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Volumn 54, Issue 1, 2011, Pages 68-74

Host cellular signaling induced by influenza virus

Author keywords

influenza virus; signal transduction; virus host interaction

Indexed keywords

ORTHOMYXOVIRIDAE;

EID: 78751651077     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-010-4116-z     Document Type: Review
Times cited : (20)

References (105)
  • 1
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • Proud C G. PKR: A new name and new roles. Trends Biochem Sci, 1995, 20: 241-246.
    • (1995) Trends Biochem Sci , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 2
    • 0033230617 scopus 로고    scopus 로고
    • PKR; a sentinel kinase for cellular stress
    • Williams B R. PKR; a sentinel kinase for cellular stress. Oncogene, 1999, 18: 6112-6120.
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 3
    • 67650917895 scopus 로고    scopus 로고
    • Influenza B virus ribonucleoprotein is a potent activator of the antiviral kinase PKR
    • Dauber B, Martinez-Sobrido L, Schneider J, et al. Influenza B virus ribonucleoprotein is a potent activator of the antiviral kinase PKR. PLoS Pathog, 2009, 5: e1000473.
    • (2009) PLoS Pathog , vol.5
    • Dauber, B.1    Martinez-Sobrido, L.2    Schneider, J.3
  • 4
    • 42449121506 scopus 로고    scopus 로고
    • PKR in innate immunity, cancer, and viral oncolysis
    • Balachandran S, Barber G N. PKR in innate immunity, cancer, and viral oncolysis. Methods Mol Biol, 2007, 383: 277-301.
    • (2007) Methods Mol Biol , vol.383 , pp. 277-301
    • Balachandran, S.1    Barber, G.N.2
  • 5
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: virus and cell control
    • Garcia M A, Meurs E F, Esteban M. The dsRNA protein kinase PKR: virus and cell control. Biochimie, 2007, 89: 799-811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 6
    • 0033679958 scopus 로고    scopus 로고
    • Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection
    • Balachandran S, Roberts P C, Brown L E, et al. Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection. Immunity, 2000, 13: 129-141.
    • (2000) Immunity , vol.13 , pp. 129-141
    • Balachandran, S.1    Roberts, P.C.2    Brown, L.E.3
  • 7
    • 0029842883 scopus 로고    scopus 로고
    • Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection
    • Takizawa T, Ohashi K, Nakanishi Y. Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J Virol, 1996, 70: 8128-8132.
    • (1996) J Virol , vol.70 , pp. 8128-8132
    • Takizawa, T.1    Ohashi, K.2    Nakanishi, Y.3
  • 8
    • 0033970831 scopus 로고    scopus 로고
    • Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/Caspase-8 death signaling pathway
    • Balachandran S, Roberts P C, Kipperman T, et al. Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/Caspase-8 death signaling pathway. J Virol, 2000, 74: 1513-1523.
    • (2000) J Virol , vol.74 , pp. 1513-1523
    • Balachandran, S.1    Roberts, P.C.2    Kipperman, T.3
  • 9
    • 33646517711 scopus 로고    scopus 로고
    • Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA
    • Li S, Min J Y, Krug R M, et al. Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology, 2006, 349: 13-21.
    • (2006) Virology , vol.349 , pp. 13-21
    • Li, S.1    Min, J.Y.2    Krug, R.M.3
  • 10
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor
    • Lu Y, Wambach M, Katze M G, et al. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor. Virology, 1995, 214: 222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3
  • 12
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K. Toll-like receptor signalling. Nat Rev Immunol, 2004, 4: 499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 13
    • 1542317550 scopus 로고    scopus 로고
    • Innate Antiviral responses by means of TLR7-Mediated recognition of single-stranded RNA
    • Diebold S S, Kaisho T, Hemmi H, et al. Innate Antiviral responses by means of TLR7-Mediated recognition of single-stranded RNA. Science, 2004, 303: 1529-1531.
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3
  • 14
    • 1842631428 scopus 로고    scopus 로고
    • Recognition of sin gle-stranded RNA viruses by Toll-like receptor 7
    • Lund J M, Alexopoulou L, Sato A, et al. Recognition of sin gle-stranded RNA viruses by Toll-like receptor 7. Proc Natl Acad Sci USA, 2004, 101: 5598-5603.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5598-5603
    • Lund, J.M.1    Alexopoulou, L.2    Sato, A.3
  • 15
    • 14044267522 scopus 로고    scopus 로고
    • Involvement of toll-like receptor 3 in the immune response of lung epithelial cells to double-stranded RNA and influenza A virus
    • Guillot L, Le Goffic R, Bloch S, et al. Involvement of toll-like receptor 3 in the immune response of lung epithelial cells to double-stranded RNA and influenza A virus. J Biol Chem, 2005, 280: 5571-5580.
    • (2005) J Biol Chem , vol.280 , pp. 5571-5580
    • Guillot, L.1    Le Goffic, R.2    Bloch, S.3
  • 16
    • 23244461479 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent hyperinduction of tumor necrosis factor alpha expression in response to avian influenza virus H5N1
    • Lee D C, Cheung C Y, Law A H, et al. p38 mitogen-activated protein kinase-dependent hyperinduction of tumor necrosis factor alpha expression in response to avian influenza virus H5N1. J Virol, 2005, 79: 10147-10154.
