메뉴 건너뛰기
Journal of Virology
Volumn 90, Issue 5, 2016, Pages 2403-2417
Hemagglutinin of influenza A virus antagonizes type I interferon (IFN) responses by inducing degradation of type I IFN receptor 1
Author keywords

[No Author keywords available]
Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; INTERFERON; INTERFERON RECEPTOR; STAT1 PROTEIN; STAT2 PROTEIN; TYPE I INTERFERON RECEPTOR 1; UNCLASSIFIED DRUG; ALPHA BETA INTERFERON RECEPTOR; IFNAR1 PROTEIN, HUMAN;
EID: 84961134192     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02749-15     Document Type: Article
Times cited : (73)
References (87)
  • 5
    • 51449086295 scopus 로고    scopus 로고
    • The biology of influenza viruses
    • Bouvier NM, Palese P. 2008. The biology of influenza viruses. Vaccine 26(Suppl 4):D49-D53. http://dx.doi.org/10.1016/j.vaccine.2008.07.039.
    • (2008) Vaccine , vol.26 , pp. D49-D53
    • Bouvier, N.M.1    Palese, P.2
  • 7
    • 65549113423 scopus 로고    scopus 로고
    • Influenza virus resistance to antiviral agents: a plea for rational use
    • Poland GA, Jacobson RM, Ovsyannikova IG. 2009. Influenza virus resistance to antiviral agents: a plea for rational use. Clin Infect Dis 48: 1254-1256. http://dx.doi.org/10.1086/598989.
    • (2009) Clin Infect Dis , vol.48 , pp. 1254-1256
    • Poland, G.A.1    Jacobson, R.M.2    Ovsyannikova, I.G.3
  • 9
    • 77956113383 scopus 로고    scopus 로고
    • Type I interferon modulates the battle of host immune system against viruses
    • Seo YJ, Hahm B. 2010. Type I interferon modulates the battle of host immune system against viruses. Adv Appl Microbiol 73:83-101. http://dx.doi.org/10.1016/S0065-2164(10)73004-5.
    • (2010) Adv Appl Microbiol , vol.73 , pp. 83-101
    • Seo, Y.J.1    Hahm, B.2
  • 10
    • 33748470359 scopus 로고    scopus 로고
    • Fifty years of interferon research: aiming at a moving target
    • Vilcek J. 2006. Fifty years of interferon research: aiming at a moving target. Immunity 25:343-348. http://dx.doi.org/10.1016/j.immuni.2006.08.008.
    • (2006) Immunity , vol.25 , pp. 343-348
    • Vilcek, J.1
  • 11
  • 12
    • 73949157600 scopus 로고    scopus 로고
    • Pandemic H1N1 2009 influenza A virus induces weak cytokine responses in human macrophages and dendritic cells and is highly sensitive to the antiviral actions of interferons
    • Osterlund P, Pirhonen J, Ikonen N, Ronkko E, Strengell M, Makela SM, Broman M, Hamming OJ, Hartmann R, Ziegler T, Julkunen I. 2010. Pandemic H1N1 2009 influenza A virus induces weak cytokine responses in human macrophages and dendritic cells and is highly sensitive to the antiviral actions of interferons. J Virol 84:1414-1422. http://dx.doi.org/10.1128/JVI.01619-09.
    • (2010) J Virol , vol.84 , pp. 1414-1422
    • Osterlund, P.1    Pirhonen, J.2    Ikonen, N.3    Ronkko, E.4    Strengell, M.5    Makela, S.M.6    Broman, M.7    Hamming, O.J.8    Hartmann, R.9    Ziegler, T.10    Julkunen, I.11
  • 13
    • 0036105482 scopus 로고    scopus 로고
    • The interferon antiviral response: from viral invasion to evasion
    • Grandvaux N, ten Oever BR, Servant MJ, Hiscott J. 2002. The interferon antiviral response: from viral invasion to evasion. Curr Opin Infect Dis 15:259-267. http://dx.doi.org/10.1097/00001432-200206000-00008.
    • (2002) Curr Opin Infect Dis , vol.15 , pp. 259-267
    • Grandvaux, N.1    ten Oever, B.R.2    Servant, M.J.3    Hiscott, J.4
  • 14
    • 81555200097 scopus 로고    scopus 로고
    • Induction and evasion of type I interferon responses by influenza viruses
    • Garcia-Sastre A. 2011. Induction and evasion of type I interferon responses by influenza viruses. Virus Res 162:12-18. http://dx.doi.org/10.1016/j.virusres.2011.10.017.
    • (2011) Virus Res , vol.162 , pp. 12-18
    • Garcia-Sastre, A.1
  • 15
    • 84959511733 scopus 로고    scopus 로고
    • Influenza virus activation of the interferon system
    • Killip MJ, Fodor E, Randall RE. 2015. Influenza virus activation of the interferon system. Virus Res 209:11-22. http://dx.doi.org/10.1016/j.virusres.2015.02.003.
