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Volumn 85, Issue 17, 2011, Pages 8569-8581

Comprehensive proteomic analysis of influenza virus polymerase complex reveals a novel association with mitochondrial proteins and RNA polymerase accessory factors

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; APOPTOSIS INDUCING FACTOR; DNA DIRECTED RNA POLYMERASE; EPIDERMAL GROWTH FACTOR RECEPTOR; KARYOPHERIN ALPHA; MITOCHONDRIAL PROTEIN; RNA DIRECTED RNA POLYMERASE; RNA POLYMERASE; RNA POLYMERASE II; SIALIDASE; TRANSACTIVATOR PROTEIN;

EID: 80052274996     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00496-11     Document Type: Article
Times cited : (93)

References (70)
  • 1
    • 0142060863 scopus 로고    scopus 로고
    • Expression of the zinc-finger antiviral protein inhibits alphavirus replication
    • Bick, M. J., et al. 2003. Expression of the zinc-finger antiviral protein inhibits alphavirus replication. J. Virol. 77:11555-11562.
    • (2003) J. Virol. , vol.77 , pp. 11555-11562
    • Bick, M.J.1
  • 2
    • 58149388469 scopus 로고    scopus 로고
    • The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit
    • Bradel-Tretheway, B. G., et al. 2008. The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit. J. Gen. Virol. 89:2923-2932.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2923-2932
    • Bradel-Tretheway, B.G.1
  • 3
    • 70349193390 scopus 로고    scopus 로고
    • Identification of gemin5 as a novel 7-methylguanosine cap-binding protein
    • Bradrick, S. S., and M. Gromeier. 2009. Identification of gemin5 as a novel 7-methylguanosine cap-binding protein. PLoS One 4:e7030.
    • (2009) PLoS One , vol.4
    • Bradrick, S.S.1    Gromeier, M.2
  • 4
    • 72549116887 scopus 로고    scopus 로고
    • The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus
    • Brass, A. L., et al. 2009. The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus. Cell 139:1243-1254.
    • (2009) Cell , vol.139 , pp. 1243-1254
    • Brass, A.L.1
  • 5
    • 77950835010 scopus 로고    scopus 로고
    • PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells
    • Bussey, K. A., T. L. Bousse, E. A. Desmet, B. Kim, and T. Takimoto. 2010. PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells. J. Virol. 84:4395-4406.
    • (2010) J. Virol. , vol.84 , pp. 4395-4406
    • Bussey, K.A.1    Bousse, T.L.2    Desmet, E.A.3    Kim, B.4    Takimoto, T.5
  • 6
    • 30044445273 scopus 로고    scopus 로고
    • Characterization of a mitochondrial-targeting signal in the PB2 protein of influenza viruses
    • Carr, S. M., E. Carnero, A. Garcia-Sastre, G. G. Brownlee, and E. Fodor. 2006. Characterization of a mitochondrial-targeting signal in the PB2 protein of influenza viruses. Virology 344:492-508.
    • (2006) Virology , vol.344 , pp. 492-508
    • Carr, S.M.1    Carnero, E.2    Garcia-Sastre, A.3    Brownlee, G.G.4    Fodor, E.5
  • 7
    • 47049088602 scopus 로고    scopus 로고
    • The hepatitis E virus ORF3 protein modulates epidermal growth factor receptor trafficking, STAT3 translocation, and the acute-phase response
    • Chandra, V., A. Kar-Roy, S. Kumari, S. Mayor, and S. Jameel. 2008. The hepatitis E virus ORF3 protein modulates epidermal growth factor receptor trafficking, STAT3 translocation, and the acute-phase response. J. Virol. 82:7100-7110.
    • (2008) J. Virol. , vol.82 , pp. 7100-7110
    • Chandra, V.1    Kar-Roy, A.2    Kumari, S.3    Mayor, S.4    Jameel, S.5
  • 8
    • 77956826339 scopus 로고    scopus 로고
    • Differential localization and function of PB1-F2 derived from different strains of influenza A virus
    • Chen, C. J., et al. 2010. Differential localization and function of PB1-F2 derived from different strains of influenza A virus. J. Virol. 84:10051-10062.