    • (2005) J Virol , vol.79 , pp. 10147-10154
    • Lee, D.C.1    Cheung, C.Y.2    Law, A.H.3
  • 17
    • 0038105474 scopus 로고    scopus 로고
    • ASK1 regulates influenza virus infection-induced apoptotic cell death
    • Maruoka S, Hashimoto S, Gon Y, et al. ASK1 regulates influenza virus infection-induced apoptotic cell death. Biochem Biophys Res Commun, 2003, 307: 870-876.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 870-876
    • Maruoka, S.1    Hashimoto, S.2    Gon, Y.3
  • 18
    • 0034653508 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase and c-jun-NH2-terminal kinase regulate RANTES production by influenza virus-infected human bronchial epithelial cells
    • Kujime K, Hashimoto S, Gon Y, et al. p38 mitogen-activated protein kinase and c-jun-NH2-terminal kinase regulate RANTES production by influenza virus-infected human bronchial epithelial cells. J Immunol, 2000, 164: 3222-3228.
    • (2000) J Immunol , vol.164 , pp. 3222-3228
    • Kujime, K.1    Hashimoto, S.2    Gon, Y.3
  • 19
    • 0035815684 scopus 로고    scopus 로고
    • Influenza virus-induced AP-1-dependent gene expression requires activation of the JNK signaling pathway
    • Ludwig S, Ehrhardt C, Neumeier E R, et al. Influenza virus-induced AP-1-dependent gene expression requires activation of the JNK signaling pathway. J Biol Chem, 2001, 276: 10990-10998.
    • (2001) J Biol Chem , vol.276 , pp. 10990-10998
    • Ludwig, S.1    Ehrhardt, C.2    Neumeier, E.R.3
  • 20
    • 78751674806 scopus 로고    scopus 로고
    • The MAPK-activated kinase RSK2 plays a role in innate immune responses to influenza virus infection
    • Kakugawa S, Shimojima M, Goto H, et al. The MAPK-activated kinase RSK2 plays a role in innate immune responses to influenza virus infection. J Virol, 2009.
    • (2009) J Virol
    • Kakugawa, S.1    Shimojima, M.2    Goto, H.3
  • 21
    • 50449106423 scopus 로고    scopus 로고
    • Toll-like receptor 2 expression level on monocytes in patients with viral infections: Monitoring infection severity
    • Kajiya T, Orihara K, Hamasaki S, et al. Toll-like receptor 2 expression level on monocytes in patients with viral infections: Monitoring infection severity. J Infect, 2008, 57: 249-259.
    • (2008) J Infect , vol.57 , pp. 249-259
    • Kajiya, T.1    Orihara, K.2    Hamasaki, S.3
  • 22
    • 33645091208 scopus 로고    scopus 로고
    • Influenza a viruses upregulate neutrophil toll-like receptor 2 expression and function
    • Lee R M, White M R, Hartshorn K L. Influenza a viruses upregulate neutrophil toll-like receptor 2 expression and function. Scand J Immunol, 2006, 63: 81-89.
    • (2006) Scand J Immunol , vol.63 , pp. 81-89
    • Lee, R.M.1    White, M.R.2    Hartshorn, K.L.3
  • 23
    • 35748973890 scopus 로고    scopus 로고
    • Negative regulation of TLR-signaling pathways by activating transcription factor-3
    • Whitmore M M, Iparraguirre A, Kubelka L, et al. Negative regulation of TLR-signaling pathways by activating transcription factor-3. J Immunol, 2007, 179: 3622-3630.
    • (2007) J Immunol , vol.179 , pp. 3622-3630
    • Whitmore, M.M.1    Iparraguirre, A.2    Kubelka, L.3
  • 24
    • 70349139611 scopus 로고    scopus 로고
    • Functions of the cytoplasmic RNA sensors RIG-I and MDA-5: Key regulators of innate immunity
    • Barral P M, Sarkar D, Su Z-z, et al. Functions of the cytoplasmic RNA sensors RIG-I and MDA-5: Key regulators of innate immunity. Pharmacol Ther, 2009, 124: 219-234.
    • (2009) Pharmacol Ther , vol.124 , pp. 219-234
    • Barral, P.M.1    Sarkar, D.2    Su, Z.-Z.3
  • 25
    • 34548126512 scopus 로고    scopus 로고
    • RIG-I family RNA helicases: Cytoplasmic sensor for antiviral innate immunity
    • Yoneyama M, Fujita T. RIG-I family RNA helicases: Cytoplasmic sensor for antiviral innate immunity. Cytokine Growth Factor Rev, 2007, 18: 545-551.
    • (2007) Cytokine Growth Factor Rev , vol.18 , pp. 545-551
    • Yoneyama, M.1    Fujita, T.2
  • 26
    • 39149107423 scopus 로고    scopus 로고
    • MDA5/RIG-I and virus recognition
    • Takeuchi O, Akira S. MDA5/RIG-I and virus recognition. Curr Opin Immunol, 2008, 20: 17-22.
    • (2008) Curr Opin Immunol , vol.20 , pp. 17-22
    • Takeuchi, O.1    Akira, S.2
  • 27
    • 33947206046 scopus 로고    scopus 로고
    • Cutting edge: Influenza A virus activates TLR3-dependent inflammatory and RIG-I-dependent antiviral responses in human lung epithelial cells
    • Le Goffic R, Pothlichet J, Vitour D, et al. Cutting edge: Influenza A virus activates TLR3-dependent inflammatory and RIG-I-dependent antiviral responses in human lung epithelial cells. J Immunol, 2007, 178: 3368-3372.