    • (2015) Virus Res , vol.209 , pp. 11-22
    • Killip, M.J.1    Fodor, E.2    Randall, R.E.3
  • 16
    • 84908279593 scopus 로고    scopus 로고
    • Activation and regulation of pathogen sensor RIG-I
    • Patel JR, Garcia-Sastre A. 2014. Activation and regulation of pathogen sensor RIG-I. Cytokine Growth Factor Rev 25:513-523. http://dx.doi.org/10.1016/j.cytogfr.2014.08.005.
    • (2014) Cytokine Growth Factor Rev , vol.25 , pp. 513-523
    • Patel, J.R.1    Garcia-Sastre, A.2
  • 17
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I-and type-II-interferonmediated signalling
    • Platanias LC. 2005. Mechanisms of type-I-and type-II-interferonmediated signalling. Nat Rev Immunol 5:375-386. http://dx.doi.org/10.1038/nri1604.
    • (2005) Nat Rev Immunol , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 18
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE, Jr, Kerr IM, Stark GR. 1994. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415-1421. http://dx.doi.org/10.1126/science.8197455.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 19
    • 0037204953 scopus 로고    scopus 로고
    • A road map for those who don't know JAK-STAT
    • Aaronson DS, Horvath CM. 2002. A road map for those who don't know JAK-STAT. Science 296:1653-1655. http://dx.doi.org/10.1126/science.1071545.
    • (2002) Science , vol.296 , pp. 1653-1655
    • Aaronson, D.S.1    Horvath, C.M.2
  • 20
    • 84876100198 scopus 로고    scopus 로고
    • Hope and fear for interferon: the receptor-centric outlook on the future of interferon therapy
    • Fuchs SY. 2013. Hope and fear for interferon: the receptor-centric outlook on the future of interferon therapy. J Interferon Cytokine Res 33:211-225. http://dx.doi.org/10.1089/jir.2012.0117.
    • (2013) J Interferon Cytokine Res , vol.33 , pp. 211-225
    • Fuchs, S.Y.1
  • 21
    • 79251574143 scopus 로고    scopus 로고
    • Ligandstimulated downregulation of the alpha interferon receptor: role of protein kinase D2
    • Zheng H, Qian J, Varghese B, Baker DP, Fuchs S. 2011. Ligandstimulated downregulation of the alpha interferon receptor: role of protein kinase D2. Mol Cell Biol 31:710-720. http://dx.doi.org/10.1128/MCB.01154-10.
    • (2011) Mol Cell Biol , vol.31 , pp. 710-720
    • Zheng, H.1    Qian, J.2    Varghese, B.3    Baker, D.P.4    Fuchs, S.5
  • 22
    • 58249084172 scopus 로고    scopus 로고
    • Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor
    • Liu J, HuangFu WC, Kumar KG, Qian J, Casey JP, Hamanaka RB, Grigoriadou C, Aldabe R, Diehl JA, Fuchs SY. 2009. Virus-induced unfolded protein response attenuates antiviral defenses via phosphorylation-dependent degradation of the type I interferon receptor. Cell Host Microbe 5:72-83. http://dx.doi.org/10.1016/j.chom.2008.11.008.
    • (2009) Cell Host Microbe , vol.5 , pp. 72-83
    • Liu, J.1    HuangFu, W.C.2    Kumar, K.G.3    Qian, J.4    Casey, J.P.5    Hamanaka, R.B.6    Grigoriadou, C.7    Aldabe, R.8    Diehl, J.A.9    Fuchs, S.Y.10
  • 23
    • 79959855146 scopus 로고    scopus 로고
    • Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1
    • Qian J, Zheng H, Huangfu WC, Liu J, Carbone CJ, Leu NA, Baker DP, Fuchs SY. 2011. Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1. PLoS Pathog 7:e1002065. http://dx.doi.org/10.1371/journal.ppat.1002065.
    • (2011) PLoS Pathog , vol.7
    • Qian, J.1    Zheng, H.2    Huangfu, W.C.3    Liu, J.4    Carbone, C.J.5    Leu, N.A.6    Baker, D.P.7    Fuchs, S.Y.8
  • 25
    • 84873745999 scopus 로고    scopus 로고
    • Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins
    • Patel D, Schultz LW, Umland TC. 2013. Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins. Virus Res 172:75-80. http://dx.doi.org/10.1016/j.virusres.2012.12.003.
    • (2013) Virus Res , vol.172 , pp. 75-80
    • Patel, D.1    Schultz, L.W.2    Umland, T.C.3
  • 26
    • 84865095316 scopus 로고    scopus 로고
    • Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential
    • Varga ZT, Grant A, Manicassamy B, Palese P. 2012. Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potential. J Virol 86: 8359-8366. http://dx.doi.org/10.1128/JVI.01122-12.
