메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Genomic and protein structural maps of adaptive evolution of human influenza a virus to increased virulence in the mouse

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; NONSTRUCTURAL PROTEIN 1; RNA POLYMERASE; VIRUS NUCLEOPROTEIN; VIRUS SIALIDASE; VIRUS PROTEIN;

EID: 79959725144     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021740     Document Type: Article
Times cited : (73)

References (125)
  • 2
    • 33744942931 scopus 로고    scopus 로고
    • Host range restriction and pathogenicity in the context of influenza pandemic
    • Neumann G, Kawaoka Y, (2006) Host range restriction and pathogenicity in the context of influenza pandemic. Emerg Infect Dis 12: 881-886.
    • (2006) Emerg Infect Dis , vol.12 , pp. 881-886
    • Neumann, G.1    Kawaoka, Y.2
  • 3
    • 77956499048 scopus 로고    scopus 로고
    • Influenza virus evolution, host adaptation, and pandemic formation
    • S1931-3128(10)00172-1 [pii];10.1016/j.chom.2010.05.009 [doi]
    • Taubenberger JK, Kash JC, (2010) Influenza virus evolution, host adaptation, and pandemic formation. Cell Host Microbe 7: 440-451 S1931-3128(10)00172-1 [pii];10.1016/j.chom.2010.05.009 [doi].
    • (2010) Cell Host Microbe , vol.7 , pp. 440-451
    • Taubenberger, J.K.1    Kash, J.C.2
  • 4
    • 58549116149 scopus 로고    scopus 로고
    • Virulence evolution and the trade-off hypothesis: history, current state of affairs and the future
    • JEB1658 [pii];10.1111/j.1420-9101.2008.01658.x [doi]
    • Alizon S, Hurford A, Mideo N, Van BM, (2009) Virulence evolution and the trade-off hypothesis: history, current state of affairs and the future. J Evol Biol 22: 245-259 JEB1658 [pii];10.1111/j.1420-9101.2008.01658.x [doi].
    • (2009) J Evol Biol , vol.22 , pp. 245-259
    • Alizon, S.1    Hurford, A.2    Mideo, N.3    Van, B.M.4
  • 5
    • 77958113527 scopus 로고    scopus 로고
    • Identifying genetic markers of adaptation for surveillance of viral host jumps
    • nrmicro2440 [pii];10.1038/nrmicro2440 [doi]
    • Pepin KM, Lass S, Pulliam JR, Read AF, Lloyd-Smith JO, (2010) Identifying genetic markers of adaptation for surveillance of viral host jumps. Nat Rev Microbiol 8: 802-813 nrmicro2440 [pii];10.1038/nrmicro2440 [doi].
    • (2010) Nat Rev Microbiol , vol.8 , pp. 802-813
    • Pepin, K.M.1    Lass, S.2    Pulliam, J.R.3    Read, A.F.4    Lloyd-Smith, J.O.5
  • 6
    • 67650407532 scopus 로고    scopus 로고
    • Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans
    • Garten RJ, Davis CT, Russell CA, Shu B, Lindstrom, et al. (2009) Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science 325: 197-201.
    • (2009) Science , vol.325 , pp. 197-201
    • Garten, R.J.1    Davis, C.T.2    Russell, C.A.3    Shu, B.4    Lindstrom5
  • 7
    • 77950472820 scopus 로고    scopus 로고
    • Introduction of virulence markers in PB2 of pandemic swine-origin influenza virus does not result in enhanced virulence or transmission
    • Herfst S, Chutinimitkul S, Ye J, de Wit E, Munster VJ, et al. (2010) Introduction of virulence markers in PB2 of pandemic swine-origin influenza virus does not result in enhanced virulence or transmission. J Virol 84: 3752-3758.
    • (2010) J Virol , vol.84 , pp. 3752-3758
    • Herfst, S.1    Chutinimitkul, S.2    Ye, J.3    de Wit, E.4    Munster, V.J.5
  • 8
    • 69149093400 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses
    • Itoh Y, Shinya K, Kiso M, Watanabe T, Sakoda Y, et al. (2009) In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses. Nature %20;460: 1021-1025.
    • (2009) Nature %20 , vol.460 , pp. 1021-1025
    • Itoh, Y.1    Shinya, K.2    Kiso, M.3    Watanabe, T.4    Sakoda, Y.5
  • 9
    • 78651247566 scopus 로고    scopus 로고
    • Influenza A virus NS1 gene mutations F103L and M106I increase replication and virulence
    • 1743-422X-8-13. [pii];10.1186/1743-422X-8-13 [doi]
    • Dankar SK, Wang S, Ping J, Forbes NE, Keleta L, et al. (2011) Influenza A virus NS1 gene mutations F103L and M106I increase replication and virulence. Virol J 8: 13. 1743-422X-8-13 [pii];10.1186/1743-422X-8-13 [doi].
    • (2011) Virol J , vol.8 , pp. 13
    • Dankar, S.K.1    Wang, S.2    Ping, J.3    Forbes, N.E.4    Keleta, L.5
  • 10
    • 56449102489 scopus 로고    scopus 로고
    • Experimental evolution of human influenza virus H3 hemagglutinin in the mouse lung identifies adaptive regions in HA1 and HA2
    • Keleta L, Ibricevic A, Bovin NV, Brody SL, Brown EG, (2008) Experimental evolution of human influenza virus H3 hemagglutinin in the mouse lung identifies adaptive regions in HA1 and HA2. J Virol 82: 11599-11608.
    • (2008) J Virol , vol.82 , pp. 11599-11608
    • Keleta, L.1    Ibricevic, A.2    Bovin, N.V.3    Brody, S.L.4    Brown, E.G.5
  • 11
    • 37549017103 scopus 로고    scopus 로고
    • Convergence and parallelism reconsidered: what have we learned about the genetics of adaptation?
    • S0169-5347(07)00287-X [pii];10.1016/j.tree.2007.09.011 [doi]
    • Arendt J, Reznick D, (2008) Convergence and parallelism reconsidered: what have we learned about the genetics of adaptation? Trends Ecol Evol 23: 26-32 S0169-5347(07)00287-X [pii];10.1016/j.tree.2007.09.011 [doi].
    • (2008) Trends Ecol Evol , vol.23 , pp. 26-32
    • Arendt, J.1    Reznick, D.2
  • 12
    • 78951480118 scopus 로고    scopus 로고
    • Parallel adaptation: one or many waves of advance of an advantageous allele?
    • genetics.110.119594 [pii];10.1534/genetics.110.119594 [doi]
    • Ralph P, Coop G, (2010) Parallel adaptation: one or many waves of advance of an advantageous allele? Genetics 186: 647-668 genetics.110.119594 [pii];10.1534/genetics.110.119594 [doi].
    • (2010) Genetics , vol.186 , pp. 647-668
    • Ralph, P.1    Coop, G.2
  • 13
    • 16344387924 scopus 로고    scopus 로고
    • Parallel genotypic adaptation: when evolution repeats itself
    • Wood TE, Burke JM, Rieseberg LH, (2005) Parallel genotypic adaptation: when evolution repeats itself. Genetica 123: 157-170.
