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Volumn 56, Issue 2, 2012, Pages 647-657

Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus

Author keywords

[No Author keywords available]

Indexed keywords

4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; 6 BROMO 2 [1 (2,5 DIMETHYLPHENYL) 5 METHYL 1H PYRAZOL 4 YL] QUINOLINE 4 CARBOXYLIC ACID; AMANTADINE; ANTIVIRUS AGENT; BPR 3P0128; COMPLEMENTARY RNA; MESSENGER RNA; PRIMER RNA; RIBONUCLEASE; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 84862908885     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00125-11     Document Type: Article
Times cited : (48)

References (63)
  • 2
    • 0031778876 scopus 로고    scopus 로고
    • Influenza virus nucleoprotein interacts with influenza virus polymerase proteins
    • Biswas SK, Boutz PL, Nayak DP. 1998. Influenza virus nucleoprotein interacts with influenza virus polymerase proteins. J. Virol. 72:5493-5501. (Pubitemid 28283331)
    • (1998) Journal of Virology , vol.72 , Issue.7 , pp. 5493-5501
    • Biswas, S.K.1    Boutz, P.L.2    Nayak, D.P.3
  • 3
    • 0020480480 scopus 로고
    • Identification of the cap binding protein of influenza virus
    • Blaas D, Patzelt E, Kuechler E. 1982. Identification of the cap binding protein of influenza virus. Nucleic Acids Res. 10:4803-4812.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 4803-4812
    • Blaas, D.1    Patzelt, E.2    Kuechler, E.3
  • 4
    • 33846822057 scopus 로고    scopus 로고
    • Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes
    • DOI 10.1016/j.virusres.2006.09.013, PII S0168170206002966
    • Boulo S, Akarsu H, Ruigrok RW, Baudin F. 2007. Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res. 124:12-21. (Pubitemid 46216557)
    • (2007) Virus Research , vol.124 , Issue.1-2 , pp. 12-21
    • Boulo, S.1    Akarsu, H.2    Ruigrok, R.W.H.3    Baudin, F.4
  • 5
    • 44949237145 scopus 로고    scopus 로고
    • Hsp90 inhibitors reduce influenza virus replication in cell culture
    • DOI 10.1016/j.virol.2008.04.040, PII S0042682208002973
    • Chase G, et al. 2008. Hsp90 inhibitors reduce influenza virus replication in cell culture. Virology 377:431-439. (Pubitemid 351822379)
    • (2008) Virology , vol.377 , Issue.2 , pp. 431-439
    • Chase, G.1    Deng, T.2    Fodor, E.3    Leung, B.W.4    Mayer, D.5    Schwemmle, M.6    Brownlee, G.7
  • 6
    • 0029048936 scopus 로고
    • Differential activation of the influenza virus polymerase via template RNA binding
    • Cianci C, Tiley L, Krystal M. 1995. Differential activation of the influenza virus polymerase via template RNA binding. J. Virol. 69:3995-3999.
    • (1995) J. Virol. , vol.69 , pp. 3995-3999
    • Cianci, C.1    Tiley, L.2    Krystal, M.3
  • 8
    • 78751484574 scopus 로고    scopus 로고
    • Comparative RNAi screening reveals host factors involved in enterovirus infection of polarized endothelial monolayers
    • Coyne CB, et al. 2011. Comparative RNAi screening reveals host factors involved in enterovirus infection of polarized endothelial monolayers. Cell Host Microbe 9:70-82.
    • (2011) Cell Host Microbe , vol.9 , pp. 70-82
    • Coyne, C.B.1
  • 9
    • 77951976539 scopus 로고    scopus 로고
    • Structures of influenza A proteins and insights into antiviral drug targets
    • Das K, Aramini JM, Ma LC, Krug RM, Arnold E. 2010. Structures of influenza A proteins and insights into antiviral drug targets. Nat. Struct. Mol. Biol. 17:530-538.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 530-538
    • Das, K.1    Aramini, J.M.2    Ma, L.C.3    Krug, R.M.4    Arnold, E.5
  • 10
    • 67449110743 scopus 로고    scopus 로고
    • Emergence of a novel swine-origin influenza A (H1N1) virus in humans
    • Dawood FS, et al. 2009. Emergence of a novel swine-origin influenza A (H1N1) virus in humans. N. Engl. J. Med. 360:2605-2615.