    • (2012) J Virol , vol.86 , pp. 8359-8366
    • Varga, Z.T.1    Grant, A.2    Manicassamy, B.3    Palese, P.4
  • 27
    • 79959823372 scopus 로고    scopus 로고
    • The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein
    • Varga ZT, Ramos I, Hai R, Schmolke M, Garcia-Sastre A, Fernandez-Sesma A, Palese P. 2011. The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein. PLoS Pathog 7:e1002067. http://dx.doi.org/10.1371/journal.ppat.1002067.
    • (2011) PLoS Pathog , vol.7
    • Varga, Z.T.1    Ramos, I.2    Hai, R.3    Schmolke, M.4    Garcia-Sastre, A.5    Fernandez-Sesma, A.6    Palese, P.7
  • 28
    • 84906330873 scopus 로고    scopus 로고
    • Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I
    • Li W, Chen H, Sutton T, Obadan A, Perez DR. 2014. Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I. J Virol 88:10432-10447. http://dx.doi.org/10.1128/JVI.01383-14.
    • (2014) J Virol , vol.88 , pp. 10432-10447
    • Li, W.1    Chen, H.2    Sutton, T.3    Obadan, A.4    Perez, D.R.5
  • 29
    • 77956634918 scopus 로고    scopus 로고
    • The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon
    • Graef KM, Vreede FT, Lau YF, McCall AW, Carr SM, Subbarao K, Fodor E. 2010. The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon. J Virol 84:8433-8445. http://dx.doi.org/10.1128/JVI.00879-10.
    • (2010) J Virol , vol.84 , pp. 8433-8445
    • Graef, K.M.1    Vreede, F.T.2    Lau, Y.F.3    McCall, A.W.4    Carr, S.M.5    Subbarao, K.6    Fodor, E.7
  • 35
    • 77954967774 scopus 로고    scopus 로고
    • Sphingosine 1-phosphatemetabolizing enzymes control influenza virus propagation and viral cytopathogenicity
    • Seo YJ, Blake C, Alexander S, Hahm B. 2010. Sphingosine 1-phosphatemetabolizing enzymes control influenza virus propagation and viral cytopathogenicity. J Virol 84:8124-8131. http://dx.doi.org/10.1128/JVI.00510-10.
    • (2010) J Virol , vol.84 , pp. 8124-8131
    • Seo, Y.J.1    Blake, C.2    Alexander, S.3    Hahm, B.4
  • 36
    • 84883313477 scopus 로고    scopus 로고
    • Sphingosine kinase 1 serves as a pro-viral factor by regulating viral RNA synthesis and nuclear export of viral ribonucleoprotein complex upon influenza virus infection
    • Seo YJ, Pritzl CJ, Vijayan M, Bomb K, McClain ME, Alexander S, Hahm B. 2013. Sphingosine kinase 1 serves as a pro-viral factor by regulating viral RNA synthesis and nuclear export of viral ribonucleoprotein complex upon influenza virus infection. PLoS One 8:e75005. http://dx.doi.org/10.1371/journal.pone.0075005.
    • (2013) PLoS One , vol.8
    • Seo, Y.J.1    Pritzl, C.J.2    Vijayan, M.3    Bomb, K.4    McClain, M.E.5    Alexander, S.6    Hahm, B.7
  • 37
    • 0015862870 scopus 로고
    • Proteolytic cleavage by plasmin of theHApolypeptide of influenza virus: host cell activation of serum plasminogen
    • Lazarowitz SG, Goldberg AR, Choppin PW. 1973. Proteolytic cleavage by plasmin of theHApolypeptide of influenza virus: host cell activation of serum plasminogen. Virology 56:172-180. http://dx.doi.org/10.1016/0042-6822(73)90296-1.
    • (1973) Virology , vol.56 , pp. 172-180
    • Lazarowitz, S.G.1    Goldberg, A.R.2    Choppin, P.W.3
  • 38
    • 77956634502 scopus 로고    scopus 로고
    • Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virus
    • Sun X, Tse LV, Ferguson AD, Whittaker GR. 2010. Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virus. J Virol 84:8683-8690. http://dx.doi.org/10.1128/JVI.00797-10.
    • (2010) J Virol , vol.84 , pp. 8683-8690
    • Sun, X.1    Tse, L.V.2    Ferguson, A.D.3    Whittaker, G.R.4
  • 39
    • 84890850726 scopus 로고    scopus 로고
    • Sphingosine kinase 1 regulates measles virus replication
    • Vijayan M, Seo YJ, Pritzl CJ, Squires SA, Alexander S, Hahm B. 2014. Sphingosine kinase 1 regulates measles virus replication. Virology 450-451:55-63. http://dx.doi.org/10.1016/j.virol.2013.11.039.