    • (2010) J. Virol. , vol.84 , pp. 10051-10062
    • Chen, C.J.1
  • 9
    • 0035658084 scopus 로고    scopus 로고
    • A novel influenza A virus mitochondrial protein that induces cell death
    • Chen, W., et al. 2001. A novel influenza A virus mitochondrial protein that induces cell death. Nat. Med. 7:1306-1312.
    • (2001) Nat. Med. , vol.7 , pp. 1306-1312
    • Chen, W.1
  • 10
    • 33845406669 scopus 로고    scopus 로고
    • Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex
    • Deng, T., et al. 2006. Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex. J. Virol. 80: 11911-11919.
    • (2006) J. Virol. , vol.80 , pp. 11911-11919
    • Deng, T.1
  • 11
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff, T., E. R. Hrincius, U. Rescher, S. Ludwig, and C. Ehrhardt. 2010. The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog. 6:e1001099.
    • (2010) PLoS Pathog , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 12
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt, O. G., M. Smith, and E. Fodor. 2005. Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II. J. Virol. 79:5812-5818.
    • (2005) J. Virol. , vol.79 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 13
    • 0033152610 scopus 로고    scopus 로고
    • Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro
    • Falcon, A. M., P. Fortes, R.M. Marion, A. Beloso, and J. Ortin. 1999. Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro. Nucleic Acids Res. 27:2241-2247.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2241-2247
    • Falcon, A.M.1    Fortes, P.2    Marion, R.M.3    Beloso, A.4    Ortin, J.5
  • 14
    • 77956643301 scopus 로고    scopus 로고
    • Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT
    • Fislova, T., B. Thomas, K. M. Graef, and E. Fodor. 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
  • 15
    • 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
    • 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.
    • (2002) J. Virol. , vol.76 , pp. 8989-9001
    • Fodor, E.1
  • 16
    • 0037383156 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase promotes the generation of defective interfering RNAs
    • Fodor, E., L. J. Mingay, M. Crow, T. Deng, and G. G. Brownlee. 2003. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase promotes the generation of defective interfering RNAs. J. Virol. 77:5017-5020.
    • (2003) J. Virol. , vol.77 , pp. 5017-5020
    • Fodor, E.1    Mingay, L.J.2    Crow, M.3    Deng, T.4    Brownlee, G.G.5
  • 17
    • 40349113426 scopus 로고    scopus 로고
    • Interaction of polymerase subunit PB2 and NP with importin1 is a determinant of host range of influenza A virus
    • Gabriel, G., A. Herwig, and H. D. Klenk. 2008. Interaction of polymerase subunit PB2 and NP with importin 1 is a determinant of host range of influenza A virus. PLoS Pathog. 4:e11.
    • (2008) PLoS Pathog , vol.4
    • Gabriel, G.1    Herwig, A.2    Klenk, H.D.3
  • 18
    • 78751622104 scopus 로고    scopus 로고
    • Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus
    • Gabriel, G., et al. 2011. Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus. Nat. Commun. 2:156.
    • (2011) Nat. Commun. , vol.2 , pp. 156
    • Gabriel, G.1
  • 19
    • 0037031709 scopus 로고    scopus 로고
    • Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein
    • Gao, G., X. Guo, and S. P. Goff. 2002. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science 297:1703-1706.
    • (2002) Science , vol.297 , pp. 1703-1706
    • Gao, G.1    Guo, X.2    Goff, S.P.3
  • 20
    • 0033169059 scopus 로고    scopus 로고
    • Distinct regions of influenza virus PB1 polymerase subunit recognize vRNA and cRNA templates
    • Gonzalez, S., and J. Ortin. 1999. Distinct regions of influenza virus PB1 polymerase subunit recognize vRNA and cRNA templates. EMBO J. 18: 3767-3775.
    • (1999) EMBO J , vol.18 , pp. 3767-3775
    • Gonzalez, S.1    Ortin, J.2
  • 21
    • 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, K. M., et al. 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.
    • (2010) J. Virol. , vol.84 , pp. 8433-8445
    • Graef, K.M.1
  • 22
    • 49649127852 scopus 로고    scopus 로고
    • Drosophila RNAi screen identifies host genes important for influenza virus replication
    • Hao, L., et al. 2008. Drosophila RNAi screen identifies host genes important for influenza virus replication. Nature 454:890-893.
