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Volumn 14, Issue 6, 2010, Pages 435-445

Advances in the structural study and molecular comprehension of the transcription mechanism of influenza virus;Avancées dans l'étude structurale et la compréhension moléculaire du mécanisme de transcription du virus de la grippe

Author keywords

Cap; Flu; Replication; RNA polymerase; Structure; Transcription

Indexed keywords

CAP BINDING PROTEIN; ENDONUCLEASE; MESSENGER RNA; RIBONUCLEOPROTEIN; RNA POLYMERASE; VIRUS RNA;

EID: 78650729609     PISSN: 12678694     EISSN: 19506961     Source Type: Journal    
DOI: 10.1684/vir.2010.0328     Document Type: Review
Times cited : (2)

References (60)
  • 1
    • 77749322610 scopus 로고    scopus 로고
    • Towards an atomic resolution understanding of the influenza virus replication machinery
    • Ruigrok RW, Crepin T, Hart DJ, Cusack S. Towards an atomic resolution understanding of the influenza virus replication machinery. Curr Opin Struct Biol 2010 ; 20 : 104-13.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 104-113
    • Ruigrok, R.W.1    Crepin, T.2    Hart, D.J.3    Cusack, S.4
  • 3
    • 33644841402 scopus 로고    scopus 로고
    • Influenza virus virulence and its molecular determinants
    • Noah DL, Krug RM. Influenza virus virulence and its molecular determinants. Adv Virus Res 2005 ; 65 : 121-45.
    • (2005) Adv Virus Res , vol.65 , pp. 121-145
    • Noah, D.L.1    Krug, R.M.2
  • 4
    • 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, Stech J. The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host. Proc Natl Acad Sci U S A 2005 ; 102 : 18590-5.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18590-18595
    • Gabriel, G.1    Dauber, B.2    Wolff, T.3    Planz, O.4    Klenk, H.D.5    Stech, J.6
  • 5
    • 53849125470 scopus 로고    scopus 로고
    • Host restriction of avian influenza viruses at the level of the ribonucleoproteins
    • Naffakh N, Tomoiu A, Rameix-Welti MA, van der Werf S. Host restriction of avian influenza viruses at the level of the ribonucleoproteins. Annu Rev Microbiol 2008 ; 62 : 403-4.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 403-404
    • Naffakh, N.1    Tomoiu, A.2    Rameix-Welti, M.A.3    Van Der Werf, S.4
  • 6
    • 70450211764 scopus 로고    scopus 로고
    • Potential targets and their relevant inhibitors in anti-influenza fields
    • Gong J, Fang H, Li M, Liu Y, Yang K, Xu W. Potential targets and their relevant inhibitors in anti-influenza fields. Curr Med Chem 2009 ; 16 : 3716-39.
    • (2009) Curr Med Chem , vol.16 , pp. 3716-3739
    • Gong, J.1    Fang, H.2    Li, M.3    Liu, Y.4    Yang, K.5    Xu, W.6
  • 7
    • 68649122631 scopus 로고    scopus 로고
    • Emerging antiviral targets for influenza Avirus
    • Krug RM, Aramini JM. Emerging antiviral targets for influenza Avirus. Trends Pharmacol Sci 2009 ; 30 : 269-77.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 269-277
    • Krug, R.M.1    Aramini, J.M.2
  • 8
    • 67249108203 scopus 로고    scopus 로고
    • Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication
    • Jorba N, Coloma R, Ortin J. Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication. PLoS Pathog 2009 ; 5 : e1000462.
    • (2009) PLoS Pathog , vol.5
    • Jorba, N.1    Coloma, R.2    Ortin, J.3
  • 9
    • 0019394947 scopus 로고
    • A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM. A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 1981 ; 23 : 847-58.
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 10
    • 0027438772 scopus 로고
    • Non-viral sequences at the 5′ ends of Dugbe nairovirus S mRNAs
    • Jin H, Elliott RM. Non-viral sequences at the 5′ ends of Dugbe nairovirus S mRNAs. J Gen Virol 1993 ; 74 (Pt 10) : 2293-7.