    • (2009) N. Engl. J. Med. , vol.360 , pp. 2605-2615
    • Dawood, F.S.1
  • 11
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias A, et al. 2009. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458:914-918.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1
  • 12
    • 65549130101 scopus 로고    scopus 로고
    • A new player in a deadly game: Influenza viruses and the PI3K/Akt signalling pathway
    • Ehrhardt C, Ludwig S. 2009. A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway. Cell. Microbiol. 11:863-871.
    • (2009) Cell. Microbiol. , vol.11 , pp. 863-871
    • Ehrhardt, C.1    Ludwig, S.2
  • 13
    • 18144398494 scopus 로고    scopus 로고
    • Recognition of mRNA cap structures by viral and cellular proteins
    • DOI 10.1099/vir.0.80755-0
    • Fechter P, Brownlee GG. 2005. Recognition of mRNA cap structures by viral and cellular proteins. J. Gen. Virol. 86:1239-1249. (Pubitemid 40613240)
    • (2005) Journal of General Virology , vol.86 , Issue.5 , pp. 1239-1249
    • Fechter, P.1    Brownlee, G.G.2
  • 15
    • 77956643301 scopus 로고    scopus 로고
    • Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT
    • Fislova T, Thomas B, Graef KM, Fodor E. 2010. Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT. J. Virol. 84:8691-8699.
    • (2010) J. Virol. , vol.84 , pp. 8691-8699
    • Fislova, T.1    Thomas, B.2    Graef, K.M.3    Fodor, E.4
  • 16
    • 0036720769 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs
    • DOI 10.1128/JVI.76.18.8989-9001.2002
    • Fodor E, et al. 2002. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs. J. Virol. 76:8989-9001. (Pubitemid 34919858)
    • (2002) Journal of Virology , vol.76 , Issue.18 , pp. 8989-9001
    • Fodor, E.1    Crow, M.2    Mingay, L.J.3    Deng, T.4    Sharps, J.5    Fechter, P.6    Brownlee, G.G.7
  • 17
    • 0028245360 scopus 로고
    • The influenza virus panhandle is involved in the initiation of transcription
    • Fodor E, Pritlove DC, Brownlee GG. 1994. The influenza virus panhandle is involved in the initiation of transcription. J. Virol. 68:4092-4096. (Pubitemid 24177444)
    • (1994) Journal of Virology , vol.68 , Issue.6 , pp. 4092-4096
    • Fodor, E.1    Pritlove, D.C.2    Brownlee, G.G.3
  • 18
    • 0015325009 scopus 로고
    • Immunochemical detection of double-stranded ribonucleic acid in leaves of sugar cane infected with Fiji disease virus
    • Francki RI, Jackson AO. 1972. Immunochemical detection of double-stranded ribonucleic acid in leaves of sugar cane infected with Fiji disease virus. Virology 48:275-277.
    • (1972) Virology , vol.48 , pp. 275-277
    • Francki, R.I.1    Jackson, A.O.2
  • 19
    • 64749093901 scopus 로고    scopus 로고
    • T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections
    • Furuta Y, et al. 2009. T-705 (favipiravir) and related compounds: novel broad-spectrum inhibitors of RNA viral infections. Antiviral Res. 82:95-102.
    • (2009) Antiviral Res. , vol.82 , pp. 95-102
    • Furuta, Y.1
  • 20
    • 0037404535 scopus 로고    scopus 로고
    • Mutations in the N-terminal region of influenza virus PB2 protein affect virus RNA replication but not transcription
    • DOI 10.1128/JVI.77.9.5098-5108.2003
    • Gastaminza P, Perales B, Falcon AM, Ortin J. 2003. Mutations in the N-terminal region of influenza virus PB2 protein affect virus RNA replication but not transcription. J. Virol. 77:5098-5108. (Pubitemid 36460924)
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5098-5108
    • Gastaminza, P.1    Perales, B.2    Falcon, A.M.3    Ortin, J.4
  • 21
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • DOI 10.1101/gad.1505307
    • Geller R, Vignuzzi M, Andino R, Frydman J. 2007. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 21:195-205. (Pubitemid 46155813)
    • (2007) Genes and Development , vol.21 , Issue.2 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 22
    • 43249128376 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay D, et al. 2008. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nat. Struct. Mol. Biol. 15:500-5066.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 500-5066
    • Guilligay, D.1
  • 23
    • 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
    • DOI 10.1128/JVI.00600-06
    • 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. (Pubitemid 44182280)
    • (2006) Journal of Virology , vol.80 , Issue.16 , pp. 7789-7798
    • Hara, K.1    Schmidt, F.I.2    Crow, M.3    Brownlee, G.G.4
  • 24
    • 0024535928 scopus 로고
    • Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells
    • Hatada E, Hasegawa M, Mukaigawa J, Shimizu K, Fukuda R. 1989. Control of influenza virus gene expression: quantitative analysis of each viral RNA species in infected cells. J. Biochem. 105:537-546. (Pubitemid 19106773)
    • (1989) Journal of Biochemistry , vol.105 , Issue.4 , pp. 537-546
    • Hatada, E.1    Hasegawa, M.2    Mukaigawa, J.3    Shimizu, K.4    Fukuda, R.5
  • 25
    • 74049129476 scopus 로고    scopus 로고
    • Integrating the cell stress response: A new view of molecular chaperones as immunological and physiological homeostatic regulators
    • Henderson B. 2010. Integrating the cell stress response: a new view of molecular chaperones as immunological and physiological homeostatic regulators. Cell Biochem. Funct. 28:1-14.