    • (2008) Nature , vol.454 , pp. 890-893
    • Hao, L.1
  • 23
    • 0035071116 scopus 로고    scopus 로고
    • Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site
    • Hara, K., et al. 2001. Influenza virus RNA polymerase PA subunit is a novel serine protease with Ser624 at the active site. Genes Cells 6:87-97.
    • (2001) Genes Cells , vol.6 , pp. 87-97
    • Hara, K.1
  • 24
    • 78650310818 scopus 로고    scopus 로고
    • ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses
    • Hayakawa, S., et al. 2011. ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responses. Nat. Immunol. 12:37-44.
    • (2011) Nat. Immunol. , vol.12 , pp. 37-44
    • Hayakawa, S.1
  • 25
    • 33846466718 scopus 로고    scopus 로고
    • Host factor Ebp1: selective inhibitor of influenza virus transcriptase
    • Honda, A., T. Okamoto, and A. Ishihama. 2007. Host factor Ebp1: selective inhibitor of influenza virus transcriptase. Genes Cells 12:133-142.
    • (2007) Genes Cells , vol.12 , pp. 133-142
    • Honda, A.1    Okamoto, T.2    Ishihama, A.3
  • 26
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W., B. T. Sherman, and R. A. Lempicki. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources.Nat. Protoc. 4:44-57.
    • (2009) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 27
    • 0034892686 scopus 로고    scopus 로고
    • PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators
    • Huarte, M., J. J. Sanz-Ezquerro, F. Roncal, J. Ortin, and A. Nieto. 2001. PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators. J. Virol. 75:8597-8604.
    • (2001) J. Virol. , vol.75 , pp. 8597-8604
    • Huarte, M.1    Sanz-Ezquerro, J.J.2    Roncal, F.3    Ortin, J.4    Nieto, A.5
  • 28
    • 38849144761 scopus 로고    scopus 로고
    • Determination of carryover and contamination for mass spectrometry-based chromatographic assays
    • Hughes, N. C., E. Y. Wong, J. Fan, and N. Bajaj. 2007. Determination of carryover and contamination for mass spectrometry-based chromatographic assays. AAPS J. 9:E353-E360.
    • (2007) AAPS J , vol.9
    • Hughes, N.C.1    Wong, E.Y.2    Fan, J.3    Bajaj, N.4
  • 29
    • 77957757095 scopus 로고    scopus 로고
    • Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1
    • Iwai, A., et al. 2010. Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1. J. Biol. Chem. 285:32064-32074.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32064-32074
    • Iwai, A.1
  • 30
    • 0035863852 scopus 로고    scopus 로고
    • The transcript release factor PTRF augments ribosomal gene transcription by facilitating reinitiation of RNA polymerase I
    • Jansa, P., C. Burek, E. E. Sander, and I. Grummt. 2001. The transcript release factor PTRF augments ribosomal gene transcription by facilitating reinitiation of RNA polymerase I. Nucleic Acids Res. 29:423-429.
    • (2001) Nucleic Acids Res , vol.29 , pp. 423-429
    • Jansa, P.1    Burek, C.2    Sander, E.E.3    Grummt, I.4
  • 31
    • 76749090540 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication
    • Karlas, A., et al. 2010. Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication. Nature 463:818-822.
    • (2010) Nature , vol.463 , pp. 818-822
    • Karlas, A.1
  • 33
    • 35648936553 scopus 로고    scopus 로고
    • De novo replication of the influenza virus RNA genome is regulated by DNA replicative helicase, MCM
    • Kawaguchi, A., and K. Nagata. 2007. De novo replication of the influenza virus RNA genome is regulated by DNA replicative helicase, MCM. EMBO J. 26:4566-4575.
    • (2007) EMBO J , vol.26 , pp. 4566-4575
    • Kawaguchi, A.1    Nagata, K.2
  • 34
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., A. I. Nesvizhskii, E. Kolker, and R. Aebersold. 2002. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74:5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 35
    • 76749108989 scopus 로고    scopus 로고
    • Human host factors required for influenza virus replication
    • Konig, R., et al. 2010. Human host factors required for influenza virus replication. Nature 463:813-817.
    • (2010) Nature , vol.463 , pp. 813-817
    • Konig, R.1
  • 36
    • 79952408660 scopus 로고    scopus 로고
    • Receptor tyrosine kinase inhibitors block multiple steps of influenza A virus replication
    • Kumar, N., Y. Liang, and T. G. Parslow. 2011. Receptor tyrosine kinase inhibitors block multiple steps of influenza A virus replication. J. Virol.