    • (2007) J Immunol , vol.178 , pp. 3368-3372
    • Le Goffic, R.1    Pothlichet, J.2    Vitour, D.3
  • 28
    • 33748192461 scopus 로고    scopus 로고
    • Retinoic acid inducible gene-I and mda-5 are involved in influenza A virus-induced expression of antiviral cytokines
    • Siren J, Imaizumi T, Sarkar D, et al. Retinoic acid inducible gene-I and mda-5 are involved in influenza A virus-induced expression of antiviral cytokines. Microbes Infect, 2006, 8: 2013-2020.
    • (2006) Microbes Infect , vol.8 , pp. 2013-2020
    • Siren, J.1    Imaizumi, T.2    Sarkar, D.3
  • 29
    • 33645214581 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha enhances influenza A virus-induced expression of antiviral cytokines by activating RIG-I gene expression
    • Matikainen S, Siren J, Tissari J, et al. Tumor necrosis factor alpha enhances influenza A virus-induced expression of antiviral cytokines by activating RIG-I gene expression. J Virol, 2006, 80: 3515-3522.
    • (2006) J Virol , vol.80 , pp. 3515-3522
    • Matikainen, S.1    Siren, J.2    Tissari, J.3
  • 30
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale B G, Randall R E, Ortin J, et al. The multifunctional NS1 protein of influenza A viruses. J Gen Virol, 2008, 89: 2359-2376.
    • (2008) J Gen Virol , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3
  • 31
    • 0033870894 scopus 로고    scopus 로고
    • Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein
    • Talon J, Horvath C M, Polley R, et al. Activation of interferon regulatory factor 3 is inhibited by the influenza A virus NS1 protein. J Virol, 2000, 74: 7989-7996.
    • (2000) J Virol , vol.74 , pp. 7989-7996
    • Talon, J.1    Horvath, C.M.2    Polley, R.3
  • 32
    • 72949109523 scopus 로고    scopus 로고
    • Interplay between influenza A virus and the innate immune signaling
    • Ehrhardt C, Seyer R, Hrincius E R, et al. Interplay between influenza A virus and the innate immune signaling. Microbes Infect, 2010, 12: 81-87.
    • (2010) Microbes Infect , vol.12 , pp. 81-87
    • Ehrhardt, C.1    Seyer, R.2    Hrincius, E.R.3
  • 33
    • 33847670199 scopus 로고    scopus 로고
    • NS1 protein of influenza A virus inhibits the function of intracytoplasmic pathogen sensor, RIG-I
    • Guo Z, Chen L M, Zeng H, et al. NS1 protein of influenza A virus inhibits the function of intracytoplasmic pathogen sensor, RIG-I. Am J Respir Cell Mol Biol, 2007, 36: 263-269.
    • (2007) Am J Respir Cell Mol Biol , vol.36 , pp. 263-269
    • Guo, Z.1    Chen, L.M.2    Zeng, H.3
  • 34
    • 33846061693 scopus 로고    scopus 로고
    • Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus
    • Mibayashi M, Martinez-Sobrido L, Loo Y M, et al. Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J Virol, 2007, 81: 514-524.
    • (2007) J Virol , vol.81 , pp. 514-524
    • Mibayashi, M.1    Martinez-Sobrido, L.2    Loo, Y.M.3
  • 35
    • 33947171000 scopus 로고    scopus 로고
    • IFNbeta induction by influenza A virus is mediated by RIG-I which is regulated by the viral NS1 protein
    • Opitz B, Rejaibi A, Dauber B, et al. IFNbeta induction by influenza A virus is mediated by RIG-I which is regulated by the viral NS1 protein. Cell Microbiol, 2007, 9: 930-938.
    • (2007) Cell Microbiol , vol.9 , pp. 930-938
    • Opitz, B.1    Rejaibi, A.2    Dauber, B.3
  • 36
    • 65549164536 scopus 로고    scopus 로고
    • Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I
    • Gack M U, Albrecht R A, Urano T, et al. Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I. Cell Host Microbe, 2009, 5: 439-449.
    • (2009) Cell Host Microbe , vol.5 , pp. 439-449
    • Gack, M.U.1    Albrecht, R.A.2    Urano, T.3
  • 37
    • 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 M E, Barabino S M L, Li Y, et al. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′ end formation of cellular pre-mRNAs. Mol Cell, 1998, 1: 991-1000.
    • (1998) Mol Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.L.2    Li, Y.3
  • 38
    • 34848897191 scopus 로고    scopus 로고
    • Influenza A virus PB1-F2: A small protein with a big punch
    • Conenello G M, Palese P. Influenza A virus PB1-F2: A small protein with a big punch. Cell Host Microbe, 2007, 2: 207-209.
    • (2007) Cell Host Microbe , vol.2 , pp. 207-209
    • Conenello, G.M.1    Palese, P.2
  • 39
    • 70350736558 scopus 로고    scopus 로고
    • Phosphorylation of the influenza A virus protein PB1-F2 by PKC is crucial for apoptosis promoting functions in monocytes
    • Mitzner D, Dudek S E, Studtrucker N, et al. Phosphorylation of the influenza A virus protein PB1-F2 by PKC is crucial for apoptosis promoting functions in monocytes. Cell Microbiol, 2009, 11: 1502-1516.
    • (2009) Cell Microbiol , vol.11 , pp. 1502-1516
    • Mitzner, D.1    Dudek, S.E.2    Studtrucker, N.3
  • 40
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin D, Garcia-Sastre A, Xiao X, et al. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog, 2005, 1: e4.
