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Volumn 98, Issue 9, 2017, Pages 2267-2273

Human interactome of the influenza B virus NS1 protein

Author keywords

Influenza; Interferon; Proteomics; Virulence factor; Virus host interaction

Indexed keywords

ANXA2 PROTEIN; DHX9 PROTEIN; HNRNPA2B1 PROTEIN; HNRNPC PROTEIN; HNRNPH3 PROTEIN; HNRNPU PROTEIN; HOST FACTOR; INTERFERON; INTERFERON REGULATORY FACTOR 3; INTERLEUKIN ENHANCER BINDING FACTOR 3; MATR3 PROTEIN; MESSENGER RNA; NONSTRUCTURAL PROTEIN 1; NUCLEOPHOSMIN; PABPC1 PROTEIN; PNN PROTEIN; PRPF8 PROTEIN; RALY PROTEIN; RBMY1A1 PROTEIN; REGULATOR PROTEIN; RNA BINDING PROTEIN; RNPS1 PROTEIN; RPL3 PROTEIN; RPL6 PROTEIN; SNRNP200 PROTEIN; SRRM2 PROTEIN; STAT1 PROTEIN; UNCLASSIFIED DRUG; Y BOX BINDING PROTEIN 1; ZNF326 PROTEIN; DEAD BOX PROTEIN; DHX9 PROTEIN, HUMAN; ILF3 PROTEIN, HUMAN; INS1 PROTEIN, INFLUENZA VIRUS; PROTEIN BINDING; TUMOR PROTEIN; VIRAL PROTEIN; YBX1 PROTEIN, HUMAN;

EID: 85029595752     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/jgv.0.000909     Document Type: Article
Times cited : (18)