    • (2005) Genetica , vol.123 , pp. 157-170
    • Wood, T.E.1    Burke, J.M.2    Rieseberg, L.H.3
  • 14
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • In: Knipe DM, Howley PM, editors, Philadelphia, Lippincott Williams and Wilkins
    • Palese P, Shaw M, (2007) Orthomyxoviridae: The viruses and their replication. In: Knipe DM, Howley PM, editors. Field's Virology Philadelphia Lippincott Williams and Wilkins pp. 1647-1689.
    • (2007) Field's Virology , pp. 1647-1689
    • Palese, P.1    Shaw, M.2
  • 15
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • S1931-3128(10)00171-X [pii];10.1016/j.chom.2010.05.008 [doi]
    • Watanabe T, Watanabe S, Kawaoka Y, (2010) Cellular networks involved in the influenza virus life cycle. Cell Host Microbe 7: 427-439 S1931-3128(10)00171-X [pii];10.1016/j.chom.2010.05.008 [doi].
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 16
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira SD, Gat-Viks I, Shum BO, Dricot A, de Grace MM, et al. (2009) A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 139: 1255-1267.
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1    Gat-Viks, I.2    Shum, B.O.3    Dricot, A.4    de Grace, M.M.5
  • 17
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms
    • R110.117531 [pii];10.1074/jbc.R110.117531 [doi]
    • Boivin S, Cusack S, Ruigrok RW, Hart DJ, (2010) Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms. J Biol Chem 285: 28411-28417 R110.117531 [pii];10.1074/jbc.R110.117531 [doi].
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 18
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale BG, Randall RE, Ortin J, Jackson D, (2008) The multifunctional NS1 protein of influenza A viruses. J Gen Virol 89: 2359-2376.
    • (2008) J Gen Virol , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 19
    • 53849125470 scopus 로고    scopus 로고
    • Host restriction of avian influenza viruses at the level of the ribonucleoproteins
    • 10.1146/annurev.micro.62.081307.162746 [doi]
    • Naffakh N, Tomoiu A, Rameix-Welti MA, van der Werf S, (2008) Host restriction of avian influenza viruses at the level of the ribonucleoproteins. Annu Rev Microbiol 62: 403-424 10.1146/annurev.micro.62.081307.162746 [doi].
    • (2008) Annu Rev Microbiol , vol.62 , pp. 403-424
    • Naffakh, N.1    Tomoiu, A.2    Rameix-Welti, M.A.3    van der Werf, S.4
  • 20
    • 33846822057 scopus 로고    scopus 로고
    • Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes
    • Boulo S, Akarsu H, Ruigrok RW, Baudin F, (2007) Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res 124: 12-21.
    • (2007) Virus Res , vol.124 , pp. 12-21
    • Boulo, S.1    Akarsu, H.2    Ruigrok, R.W.3    Baudin, F.4
  • 21
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC, (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69: 531-69.:531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 23
    • 34247602190 scopus 로고    scopus 로고
    • Changing epidemiology and ecology of highly pathogenic avian H5N1 influenza viruses
    • Webster RG, Hulse-Post DJ, Sturm-Ramirez KM, Guan Y, Peiris M, et al. (2007) Changing epidemiology and ecology of highly pathogenic avian H5N1 influenza viruses. Avian Dis 51: 269-272.
    • (2007) Avian Dis , vol.51 , pp. 269-272
    • Webster, R.G.1    Hulse-Post, D.J.2    Sturm-Ramirez, K.M.3    Guan, Y.4    Peiris, M.5
  • 24
    • 79959752086 scopus 로고    scopus 로고
    • Trends in influenza A virus genetics: Can we predict the natural evolution of a H5N1 Z?
    • Brown EG, Sattar SA, Tetro JA, Liu J, (2008) Trends in influenza A virus genetics: Can we predict the natural evolution of a H5N1 Z? Current Topics in Virology 7: 99-113.
    • (2008) Current Topics in Virology , vol.7 , pp. 99-113
    • Brown, E.G.1    Sattar, S.A.2    Tetro, J.A.3    Liu, J.4
  • 26
    • 9444252844 scopus 로고    scopus 로고
    • Evidence of an absence: the genetic origins of the 1918 pandemic influenza virus
    • Reid AH, Taubenberger JK, Fanning TG, (2004) Evidence of an absence: the genetic origins of the 1918 pandemic influenza virus. Nat Rev Microbiol 2: 909-914.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 909-914
    • Reid, A.H.1    Taubenberger, J.K.2    Fanning, T.G.3
  • 27
    • 0141566293 scopus 로고    scopus 로고
    • Relationship of pre-1918 avian influenza HA and NP sequences to subsequent avian influenza strains
    • Reid AH, Fanning TG, Slemons RD, Janczewski TA, Dean J, et al. (2003) Relationship of pre-1918 avian influenza HA and NP sequences to subsequent avian influenza strains. Avian Dis 47: 921-925.
    • (2003) Avian Dis , vol.47 , pp. 921-925
    • Reid, A.H.1    Fanning, T.G.2    Slemons, R.D.3    Janczewski, T.A.4    Dean, J.5
  • 29
    • 0033760939 scopus 로고    scopus 로고
    • Molecular correlates of influenza A H5N1 virus pathogenesis in mice
    • Katz JM, Lu X, Tumpey TM, Smith CB, Shaw MW, et al. (2000) Molecular correlates of influenza A H5N1 virus pathogenesis in mice. J Virol 74: 10807-10810.
    • (2000) J Virol , vol.74 , pp. 10807-10810
    • Katz, J.M.1    Lu, X.2    Tumpey, T.M.3    Smith, C.B.4    Shaw, M.W.5
  • 30
    • 26444490055 scopus 로고    scopus 로고
    • Characterization of the reconstructed 1918 Spanish influenza pandemic virus
    • Tumpey TM, Basler CF, Aguilar PV, Zeng H, Solorzano A, et al. (2005) Characterization of the reconstructed 1918 Spanish influenza pandemic virus. Science 310: 77-80.
    • (2005) Science , vol.310 , pp. 77-80
    • Tumpey, T.M.1    Basler, C.F.2    Aguilar, P.V.3    Zeng, H.4    Solorzano, A.5
  • 31
    • 47049127117 scopus 로고    scopus 로고
    • Progress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses
    • S0166-3542(08)00289-1 [pii];10.1016/j.antiviral.2008.04.006 [doi]
    • Basler CF, Aguilar PV, (2008) Progress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses. Antiviral Res 79: 166-178 S0166-3542(08)00289-1 [pii];10.1016/j.antiviral.2008.04.006 [doi].
    • (2008) Antiviral Res , vol.79 , pp. 166-178
    • Basler, C.F.1    Aguilar, P.V.2
  • 32
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta M, Gao P, Halfmann P, Kawaoka Y, (2001) Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293: 1840-1842.
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 33
    • 0036734038 scopus 로고    scopus 로고
    • Lethal H5N1 influenza viruses escape host anti-viral cytokine responses
    • Seo SH, Hoffmann E, Webster RG, (2002) Lethal H5N1 influenza viruses escape host anti-viral cytokine responses. Nat Med 8: 950-954.