    • (2010) Cell Biochem. Funct. , vol.28 , pp. 1-14
    • Henderson, B.1
  • 26
    • 0347003598 scopus 로고    scopus 로고
    • Heat Shock Protein 70 Is Related to Thermal Inhibition of Nuclear Export of the Influenza Virus Ribonucleoprotein Complex
    • DOI 10.1128/JVI.78.3.1263-1270.2004
    • Hirayama E, Atagi H, Hiraki A, Kim J. 2004. Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex. J. Virol. 78:1263-1270. (Pubitemid 38095836)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1263-1270
    • Hirayama, E.1    Atagi, H.2    Hiraki, A.3    Kim, J.4
  • 28
    • 36949001617 scopus 로고    scopus 로고
    • Strategies of development of antiviral agents directed against influenza virus replication
    • DOI 10.2174/138161207782794248
    • Hsieh HP, Hsu JT. 2007. Strategies of development of antiviral agents directed against influenza virus replication. Curr. Pharm. Des. 13:3531-3542. (Pubitemid 350238942)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.34 , pp. 3531-3542
    • Hsieh, H.-P.1    Hsu, J.T.-A.2
  • 29
    • 0038371106 scopus 로고    scopus 로고
    • Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses
    • DOI 10.1128/JVI.77.10.6007-6013.2003
    • Huarte M, et al. 2003. Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses. J. Virol. 77: 6007-6013. (Pubitemid 36538991)
    • (2003) Journal of Virology , vol.77 , Issue.10 , pp. 6007-6013
    • Huarte, M.1    Falcon, A.2    Nakaya, Y.3    Ortin, J.4    Garcia-Sastre, A.5    Nietol, A.6
  • 30
    • 77953259427 scopus 로고    scopus 로고
    • Identification of influenza A nucleoprotein as an antiviral target
    • Kao RY, et al. 2010. Identification of influenza A nucleoprotein as an antiviral target. Nat. Biotechnol. 28:600-605.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 600-605
    • Kao, R.Y.1
  • 31
    • 79952189030 scopus 로고    scopus 로고
    • Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA
    • Kawakami E, et al. 2011. Strand-specific real-time RT-PCR for distinguishing influenza vRNA, cRNA, and mRNA. J. Virol. Methods 173:1-6.
    • (2011) J. Virol. Methods , vol.173 , pp. 1-6
    • Kawakami, E.1
  • 32
    • 62849121367 scopus 로고    scopus 로고
    • Pandemic influenza: An inconvenient mutation
    • Layne SP, Monto AS, Taubenberger JK. 2009. Pandemic influenza: an inconvenient mutation. Science 323:1560-1561.