References (46)
  • 2
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe DM and Howley PM (editors)., Lippincott Williams & Wilkins
    • Palese P, Shaw ML. Orthomyxoviridae: the viruses and their replication. In: Knipe DM and Howley PM (editors). Fields Virology. Lippincott Williams & Wilkins; 2013. pp. 1151-1185.
    • (2013) Fields Virology , pp. 1151-1185
    • Palese, P.1    Shaw, M.L.2
  • 3
    • 0842304509 scopus 로고    scopus 로고
    • The influenza B virus nonstructural NS1 protein is essential for efficient viral growth and antagonizes beta interferon induction
    • Dauber B, Heins G, Wolff T. The influenza B virus nonstructural NS1 protein is essential for efficient viral growth and antagonizes beta interferon induction. J Virol 2004;78:1865-1872.
    • (2004) J Virol , vol.78 , pp. 1865-1872
    • Dauber, B.1    Heins, G.2    Wolff, T.3
  • 4
    • 33751242334 scopus 로고    scopus 로고
    • Double-stranded RNA binding of influenza B virus nonstructural NS1 protein inhibits protein kinase R but is not essential to antagonize production of alpha/beta interferon
    • Dauber B, Schneider J, Wolff T. Double-stranded RNA binding of influenza B virus nonstructural NS1 protein inhibits protein kinase R but is not essential to antagonize production of alpha/beta interferon. J Virol 2006;80:11667-11677.
    • (2006) J Virol , vol.80 , pp. 11667-11677
    • Dauber, B.1    Schneider, J.2    Wolff, T.3
  • 5
    • 84986182412 scopus 로고    scopus 로고
    • Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins
    • Zhao C, Sridharan H, Chen R, Baker DP, Wang S et al. Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins. Nat Commun 2016;7:12754.
    • (2016) Nat Commun , vol.7 , pp. 12754
    • Zhao, C.1    Sridharan, H.2    Chen, R.3    Baker, D.P.4    Wang, S.5
  • 6
    • 84921960062 scopus 로고    scopus 로고
    • Functions of the influenza A virus NS1 protein in antiviral defense
    • Krug RM. Functions of the influenza A virus NS1 protein in antiviral defense. Curr Opin Virol 2015;12:1-6.
    • (2015) Curr Opin Virol , vol.12 , pp. 1-6
    • Krug, R.M.1
  • 7
    • 78651253025 scopus 로고    scopus 로고
    • Molecular studies of influenza B virus in the reverse genetics era
    • Jackson D, Elderfield RA, Barclay WS. Molecular studies of influenza B virus in the reverse genetics era. J Gen Virol 2011;92:1-17.
    • (2011) J Gen Virol , vol.92 , pp. 1-17
    • Jackson, D.1    Elderfield, R.A.2    Barclay, W.S.3
  • 8
    • 6344278510 scopus 로고    scopus 로고
    • The Nand C-terminal domains of the NS1 protein of influenza B virus can independently inhibit IRF-3 and beta interferon promoter activation
    • Donelan NR, Dauber B, Wang X, Basler CF, Wolff T et al. The Nand C-terminal domains of the NS1 protein of influenza B virus can independently inhibit IRF-3 and beta interferon promoter activation. J Virol 2004;78:11574-11582.
    • (2004) J Virol , vol.78 , pp. 11574-11582
    • Donelan, N.R.1    Dauber, B.2    Wang, X.3    Basler, C.F.4    Wolff, T.5
  • 9
    • 84907212573 scopus 로고    scopus 로고
    • Conformational plasticity of the influenza A virus NS1 protein
    • Hale BG. Conformational plasticity of the influenza A virus NS1 protein. J Gen Virol 2014;95:2099-2105.
    • (2014) J Gen Virol , vol.95 , pp. 2099-2105
    • Hale, B.G.1
  • 10
    • 0030248233 scopus 로고    scopus 로고
    • The RNA-binding and effector domains of the viral NS1 protein are conserved to different extents among influenza A and B viruses
    • Wang W, Krug RM. The RNA-binding and effector domains of the viral NS1 protein are conserved to different extents among influenza A and B viruses. Virology 1996;223:41-50.
    • (1996) Virology , vol.223 , pp. 41-50
    • Wang, W.1    Krug, R.M.2
  • 11
    • 34547136235 scopus 로고    scopus 로고
    • Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses
    • Yin C, Khan JA, Swapna GV, Ertekin A, Krug RM et al. Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses. J Biol Chem 2007;282:20584-20592.
    • (2007) J Biol Chem , vol.282 , pp. 20584-20592
    • Yin, C.1    Khan, J.A.2    Swapna, G.V.3    Ertekin, A.4    Krug, R.M.5
  • 12
    • 0037444193 scopus 로고    scopus 로고
    • Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS
    • Noah DL, Twu KY, Krug RM. Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS. Virology 2003;307:386-395.
    • (2003) Virology , vol.307 , pp. 386-395
    • Noah, D.L.1    Twu, K.Y.2    Krug, R.M.3
  • 13
    • 35448948397 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase signaling by the nonstructural NS1 protein is not conserved among type A and B influenza viruses
    • Ehrhardt C, Wolff T, Ludwig S. Activation of phosphatidylinositol 3-kinase signaling by the nonstructural NS1 protein is not conserved among type A and B influenza viruses. J Virol 2007;81:12097-12100.
    • (2007) J Virol , vol.81 , pp. 12097-12100
    • Ehrhardt, C.1    Wolff, T.2    Ludwig, S.3
  • 14
    • 33749004778 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein binds p85b and activates phosphatidylinositol-3-kinase signaling
    • Hale BG, Jackson D, Chen YH, Lamb RA, Randall RE. Influenza A virus NS1 protein binds p85b 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    Lamb, R.A.4    Randall, R.E.5
  • 15
    • 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. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. Embo J 2001;20:362-371.
    • (2001) Embo J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 16
    • 80051970948 scopus 로고    scopus 로고
    • Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus
    • Guan R, Ma LC, Leonard PG, Amer BR, Sridharan H et al. Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus. Proc Natl Acad Sci USA 2011;108:13468-13473.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13468-13473
    • Guan, R.1    Ma, L.C.2    Leonard, P.G.3    Amer, B.R.4    Sridharan, H.5
  • 17
    • 77951480439 scopus 로고    scopus 로고
    • Species-specific antagonism of host ISGylation by the influenza B virus NS1 protein