    • (2002) Nat Med , vol.8 , pp. 950-954
    • Seo, S.H.1    Hoffmann, E.2    Webster, R.G.3
  • 34
    • 41949123710 scopus 로고    scopus 로고
    • A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity
    • 0800482105 [pii];10.1073/pnas.0800482105 [doi]
    • Jackson D, Hossain MJ, Hickman D, Perez DR, Lamb RA, (2008) A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity. Proc Natl Acad Sci U S A 105: 4381-4386 0800482105 [pii];10.1073/pnas.0800482105 [doi].
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4381-4386
    • Jackson, D.1    Hossain, M.J.2    Hickman, D.3    Perez, D.R.4    Lamb, R.A.5
  • 35
    • 36049034216 scopus 로고    scopus 로고
    • A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence
    • 07-PLPA-RA-0345 [pii];10.1371/journal.ppat.0030141 [doi]
    • Conenello GM, Zamarin D, Perrone LA, Tumpey T, Palese P, (2007) A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulence. PLoS Pathog 3: 1414-1421 07-PLPA-RA-0345 [pii];10.1371/journal.ppat.0030141 [doi].
    • (2007) PLoS Pathog , vol.3 , pp. 1414-1421
    • Conenello, G.M.1    Zamarin, D.2    Perrone, L.A.3    Tumpey, T.4    Palese, P.5
  • 36
    • 78650648417 scopus 로고    scopus 로고
    • A single N66S mutation in the PB1-F2 protein of influenza A virus increases virulence by inhibiting the early interferon response in vivo
    • JVI.01987-10 [pii];10.1128/JVI.01987-10 [doi]
    • Conenello GM, Tisoncik JR, Rosenzweig E, Varga ZT, Palese P, et al. (2011) A single N66S mutation in the PB1-F2 protein of influenza A virus increases virulence by inhibiting the early interferon response in vivo. J Virol 85: 652-662 JVI.01987-10 [pii];10.1128/JVI.01987-10 [doi].
    • (2011) J Virol , vol.85 , pp. 652-662
    • Conenello, G.M.1    Tisoncik, J.R.2    Rosenzweig, E.3    Varga, Z.T.4    Palese, P.5
  • 37
    • 79959727191 scopus 로고
    • On the Origin of Species by Means of Natrual Selection
    • London reprint 1979 by Gramercy Books N.Y
    • Charles Dar win, (1859) On the Origin of Species by Means of Natrual Selection. J. Murray London reprint 1979 by Gramercy Books N.Y.
    • (1859) J. Murray
    • Charles, D.1
  • 38
    • 13144257707 scopus 로고    scopus 로고
    • The genetic theory of adaptation: a brief history
    • Orr HA, (2005) The genetic theory of adaptation: a brief history. Nat Rev Genet 6: 119-127.
    • (2005) Nat Rev Genet , vol.6 , pp. 119-127
    • Orr, H.A.1
  • 39
    • 0036245475 scopus 로고    scopus 로고
    • Understanding quantitative genetic variation
    • 10.1038/nrg700 [doi];nrg700 [pii]
    • Barton NH, Keightley PD, (2002) Understanding quantitative genetic variation. Nat Rev Genet 3: 11-21 10.1038/nrg700 [doi];nrg700 [pii].
    • (2002) Nat Rev Genet , vol.3 , pp. 11-21
    • Barton, N.H.1    Keightley, P.D.2
  • 41
    • 33750447962 scopus 로고    scopus 로고
    • The role of compensatory mutations in the emergence of drug resistance
    • 05-PLCB-RA-0334R3 [pii];10.1371/journal.pcbi.0020137 [doi]
    • Handel A, Regoes RR, Antia R, (2006) The role of compensatory mutations in the emergence of drug resistance. PLoS Comput Biol 2: e137 05-PLCB-RA-0334R3 [pii];10.1371/journal.pcbi.0020137 [doi].
    • (2006) PLoS Comput Biol , vol.2
    • Handel, A.1    Regoes, R.R.2    Antia, R.3
  • 43
    • 0033575348 scopus 로고    scopus 로고
    • Different trajectories of parallel evolution during viral adaptation
    • 7680 [pii]
    • Wichman HA, Badgett MR, Scott LA, Boulianne CM, Bull JJ, (1999) Different trajectories of parallel evolution during viral adaptation. Science 285: 422-424 7680 [pii].
    • (1999) Science , vol.285 , pp. 422-424
    • Wichman, H.A.1    Badgett, M.R.2    Scott, L.A.3    Boulianne, C.M.4    Bull, J.J.5
  • 44
    • 13244264987 scopus 로고    scopus 로고
    • The probability of parallel evolution
    • Orr HA, (2005) The probability of parallel evolution. Evolution 59: 216-220.
    • (2005) Evolution , vol.59 , pp. 216-220
    • Orr, H.A.1
  • 45
    • 78649414880 scopus 로고    scopus 로고
    • Microevolution of canine influenza virus in shelters and its molecular epidemiology in the United States
    • JVI.01350-10 [pii];10.1128/JVI.01350-10 [doi]
    • Hayward JJ, Dubovi EJ, Scarlett JM, Janeczko S, Holmes EC, et al. (2010) Microevolution of canine influenza virus in shelters and its molecular epidemiology in the United States. J Virol 84: 12636-12645 JVI.01350-10 [pii];10.1128/JVI.01350-10 [doi].
    • (2010) J Virol , vol.84 , pp. 12636-12645
    • Hayward, J.J.1    Dubovi, E.J.2    Scarlett, J.M.3    Janeczko, S.4    Holmes, E.C.5
  • 46
    • 33846007284 scopus 로고    scopus 로고
    • Stochastic processes are key determinants of short-term evolution in influenza a virus
    • 06-PLPA-RA-0281R2 [pii];10.1371/journal.ppat.0020125 [doi]
    • Nelson MI, Simonsen L, Viboud C, Miller MA, Taylor J, et al. (2006) Stochastic processes are key determinants of short-term evolution in influenza a virus. PLoS Pathog 2: e125 06-PLPA-RA-0281R2 [pii];10.1371/journal.ppat.0020125 [doi].
    • (2006) PLoS Pathog , vol.2
    • Nelson, M.I.1    Simonsen, L.2    Viboud, C.3    Miller, M.A.4    Taylor, J.5
  • 47
    • 44449164435 scopus 로고    scopus 로고
    • The genomic and epidemiological dynamics of human influenza A virus
    • nature06945 [pii];10.1038/nature06945 [doi]
    • Rambaut A, Pybus OG, Nelson MI, Viboud C, Taubenberger JK, et al. (2008) The genomic and epidemiological dynamics of human influenza A virus. Nature 453: 615-619 nature06945 [pii];10.1038/nature06945 [doi].
    • (2008) Nature , vol.453 , pp. 615-619
    • Rambaut, A.1    Pybus, O.G.2    Nelson, M.I.3    Viboud, C.4    Taubenberger, J.K.5
  • 48
    • 0026561520 scopus 로고
    • Heterogeneity of the mutation rates of influenza A viruses: isolation of mutator mutants
    • Suarez P, Valcarcel J, Ortin J, (1992) Heterogeneity of the mutation rates of influenza A viruses: isolation of mutator mutants. J Virol 66: 2491-2494.