    • (1993) J Gen Virol , vol.74 , Issue.PART 10 , pp. 2293-2297
    • Jin, H.1    Elliott, R.M.2
  • 11
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M, Tordo N. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. Embo J 1989 ; 8 : 3867-74.
    • (1989) Embo J , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 12
    • 0028118520 scopus 로고
    • Mutational analysis of the conserved motifs of influenza Avirus polymerase basic protein 1
    • Biswas SK, Nayak DP. Mutational analysis of the conserved motifs of influenza Avirus polymerase basic protein 1. J Virol 1994 ; 68 : 1819-26.
    • (1994) J Virol , vol.68 , pp. 1819-1826
    • Biswas, S.K.1    Nayak, D.P.2
  • 13
    • 0035901509 scopus 로고    scopus 로고
    • The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
    • Li ML, Rao P, Krug RM. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. Embo J 2001 ; 20 : 2078-86.
    • (2001) Embo J , vol.20 , pp. 2078-2086
    • Li, M.L.1    Rao, P.2    Krug, R.M.3
  • 14
    • 43249128376 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay D, Tarendeau F, Resa-Infante P, et al. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nat Struct Mol Biol 2008 ; 15 : 500-6.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 500-506
    • Guilligay, D.1    Tarendeau, F.2    Resa-Infante, P.3
  • 15
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias A, Bouvier D, Crepin T, et al. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 2009 ; 458 : 914-8.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crepin, T.3
  • 16
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, Bartlam M, Lou Z, et al. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 2009 ; 458 : 909-13.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1    Bartlam, M.2    Lou, Z.3
  • 18
    • 0031003878 scopus 로고    scopus 로고
    • Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure
    • Klumpp K, Ruigrok RW, Baudin F. Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure. Embo J 1997 ; 16 : 1248-57.
    • (1997) Embo J , vol.16 , pp. 1248-1257
    • Klumpp, K.1    Ruigrok, R.W.2    Baudin, F.3
  • 19
    • 0035033091 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle
    • Martin-Benito J, Area E, Ortega J, et al. Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle. EMBO Rep 2001 ; 2 : 313-7.
    • (2001) EMBO Rep , vol.2 , pp. 313-317
    • Martin-Benito, J.1    Area, E.2    Ortega, J.3
  • 20
    • 0347719363 scopus 로고    scopus 로고
    • 3D structure of the influenza virus polymerase complex: Localization of subunit domains
    • Area E, Martin-Benito J, Gastaminza P, et al. 3D structure of the influenza virus polymerase complex: localization of subunit domains. Proc Natl Acad Sci U S A 2004 ; 101 : 308-13.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 308-313
    • Area, E.1    Martin-Benito, J.2    Gastaminza, P.3
  • 22
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega J, Martin-Benito J, Zurcher T, Valpuesta JM, Carrascosa JL, Ortin J. Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J Virol 2000 ; 74 : 156-63.
    • (2000) J Virol , vol.74 , pp. 156-163
    • Ortega, J.1    Martin-Benito, J.2    Zurcher, T.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Ortin, J.6
  • 23
    • 58149402434 scopus 로고    scopus 로고
    • Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication
    • Newcomb LL, Kuo RL, Ye Q, Jiang Y, Tao YJ, Krug RM. Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication. J Virol 2009 ; 83 : 29-36.
    • (2009) J Virol , vol.83 , pp. 29-36
    • Newcomb, L.L.1    Kuo, R.L.2    Ye, Q.3    Jiang, Y.4    Tao, Y.J.5    Krug, R.M.6
  • 24
    • 34547137695 scopus 로고    scopus 로고
    • Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
    • Torreira E, Schoehn G, Fernandez Y, et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Res 2007 ; 35 : 3774-83.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3774-3783
    • Torreira, E.1    Schoehn, G.2    Fernandez, Y.3
  • 25
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza Avirus nucleoprotein forms oligomers and binds RNA
    • Ye Q, Krug RM, Tao YJ. The mechanism by which influenza Avirus nucleoprotein forms oligomers and binds RNA. Nature 2006 ; 444 : 1078-82.
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 26
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design
    • Ng AK, Zhang H, Tan K, et al. Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design. Faseb J 2008 ; 22 : 3638-47.