    • (2014) Virology , vol.450-451 , pp. 55-63
    • Vijayan, M.1    Seo, Y.J.2    Pritzl, C.J.3    Squires, S.A.4    Alexander, S.5    Hahm, B.6
  • 40
    • 73349141113 scopus 로고    scopus 로고
    • Essential and synergistic roles of IL1 and IL6 in human Th17 differentiation directed by TLR ligand-activated dendritic cells
    • Benwell RK, Lee DR. 2010. Essential and synergistic roles of IL1 and IL6 in human Th17 differentiation directed by TLR ligand-activated dendritic cells. Clin Immunol 134:178-187. http://dx.doi.org/10.1016/j.clim.2009.09.013.
    • (2010) Clin Immunol , vol.134 , pp. 178-187
    • Benwell, R.K.1    Lee, D.R.2
  • 42
    • 49649111204 scopus 로고    scopus 로고
    • Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif
    • Kumar KG, Varghese B, Banerjee A, Baker DP, Constantinescu SN, Pellegrini S, Fuchs SY. 2008. Basal ubiquitin-independent internalization of interferon alpha receptor is prevented by Tyk2-mediated masking of a linear endocytic motif. J Biol Chem 283:18566-18572. http://dx.doi.org/10.1074/jbc.M800991200.
    • (2008) J Biol Chem , vol.283 , pp. 18566-18572
    • Kumar, K.G.1    Varghese, B.2    Banerjee, A.3    Baker, D.P.4    Constantinescu, S.N.5    Pellegrini, S.6    Fuchs, S.Y.7
  • 43
    • 8744247500 scopus 로고    scopus 로고
    • Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor
    • Kumar KG, Krolewski JJ, Fuchs SY. 2004. Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor. J Biol Chem 279:46614-46620. http://dx.doi.org/10.1074/jbc.M407082200.
    • (2004) J Biol Chem , vol.279 , pp. 46614-46620
    • Kumar, K.G.1    Krolewski, J.J.2    Fuchs, S.Y.3
  • 44
    • 82755166980 scopus 로고    scopus 로고
    • Modulation of phototropic responsiveness in Arabidopsis through ubiquitination of phototropin 1 by the CUL3-Ring E3 ubiquitin ligase CRL3(NPH3)
    • Roberts D, Pedmale UV, Morrow J, Sachdev S, Lechner E, Tang X, Zheng N, Hannink M, Genschik P, Liscum E. 2011. Modulation of phototropic responsiveness in Arabidopsis through ubiquitination of phototropin 1 by the CUL3-Ring E3 ubiquitin ligase CRL3(NPH3). Plant Cell 23:3627-3640. http://dx.doi.org/10.1105/tpc.111.087999.
    • (2011) Plant Cell , vol.23 , pp. 3627-3640
    • Roberts, D.1    Pedmale, U.V.2    Morrow, J.3    Sachdev, S.4    Lechner, E.5    Tang, X.6    Zheng, N.7    Hannink, M.8    Genschik, P.9    Liscum, E.10
  • 45
    • 45749084541 scopus 로고    scopus 로고
    • Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus
    • Wei CJ, Xu L, Kong WP, Shi W, Canis K, Stevens J, Yang ZY, Dell A, Haslam SM, Wilson IA, Nabel GJ. 2008. Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus. J Virol 82:6200-6208. http://dx.doi.org/10.1128/JVI.00187-08.
    • (2008) J Virol , vol.82 , pp. 6200-6208
    • Wei, C.J.1    Xu, L.2    Kong, W.P.3    Shi, W.4    Canis, K.5    Stevens, J.6    Yang, Z.Y.7    Dell, A.8    Haslam, S.M.9    Wilson, I.A.10    Nabel, G.J.11
  • 46
    • 34547886820 scopus 로고    scopus 로고
    • Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity
    • Yang ZY, Wei CJ, Kong WP, Wu L, Xu L, Smith DF, Nabel GJ. 2007. Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity. Science 317:825-828. http://dx.doi.org/10.1126/science.1135165.
    • (2007) Science , vol.317 , pp. 825-828
    • Yang, Z.Y.1    Wei, C.J.2    Kong, W.P.3    Wu, L.4    Xu, L.5    Smith, D.F.6    Nabel, G.J.7
  • 48
    • 84925325088 scopus 로고    scopus 로고
    • The cytoplasmic domain of a disintegrin and metalloproteinase 10 (ADAM10) regulates its constitutive activity but is dispensable for stimulated ADAM10-dependent shedding
    • Maretzky T, Evers A, Le Gall S, Alabi RO, Speck N, Reiss K, Blobel CP. 2015. The cytoplasmic domain of a disintegrin and metalloproteinase 10 (ADAM10) regulates its constitutive activity but is dispensable for stimulated ADAM10-dependent shedding. J Biol Chem 290:7416-7425. http://dx.doi.org/10.1074/jbc.M114.603753.