    • (2005) PLoS Pathog , vol.1
    • Zamarin, D.1    Garcia-Sastre, A.2    Xiao, X.3
  • 41
    • 34848926238 scopus 로고    scopus 로고
    • Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumonia
    • McAuley J L, Hornung F, Boyd K L, et al. Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumonia. Cell Host Microbe, 2007, 2: 240-249.
    • (2007) Cell Host Microbe , vol.2 , pp. 240-249
    • McAuley, J.L.1    Hornung, F.2    Boyd, K.L.3
  • 42
    • 33746858906 scopus 로고    scopus 로고
    • Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice
    • Zamarin D, Ortigoza M B, Palese P. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. J Virol, 2006, 80: 7976-7983.
    • (2006) J Virol , vol.80 , pp. 7976-7983
    • Zamarin, D.1    Ortigoza, M.B.2    Palese, P.3
  • 43
    • 34250783318 scopus 로고    scopus 로고
    • Acetylsalicylic acid (ASA) blocks influenza virus propagation via its NF-kB-inhibiting activity
    • Mazur I, Wurzer W J, Ehrhardt C, et al. Acetylsalicylic acid (ASA) blocks influenza virus propagation via its NF-kB-inhibiting activity. Cell Microbiol, 2007, 9: 1683-1694.
    • (2007) Cell Microbiol , vol.9 , pp. 1683-1694
    • Mazur, I.1    Wurzer, W.J.2    Ehrhardt, C.3
  • 44
    • 0032209522 scopus 로고    scopus 로고
    • Signaling through protein kinase C
    • Toker A. Signaling through protein kinase C. Front Biosci, 1998, 3: D1134-1147.
    • (1998) Front Biosci , vol.3
    • Toker, A.1
  • 45
    • 53249140699 scopus 로고    scopus 로고
    • Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity
    • Hoffmann H H, Palese P, Shaw M L. Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity. Antiviral Res, 2008, 80: 124-134.
    • (2008) Antiviral Res , vol.80 , pp. 124-134
    • Hoffmann, H.H.1    Palese, P.2    Shaw, M.L.3
  • 47
    • 70350524014 scopus 로고    scopus 로고
    • Influenza virus M2 protein inhibits epithelial sodium channels by increasing reactive oxygen species
    • Lazrak A, Iles K E, Liu G, et al. Influenza virus M2 protein inhibits epithelial sodium channels by increasing reactive oxygen species. FASEB J, 2009, 23: 3829-3842.
    • (2009) FASEB J , vol.23 , pp. 3829-3842
    • Lazrak, A.1    Iles, K.E.2    Liu, G.3
  • 48
    • 23844500631 scopus 로고    scopus 로고
    • Characterization of the host cell entry of filamentous influenza virus
    • Sieczkarski S B, Whittaker G R. Characterization of the host cell entry of filamentous influenza virus. Arch Virol, 2005, 150: 1783-1796.
    • (2005) Arch Virol , vol.150 , pp. 1783-1796
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 49
    • 0025943243 scopus 로고
    • Effects of protein kinase C inhibitors on viral entry and infectivity
    • Constantinescu S N, Cernescu C D, Popescu L M. Effects of protein kinase C inhibitors on viral entry and infectivity. FEBS Lett, 1991, 292: 31-33.
    • (1991) FEBS Lett , vol.292 , pp. 31-33
    • Constantinescu, S.N.1    Cernescu, C.D.2    Popescu, L.M.3
  • 50
    • 0031758998 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin stimulates the protein kinase C activity of human polymorphonuclear leucocytes
    • Arora D J, Gasse N. Influenza virus hemagglutinin stimulates the protein kinase C activity of human polymorphonuclear leucocytes. Arch Virol, 1998, 143: 2029-2037.
    • (1998) Arch Virol , vol.143 , pp. 2029-2037
    • Arora, D.J.1    Gasse, N.2
  • 51
    • 0033767394 scopus 로고    scopus 로고
    • Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor
    • Root C N, Wills E G, McNair L L, et al. Entry of influenza viruses into cells is inhibited by a highly specific protein kinase C inhibitor. J Gen Virol, 2000, 81: 2697-2705.
    • (2000) J Gen Virol , vol.81 , pp. 2697-2705
    • Root, C.N.1    Wills, E.G.2    McNair, L.L.3
  • 52
    • 0037213578 scopus 로고    scopus 로고
    • Role of protein kinase C betaII in influenza virus entry via late endosomes
    • Sieczkarski S B, Brown H A, Whittaker G R. Role of protein kinase C betaII in influenza virus entry via late endosomes. J Virol, 2003, 77: 460-469.
    • (2003) J Virol , vol.77 , pp. 460-469
    • Sieczkarski, S.B.1    Brown, H.A.2    Whittaker, G.R.3
  • 53
    • 54049131196 scopus 로고    scopus 로고
    • RNA viruses and the mitogenic Raf/MEK/ERK signal transduction cascade
    • Pleschka S. RNA viruses and the mitogenic Raf/MEK/ERK signal transduction cascade. Biol Chem, 2008, 389: 1273-1282.
    • (2008) Biol Chem , vol.389 , pp. 1273-1282
    • Pleschka, S.1
  • 54
    • 0035450255 scopus 로고    scopus 로고
    • Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
    • Huang X, Liu T, Muller J, et al. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology, 2001, 287: 405-416.