    • (2008) Faseb J , vol.22 , pp. 3638-3647
    • Ng, A.K.1    Zhang, H.2    Tan, K.3
  • 27
    • 33746558802 scopus 로고    scopus 로고
    • Crystal structure of the rabies virus nucleoprotein-RNA complex
    • Albertini AA, Wernimont AK, Muziol T, et al. Crystal structure of the rabies virus nucleoprotein-RNA complex. Science 2006 ; 313 : 360-3.
    • (2006) Science , vol.313 , pp. 360-363
    • Albertini, A.A.1    Wernimont, A.K.2    Muziol, T.3
  • 28
    • 70849108252 scopus 로고    scopus 로고
    • Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus
    • Tawar RG, Duquerroy S, Vonrhein C, et al. Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus. Science 2009 ; 326 : 1279-83.
    • (2009) Science , vol.326 , pp. 1279-1283
    • Tawar, R.G.1    Duquerroy, S.2    Vonrhein, C.3
  • 30
    • 78650737672 scopus 로고    scopus 로고
    • Nucleoproteins of negative strand RNA viruses; RNA binding, oligomerisation and binding to polymerase co-factor
    • Ruigrok RW, Crepin T. Nucleoproteins of negative strand RNA viruses; RNA binding, oligomerisation and binding to polymerase co-factor. Viruses 2010 ; 2 : 27-32.
    • (2010) Viruses , vol.2 , pp. 27-32
    • Ruigrok, R.W.1    Crepin, T.2
  • 31
    • 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. 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 2006 ; 80 : 7789-98.
    • (2006) J Virol , vol.80 , pp. 7789-7798
    • Hara, K.1    Schmidt, F.I.2    Crow, M.3    Brownlee, G.G.4
  • 32
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus
    • He X, Zhou J, Bartlam M, et al. Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 2008 ; 454 : 1123-6.
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1    Zhou, J.2    Bartlam, M.3
  • 33
    • 50649122962 scopus 로고    scopus 로고
    • The structural basis for an essential subunit interaction in influenza virus RNA polymerase
    • Obayashi E, Yoshida H, Kawai F, et al. The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 2008 ; 454 : 1127-31.
    • (2008) Nature , vol.454 , pp. 1127-1131
    • Obayashi, E.1    Yoshida, H.2    Kawai, F.3
  • 34
    • 34447263302 scopus 로고    scopus 로고
    • Peptide-mediated interference with influenza A virus polymerase
    • Ghanem A, Mayer D, Chase G, et al. Peptide-mediated interference with influenza A virus polymerase. J Virol 2007 ; 81 : 7801-4.
    • (2007) J Virol , vol.81 , pp. 7801-7804
    • Ghanem, A.1    Mayer, D.2    Chase, G.3
  • 35
    • 70449571952 scopus 로고    scopus 로고
    • Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication
    • Wunderlich K, Mayer D, Ranadheera C, et al. Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication. PLoS One 2009 ; 4 : e7517.
    • (2009) PLoS One , vol.4
    • Wunderlich, K.1    Mayer, D.2    Ranadheera, C.3
  • 36
    • 0033608967 scopus 로고    scopus 로고
    • Metal ion catalysis of RNA cleavage by the influenza virus endonuclease
    • Doan L, Handa B, Roberts NA, Klumpp K. Metal ion catalysis of RNA cleavage by the influenza virus endonuclease. Biochemistry 1999 ; 38 : 5612-9.
    • (1999) Biochemistry , vol.38 , pp. 5612-5619
    • Doan, L.1    Handa, B.2    Roberts, N.A.3    Klumpp, K.4
  • 37
    • 77956030336 scopus 로고    scopus 로고
    • Mutational and metal binding analysis of the endonuclease domain of the influenza virus polymerase PA subunit
    • Crepin T, Dias A, Palencia A, Swale C, Cusack S, Ruigrok RW. Mutational and metal binding analysis of the endonuclease domain of the influenza virus polymerase PA subunit. J Virol 2010 ; 84 : 9096-104.