    • (2011) J. Virol.
    • Kumar, N.1    Liang, Y.2    Parslow, T.G.3
  • 37
    • 78650909416 scopus 로고    scopus 로고
    • Inhibition of poxvirus spreading by the anti-tumor drug gefitinib (Iressa)
    • Langhammer, S., R. Koban, C. Yue, and H. Ellerbrok. 2011. Inhibition of poxvirus spreading by the anti-tumor drug gefitinib (Iressa). Antiviral Res. 89:64-70.
    • (2011) Antiviral Res , vol.89 , pp. 64-70
    • Langhammer, S.1    Koban, R.2    Yue, C.3    Ellerbrok, H.4
  • 38
    • 17644398753 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infected cell protein 0 forms a complex with CIN85 and Cbl and mediates the degradation of EGF receptor from cell surfaces
    • Liang, Y., A. Kurakin, and B. Roizman. 2005. Herpes simplex virus 1 infected cell protein 0 forms a complex with CIN85 and Cbl and mediates the degradation of EGF receptor from cell surfaces. Proc. Natl. Acad. Sci. U. S. A. 102:5838-5843.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5838-5843
    • Liang, Y.1    Kurakin, A.2    Roizman, B.3
  • 39
    • 77957970275 scopus 로고    scopus 로고
    • The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble
    • Liu, H., et al. 2010. The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble. J. Virol. 84:11164-11174.
    • (2010) J. Virol. , vol.84 , pp. 11164-11174
    • Liu, H.1
  • 40
    • 49749092090 scopus 로고    scopus 로고
    • The hepatitis C virus nonstructural protein NS5A alters the trafficking profile of the epidermal growth factor receptor
    • Mankouri, J., S. Griffin, and M. Harris. 2008. The hepatitis C virus nonstructural protein NS5A alters the trafficking profile of the epidermal growth factor receptor. Traffic 9:1497-1509.
    • (2008) Traffic , vol.9 , pp. 1497-1509
    • Mankouri, J.1    Griffin, S.2    Harris, M.3
  • 41
    • 33847421368 scopus 로고    scopus 로고
    • Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches
    • Mayer, D., et al. 2007. Identification of cellular interaction partners of the influenza virus ribonucleoprotein complex and polymerase complex using proteomic-based approaches. J. Proteome Res. 6:672-682.
    • (2007) J. Proteome Res. , vol.6 , pp. 672-682
    • Mayer, D.1
  • 42
    • 34249785982 scopus 로고    scopus 로고
    • Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes
    • Melen, K., et al. 2007. Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J. Virol. 81:5995-6006.
    • (2007) J. Virol. , vol.81 , pp. 5995-6006
    • Melen, K.1
  • 43
    • 0035133124 scopus 로고    scopus 로고
    • Cellular splicing factor RAF-2p48/NPI-5/BAT1/UAP56 interacts with the influenza virus nucleoprotein and enhances viral RNA synthesis
    • Momose, F., et al. 2001. Cellular splicing factor RAF-2p48/NPI-5/BAT1/UAP56 interacts with the influenza virus nucleoprotein and enhances viral RNA synthesis. J. Virol. 75:1899-1908.
    • (2001) J. Virol. , vol.75 , pp. 1899-1908
    • Momose, F.1
  • 44
    • 77956839458 scopus 로고    scopus 로고
    • Evidence for avian and human host cell factors that affect the activity of influenza virus polymerase
    • Moncorge, O., M. Mura, and W. S. Barclay. 2010. Evidence for avian and human host cell factors that affect the activity of influenza virus polymerase. J. Virol. 84:9978-9986.
    • (2010) J. Virol. , vol.84 , pp. 9978-9986
    • Moncorge, O.1    Mura, M.2    Barclay, W.S.3
  • 45
    • 36749077601 scopus 로고    scopus 로고
    • An influenza virus replicon system in yeast identified Tat-SF1 as a stimulatory host factor for viral RNA synthesis
    • Naito, T., et al. 2007. An influenza virus replicon system in yeast identified Tat-SF1 as a stimulatory host factor for viral RNA synthesis. Proc. Natl. Acad. Sci. U. S. A. 104:18235-18240.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18235-18240
    • Naito, T.1
  • 46
    • 33846491250 scopus 로고    scopus 로고
    • Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits
    • Naito, T., F. Momose, A. Kawaguchi, and K. Nagata. 2007. Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J. Virol. 81:1339-1349.