    • (2001) Virology , vol.287 , pp. 405-416
    • Huang, X.1    Liu, T.2    Muller, J.3
  • 55
    • 0037440711 scopus 로고    scopus 로고
    • Nuclear export of influenza viral ribonucleoprotein is temperature-dependently inhibited by dissociation of viral matrix protein
    • Sakaguchi A, Hirayama E, Hiraki A, et al. Nuclear export of influenza viral ribonucleoprotein is temperature-dependently inhibited by dissociation of viral matrix protein. Virology, 2003, 306: 244-253.
    • (2003) Virology , vol.306 , pp. 244-253
    • Sakaguchi, A.1    Hirayama, E.2    Hiraki, A.3
  • 56
    • 1542358150 scopus 로고    scopus 로고
    • MEK inhibition impairs influenza B virus propagation without emergence of resistant variants
    • Ludwig S, Wolff T, Ehrhardt C, et al. MEK inhibition impairs influenza B virus propagation without emergence of resistant variants. FEBS Letters, 2004, 561: 37-43.
    • (2004) FEBS Letters , vol.561 , pp. 37-43
    • Ludwig, S.1    Wolff, T.2    Ehrhardt, C.3
  • 57
    • 0035090589 scopus 로고    scopus 로고
    • Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade
    • Pleschka S, Wolff T, Ehrhardt C, et al. Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade. Nat Cell Biol, 2001, 3: 301-305.
    • (2001) Nat Cell Biol , vol.3 , pp. 301-305
    • Pleschka, S.1    Wolff, T.2    Ehrhardt, C.3
  • 58
    • 33745186230 scopus 로고    scopus 로고
    • Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling
    • Marjuki H, Alam M I, Ehrhardt C, et al. Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling. J Biol Chem, 2006, 281: 16707-16715.
    • (2006) J Biol Chem , vol.281 , pp. 16707-16715
    • Marjuki, H.1    Alam, M.I.2    Ehrhardt, C.3
  • 59
    • 38849122079 scopus 로고    scopus 로고
    • Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade
    • Marjuki H, Yen H L, Franks J, et al. Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade. Virol J, 2007, 4: 134.
    • (2007) Virol J , vol.4 , pp. 134
    • Marjuki, H.1    Yen, H.L.2    Franks, J.3
  • 60
    • 0019850995 scopus 로고
    • Selected host cell capped RNA fragments prime influenza viral RNA transcription in vivo
    • Beaton A R, Krug R M. Selected host cell capped RNA fragments prime influenza viral RNA transcription in vivo. Nucleic Acids Res, 1981, 9: 4423-4436.
    • (1981) Nucleic Acids Res , vol.9 , pp. 4423-4436
    • Beaton, A.R.1    Krug, R.M.2
  • 61
    • 0019343607 scopus 로고
    • Priming of influenza viral RNA transcription by capped heterologous RNAs
    • Krug R M. Priming of influenza viral RNA transcription by capped heterologous RNAs. Curr Top Microbiol Immunol, 1981, 93: 125-149.
    • (1981) Curr Top Microbiol Immunol , vol.93 , pp. 125-149
    • Krug, R.M.1
  • 62
    • 0033560753 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein targetspoly(A)-binding protein II of the cellular 3[prime]-end processing machinery
    • Chen Z, Li Y, Krug R M. Influenza A virus NS1 protein targetspoly(A)-binding protein II of the cellular 3[prime]-end processing machinery. EMBO J, 1999, 18: 2273-2283.
    • (1999) EMBO J , vol.18 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 63
    • 0028040760 scopus 로고
    • The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing
    • Lu Y, Qian X Y, Krug R M. The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing. Genes Dev, 1994, 8: 1817-1828.
    • (1994) Genes Dev , vol.8 , pp. 1817-1828
    • Lu, Y.1    Qian, X.Y.2    Krug, R.M.3
  • 64
    • 0027518202 scopus 로고
    • Translational control by influenza virus. Selective translation is mediated by sequences within the viral mRNA 5′-untranslated region
    • Garfinkel M S, Katze M G. Translational control by influenza virus. Selective translation is mediated by sequences within the viral mRNA 5′-untranslated region. J Biol Chem, 1993, 268: 22223-22226.
    • (1993) J Biol Chem , vol.268 , pp. 22223-22226
    • Garfinkel, M.S.1    Katze, M.G.2
  • 65
    • 0028923921 scopus 로고
    • Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs
    • de la Luna S, Fortes P, Beloso A, et al. Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs. J Virol, 1995, 69: 2427-2433.
    • (1995) J Virol , vol.69 , pp. 2427-2433
    • de la Luna, S.1    Fortes, P.2    Beloso, A.3
  • 66
    • 0028055149 scopus 로고
    • Influenza virus NS1 protein stimulates translation of the M1 protein
    • Enami K, Sato T A, Nakada S, et al. Influenza virus NS1 protein stimulates translation of the M1 protein. J Virol, 1994, 68: 1432-1437.
    • (1994) J Virol , vol.68 , pp. 1432-1437
    • Enami, K.1    Sato, T.A.2    Nakada, S.3
  • 67
    • 0022976677 scopus 로고
    • Cellular mRNA translation is blocked at both initiation and elongation after infection by influenza virus or adenovirus
    • Katze M G, DeCorato D, Krug R M. Cellular mRNA translation is blocked at both initiation and elongation after infection by influenza virus or adenovirus. J Virol, 1986, 60: 1027-1039.