    • (2015) J Biol Chem , vol.290 , pp. 7416-7425
    • Maretzky, T.1    Evers, A.2    Le Gall, S.3    Alabi, R.O.4    Speck, N.5    Reiss, K.6    Blobel, C.P.7
  • 49
    • 84930620010 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor interacting protein targets IRF7 to suppress antiviral signaling and the induction of type I interferon
    • Zhou Q, Lavorgna A, Bowman M, Hiscott J, Harhaj EW. 2015. Aryl hydrocarbon receptor interacting protein targets IRF7 to suppress antiviral signaling and the induction of type I interferon. J Biol Chem 290: 14729-14739. http://dx.doi.org/10.1074/jbc.M114.633065.
    • (2015) J Biol Chem , vol.290 , pp. 14729-14739
    • Zhou, Q.1    Lavorgna, A.2    Bowman, M.3    Hiscott, J.4    Harhaj, E.W.5
  • 50
    • 84928485431 scopus 로고    scopus 로고
    • A ceramide analogue stimulates dendritic cells to promote T cell responses upon virus infections
    • Pritzl CJ, Seo YJ, Xia C, Vijayan M, Stokes ZD, Hahm B. 2015. A ceramide analogue stimulates dendritic cells to promote T cell responses upon virus infections. J Immunol 194:4339-4349. http://dx.doi.org/10.4049/jimmunol.1402672.
    • (2015) J Immunol , vol.194 , pp. 4339-4349
    • Pritzl, C.J.1    Seo, Y.J.2    Xia, C.3    Vijayan, M.4    Stokes, Z.D.5    Hahm, B.6
  • 52
    • 80053906125 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase D2 mediates ligand-inducible elimination of the type 1 interferon receptor
    • Zheng H, Qian J, Baker DP, Fuchs SY. 2011. Tyrosine phosphorylation of protein kinase D2 mediates ligand-inducible elimination of the type 1 interferon receptor. J Biol Chem 286:35733-35741. http://dx.doi.org/10.1074/jbc.M111.263608.
    • (2011) J Biol Chem , vol.286 , pp. 35733-35741
    • Zheng, H.1    Qian, J.2    Baker, D.P.3    Fuchs, S.Y.4
  • 54
    • 73849105294 scopus 로고    scopus 로고
    • Adeno-associated virus small rep proteins are modified with at least two types of polyubiquitination
    • Farris KD, Fasina O, Sukhu L, Li L, Pintel DJ. 2010. Adeno-associated virus small rep proteins are modified with at least two types of polyubiquitination. J Virol 84:1206-1211. http://dx.doi.org/10.1128/JVI.01660-09.
    • (2010) J Virol , vol.84 , pp. 1206-1211
    • Farris, K.D.1    Fasina, O.2    Sukhu, L.3    Li, L.4    Pintel, D.J.5
  • 55
    • 0142105396 scopus 로고    scopus 로고
    • SCF(HOS) ubiquitin ligase mediates the ligand-induced downregulation of the interferon-alpha receptor
    • Kumar KG, Tang W, Ravindranath AK, Clark WA, Croze E, Fuchs SY. 2003. SCF(HOS) ubiquitin ligase mediates the ligand-induced downregulation of the interferon-alpha receptor. EMBO J 22:5480-5490. http://dx.doi.org/10.1093/emboj/cdg524.
    • (2003) EMBO J , vol.22 , pp. 5480-5490
    • Kumar, K.G.1    Tang, W.2    Ravindranath, A.K.3    Clark, W.A.4    Croze, E.5    Fuchs, S.Y.6
  • 57
    • 77956044811 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system affects influenzaAvirus infection at a postfusion step
    • Widjaja I, de Vries E, Tscherne DM, Garcia-Sastre A, Rottier PJ, de Haan CA. 2010. Inhibition of the ubiquitin-proteasome system affects influenzaAvirus infection at a postfusion step. J Virol 84:9625-9631. http://dx.doi.org/10.1128/JVI.01048-10.
    • (2010) J Virol , vol.84 , pp. 9625-9631
    • Widjaja, I.1    de Vries, E.2    Tscherne, D.M.3    Garcia-Sastre, A.4    Rottier, P.J.5    de Haan, C.A.6
  • 58
    • 84920956725 scopus 로고    scopus 로고
    • The NS1 protein: a multitasking virulence factor
    • Ayllon J, Garcia-Sastre A. 2015. The NS1 protein: a multitasking virulence factor. Curr Top Microbiol Immunol 386:73-107. http://dx.doi.org/10.1007/82_2014_400.