    • (2007) J. Virol. , vol.81 , pp. 1339-1349
    • Naito, T.1    Momose, F.2    Kawaguchi, A.3    Nagata, K.4
  • 47
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., A. Keller, E. Kolker, and R. Aebersold. 2003. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75:4646-4658.
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 48
    • 0028979910 scopus 로고
    • NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein
    • O'Neill, R. E., and P. Palese. 1995. NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein. Virology 206:116-125.
    • (1995) Virology , vol.206 , pp. 116-125
    • O'Neill, R.E.1    Palese, P.2
  • 49
    • 33748461366 scopus 로고    scopus 로고
    • hCLE/CGI-99, a human protein that interacts with the influenza virus polymerase, is a mRNA transcription modulator
    • Perez-Gonzalez, A., A. Rodriguez, M. Huarte, I. J. Salanueva, and A. Nieto. 2006. hCLE/CGI-99, a human protein that interacts with the influenza virus polymerase, is a mRNA transcription modulator. J. Mol. Biol. 362:887-900.
    • (2006) J. Mol. Biol. , vol.362 , pp. 887-900
    • Perez-Gonzalez, A.1    Rodriguez, A.2    Huarte, M.3    Salanueva, I.J.4    Nieto, A.5
  • 51
    • 0030053530 scopus 로고    scopus 로고
    • The amino-terminal one-third of the influenza virus PA protein is responsible for the induction of proteolysis
    • Sanz-Ezquerro, J. J., T. Zurcher, S. de la Luna, J. Ortin, and A. Nieto. 1996. The amino-terminal one-third of the influenza virus PA protein is responsible for the induction of proteolysis. J. Virol. 70:1905-1911.
    • (1996) J. Virol. , vol.70 , pp. 1905-1911
    • Sanz-Ezquerro, J.J.1    Zurcher, T.2    de la Luna, S.3    Ortin, J.4    Nieto, A.5
  • 52
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira, S. D., et al. 2009. A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 139:1255-1267.
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1
  • 53
    • 0034618517 scopus 로고    scopus 로고
    • Transcription by RNA polymerase II in DNA-PK deficient SCID mouse cells
    • Sheppard, H. M., and X. Liu. 2000. Transcription by RNA polymerase II in DNA-PK deficient SCID mouse cells. Biochim. Biophys. Acta 1493:41-47.
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 41-47
    • Sheppard, H.M.1    Liu, X.2
  • 54
    • 79551708184 scopus 로고    scopus 로고
    • The PA protein directly contributes to the virulence of H5N1 avian influenza viruses in domestic ducks
    • Song, J., et al. 2011. The PA protein directly contributes to the virulence of H5N1 avian influenza viruses in domestic ducks. J. Virol. 85:2180-2188.
    • (2011) J. Virol. , vol.85 , pp. 2180-2188
    • Song, J.1
  • 55
    • 0027216860 scopus 로고
    • The E5 oncoprotein of human papillomavirus type 16 transforms fibroblasts and effects the downregulation of the epidermal growth factor receptor in keratinocytes
    • Straight, S. W., P. M. Hinkle, R. J. Jewers, and D. J. McCance. 1993. The E5 oncoprotein of human papillomavirus type 16 transforms fibroblasts and effects the downregulation of the epidermal growth factor receptor in keratinocytes. J. Virol. 67:4521-4532.
    • (1993) J. Virol. , vol.67 , pp. 4521-4532
    • Straight, S.W.1    Hinkle, P.M.2    Jewers, R.J.3    McCance, D.J.4
  • 56
    • 64849116933 scopus 로고    scopus 로고
    • The use of Random Homozygous Gene Perturbation to identify novel host-oriented targets for influenza
    • Sui, B., et al. 2009. The use of Random Homozygous Gene Perturbation to identify novel host-oriented targets for influenza. Virology 387:473-481.