    • (1986) J Virol , vol.60 , pp. 1027-1039
    • Katze, M.G.1    Decorato, D.2    Krug, R.M.3
  • 68
    • 0028880783 scopus 로고
    • Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation
    • Park Y W, Katze M G. Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation. J Biol Chem, 1995, 270: 28433-28439.
    • (1995) J Biol Chem , vol.270 , pp. 28433-28439
    • Park, Y.W.1    Katze, M.G.2
  • 69
    • 0033838456 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus
    • Aragon T, de la Luna S, Novoa I, et al. Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol Cell Biol, 2000, 20: 6259-6268.
    • (2000) Mol Cell Biol , vol.20 , pp. 6259-6268
    • Aragon, T.1    de la Luna, S.2    Novoa, I.3
  • 70
    • 0346121589 scopus 로고    scopus 로고
    • PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes
    • Burgui I, Aragon T, Ortin J, et al. PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes. J Gen Virol, 2003, 84: 3263-3274.
    • (2003) J Gen Virol , vol.84 , pp. 3263-3274
    • Burgui, I.1    Aragon, T.2    Ortin, J.3
  • 71
    • 0027252545 scopus 로고
    • Modification of eukaryotic initiation factor 4F during infection by influenza virus
    • Feigenblum D, Schneider R J. Modification of eukaryotic initiation factor 4F during infection by influenza virus. J Virol, 1993, 67: 3027-3035.
    • (1993) J Virol , vol.67 , pp. 3027-3035
    • Feigenblum, D.1    Schneider, R.J.2
  • 72
    • 0028815704 scopus 로고
    • Regulation of the interferon-induced PKR: can viruses cope?
    • Katze M G. Regulation of the interferon-induced PKR: can viruses cope? Trends in Microbiology, 1995, 3: 75-78.
    • (1995) Trends in Microbiology , vol.3 , pp. 75-78
    • Katze, M.G.1
  • 73
    • 33847177628 scopus 로고    scopus 로고
    • The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-Mediated mechanism
    • Goodman A G, Smith J A, Balachandran S, et al. The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-Mediated mechanism. J Virol, 2007, 81: 2221-2230.
    • (2007) J Virol , vol.81 , pp. 2221-2230
    • Goodman, A.G.1    Smith, J.A.2    Balachandran, S.3
  • 74
    • 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, et al. Control of influenza virus gene expression: quantitative analysis of each viral RNA species in infected cells. J Biochem, 1989, 105: 537-546.
    • (1989) J Biochem , vol.105 , pp. 537-546
    • Hatada, E.1    Hasegawa, M.2    Mukaigawa, J.3
  • 75
    • 0023155247 scopus 로고
    • Influenza virus gene expression: control mechanisms at early and late times of infection and nuclearcytoplasmic transport of virus-specific RNAs
    • Shapiro G I, Gurney T, Jr Krug R M. Influenza virus gene expression: control mechanisms at early and late times of infection and nuclearcytoplasmic transport of virus-specific RNAs. J Virol, 1987, 61: 764-773.
    • (1987) J Virol , vol.61 , pp. 764-773
    • Shapiro, G.I.1    Gurney Jr., T.2    Krug, R.M.3
  • 76
    • 0025984455 scopus 로고
    • Temporal control for translation of influenza virus mRNAs
    • Yamanaka K, Nagata K, Ishihama A. Temporal control for translation of influenza virus mRNAs. Arch Virol, 1991, 120: 33-42.
    • (1991) Arch Virol , vol.120 , pp. 33-42
    • Yamanaka, K.1    Nagata, K.2    Ishihama, A.3
  • 77
    • 58149175555 scopus 로고    scopus 로고
    • The life of a cell: apoptosis regulation by the PI3K/PKB pathway
    • Duronio V. The life of a cell: apoptosis regulation by the PI3K/PKB pathway. Biochem J, 2008, 415: 333-344.
    • (2008) Biochem J , vol.415 , pp. 333-344
    • Duronio, V.1
  • 78
    • 1642471831 scopus 로고    scopus 로고
    • PI3K/Akt and apoptosis: size matters
    • Franke T F, Hornik C P, Segev L, et al. PI3K/Akt and apoptosis: size matters. Oncogene, 2003, 22: 8983-8998.
    • (2003) Oncogene , vol.22 , pp. 8983-8998
    • Franke, T.F.1    Hornik, C.P.2    Segev, L.3
  • 79
    • 58149129203 scopus 로고    scopus 로고
    • PI3K-Akt signaling and viral infection
    • Ji W T, Liu H J. PI3K-Akt signaling and viral infection. Recent Pat Biotechnol, 2008, 2: 218-226.
    • (2008) Recent Pat Biotechnol , vol.2 , pp. 218-226
    • Ji, W.T.1    Liu, H.J.2
  • 80
    • 38349136199 scopus 로고    scopus 로고
    • Binding of influenza A virus NS1 protein to the inter-SH2 domain of p85 suggests a novel mechanism for phosphoinositide 3-kinase activation
    • Hale B G, Batty I H, Downes C P, et al. Binding of influenza A virus NS1 protein to the inter-SH2 domain of p85 suggests a novel mechanism for phosphoinositide 3-kinase activation. J Biol Chem, 2008, 283: 1372-1380.