    • (1992) J Virol , vol.66 , pp. 2491-2494
    • Suarez, P.1    Valcarcel, J.2    Ortin, J.3
  • 49
    • 0019827545 scopus 로고
    • Antigenic structure of influenza virus haemagglutinin defined by hybridoma antibodies
    • Gerhard W, Yewdell J, Frankel ME, Webster R, (1981) Antigenic structure of influenza virus haemagglutinin defined by hybridoma antibodies. Nature 290: 713-717.
    • (1981) Nature , vol.290 , pp. 713-717
    • Gerhard, W.1    Yewdell, J.2    Frankel, M.E.3    Webster, R.4
  • 50
    • 34447271704 scopus 로고    scopus 로고
    • Surveillance of resistance to adamantanes among influenza A(H3N2) and A(H1N1) viruses isolated worldwide
    • JID37908 [pii];10.1086/518936 [doi]
    • Deyde VM, Xu X, Bright RA, Shaw M, Smith CB, et al. (2007) Surveillance of resistance to adamantanes among influenza A(H3N2) and A(H1N1) viruses isolated worldwide. J Infect Dis 196: 249-257 JID37908 [pii];10.1086/518936 [doi].
    • (2007) J Infect Dis , vol.196 , pp. 249-257
    • Deyde, V.M.1    Xu, X.2    Bright, R.A.3    Shaw, M.4    Smith, C.B.5
  • 51
    • 72049131299 scopus 로고    scopus 로고
    • Emergence of H274Y oseltamivir-resistant A(H1N1) influenza viruses in Japan during the 2008-2009 season
    • S1386-6532(09)00544-7 [pii];10.1016/j.jcv.2009.11.003 [doi]
    • Baranovich T, Saito R, Suzuki Y, Zaraket H, Dapat C, et al. (2010) Emergence of H274Y oseltamivir-resistant A(H1N1) influenza viruses in Japan during the 2008-2009 season. J Clin Virol 47: 23-28 S1386-6532(09)00544-7 [pii];10.1016/j.jcv.2009.11.003 [doi].
    • (2010) J Clin Virol , vol.47 , pp. 23-28
    • Baranovich, T.1    Saito, R.2    Suzuki, Y.3    Zaraket, H.4    Dapat, C.5
  • 52
    • 77953262416 scopus 로고    scopus 로고
    • Permissive secondary mutations enable the evolution of influenza oseltamivir resistance
    • 328/5983/1272 [pii];10.1126/science.1187816 [doi]
    • Bloom JD, Gong LI, Baltimore D, (2010) Permissive secondary mutations enable the evolution of influenza oseltamivir resistance. Science 328: 1272-1275 328/5983/1272 [pii];10.1126/science.1187816 [doi].
    • (2010) Science , vol.328 , pp. 1272-1275
    • Bloom, J.D.1    Gong, L.I.2    Baltimore, D.3
  • 53
    • 0034194673 scopus 로고    scopus 로고
    • Influenza virus genetics
    • Brown EG, (2000) Influenza virus genetics. Biomed Pharmacother 54: 196-209.
    • (2000) Biomed Pharmacother , vol.54 , pp. 196-209
    • Brown, E.G.1
  • 54
    • 0030774559 scopus 로고    scopus 로고
    • Virulence of influenza A virus for mouse lung
    • Ward AC, (1997) Virulence of influenza A virus for mouse lung. Virus Genes 14: 187-194.
    • (1997) Virus Genes , vol.14 , pp. 187-194
    • Ward, A.C.1
  • 55
    • 75849136881 scopus 로고    scopus 로고
    • Adaptive strategies of the influenza virus polymerase for replication in humans
    • Mehle A, Doudna JA, (2009) Adaptive strategies of the influenza virus polymerase for replication in humans. Proc Natl Acad Sci U S A 106: 21312-21316.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21312-21316
    • Mehle, A.1    Doudna, J.A.2
  • 57
    • 0025075756 scopus 로고
    • Increased virulence of a mouse-adapted variant of influenza A/FM/1/47 virus is controlled by mutations in genome segments 4, 5, 7, and 8
    • Brown EG, (1990) Increased virulence of a mouse-adapted variant of influenza A/FM/1/47 virus is controlled by mutations in genome segments 4, 5, 7, and 8. J Virol 64: 4523-4533.
    • (1990) J Virol , vol.64 , pp. 4523-4533
    • Brown, E.G.1
  • 58
    • 0033067395 scopus 로고    scopus 로고
    • Genetic analysis of mouse-adapted influenza A virus identifies roles for the NA, PB1, and PB2 genes in virulence
    • Brown EG, Bailly JE, (1999) Genetic analysis of mouse-adapted influenza A virus identifies roles for the NA, PB1, and PB2 genes in virulence. Virus Res 61: 63-76.
    • (1999) Virus Res , vol.61 , pp. 63-76
    • Brown, E.G.1    Bailly, J.E.2
  • 59
    • 0035811003 scopus 로고    scopus 로고
    • Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: identification of functional themes
    • Brown EG, Liu H, Kit LC, Baird S, Nesrallah M, (2001) Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: identification of functional themes. Proc Natl Acad Sci U S A 98: 6883-6888.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6883-6888
    • Brown, E.G.1    Liu, H.2    Kit, L.C.3    Baird, S.4    Nesrallah, M.5
  • 60
    • 29444438899 scopus 로고    scopus 로고
    • The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host
    • Gabriel G, Dauber B, Wolff T, Planz O, Klenk HD, et al. (2005) The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proc Natl Acad Sci U S A %20;102: 18590-18595.
    • (2005) Proc Natl Acad Sci U S A %20 , vol.102 , pp. 18590-18595
    • Gabriel, G.1    Dauber, B.2    Wolff, T.3    Planz, O.4    Klenk, H.D.5
  • 61
    • 69349096064 scopus 로고    scopus 로고
    • Single mutation at the amino acid position 627 of PB2 that leads to increased virulence of an H5N1 avian influenza virus during adaptation in mice can be compensated by multiple mutations at other sites of PB2
    • Li J, Ishaq M, Prudence M, Xi X, Hu T, et al. (2009) Single mutation at the amino acid position 627 of PB2 that leads to increased virulence of an H5N1 avian influenza virus during adaptation in mice can be compensated by multiple mutations at other sites of PB2. Virus Res 144: 123-129.
    • (2009) Virus Res , vol.144 , pp. 123-129
    • Li, J.1    Ishaq, M.2    Prudence, M.3    Xi, X.4    Hu, T.5
  • 62
    • 58349121196 scopus 로고    scopus 로고
    • Adaptation of human influenza H3N2 virus in a mouse pneumonitis model: insights into viral virulence, tissue tropism and host pathogenesis
    • Narasaraju T, Sim MK, Ng HH, Phoon MC, Shanker N, et al. (2009) Adaptation of human influenza H3N2 virus in a mouse pneumonitis model: insights into viral virulence, tissue tropism and host pathogenesis. Microbes Infect 11: 2-11.