    • (2015) Curr Top Microbiol Immunol , vol.386 , pp. 73-107
    • Ayllon, J.1    Garcia-Sastre, A.2
  • 59
    • 84905660674 scopus 로고    scopus 로고
    • ER stress, autophagy, and RNA viruses
    • Jheng JR, Ho JY, Horng JT. 2014. ER stress, autophagy, and RNA viruses. Front Microbiol 5:388. http://dx.doi.org/10.3389/fmicb.2014.00388.
    • (2014) Front Microbiol , vol.5 , pp. 388
    • Jheng, J.R.1    Ho, J.Y.2    Horng, J.T.3
  • 60
    • 0037415720 scopus 로고    scopus 로고
    • The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression
    • Ragimbeau J, Dondi E, Alcover A, Eid P, Uze G, Pellegrini S. 2003. The tyrosine kinase Tyk2 controls IFNAR1 cell surface expression. EMBO J 22:537-547. http://dx.doi.org/10.1093/emboj/cdg038.
    • (2003) EMBO J , vol.22 , pp. 537-547
    • Ragimbeau, J.1    Dondi, E.2    Alcover, A.3    Eid, P.4    Uze, G.5    Pellegrini, S.6
  • 62
    • 79959332082 scopus 로고    scopus 로고
    • Role of p38 protein kinase in the ligand-independent ubiquitination and down-regulation of the IFNAR1 chain of type I interferon receptor
    • Bhattacharya S, Qian J, Tzimas C, Baker DP, Koumenis C, Diehl JA, Fuchs SY. 2011. Role of p38 protein kinase in the ligand-independent ubiquitination and down-regulation of the IFNAR1 chain of type I interferon receptor. J Biol Chem 286:22069-22076. http://dx.doi.org/10.1074/jbc.M111.238766.
    • (2011) J Biol Chem , vol.286 , pp. 22069-22076
    • Bhattacharya, S.1    Qian, J.2    Tzimas, C.3    Baker, D.P.4    Koumenis, C.5    Diehl, J.A.6    Fuchs, S.Y.7
  • 63
    • 84888029430 scopus 로고    scopus 로고
    • Influenza A virus proteins NS1 and hemagglutinin along with M2 are involved in stimulation of autophagy in infected cells
    • Zhirnov OP, Klenk HD. 2013. Influenza A virus proteins NS1 and hemagglutinin along with M2 are involved in stimulation of autophagy in infected cells. J Virol 87:13107-13114. http://dx.doi.org/10.1128/JVI.02148-13.
    • (2013) J Virol , vol.87 , pp. 13107-13114
    • Zhirnov, O.P.1    Klenk, H.D.2
  • 66
    • 33646478272 scopus 로고    scopus 로고
    • The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway
    • Min JY, Krug RM. 2006. The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway. Proc Natl Acad Sci U S A 103:7100-7105. http://dx.doi.org/10.1073/pnas.0602184103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7100-7105
    • Min, J.Y.1    Krug, R.M.2
  • 67
    • 84910684859 scopus 로고    scopus 로고
    • Influenza virus non-structural protein NS1: interferon antagonism and beyond
    • Marc D. 2014. Influenza virus non-structural protein NS1: interferon antagonism and beyond. J Gen Virol 95:2594-2611. http://dx.doi.org/10.1099/vir.0.069542-0.
    • (2014) J Gen Virol , vol.95 , pp. 2594-2611
    • Marc, D.1
  • 68
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan W, Krug RM. 2001. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J 20:362-371. http://dx.doi.org/10.1093/emboj/20.3.362.
    • (2001) EMBO J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 69
    • 0037864215 scopus 로고    scopus 로고
    • Measles virus V protein blocks interferon (IFN)-alpha/beta but not IFNgamma signaling by inhibiting STAT1 and STAT2 phosphorylation
    • Takeuchi K, Kadota SI, Takeda M, Miyajima N, Nagata K. 2003. Measles virus V protein blocks interferon (IFN)-alpha/beta but not IFNgamma signaling by inhibiting STAT1 and STAT2 phosphorylation. FEBS Lett 545:177-182. http://dx.doi.org/10.1016/S0014-5793(03)00528-3.
    • (2003) FEBS Lett , vol.545 , pp. 177-182
    • Takeuchi, K.1    Kadota, S.I.2    Takeda, M.3    Miyajima, N.4    Nagata, K.5
  • 70
    • 57149103678 scopus 로고    scopus 로고
    • Inhibition of IFN-alpha/beta signaling by two discrete peptides within measles virus V protein that specifically bind STAT1 and STAT2
    • Caignard G, Bourai M, Jacob Y, Infection MAPping Project I-MAP, Tangy F, Vidalain PO. 2009. Inhibition of IFN-alpha/beta signaling by two discrete peptides within measles virus V protein that specifically bind STAT1 and STAT2. Virology 383:112-120. http://dx.doi.org/10.1016/j.virol.2008.10.014.