    • (2009) Science , vol.323 , pp. 1560-1561
    • Layne, S.P.1    Monto, A.S.2    Taubenberger, J.K.3
  • 33
    • 0032189818 scopus 로고    scopus 로고
    • RNA-dependent activation of primer RNA production by influenza virus polymerase: Different regions of the same protein subunit constitute the two required RNA-binding sites
    • DOI 10.1093/emboj/17.19.5844
    • Li ML, Ramirez BC, Krug RM. 1998. RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites. EMBO J. 17:5844-5852. (Pubitemid 28445995)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5844-5852
    • Li, M.-L.1    Ramirez, B.C.2    Krug, R.M.3
  • 34
    • 0035901509 scopus 로고    scopus 로고
    • The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
    • DOI 10.1093/emboj/20.8.2078
    • Li ML, Rao P, Krug RM. 2001. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. EMBO J. 20:2078-2086. (Pubitemid 32397409)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 2078-2086
    • Li, M.-L.1    Rao, P.2    Krug, R.M.3
  • 35
    • 0032837329 scopus 로고    scopus 로고
    • Temperature-sensitive lesions in two influenza a viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein
    • Medcalf L, Poole E, Elton D, Digard P. 1999. Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein. J. Virol. 73:7349-7356. (Pubitemid 29383218)
    • (1999) Journal of Virology , vol.73 , Issue.9 , pp. 7349-7356
    • Medcalf, L.1    Poole, E.2    Elton, D.3    Digard, P.4
  • 38
    • 9944250866 scopus 로고    scopus 로고
    • Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication
    • DOI 10.1099/vir.0.80518-0
    • Mullin AE, Dalton RM, Amorim MJ, Elton D, Digard P. 2004. Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication. J. Gen. Virol. 85:3689-3698. (Pubitemid 39591876)
    • (2004) Journal of General Virology , vol.85 , Issue.12 , pp. 3689-3698
    • Mullin, A.E.1    Dalton, R.M.2    Joao, A.M.3    Elton, D.4    Digard, P.5
  • 39
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • DOI 10.1128/JVI.01917-06
    • Naito T, Momose F, Kawaguchi A, Nagata K. 2007. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J. Virol. 81:1339-1349. (Pubitemid 46167855)
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 40
    • 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, et al. 2009. Interaction of the influenza A virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication. J. Virol. 83:29-36.
    • (2009) J. Virol. , vol.83 , pp. 29-36
    • Newcomb, L.L.1
  • 41
    • 0034608946 scopus 로고    scopus 로고
    • Inhibition of the RNA-dependent transactivation and replication of human immunodeficiency virus type 1 by a fluoroquinoline derivative K-37
    • DOI 10.1006/viro.2000.0396
    • Okamoto H, et al. 2000. Inhibition of the RNA-dependent transactivation and replication of human immunodeficiency virus type 1 by a fluoroquinoline derivative K-37. Virology 272:402-408. (Pubitemid 30480200)
    • (2000) Virology , vol.272 , Issue.2 , pp. 402-408
    • Okamoto, H.1    Cujec, T.P.2    Okamoto, M.3    Peterlin, B.M.4    Baba, M.5    Okamoto, T.6
  • 43
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed), 5th ed, Lippincott Williams & Wilkins, Philadelphia, PA
    • Palese P, Shaw ML. 2007. Orthomyxoviridae: the viruses and their replication, p 1647-1689. In D. M. Knipe and P. M. Howley (ed), Fields virology, 5th ed, vol. 2. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields Virology , vol.2 , pp. 1647-1689
    • Palese, P.1    Shaw, M.L.2
  • 44
    • 77954912141 scopus 로고    scopus 로고
    • Influenza A virus-generated small RNAs regulate the switch from transcription to replication
    • Perez JT, et al. 2010. Influenza A virus-generated small RNAs regulate the switch from transcription to replication. Proc. Natl. Acad. Sci. U. S. A. 107:11525-11530.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11525-11530
    • Perez, J.T.1
  • 45
    • 0019394947 scopus 로고
    • 7 GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM. 1981. A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23:847-858. (Pubitemid 11156997)
    • (1981) Cell , vol.23 , Issue.3 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 46
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication
    • Portela A, Digard P. 2002. The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. J. Gen. Virol. 83:723-734. (Pubitemid 34284855)
    • (2002) Journal of General Virology , vol.83 , Issue.4 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 47
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: A promising pathway for cancer therapy
    • Porter JR, Fritz CC, Depew KM. 2010. Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr. Opin. Chem. Biol. 14:412-420.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 412-420
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 48
    • 67649227447 scopus 로고    scopus 로고
    • NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
    • Robb NC, Smith M, Vreede FT, Fodor E. 2009. NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J. Gen. Virol. 90:1398-1407.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1398-1407
    • Robb, N.C.1    Smith, M.2    Vreede, F.T.3    Fodor, E.4
  • 49
    • 77749322610 scopus 로고    scopus 로고
    • Towards an atomic resolution understanding of the influenza virus replication machinery
    • Ruigrok RW, Crepin T, Hart DJ, Cusack S. 2010. Towards an atomic resolution understanding of the influenza virus replication machinery. Curr. Opin. Struct. Biol. 20:104-113.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 104-113
    • Ruigrok, R.W.1    Crepin, T.2    Hart, D.J.3    Cusack, S.4
  • 51
    • 77954929676 scopus 로고    scopus 로고
    • A big role for small RNAs in influenza virus replication
    • Scull MA, Rice CM. 2010. A big role for small RNAs in influenza virus replication. Proc. Natl. Acad. Sci. U. S. A. 107:11153-11154.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11153-11154
    • Scull, M.A.1    Rice, C.M.2
  • 52
    • 77649295601 scopus 로고    scopus 로고
    • Pyrazole compound BPR1P0034 with potent and selective anti-influenza virus activity
    • Shih SR, et al. 2010. Pyrazole compound BPR1P0034 with potent and selective anti-influenza virus activity. J. Biomed. Sci. 17:13.