    • (2009) Microbes Infect , vol.11 , pp. 2-11
    • Narasaraju, T.1    Sim, M.K.2    Ng, H.H.3    Phoon, M.C.4    Shanker, N.5
  • 63
    • 67449101824 scopus 로고    scopus 로고
    • Adaptive mutations resulting in enhanced polymerase activity contribute to high virulence of influenza A virus in mice
    • Rolling T, Koerner I, Zimmermann P, Holz K, Haller O, et al. (2009) Adaptive mutations resulting in enhanced polymerase activity contribute to high virulence of influenza A virus in mice. J Virol 83: 6673-6680.
    • (2009) J Virol , vol.83 , pp. 6673-6680
    • Rolling, T.1    Koerner, I.2    Zimmermann, P.3    Holz, K.4    Haller, O.5
  • 64
  • 65
    • 0028107688 scopus 로고
    • The influenza virus variant A/FM/1/47-MA possesses single amino acid replacements in the hemagglutinin, controlling virulence, and in the matrix protein, controlling virulence as well as growth
    • Smeenk CA, Brown EG, (1994) The influenza virus variant A/FM/1/47-MA possesses single amino acid replacements in the hemagglutinin, controlling virulence, and in the matrix protein, controlling virulence as well as growth. J Virol 68: 530-534.
    • (1994) J Virol , vol.68 , pp. 530-534
    • Smeenk, C.A.1    Brown, E.G.2
  • 66
    • 0030271198 scopus 로고    scopus 로고
    • Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis
    • Smeenk CA, Wright KE, Burns BF, Thaker AJ, Brown EG, (1996) Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis. Virus Res 44: 79-95.
    • (1996) Virus Res , vol.44 , pp. 79-95
    • Smeenk, C.A.1    Wright, K.E.2    Burns, B.F.3    Thaker, A.J.4    Brown, E.G.5
  • 67
    • 70450170087 scopus 로고    scopus 로고
    • The polymerase acidic protein gene of influenza a virus contributes to pathogenicity in a mouse model
    • Song MS, Pascua PN, Lee JH, Baek YH, Lee OJ, et al. (2009) The polymerase acidic protein gene of influenza a virus contributes to pathogenicity in a mouse model. J Virol 83: 12325-12335.
    • (2009) J Virol , vol.83 , pp. 12325-12335
    • Song, M.S.1    Pascua, P.N.2    Lee, J.H.3    Baek, Y.H.4    Lee, O.J.5
  • 68
    • 67349122005 scopus 로고    scopus 로고
    • Multiple amino acid substitutions are involved in the adaptation of H9N2 avian influenza virus to mice
    • Wu R, Zhang H, Yang K, Liang W, Xiong Z, et al. (2009) Multiple amino acid substitutions are involved in the adaptation of H9N2 avian influenza virus to mice. Vet Microbiol 138: 85-91.
    • (2009) Vet Microbiol , vol.138 , pp. 85-91
    • Wu, R.1    Zhang, H.2    Yang, K.3    Liang, W.4    Xiong, Z.5
  • 69
    • 52649172251 scopus 로고    scopus 로고
    • Evidence of expanded host range and mammalian-associated genetic changes in a duck H9N2 influenza virus following adaptation in quail and chickens
    • Hossain MJ, Hickman D, Perez DR, (2008) Evidence of expanded host range and mammalian-associated genetic changes in a duck H9N2 influenza virus following adaptation in quail and chickens. PLoS One 3: e3170.
    • (2008) PLoS One , vol.3
    • Hossain, M.J.1    Hickman, D.2    Perez, D.R.3
  • 70
    • 41349092581 scopus 로고    scopus 로고
    • Influenza A (H1N1) virus resistance to cyanovirin-N arises naturally during adaptation to mice and by passage in cell culture in the presence of the inhibitor
    • Smee DF, Wandersee MK, Checketts MB, O'Keefe BR, Saucedo C, et al. (2007) Influenza A (H1N1) virus resistance to cyanovirin-N arises naturally during adaptation to mice and by passage in cell culture in the presence of the inhibitor. Antivir Chem Chemother 18: 317-327.
    • (2007) Antivir Chem Chemother , vol.18 , pp. 317-327
    • Smee, D.F.1    Wandersee, M.K.2    Checketts, M.B.3    O'Keefe, B.R.4    Saucedo, C.5
  • 71
    • 77956625295 scopus 로고    scopus 로고
    • Adaptation of pandemic H1N1 influenza viruses in mice
    • JVI.00159-10 [pii];10.1128/JVI.00159-10 [doi]
    • Ilyushina NA, Khalenkov AM, Seiler JP, Forrest HL, Bovin NV, et al. (2010) Adaptation of pandemic H1N1 influenza viruses in mice. J Virol 84: 8607-8616 JVI.00159-10 [pii];10.1128/JVI.00159-10 [doi].
    • (2010) J Virol , vol.84 , pp. 8607-8616
    • Ilyushina, N.A.1    Khalenkov, A.M.2    Seiler, J.P.3    Forrest, H.L.4    Bovin, N.V.5
  • 72
    • 78449245226 scopus 로고    scopus 로고
    • Variations in the hemagglutinin of the 2009 H1N1 pandemic virus: potential for strains with altered virulence phenotype?
    • 10.1371/journal.ppat.1001145 [doi]
    • Ye J, Sorrell EM, Cai Y, Shao H, Xu K, et al. (2010) Variations in the hemagglutinin of the 2009 H1N1 pandemic virus: potential for strains with altered virulence phenotype? PLoS Pathog 6: e1001145 10.1371/journal.ppat.1001145 [doi].
    • (2010) PLoS Pathog , vol.6
    • Ye, J.1    Sorrell, E.M.2    Cai, Y.3    Shao, H.4    Xu, K.5
  • 73
    • 78650037441 scopus 로고    scopus 로고
    • PB2 residue 158 is a pathogenic determinant of pandemic H1N1 and H5 influenza a viruses in mice
    • JVI.01694-10 [pii];10.1128/JVI.01694-10 [doi]
    • Zhou B, Li Y, Halpin R, Hine E, Spiro DJ, et al. (2011) PB2 residue 158 is a pathogenic determinant of pandemic H1N1 and H5 influenza a viruses in mice. J Virol 85: 357-365 JVI.01694-10 [pii];10.1128/JVI.01694-10 [doi].
    • (2011) J Virol , vol.85 , pp. 357-365
    • Zhou, B.1    Li, Y.2    Halpin, R.3    Hine, E.4    Spiro, D.J.5
  • 74
    • 77957197059 scopus 로고    scopus 로고
    • PB2 and HA Mutations are Major Determinants of Host Range and Virulence in Mouse-Adapted Influenza A Virus
    • JVI.01187-10 [pii];10.1128/JVI.01187-10 [doi]
    • Ping J, Dankar SK, Forbes NE, Keleta L, Zhou Y, et al. (2010) PB2 and HA Mutations are Major Determinants of Host Range and Virulence in Mouse-Adapted Influenza A Virus. J Virol JVI.01187-10 [pii];10.1128/JVI.01187-10 [doi].
    • (2010) J Virol
    • Ping, J.1    Dankar, S.K.2    Forbes, N.E.3    Keleta, L.4    Zhou, Y.5
  • 76
    • 33847624936 scopus 로고    scopus 로고
    • Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Boudet J, Guilligay D, Mas PJ, Bougault CM, et al. (2007) Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol 14: 229-233.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 229-233
    • Tarendeau, F.1    Boudet, J.2    Guilligay, D.3    Mas, P.J.4    Bougault, C.M.5
  • 77
    • 33746815630 scopus 로고    scopus 로고
    • Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding
    • Hara K, Schmidt FI, Crow M, Brownlee GG, (2006) Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J Virol 80: 7789-7798.