    • (2010) J Virol , vol.84 , pp. 9096-9104
    • Crepin, T.1    Dias, A.2    Palencia, A.3    Swale, C.4    Cusack, S.5    Ruigrok, R.W.6
  • 38
    • 0028171260 scopus 로고
    • Inhibition of cap (m7GpppXm)-dependent endonuclease of influenza virus by 4-substituted 2,4-dioxobutanoic acid compounds
    • Tomassini J, Selnick H, Davies ME, et al. Inhibition of cap (m7GpppXm)-dependent endonuclease of influenza virus by 4-substituted 2,4-dioxobutanoic acid compounds. Antimicrob Agents Chemother 1994 ; 38 : 2827-37.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2827-2837
    • Tomassini, J.1    Selnick, H.2    Davies, M.E.3
  • 39
    • 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, et al. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol 2007 ; 14 : 229-33.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 229-233
    • Tarendeau, F.1    Boudet, J.2    Guilligay, D.3
  • 40
    • 58449090154 scopus 로고    scopus 로고
    • Expression of Helicobacter pylori CagA domains by library-based construct screening
    • Angelini A, Tosi T, Mas P, et al. Expression of Helicobacter pylori CagA domains by library-based construct screening. Febs J 2009 ; 276 : 816-24.
    • (2009) Febs J , vol.276 , pp. 816-824
    • Angelini, A.1    Tosi, T.2    Mas, P.3
  • 41
    • 50849137828 scopus 로고    scopus 로고
    • Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Crepin T, Guilligay D, Ruigrok RW, Cusack S, Hart DJ. Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit. PLoS Pathog 2008 ; 4 : e1000136.
    • (2008) PLoS Pathog , vol.4
    • Tarendeau, F.1    Crepin, T.2    Guilligay, D.3    Ruigrok, R.W.4    Cusack, S.5    Hart, D.J.6
  • 42
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 1997 ; 89 : 951-61.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 43
    • 0037107401 scopus 로고    scopus 로고
    • Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex
    • Mazza C, Segref A, Mattaj IW, Cusack S. Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. Embo J 2002 ; 21 : 5548-57.
    • (2002) Embo J , vol.21 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 44
    • 65449163086 scopus 로고    scopus 로고
    • Structural basis of the influenza Avirus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue
    • Kuzuhara T, Kise D, Yoshida H, et al. Structural basis of the influenza Avirus RNA polymerase PB2 RNA-binding domain containing the pathogenicity- determinant lysine 627 residue. J Biol Chem 2009 ; 284 : 6855-60.
    • (2009) J Biol Chem , vol.284 , pp. 6855-6860
    • Kuzuhara, T.1    Kise, D.2    Yoshida, H.3
  • 45
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama K, Obayashi E, Kawaguchi A, et al. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. Embo J 2009 ; 28 : 1803-11.
    • (2009) Embo J , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3
  • 46
    • 0028176691 scopus 로고
    • Rift Valley fever virus L segment: Correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases
    • Muller R, Poch O, Delarue M, Bishop DH, Bouloy M. Rift Valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases. J Gen Virol 1994 ; 75 (Pt 6) : 1345-52.
    • (1994) J Gen Virol , vol.75 , Issue.PART 6 , pp. 1345-1352
    • Muller, R.1    Poch, O.2    Delarue, M.3    Bishop, D.H.4    Bouloy, M.5
  • 47
    • 40649100793 scopus 로고    scopus 로고
    • Structure-function relationships among RNA-dependent RNA polymerases
    • Ng KK, Arnold JJ, Cameron CE. Structure-function relationships among RNA-dependent RNA polymerases. Curr Top Microbiol Immunol 2008 ; 320 : 137-56.
    • (2008) Curr Top Microbiol Immunol , vol.320 , pp. 137-156
    • Ng, K.K.1    Arnold, J.J.2    Cameron, C.E.3
  • 49
    • 70449527786 scopus 로고    scopus 로고
    • Using non-homogeneous models of nucleotide substitution to identify host shift events: Application to the origin of the 1918 "Spanish" influenza pandemic virus
    • dos Reis M, Hay AJ, Goldstein RA. Using non-homogeneous models of nucleotide substitution to identify host shift events: application to the origin of the 1918 "Spanish" influenza pandemic virus. J Mol Evol 2009 ; 69 : 333-45.