    • (2009) Virology , vol.383 , pp. 112-120
    • Caignard, G.1    Bourai, M.2    Jacob, Y.3    Tangy, F.4    Vidalain, P.O.5
  • 71
    • 0037196382 scopus 로고    scopus 로고
    • Sendai virus C protein impairs both phosphorylation and dephosphorylation processes of Stat1
    • Komatsu T, Takeuchi K, Yokoo J, Gotoh B. 2002. Sendai virus C protein impairs both phosphorylation and dephosphorylation processes of Stat1. FEBS Lett 511:139-144. http://dx.doi.org/10.1016/S0014-5793(01)03301-4.
    • (2002) FEBS Lett , vol.511 , pp. 139-144
    • Komatsu, T.1    Takeuchi, K.2    Yokoo, J.3    Gotoh, B.4
  • 72
    • 2942538463 scopus 로고    scopus 로고
    • Inhibition of the gamma interferon response by a Sendai virus C protein mutant with no STAT1-binding ability
    • Gotoh B, Takeuchi K, Komatsu T. 2004. Inhibition of the gamma interferon response by a Sendai virus C protein mutant with no STAT1-binding ability. FEBS Lett 567:291-296. http://dx.doi.org/10.1016/j.febslet.2004.05.001.
    • (2004) FEBS Lett , vol.567 , pp. 291-296
    • Gotoh, B.1    Takeuchi, K.2    Komatsu, T.3
  • 73
    • 0037334497 scopus 로고    scopus 로고
    • The STAT2 activation process is a crucial target of Sendai virus C protein for the blockade of alpha interferon signaling
    • Gotoh B, Takeuchi K, Komatsu T, Yokoo J. 2003. The STAT2 activation process is a crucial target of Sendai virus C protein for the blockade of alpha interferon signaling. J Virol 77:3360-3370. http://dx.doi.org/10.1128/JVI.77.6.3360-3370.2003.
    • (2003) J Virol , vol.77 , pp. 3360-3370
    • Gotoh, B.1    Takeuchi, K.2    Komatsu, T.3    Yokoo, J.4
  • 74
    • 0142060816 scopus 로고    scopus 로고
    • Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation
    • Rodriguez JJ, Wang LF, Horvath CM. 2003. Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation. J Virol 77:11842-11845. http://dx.doi.org/10.1128/JVI.77.21.11842-11845.2003.
    • (2003) J Virol , vol.77 , pp. 11842-11845
    • Rodriguez, J.J.1    Wang, L.F.2    Horvath, C.M.3
  • 75
    • 1942496600 scopus 로고    scopus 로고
    • Identification of the nuclear export signal and STAT-binding domains of the Nipah virus V protein reveals mechanisms underlying interferon evasion
    • Rodriguez JJ, Cruz CD, Horvath CM. 2004. Identification of the nuclear export signal and STAT-binding domains of the Nipah virus V protein reveals mechanisms underlying interferon evasion. J Virol 78:5358-5367. http://dx.doi.org/10.1128/JVI.78.10.5358-5367.2004.
    • (2004) J Virol , vol.78 , pp. 5358-5367
    • Rodriguez, J.J.1    Cruz, C.D.2    Horvath, C.M.3
  • 76
    • 84863149924 scopus 로고    scopus 로고
    • Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway
    • Hassan IH, Zhang MS, Powers LS, Shao JQ, Baltrusaitis J, Rutkowski DT, Legge K, Monick MM. 2012. Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J Biol Chem 287:4679-4689. http://dx.doi.org/10.1074/jbc.M111.284695.
    • (2012) J Biol Chem , vol.287 , pp. 4679-4689
    • Hassan, I.H.1    Zhang, M.S.2    Powers, L.S.3    Shao, J.Q.4    Baltrusaitis, J.5    Rutkowski, D.T.6    Legge, K.7    Monick, M.M.8
  • 77
    • 70449110086 scopus 로고    scopus 로고
    • The EBV-encoded latent membrane proteins, LMP2A and LMP2B, limit the actions of interferon by targeting interferon receptors for degradation
    • Shah KM, Stewart SE, Wei W, Woodman CB, O'Neil JD, Dawson CW, Young LS. 2009. The EBV-encoded latent membrane proteins, LMP2A and LMP2B, limit the actions of interferon by targeting interferon receptors for degradation. Oncogene 28:3903-3914. http://dx.doi.org/10.1038/onc.2009.249.