    • (2006) J Virol , vol.80 , pp. 7789-7798
    • Hara, K.1    Schmidt, F.I.2    Crow, M.3    Brownlee, G.G.4
  • 78
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs
    • Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM, (1998) Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol Cell 1: 991-1000.
    • (1998) Mol Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 79
    • 34548169547 scopus 로고    scopus 로고
    • Differential polymerase activity in avian and mammalian cells determines host range of influenza virus
    • JVI.00666-07 [pii];10.1128/JVI.00666-07 [doi]
    • Gabriel G, Abram M, Keiner B, Wagner R, Klenk HD, et al. (2007) Differential polymerase activity in avian and mammalian cells determines host range of influenza virus. J Virol 81: 9601-9604 JVI.00666-07 [pii];10.1128/JVI.00666-07 [doi].
    • (2007) J Virol , vol.81 , pp. 9601-9604
    • Gabriel, G.1    Abram, M.2    Keiner, B.3    Wagner, R.4    Klenk, H.D.5
  • 80
    • 40349113426 scopus 로고    scopus 로고
    • Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus
    • Gabriel G, Herwig A, Klenk HD, (2008) Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus. PLoS Pathog 4: e11.
    • (2008) PLoS Pathog , vol.4
    • Gabriel, G.1    Herwig, A.2    Klenk, H.D.3
  • 81
    • 34547110101 scopus 로고    scopus 로고
    • The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells
    • Twu KY, Kuo RL, Marklund J, Krug RM, (2007) The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells. J Virol 81: 8112-8121.
    • (2007) J Virol , vol.81 , pp. 8112-8121
    • Twu, K.Y.1    Kuo, R.L.2    Marklund, J.3    Krug, R.M.4
  • 82
    • 59649123636 scopus 로고    scopus 로고
    • Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells
    • Kuo RL, Krug RM, (2009) Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells. J Virol 83: 1611-1616.
    • (2009) J Virol , vol.83 , pp. 1611-1616
    • Kuo, R.L.1    Krug, R.M.2
  • 83
    • 34250810666 scopus 로고    scopus 로고
    • Multiple anti-interferon actions of the Influenza A virus NS1 protein
    • Kochs G, Garcia-Sastre A, Martinez-Sobrido L, (2007) Multiple anti-interferon actions of the Influenza A virus NS1 protein. J Virol.
    • (2007) J Virol
    • Kochs, G.1    Garcia-Sastre, A.2    Martinez-Sobrido, L.3
  • 84
    • 77953784997 scopus 로고    scopus 로고
    • Inefficient control of host gene expression by the 2009 pandemic H1N1 influenza A virus NS1 protein
    • JVI.00081-10 [pii];10.1128/JVI.00081-10 [doi]
    • Hale BG, Steel J, Medina RA, Manicassamy B, Ye J, et al. (2010) Inefficient control of host gene expression by the 2009 pandemic H1N1 influenza A virus NS1 protein. J Virol 84: 6909-6922 JVI.00081-10 [pii];10.1128/JVI.00081-10 [doi].
    • (2010) J Virol , vol.84 , pp. 6909-6922
    • Hale, B.G.1    Steel, J.2    Medina, R.A.3    Manicassamy, B.4    Ye, J.5
  • 85
    • 51349124912 scopus 로고    scopus 로고
    • Structural basis for suppression of a host antiviral response by influenza A virus
    • Das K, Ma LC, Xiao R, Radvansky B, Aramini J, et al. (2008) Structural basis for suppression of a host antiviral response by influenza A virus. Proc Natl Acad Sci U S A 105: 13093-13098.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13093-13098
    • Das, K.1    Ma, L.C.2    Xiao, R.3    Radvansky, B.4    Aramini, J.5
  • 86
    • 33749330704 scopus 로고    scopus 로고
    • Functional association between viral and cellular transcription during influenza virus infection
    • Engelhardt OG, Fodor E, (2006) Functional association between viral and cellular transcription during influenza virus infection. Rev Med Virol 16: 329-345.
    • (2006) Rev Med Virol , vol.16 , pp. 329-345
    • Engelhardt, O.G.1    Fodor, E.2
  • 87
    • 77957192535 scopus 로고    scopus 로고
    • Quantitative Proteomic Analyses of Influenza virus-Infected Cultured Human Lung Cells
    • JVI.00431-10 [pii];10.1128/JVI.00431-10 [doi]
    • Coombs KM, Berard A, Xu W, Krokhin O, Meng X, Cortens JP, et al. (2010) Quantitative Proteomic Analyses of Influenza virus-Infected Cultured Human Lung Cells. J Virol JVI.00431-10 [pii];10.1128/JVI.00431-10 [doi].
    • (2010) J Virol
    • Coombs, K.M.1    Berard, A.2    Xu, W.3    Krokhin, O.4    Meng, X.5    Cortens, J.P.6
  • 88
    • 0023341238 scopus 로고
    • The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies
    • Daniels PS, Jeffries S, Yates P, Schild GC, Rogers GN, et al. (1987) The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies. EMBO J 6: 1459-1465.
    • (1987) EMBO J , vol.6 , pp. 1459-1465
    • Daniels, P.S.1    Jeffries, S.2    Yates, P.3    Schild, G.C.4    Rogers, G.N.5
  • 89
    • 33746215109 scopus 로고    scopus 로고
    • Influenza virus receptor specificity and cell tropism in mouse and human airway epithelial cells
    • Ibricevic A, Pekosz A, Walter MJ, Newby C, Battaile JT, et al. (2006) Influenza virus receptor specificity and cell tropism in mouse and human airway epithelial cells. J Virol 80: 7469-7480.
    • (2006) J Virol , vol.80 , pp. 7469-7480
    • Ibricevic, A.1    Pekosz, A.2    Walter, M.J.3    Newby, C.4    Battaile, J.T.5
  • 90
    • 0021739837 scopus 로고
    • Biological properties of a hemagglutinin mutant of influenza virus selected by host cells
    • Crecelius DM, Deom CM, Schulze IT, (1984) Biological properties of a hemagglutinin mutant of influenza virus selected by host cells. Virology 139: 164-177.
    • (1984) Virology , vol.139 , pp. 164-177
    • Crecelius, D.M.1    Deom, C.M.2    Schulze, I.T.3
  • 91
    • 78650125730 scopus 로고    scopus 로고
    • The low-pH stability discovered in neuraminidase of 1918 pandemic influenza A virus enhances virus replication
    • 10.1371/journal.pone.0015556 [doi]
    • Takahashi T, Kurebayashi Y, Ikeya K, Mizuno T, Fukushima K, et al. (2010) The low-pH stability discovered in neuraminidase of 1918 pandemic influenza A virus enhances virus replication. PLoS One 5: e15556 10.1371/journal.pone.0015556 [doi].