    • (2010) J. Biomed. Sci. , vol.17 , pp. 13
    • Shih, S.R.1
  • 53
    • 77950356637 scopus 로고    scopus 로고
    • BPR2-D2 targeting viral ribonucleoprotein complex-associated function inhibits oseltamivir-resistant influenza viruses
    • Shih SR, et al. 2010. BPR2-D2 targeting viral ribonucleoprotein complex-associated function inhibits oseltamivir-resistant influenza viruses. J. Antimicrob. Chemother. 65:63-71.
    • (2010) J. Antimicrob. Chemother. , vol.65 , pp. 63-71
    • Shih, S.R.1
  • 56
    • 4143153932 scopus 로고    scopus 로고
    • Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates
    • DOI 10.1128/JVI.78.17.9568-9572.2004
    • Vreede FT, Jung TE, Brownlee GG. 2004. Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates. J. Virol. 78:9568-9572. (Pubitemid 39096565)
    • (2004) Journal of Virology , vol.78 , Issue.17 , pp. 9568-9572
    • Vreede, F.T.1    Jung, T.E.2    Brownlee, G.G.3
  • 57
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe T, Watanabe S, Kawaoka Y. 2010. Cellular networks involved in the influenza virus life cycle. Cell Host Microbe 7:427-439.
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 58
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber F, Wagner V, Rasmussen SB, Hartmann R, Paludan SR. 2006. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J. Virol. 80:5059-5064.
    • (2006) J. Virol. , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 59
    • 33751231111 scopus 로고    scopus 로고
    • H5N1 influenza - Continuing evolution and spread
    • DOI 10.1056/NEJMp068205
    • Webster RG, Govorkova EA. 2006. H5N1 influenza - continuing evolution and spread. N. Engl. J. Med. 355:2174-2177. (Pubitemid 44791158)
    • (2006) New England Journal of Medicine , vol.355 , Issue.21 , pp. 2174-2177
    • Webster, R.G.1    Govorkova, E.A.2
  • 60
    • 67749133883 scopus 로고    scopus 로고
    • A complicated message: Identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA
    • Wise HM, et al. 2009. A complicated message: identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA. J. Virol. 83:8021-8031.
    • (2009) J. Virol. , vol.83 , pp. 8021-8031
    • Wise, H.M.1
  • 61
    • 27344446874 scopus 로고    scopus 로고
    • Phosphorylation of PI3K/Akt and MAPK/ERK in an early entry step of enterovirus 71
    • Wong WR, Chen YY, Yang SM, Chen YL, Horng JT. 2005. Phosphorylation of PI3K/Akt and MAPK/ERK in an early entry step of enterovirus 71. Life Sci. 78:82-90.
    • (2005) Life Sci. , vol.78 , pp. 82-90
    • Wong, W.R.1    Chen, Y.Y.2    Yang, S.M.3    Chen, Y.L.4    Horng, J.T.5
  • 62
    • 77649210704 scopus 로고    scopus 로고
    • Anti-influenza drug discovery: Structure-activity relationship and mechanistic insight into novel angelicin derivatives
    • Yeh JY, et al. 2010. Anti-influenza drug discovery: structure-activity relationship and mechanistic insight into novel angelicin derivatives. J. Med. Chem. 53:1519-1533.
    • (2010) J. Med. Chem. , vol.53 , pp. 1519-1533
    • Yeh, J.Y.1
  • 63
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, et al. 2009. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458:909-913.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1


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