    • (2009) Oncogene , vol.28 , pp. 3903-3914
    • Shah, K.M.1    Stewart, S.E.2    Wei, W.3    Woodman, C.B.4    O'Neil, J.D.5    Dawson, C.W.6    Young, L.S.7
  • 78
    • 20444447772 scopus 로고    scopus 로고
    • Functional cartography of the ectodomain of the type I interferon receptor subunit ifnar1
    • Lamken P, Gavutis M, Peters I, Van der Heyden J, Uze G, Piehler J. 2005. Functional cartography of the ectodomain of the type I interferon receptor subunit ifnar1. J Mol Biol 350:476-488. http://dx.doi.org/10.1016/j.jmb.2005.05.008.
    • (2005) J Mol Biol , vol.350 , pp. 476-488
    • Lamken, P.1    Gavutis, M.2    Peters, I.3    Van der Heyden, J.4    Uze, G.5    Piehler, J.6
  • 79
    • 69949120819 scopus 로고    scopus 로고
    • Palmitoylation of interferonalpha (IFN-alpha) receptor subunit IFNAR1 is required for the activation of Stat1 and Stat2 by IFN-alpha
    • Claudinon J, Gonnord P, Beslard E, Marchetti M, Mitchell K, Boularan C, Johannes L, Eid P, Lamaze C. 2009. Palmitoylation of interferonalpha (IFN-alpha) receptor subunit IFNAR1 is required for the activation of Stat1 and Stat2 by IFN-alpha. J Biol Chem 284:24328-24340. http://dx.doi.org/10.1074/jbc.M109.021915.
    • (2009) J Biol Chem , vol.284 , pp. 24328-24340
    • Claudinon, J.1    Gonnord, P.2    Beslard, E.3    Marchetti, M.4    Mitchell, K.5    Boularan, C.6    Johannes, L.7    Eid, P.8    Lamaze, C.9
  • 80
    • 0034608951 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display ofMHCclass I chains by enhancing their endocytosis
    • Coscoy L, Ganem D. 2000. Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display ofMHCclass I chains by enhancing their endocytosis. Proc Natl Acad Sci U S A 97:8051-8056. http://dx.doi.org/10.1073/pnas.140129797.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8051-8056
    • Coscoy, L.1    Ganem, D.2
  • 81
    • 0034748469 scopus 로고    scopus 로고
    • MHC class I ubiquitination by a viral PHD/LAP finger protein
    • Boname JM, Stevenson PG. 2001. MHC class I ubiquitination by a viral PHD/LAP finger protein. Immunity 15:627-636. http://dx.doi.org/10.1016/S1074-7613(01)00213-8.
    • (2001) Immunity , vol.15 , pp. 627-636
    • Boname, J.M.1    Stevenson, P.G.2
  • 82
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat B, Gers-Huber G, Lehmann M, Zufferey M, Luban J, Piguet V. 2009. HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog 5:e1000574. http://dx.doi.org/10.1371/journal.ppat.1000574.
    • (2009) PLoS Pathog , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 83
    • 84861209115 scopus 로고    scopus 로고
    • A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction
    • Kueck T, Neil SJ. 2012. A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction. PLoS Pathog 8:e1002609. http://dx.doi.org/10.1371/journal.ppat.1002609.
    • (2012) PLoS Pathog , vol.8
    • Kueck, T.1    Neil, S.J.2
  • 84
    • 84864585610 scopus 로고    scopus 로고
    • N-linked glycosylation in the hemagglutinin of influenza A viruses
    • Kim JI, Park MS. 2012. N-linked glycosylation in the hemagglutinin of influenza A viruses. Yonsei Med J 53:886-893. http://dx.doi.org/10.3349/ymj.2012.53.5.886.
    • (2012) Yonsei Med J , vol.53 , pp. 886-893
    • Kim, J.I.1    Park, M.S.2
  • 85
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman JS, Lamb RA. 2011. Influenza virus assembly and budding. Virology 411:229-236. http://dx.doi.org/10.1016/j.virol.2010.12.003.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 86
    • 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 MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S. 2006. 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 281: 16707-16715. http://dx.doi.org/10.1074/jbc.M510233200.
    • (2006) J Biol Chem , vol.281 , pp. 16707-16715
    • Marjuki, H.1    Alam, M.I.2    Ehrhardt, C.3    Wagner, R.4    Planz, O.5    Klenk, H.D.6    Ludwig, S.7    Pleschka, S.8
  • 87
    • 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 HL, Franks J, Webster RG, Pleschka S, Hoffmann E. 2007. Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade. Virol J 4:134. http://dx.doi.org/10.1186/1743-422X-4-134.
    • (2007) Virol J , vol.4 , pp. 134
    • Marjuki, H.1    Yen, H.L.2    Franks, J.3    Webster, R.G.4    Pleschka, S.5    Hoffmann, E.6

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.