 176
    • 83455162535 scopus 로고    scopus 로고
    • Inhibition of influenza A virus (H1N1) fusion by benzenesulfonamide derivatives targeting viral hemagglutinin
    • other authors
    • Zhu, L., Li, Y., Li, S., Li, H., Qiu, Z., Lee, C., Lu, H., Lin, X., Zhao, R. & other authors (2011). Inhibition of influenza A virus (H1N1) fusion by benzenesulfonamide derivatives targeting viral hemagglutinin. PLoS ONE 6, e29120.
    • (2011) PLoS ONE , vol.6
    • Zhu, L.1    Li, Y.2    Li, S.3    Li, H.4    Qiu, Z.5    Lee, C.6    Lu, H.7    Lin, X.8    Zhao, R.9
  • 177
    • 84892622601 scopus 로고    scopus 로고
    • PLC-c1 signaling plays a subtypespecific role in post-binding cell entry of influenza A virus
    • [Epub ahead of print]
    • Zhu, L., Ly, H. & Liang, Y. (2013a). PLC-c1 signaling plays a subtypespecific role in post-binding cell entry of influenza A virus. J Virol [Epub ahead of print].
    • (2013) J Virol
    • Zhu, L.1    Ly, H.2    Liang, Y.3
  • 178
    • 84872831242 scopus 로고    scopus 로고
    • Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities
    • Zhu, X., Yu, W., McBride, R., Li, Y., Chen, L. M., Donis, R. O., Tong, S., Paulson, J. C. & Wilson, I. A. (2013b). Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities. Proc Natl Acad Sci U S A 110, 1458-1463.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1458-1463
    • Zhu, X.1    Yu, W.2    McBride, R.3    Li, Y.4    Chen, L.M.5    Donis, R.O.6    Tong, S.7    Paulson, J.C.8    Wilson, I.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.