    • (2009) J Mol Evol , vol.69 , pp. 333-345
    • Dos Reis, M.1    Hay, A.J.2    Goldstein, R.A.3
  • 50
    • 44649108325 scopus 로고    scopus 로고
    • Analysis of the interaction of influenza virus polymerase complex with human cell factors
    • Jorba N, Juarez S, Torreira E, et al. Analysis of the interaction of influenza virus polymerase complex with human cell factors. Proteomics 2008 ; 8 : 2077-88.
    • (2008) Proteomics , vol.8 , pp. 2077-2088
    • Jorba, N.1    Juarez, S.2    Torreira, E.3
  • 51
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe T, Watanabe S, Kawaoka Y. Cellular networks involved in the influenza virus life cycle. Cell Host Microbe 2010 ; 7 : 427-39.
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 52
  • 53
    • 77949348063 scopus 로고    scopus 로고
    • Complete-proteome mapping of human influenza A adaptive mutations: Implications for human transmissibility of zoonotic strains
    • Miotto O, Heiny AT, Albrecht R, et al. Complete-proteome mapping of human influenza A adaptive mutations: implications for human transmissibility of zoonotic strains. PLoS One 2010 ; 5 : e9025.
    • (2010) PLoS One , vol.5
    • Miotto, O.1    Heiny, A.T.2    Albrecht, R.3
  • 54
    • 33749020042 scopus 로고    scopus 로고
    • Genomic signatures of human versus avian influenza Aviruses
    • Chen GW, Chang SC, Mok CK, et al. Genomic signatures of human versus avian influenza Aviruses. Emerg Infect Dis 2006 ; 12 : 1353-60.
    • (2006) Emerg Infect Dis , vol.12 , pp. 1353-1360
    • Chen, G.W.1    Chang, S.C.2    Mok, C.K.3
  • 55
    • 75849136881 scopus 로고    scopus 로고
    • Adaptive strategies of the influenza virus polymerase for replication in humans
    • Mehle A, Doudna JA. Adaptive strategies of the influenza virus polymerase for replication in humans. Proc Natl Acad Sci U S A 2009 ; 106 : 21312-6.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21312-21316
    • Mehle, A.1    Doudna, J.A.2
  • 56
    • 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, et al. Molecular basis of replication of duck H5N1 influenza viruses in a mammalian mouse model. J Virol 2005 ; 79 : 12058-64.
    • (2005) J Virol , vol.79 , pp. 12058-12064
    • Li, Z.1    Chen, H.2    Jiao, P.3    Deng, G.4
  • 57
    • 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. Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus. PLoS Pathog 2008 ; 4 : e11.
    • (2008) PLoS Pathog , vol.4
    • Gabriel, G.1    Herwig, A.2    Klenk, H.D.3
  • 58
    • 57549086823 scopus 로고    scopus 로고
    • The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication
    • Resa-Infante P, Jorba N, Zamarreno N, Fernandez Y, Juarez S, Ortin J. The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication. PLoS One 2008 ; 3 : e3904.
    • (2008) PLoS One , vol.3
    • Resa-Infante, P.1    Jorba, N.2    Zamarreno, N.3    Fernandez, Y.4    Juarez, S.5    Ortin, J.6
  • 59
    • 0344453794 scopus 로고    scopus 로고
    • Use of a pharmacophore model to discover a new class of influenza endonuclease inhibitors
    • Parkes KE, Ermert P, Fassler J, et al. Use of a pharmacophore model to discover a new class of influenza endonuclease inhibitors. J Med Chem 2003 ; 46 : 1153-64.
    • (2003) J Med Chem , vol.46 , pp. 1153-1164
    • Parkes, K.E.1    Ermert, P.2    Fassler, J.3
  • 60
    • 64749093901 scopus 로고    scopus 로고
    • T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections
    • Furuta Y, Takahashi K, Shiraki K, et al. T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections. Antiviral Res 2009 ; 82 : 95-102.
    • (2009) Antiviral Res , vol.82 , pp. 95-102
    • Furuta, Y.1    Takahashi, K.2    Shiraki, K.3


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