    • (2009) Virology , vol.387 , pp. 473-481
    • Sui, B.1
  • 57
    • 79952774962 scopus 로고    scopus 로고
    • High genetic compatibility and increased pathogenicity of reassortants derived from avian H9N2 and pandemic H1N1/2009 influenza viruses
    • Sun, Y., et al. 2011. High genetic compatibility and increased pathogenicity of reassortants derived from avian H9N2 and pandemic H1N1/2009 influenza viruses. Proc. Natl. Acad. Sci. U. S. A. 108:4164-4169.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4164-4169
    • Sun, Y.1
  • 58
    • 77957201861 scopus 로고    scopus 로고
    • The human papillomavirus type 16 E5 oncoprotein inhibits epidermal growth factor trafficking independently of endosome acidification
    • Suprynowicz, F. A., et al. 2010. The human papillomavirus type 16 E5 oncoprotein inhibits epidermal growth factor trafficking independently of endosome acidification. J. Virol. 84:10619-10629.
    • (2010) J. Virol. , vol.84 , pp. 10619-10629
    • Suprynowicz, F.A.1
  • 59
    • 33847624936 scopus 로고    scopus 로고
    • Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit
    • Tarendeau, F., et al. 2007. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat. Struct. Mol. Biol. 14:229-233.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 229-233
    • Tarendeau, F.1
  • 60
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: an essential player in apoptosis
    • Tsujimoto, Y., and S. Shimizu. 2002. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84:187-193.
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 61
    • 1342285200 scopus 로고    scopus 로고
    • Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome
    • Turan, K., et al. 2004. Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome. Nucleic Acids Res. 32:643-652.
    • (2004) Nucleic Acids Res , vol.32 , pp. 643-652
    • Turan, K.1
  • 62
    • 77649120021 scopus 로고    scopus 로고
    • Highly pathogenic H5N1 avian influenza virus induces extracellular Ca2_ influx, leading to apoptosis in avian cells
    • Ueda, M., et al. 2010. Highly pathogenic H5N1 avian influenza virus induces extracellular Ca2_ influx, leading to apoptosis in avian cells. J. Virol. 84: 3068-3078.
    • (2010) J. Virol. , vol.84 , pp. 3068-3078
    • Ueda, M.1
  • 63
    • 70649087924 scopus 로고    scopus 로고
    • Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells
    • Vreede, F. T., A. Y. Chan, J. Sharps, and E. Fodor. 2010. Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells. Virology 396:125-134.
    • (2010) Virology , vol.396 , pp. 125-134
    • Vreede, F.T.1    Chan, A.Y.2    Sharps, J.3    Fodor, E.4
  • 64
    • 78349236605 scopus 로고    scopus 로고
    • The role of the influenza virus RNA polymerase in host shut-off
    • Vreede, F. T., and E. Fodor. 2010. The role of the influenza virus RNA polymerase in host shut-off. Virulence 1:436-439.
    • (2010) Virulence , vol.1 , pp. 436-439
    • Vreede, F.T.1    Fodor, E.2
  • 65
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., P. Palese, and R. E. O'Neill. 1997. The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71:1850-1856.
    • (1997) J. Virol. , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 66
    • 67749127718 scopus 로고    scopus 로고
    • Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein
    • Wang, P., et al. 2009. Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein. J. Virol. 83:7850-7861.
    • (2009) J. Virol. , vol.83 , pp. 7850-7861
    • Wang, P.1
  • 67
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe, T., S. Watanabe, and Y. Kawaoka. 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
  • 68
    • 0032571254 scopus 로고    scopus 로고
    • Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation. J
    • Wu-Baer, F., W. S. Lane, and R. B. Gaynor. 1998. Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation. J. Mol. Biol. 277:179-197.
    • (1998) Mol. Biol. , vol.277 , pp. 179-197
    • Wu-Baer, F.1    Lane, W.S.2    Gaynor, R.B.3
  • 69
    • 77951059450 scopus 로고    scopus 로고
    • Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1
    • Zamarin, D., A. Garcia-Sastre, X. Xiao, R. Wang, and P. Palese. 2005. Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1. PLoS Pathog. 1:e4.
    • (2005) PLoS Pathog , vol.1
    • Zamarin, D.1    Garcia-Sastre, A.2    Xiao, X.3    Wang, R.4    Palese, P.5
  • 70
    • 0029834383 scopus 로고    scopus 로고
    • Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat
    • Zhou, Q., and P. A. Sharp. 1996. Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science 274:605-610.
    • (1996) Science , vol.274 , pp. 605-610
    • Zhou, Q.1    Sharp, P.A.2


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