    • (2008) J Biol Chem , vol.283 , pp. 1372-1380
    • Hale, B.G.1    Batty, I.H.2    Downes, C.P.3
  • 81
    • 33749004778 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling
    • Hale B G, Jackson D, Chen Y H, et al. Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling. Proc Natl Acad Sci USA, 2006, 103: 14194-14199.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14194-14199
    • Hale, B.G.1    Jackson, D.2    Chen, Y.H.3
  • 82
    • 34247105759 scopus 로고    scopus 로고
    • PI3K signalling during influenza A virus infections
    • Hale B G, Randall R E. PI3K signalling during influenza A virus infections. Biochem Soc Trans, 2007, 35: 186-187.
    • (2007) Biochem Soc Trans , vol.35 , pp. 186-187
    • Hale, B.G.1    Randall, R.E.2
  • 83
    • 36349018937 scopus 로고    scopus 로고
    • SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation
    • Shin Y K, Li Y, Liu Q, et al. SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation. J Virol, 2007, 81: 12730-12739.
    • (2007) J Virol , vol.81 , pp. 12730-12739
    • Shin, Y.K.1    Li, Y.2    Liu, Q.3
  • 84
    • 33846160497 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K
    • Shin Y K, Liu Q, Tikoo S K, et al. Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K. J Gen Virol, 2007, 88: 13-18.
    • (2007) J Gen Virol , vol.88 , pp. 13-18
    • Shin, Y.K.1    Liu, Q.2    Tikoo, S.K.3
  • 85
    • 33947381763 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses
    • Ehrhardt C, Wolff T, Pleschka S, et al. Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses. J Virol, 2007, 81: 3058-3067.
    • (2007) J Virol , vol.81 , pp. 3058-3067
    • Ehrhardt, C.1    Wolff, T.2    Pleschka, S.3
  • 86
    • 34250828457 scopus 로고    scopus 로고
    • Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling
    • Zhirnov O P, Klenk H D. Control of apoptosis in influenza virus-infected cells by up-regulation of Akt and p53 signaling. Apoptosis, 2007, 12: 1419-1432.
    • (2007) Apoptosis , vol.12 , pp. 1419-1432
    • Zhirnov, O.P.1    Klenk, H.D.2
  • 87
    • 77952701390 scopus 로고    scopus 로고
    • The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1
    • Lu X Y, Masic A, Li Y, et al. The PI3K/Akt pathway inhibits influenza A virus-induced Bax-mediated apoptosis by negatively regulating the JNK pathway via ASK1. J Gen Virol, 2010, 91: 1439-1449.
    • (2010) J Gen Virol , vol.91 , pp. 1439-1449
    • Lu, X.Y.1    Masic, A.2    Li, Y.3
  • 88
    • 65549130101 scopus 로고    scopus 로고
    • A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway
    • Ehrhardt C, Ludwig S. A new player in a deadly game: influenza viruses and the PI3K/Akt signalling pathway. Cell Microbiol, 2009, 11: 863-871.
    • (2009) Cell Microbiol , vol.11 , pp. 863-871
    • Ehrhardt, C.1    Ludwig, S.2
  • 89
    • 33745753573 scopus 로고    scopus 로고
    • Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence
    • Ehrhardt C, Marjuki H, Wolff T, et al. Bivalent role of the phosphatidylinositol-3-kinase (PI3K) during influenza virus infection and host cell defence. Cell Microbiol, 2006, 8: 1336-1348.
    • (2006) Cell Microbiol , vol.8 , pp. 1336-1348
    • Ehrhardt, C.1    Marjuki, H.2    Wolff, T.3
  • 90
    • 33847644660 scopus 로고    scopus 로고
    • Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation
    • Shin Y K, Liu Q, Tikoo S K, et al. Effect of the phosphatidylinositol 3-kinase/Akt pathway on influenza A virus propagation. J Gen Virol, 2007, 88: 942-950.
    • (2007) J Gen Virol , vol.88 , pp. 942-950
    • Shin, Y.K.1    Liu, Q.2    Tikoo, S.K.3
  • 91
    • 0034708454 scopus 로고    scopus 로고
    • Influenza virus-induced NF-kappaB-dependent gene expression is mediated by overexpression of viral proteins and involves oxidative radicals and activation of IkappaB kinase
    • Flory E, Kunz M, Scheller C, et al. Influenza virus-induced NF-kappaB-dependent gene expression is mediated by overexpression of viral proteins and involves oxidative radicals and activation of IkappaB kinase. J Biol Chem, 2000, 275: 8307-8314.
    • (2000) J Biol Chem , vol.275 , pp. 8307-8314
    • Flory, E.1    Kunz, M.2    Scheller, C.3
  • 92
    • 33847687659 scopus 로고    scopus 로고
    • Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity
    • Tenoever B R, Ng S L, Chua M A, et al. Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity. Science, 2007, 315: 1274-1278.
    • (2007) Science , vol.315 , pp. 1274-1278
    • Tenoever, B.R.1    Ng, S.L.2    Chua, M.A.3
  • 93
    • 0028797157 scopus 로고
    • Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B
    • Pahl H L, Baeuerle P A. Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B. J Virol, 1995, 69: 1480-1484.
    • (1995) J Virol , vol.69 , pp. 1480-1484
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 94
    • 0037975504 scopus 로고    scopus 로고
    • Double-stranded RNA induces the synthesis of specific chemokines by bronchial epithelial cells
    • Gern J E, French D A, Grindle K A, et al. Double-stranded RNA induces the synthesis of specific chemokines by bronchial epithelial cells. Am J Respir Cell Mol Biol, 2003, 28: 731-737.