    • (2010) PLoS One , vol.5
    • Takahashi, T.1    Kurebayashi, Y.2    Ikeya, K.3    Mizuno, T.4    Fukushima, K.5
  • 92
    • 1642491743 scopus 로고    scopus 로고
    • Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity
    • S0014579303015035 [pii]
    • Suzuki T, Takahashi T, Saito T, Guo CT, Hidari KI, et al. (2004) Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity. FEBS Lett 557: 228-232 S0014579303015035 [pii].
    • (2004) FEBS Lett , vol.557 , pp. 228-232
    • Suzuki, T.1    Takahashi, T.2    Saito, T.3    Guo, C.T.4    Hidari, K.I.5
  • 93
    • 0038393119 scopus 로고    scopus 로고
    • A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases
    • S0014579303004034 [pii]
    • Takahashi T, Suzuki T, Hidari KI, Miyamoto D, Suzuki Y, (2003) A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases. FEBS Lett 543: 71-75 S0014579303004034 [pii].
    • (2003) FEBS Lett , vol.543 , pp. 71-75
    • Takahashi, T.1    Suzuki, T.2    Hidari, K.I.3    Miyamoto, D.4    Suzuki, Y.5
  • 94
    • 0034867326 scopus 로고    scopus 로고
    • Duck and human pandemic influenza A viruses retain sialidase activity under low pH conditions
    • Takahashi T, Suzuki Y, Nishinaka D, Kawase N, Kobayashi Y, et al. (2001) Duck and human pandemic influenza A viruses retain sialidase activity under low pH conditions. J Biochem 130: 279-283.
    • (2001) J Biochem , vol.130 , pp. 279-283
    • Takahashi, T.1    Suzuki, Y.2    Nishinaka, D.3    Kawase, N.4    Kobayashi, Y.5
  • 95
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • nature06531 [pii];10.1038/nature06531 [doi]
    • Schnell JR, Chou JJ, (2008) Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451: 591-595 nature06531 [pii];10.1038/nature06531 [doi].
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 96
    • 66149112971 scopus 로고    scopus 로고
    • Mechanism of drug inhibition and drug resistance of influenza A M2 channel
    • 0902548106 [pii];10.1073/pnas.0902548106 [doi]
    • Pielak RM, Schnell JR, Chou JJ, (2009) Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Proc Natl Acad Sci U S A 106: 7379-7384 0902548106 [pii];10.1073/pnas.0902548106 [doi].
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7379-7384
    • Pielak, R.M.1    Schnell, J.R.2    Chou, J.J.3
  • 97
    • 0026343370 scopus 로고
    • Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles
    • Steinhauer DA, Wharton SA, Skehel JJ, Wiley DC, Hay AJ, (1991) Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles. Proc Natl Acad Sci U S A 88: 11525-11529.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 11525-11529
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Hay, A.J.5
  • 99
    • 24644484686 scopus 로고    scopus 로고
    • Molecular basis of replication of duck H5N1 influenza viruses in a mammalian mouse model
    • Li Z, Chen H, Jiao P, Deng G, Tian G, et al. (2005) Molecular basis of replication of duck H5N1 influenza viruses in a mammalian mouse model. J Virol 79: 12058-12064.
    • (2005) J Virol , vol.79 , pp. 12058-12064
    • Li, Z.1    Chen, H.2    Jiao, P.3    Deng, G.4    Tian, G.5
  • 100
    • 65349192767 scopus 로고    scopus 로고
    • Selection of H5N1 influenza virus PB2 during replication in humans
    • JVI.00063-09 [pii];10.1128/JVI.00063-09 [doi]
    • Le QM, Sakai-Tagawa Y, Ozawa M, Ito M, Kawaoka Y, (2009) Selection of H5N1 influenza virus PB2 during replication in humans. J Virol 83: 5278-5281 JVI.00063-09 [pii];10.1128/JVI.00063-09 [doi].
    • (2009) J Virol , vol.83 , pp. 5278-5281
    • Le, Q.M.1    Sakai-Tagawa, Y.2    Ozawa, M.3    Ito, M.4    Kawaoka, Y.5
  • 101
    • 0037334413 scopus 로고    scopus 로고
    • Neurovirulence in mice of H5N1 influenza virus genotypes isolated from Hong Kong poultry in 2001
    • Lipatov AS, Krauss S, Guan Y, Peiris M, Rehg JE, et al. (2003) Neurovirulence in mice of H5N1 influenza virus genotypes isolated from Hong Kong poultry in 2001. J Virol 77: 3816-3823.
    • (2003) J Virol , vol.77 , pp. 3816-3823
    • Lipatov, A.S.1    Krauss, S.2    Guan, Y.3    Peiris, M.4    Rehg, J.E.5
  • 102
    • 34249694755 scopus 로고    scopus 로고
    • Pneumo- and neurotropism of avian origin Italian highly pathogenic avian influenza H7N1 isolates in experimentally infected mice
    • Rigoni M, Shinya K, Toffan A, Milani A, Bettini F, et al. (2007) Pneumo- and neurotropism of avian origin Italian highly pathogenic avian influenza H7N1 isolates in experimentally infected mice. Virology %20;364: 28-35.
    • (2007) Virology %20 , vol.364 , pp. 28-35
    • Rigoni, M.1    Shinya, K.2    Toffan, A.3    Milani, A.4    Bettini, F.5
  • 103
    • 2942655386 scopus 로고    scopus 로고
    • A computer program for Spearman-Karber and probit analysis of psychometric function data
    • Miller J, Ulrich R, (2004) A computer program for Spearman-Karber and probit analysis of psychometric function data. Behav Res Methods Instrum Comput 36: 11-16.
    • (2004) Behav Res Methods Instrum Comput , vol.36 , pp. 11-16
    • Miller, J.1    Ulrich, R.2
  • 104
    • 0022477122 scopus 로고
    • Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1
    • Parvin JD, Moscona A, Pan WT, Leider JM, Palese P, (1986) Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1. J Virol 59: 377-383.
    • (1986) J Virol , vol.59 , pp. 377-383
    • Parvin, J.D.1    Moscona, A.2    Pan, W.T.3    Leider, J.M.4    Palese, P.5
  • 105
    • 77954213124 scopus 로고    scopus 로고
    • Improved and simplified recombineering approach for influenza virus reverse genetics
    • Liu Q, Wang S, Ma G, Pu J, Forbes NE, et al. (2009) Improved and simplified recombineering approach for influenza virus reverse genetics. J Mol Genet Med 3: 225-231.
    • (2009) J Mol Genet Med , vol.3 , pp. 225-231
    • Liu, Q.1    Wang, S.2    Ma, G.3    Pu, J.4    Forbes, N.E.5
  • 106
    • 70349272201 scopus 로고    scopus 로고
    • Single-reaction genomic amplification accelerates sequencing and vaccine production for classical and Swine origin human influenza a viruses
    • JVI.01109-09 [pii];10.1128/JVI.01109-09 [doi]
    • Zhou B, Donnelly ME, Scholes DT, St GK, Hatta M, et al. (2009) Single-reaction genomic amplification accelerates sequencing and vaccine production for classical and Swine origin human influenza a viruses. J Virol 83: 10309-10313 JVI.01109-09 [pii];10.1128/JVI.01109-09 [doi].
    • (2009) J Virol , vol.83 , pp. 10309-10313
    • Zhou, B.1    Donnelly, M.E.2    Scholes, D.T.3    St, G.K.4    Hatta, M.5
  • 107
    • 27144474904 scopus 로고    scopus 로고
    • Large-scale sequencing of human influenza reveals the dynamic nature of viral genome evolution
    • Ghedin E, Sengamalay NA, Shumway M, Zaborsky J, Feldblyum T, et al. (2005) Large-scale sequencing of human influenza reveals the dynamic nature of viral genome evolution. Nature 437: 1162-1166.
    • (2005) Nature , vol.437 , pp. 1162-1166
    • Ghedin, E.1    Sengamalay, N.A.2    Shumway, M.3    Zaborsky, J.4    Feldblyum, T.5
  • 109
    • 56449104723 scopus 로고    scopus 로고
    • Compatibility among polymerase subunit proteins is a restricting factor in reassortment between equine H7N7 and human H3N2 influenza viruses
    • Li C, Hatta M, Watanabe S, Neumann G, Kawaoka Y, (2008) Compatibility among polymerase subunit proteins is a restricting factor in reassortment between equine H7N7 and human H3N2 influenza viruses. J Virol 82: 11880-11888.
    • (2008) J Virol , vol.82 , pp. 11880-11888
    • Li, C.1    Hatta, M.2    Watanabe, S.3    Neumann, G.4    Kawaoka, Y.5
  • 110
    • 0032884864 scopus 로고    scopus 로고
    • Interaction of influenza virus polymerase with viral RNA in the 'corkscrew' conformation
    • Flick R, Hobom G, (1999) Interaction of influenza virus polymerase with viral RNA in the 'corkscrew' conformation. J Gen Virol 80: 2565-2572.
    • (1999) J Gen Virol , vol.80 , pp. 2565-2572
    • Flick, R.1    Hobom, G.2
  • 111
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC, (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69: 531-69.531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 112
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus
    • Stevens J, Corper AL, Basler CF, Taubenberger JK, Palese P, et al. (2004) Structure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus. Science.
    • (2004) Science
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5
  • 113
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • Varghese JN, Laver WG, Colman PM, (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303: 35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 114
    • 0024452967 scopus 로고
    • Structural domains and organizational conformation involved in the sorting and transport of influenza virus transmembrane proteins
    • 10.1146/annurev.mi.43.100189.002341 [doi]
    • Nayak DP, Jabbar MA, (1989) Structural domains and organizational conformation involved in the sorting and transport of influenza virus transmembrane proteins. Annu Rev Microbiol 43: 465-501 10.1146/annurev.mi.43.100189.002341 [doi].
    • (1989) Annu Rev Microbiol , vol.43 , pp. 465-501
    • Nayak, D.P.1    Jabbar, M.A.2
  • 115
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • 10.1006/viro.2000.0804 [doi];S0042-6822(00)90804-3 [pii]
    • Baudin F, Petit I, Weissenhorn W, Ruigrok RW, (2001) In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281: 102-108 10.1006/viro.2000.0804 [doi];S0042-6822(00)90804-3 [pii].
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 116
    • 0028835724 scopus 로고
    • Nucleus-targeting domain of the matrix protein (M1) of influenza virus
    • Ye Z, Robinson D, Wagner RR, (1995) Nucleus-targeting domain of the matrix protein (M1) of influenza virus. J Virol 69: 1964-1970.
    • (1995) J Virol , vol.69 , pp. 1964-1970
    • Ye, Z.1    Robinson, D.2    Wagner, R.R.3
  • 117
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye Z, Liu T, Offringa DP, McInnis J, Levandowski RA, (1999) Association of influenza virus matrix protein with ribonucleoproteins. J Virol 73: 7467-7473.
    • (1999) J Virol , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5
  • 118
    • 0023106182 scopus 로고
    • Functional and antigenic domains of the matrix (M1) protein of influenza A virus
    • Ye ZP, Pal R, Fox JW, Wagner RR, (1987) Functional and antigenic domains of the matrix (M1) protein of influenza A virus. J Virol 61: 239-246.
    • (1987) J Virol , vol.61 , pp. 239-246
    • Ye, Z.P.1    Pal, R.2    Fox, J.W.3    Wagner, R.R.4
  • 119
    • 0024319381 scopus 로고
    • Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides
    • Ye ZP, Baylor NW, Wagner RR, (1989) Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides. J Virol 63: 3586-3594.
    • (1989) J Virol , vol.63 , pp. 3586-3594
    • Ye, Z.P.1    Baylor, N.W.2    Wagner, R.R.3
  • 120
    • 0021893484 scopus 로고
    • Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface
    • 0092-8674(85)90211-9 [pii]
    • Lamb RA, Zebedee SL, Richardson CD, (1985) Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface. Cell 40: 627-633 0092-8674(85)90211-9 [pii].
    • (1985) Cell , vol.40 , pp. 627-633
    • Lamb, R.A.1    Zebedee, S.L.2    Richardson, C.D.3
  • 121
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • 10.1093/emboj/17.1.288 [doi]
    • O'Neill RE, Talon J, Palese P, (1998) The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J 17: 288-296 10.1093/emboj/17.1.288 [doi].
    • (1998) EMBO J , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 122
    • 25444436686 scopus 로고    scopus 로고
    • The Molecular Biology Toolkit (MBT): a modular platform for developing molecular visualization applications
    • Moreland JL, Gramada A, Buzko OV, Zhang Q, Bourne PE, (2005) The Molecular Biology Toolkit (MBT): a modular platform for developing molecular visualization applications. BMC Bioinformatics 6: 21.:21.
    • (2005) BMC Bioinformatics , vol.6 , pp. 21
    • Moreland, J.L.1    Gramada, A.2    Buzko, O.V.3    Zhang, Q.4    Bourne, P.E.5
  • 123
    • 19944431013 scopus 로고    scopus 로고
    • Immunoglobulin mimicry by Hepatitis C Virus envelope protein E2
    • Hu YW, Rocheleau L, Larke B, Chui L, Lee B, et al. (2005) Immunoglobulin mimicry by Hepatitis C Virus envelope protein E2. Virology %20;332: 538-549.
    • (2005) Virology %20 , vol.332 , pp. 538-549
    • Hu, Y.W.1    Rocheleau, L.2    Larke, B.3    Chui, L.4    Lee, B.5
  • 124
    • 0034892686 scopus 로고    scopus 로고
    • PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators
    • Huarte M, Sanz-Ezquerro JJ, Roncal F, Ortin J, Nieto A, (2001) PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators. J Virol 75: 8597-8604.
    • (2001) J Virol , vol.75 , pp. 8597-8604
    • Huarte, M.1    Sanz-Ezquerro, J.J.2    Roncal, F.3    Ortin, J.4    Nieto, A.5
  • 125
    • 50649122962 scopus 로고    scopus 로고
    • The structural basis for an essential subunit interaction in influenza virus RNA polymerase
    • Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, et al. (2008) The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 454: 1127-1131.
    • (2008) Nature , vol.454 , pp. 1127-1131
    • Obayashi, E.1    Yoshida, H.2    Kawai, F.3    Shibayama, N.4    Kawaguchi, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.