    • (2003) Am J Respir Cell Mol Biol , vol.28 , pp. 731-737
    • Gern, J.E.1    French, D.A.2    Grindle, K.A.3
  • 95
    • 38449122497 scopus 로고    scopus 로고
    • TLR-mediated activation of type I IFN during antiviral immune responses: fighting the battle to win the war
    • Severa M, Fitzgerald K A. TLR-mediated activation of type I IFN during antiviral immune responses: fighting the battle to win the war. Curr Top Microbiol Immunol, 2007, 316: 167-192.
    • (2007) Curr Top Microbiol Immunol , vol.316 , pp. 167-192
    • Severa, M.1    Fitzgerald, K.A.2
  • 96
    • 4043118343 scopus 로고    scopus 로고
    • Active NF-kappaB signalling is a prerequisite for influenza virus infection
    • Nimmerjahn F, Dudziak D, Dirmeier U, et al. Active NF-kappaB signalling is a prerequisite for influenza virus infection. J Gen Virol, 2004, 85: 2347-2356.
    • (2004) J Gen Virol , vol.85 , pp. 2347-2356
    • Nimmerjahn, F.1    Dudziak, D.2    Dirmeier, U.3
  • 97
    • 53749106185 scopus 로고    scopus 로고
    • NF-kappaB signaling differentially regulates influenza virus RNA synthesis
    • Kumar N, Xin Z T, Liang Y, et al. NF-kappaB signaling differentially regulates influenza virus RNA synthesis. J Virol, 2008, 82: 9880-9889.
    • (2008) J Virol , vol.82 , pp. 9880-9889
    • Kumar, N.1    Xin, Z.T.2    Liang, Y.3
  • 98
    • 3843130838 scopus 로고    scopus 로고
    • NF-kappaB-dependent induction of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas/FasL is crucial for efficient influenza virus propagation
    • Wurzer W J, Ehrhardt C, Pleschka S, et al. NF-kappaB-dependent induction of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and Fas/FasL is crucial for efficient influenza virus propagation. J Biol Chem, 2004, 279: 30931-30937.
    • (2004) J Biol Chem , vol.279 , pp. 30931-30937
    • Wurzer, W.J.1    Ehrhardt, C.2    Pleschka, S.3
  • 99
    • 33748171464 scopus 로고    scopus 로고
    • The interferon-inducible RNA helicase, mda-5, is involved in measles virus-induced expression of antiviral cytokines
    • Berghall H, Siren J, Sarkar D, et al. The interferon-inducible RNA helicase, mda-5, is involved in measles virus-induced expression of antiviral cytokines. Microbes Infection, 2006, 8: 2138-2144.
    • (2006) Microbes Infection , vol.8 , pp. 2138-2144
    • Berghall, H.1    Siren, J.2    Sarkar, D.3
  • 100
    • 33846554134 scopus 로고    scopus 로고
    • Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells
    • Liu P, Jamaluddin M, Li K, et al. Retinoic acid-inducible gene I mediates early antiviral response and Toll-like receptor 3 expression in respiratory syncytial virus-infected airway epithelial cells. J Virol, 2007, 81: 1401-1411.
    • (2007) J Virol , vol.81 , pp. 1401-1411
    • Liu, P.1    Jamaluddin, M.2    Li, K.3
  • 101
    • 34548418935 scopus 로고    scopus 로고
    • Toll-like receptors, RIG-I-like RNA helicases and the antiviral innate immune response
    • Thompson A J, Locarnini S A. Toll-like receptors, RIG-I-like RNA helicases and the antiviral innate immune response. Immunol Cell Biol, 2007, 85: 435-445.
    • (2007) Immunol Cell Biol , vol.85 , pp. 435-445
    • Thompson, A.J.1    Locarnini, S.A.2
  • 102
    • 42149119018 scopus 로고    scopus 로고
    • Cutting edge: innate immune response triggered by influenza A virus is negatively regulated by SOCS1 and SOCS3 through a RIG-I/IFNAR1-dependent pathway
    • Pothlichet J, Chignard M, Si-Tahar M. Cutting edge: innate immune response triggered by influenza A virus is negatively regulated by SOCS1 and SOCS3 through a RIG-I/IFNAR1-dependent pathway. J Immunol, 2008, 180: 2034-2038.
    • (2008) J Immunol , vol.180 , pp. 2034-2038
    • Pothlichet, J.1    Chignard, M.2    Si-Tahar, M.3
  • 103
    • 40749162423 scopus 로고    scopus 로고
    • Cytosolic antiviral RNA recognition pathway activates caspases 1 and 3
    • Rintahaka J, Wiik D, Kovanen P E, et al. Cytosolic antiviral RNA recognition pathway activates caspases 1 and 3. J Immunol, 2008, 180: 1749-1757.
    • (2008) J Immunol , vol.180 , pp. 1749-1757
    • Rintahaka, J.1    Wiik, D.2    Kovanen, P.E.3
  • 104
    • 76749090540 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication
    • Karlas A, Machuy N, Shin Y, et al. Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication. Nature, 2010, 463: 818-822.
    • (2010) Nature , vol.463 , pp. 818-822
    • Karlas, A.1    Machuy, N.2    Shin, Y.3
  • 105
    • 76749108989 scopus 로고    scopus 로고
    • Human host factors required for influenza virus replication
    • Konig R, Stertz S, Zhou Y, et al. Human host factors required for influenza virus replication. Nature, 2010, 463: 813-817.
    • (2010) Nature , vol.463 , pp. 813-817
    • Konig, R.1    Stertz, S.2    Zhou, Y.3


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