    • Versteeg GA, Hale BG, van Boheemen S, Wolff T, Lenschow DJ et al. Species-specific antagonism of host ISGylation by the influenza B virus NS1 protein. J Virol 2010;84:5423-5430.
    • (2010) J Virol , vol.84 , pp. 5423-5430
    • Versteeg, G.A.1    Hale, B.G.2    van Boheemen, S.3    Wolff, T.4    Lenschow, D.J.5
  • 18
    • 34250810666 scopus 로고    scopus 로고
    • Multiple anti-interferon actions of the influenza A virus NS1 protein
    • Kochs G, García-Sastre A, Martínez-Sobrido L. Multiple anti-interferon actions of the influenza A virus NS1 protein. J Virol 2007;81:7011-7021.
    • (2007) J Virol , vol.81 , pp. 7011-7021
    • Kochs, G.1    García-Sastre, A.2    Martínez-Sobrido, L.3
  • 19
    • 84907915259 scopus 로고    scopus 로고
    • A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence
    • Ayllon J, Domingues P, Rajsbaum R, Miorin L, Schmolke M et al. A single amino acid substitution in the novel H7N9 influenza A virus NS1 protein increases CPSF30 binding and virulence. J Virol 2014;88:12146-12151.
    • (2014) J Virol , vol.88 , pp. 12146-12151
    • Ayllon, J.1    Domingues, P.2    Rajsbaum, R.3    Miorin, L.4    Schmolke, M.5
  • 20
    • 34249785982 scopus 로고    scopus 로고
    • Nuclear and nucleolar targeting of influenza A virus NS1 protein: Striking differences between different virus subtypes
    • Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY et al. Nuclear and nucleolar targeting of influenza A virus NS1 protein:striking differences between different virus subtypes. J Virol 2007;81:5995-6006.
    • (2007) J Virol , vol.81 , pp. 5995-6006
    • Melén, K.1    Kinnunen, L.2    Fagerlund, R.3    Ikonen, N.4    Twu, K.Y.5
  • 21
    • 58149517735 scopus 로고    scopus 로고
    • Analysis of influenza B Virus NS1 protein trafficking reveals a novel interaction with nuclear speckle domains
    • Schneider J, Dauber B, Melén K, Julkunen I, Wolff T. Analysis of influenza B Virus NS1 protein trafficking reveals a novel interaction with nuclear speckle domains. J Virol 2009;83:701-711.
    • (2009) J Virol , vol.83 , pp. 701-711
    • Schneider, J.1    Dauber, B.2    Melén, K.3    Julkunen, I.4    Wolff, T.5
  • 22
    • 33751232040 scopus 로고    scopus 로고
    • The NPro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation
    • Hilton L, Moganeradj K, Zhang G, Chen YH, Randall RE et al. The NPro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation. J Virol 2006;80:11723-11732.
    • (2006) J Virol , vol.80 , pp. 11723-11732
    • Hilton, L.1    Moganeradj, K.2    Zhang, G.3    Chen, Y.H.4    Randall, R.E.5
  • 23
    • 0032731094 scopus 로고    scopus 로고
    • The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation
    • Didcock L, Young DF, Goodbourn S, Randall RE. The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation. J Virol 1999;73:9928-9933.
    • (1999) J Virol , vol.73 , pp. 9928-9933
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 24
    • 45149122553 scopus 로고    scopus 로고
    • Different roles for two ubiquitin-like domains of ISG15 in protein modification
    • Chang YG, Yan XZ, Xie YY, Gao XC, Song AX et al. Different roles for two ubiquitin-like domains of ISG15 in protein modification. J Biol Chem 2008;283:13370-13377.
    • (2008) J Biol Chem , vol.283 , pp. 13370-13377
    • Chang, Y.G.1    Yan, X.Z.2    Xie, Y.Y.3    Gao, X.C.4    Song, A.X.5
  • 25
    • 67650917895 scopus 로고    scopus 로고
    • Influenza B virus ribonucleoprotein is a potent activator of the antiviral kinase PKR
    • Dauber B, Martínez-Sobrido L, Schneider J, Hai R, Waibler Z 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    Martínez-Sobrido, L.2    Schneider, J.3    Hai, R.4    Waibler, Z.5
  • 26
    • 84864288635 scopus 로고    scopus 로고
    • Viral immune modulators perturb the human molecular network by common and unique strategies
    • Pichlmair A, Kandasamy K, Alvisi G, Mulhern O, Sacco R et al. Viral immune modulators perturb the human molecular network by common and unique strategies. Nature 2012;487:486-490.
    • (2012) Nature , vol.487 , pp. 486-490
    • Pichlmair, A.1    Kandasamy, K.2    Alvisi, G.3    Mulhern, O.4    Sacco, R.5
  • 27
    • 84995555394 scopus 로고    scopus 로고
    • Disruption of Src homology 3-binding motif within non-structural protein 1 of influenza B virus unexpectedly enhances viral replication in human cells
    • Sadewasser A, Saenger S, Paki K, Schwecke T, Wolff T. Disruption of Src homology 3-binding motif within non-structural protein 1 of influenza B virus unexpectedly enhances viral replication in human cells. J Gen Virol 2016;97:2856-2867.
    • (2016) J Gen Virol , vol.97 , pp. 2856-2867
    • Sadewasser, A.1    Saenger, S.2    Paki, K.3    Schwecke, T.4    Wolff, T.5
  • 28
    • 0033575228 scopus 로고    scopus 로고
    • DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR
    • Patel RC, Vestal DJ, Xu Z, Bandyopadhyay S, Guo W et al. DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR. J Biol Chem 1999;274:20432-20437.
    • (1999) J Biol Chem , vol.274 , pp. 20432-20437
    • Patel, R.C.1    Vestal, D.J.2    Xu, Z.3    Bandyopadhyay, S.4    Guo, W.5
  • 29
    • 57049148002 scopus 로고    scopus 로고
    • Molecular characterization of human Argonaute-containing ribonucleoprotein complexes and their bound target mRNAs
    • Landthaler M, Gaidatzis D, Rothballer A, Chen PY, Soll SJ et al. Molecular characterization of human Argonaute-containing ribonucleoprotein complexes and their bound target mRNAs. RNA 2008;14:2580-2596.
    • (2008) RNA , vol.14 , pp. 2580-2596
    • Landthaler, M.1    Gaidatzis, D.2    Rothballer, A.3    Chen, P.Y.4    Soll, S.J.5
  • 30
    • 80054774522 scopus 로고    scopus 로고
    • The Ebola virus VP24 protein prevents hnRNP C1/C2 binding to karyopherin a1 and partially alters its nuclear import
    • Shabman RS, Gulcicek EE, Stone KL, Basler CF. The Ebola virus VP24 protein prevents hnRNP C1/C2 binding to karyopherin a1 and partially alters its nuclear import. J Infect Dis 2011;204:S904-S910.
    • (2011) J Infect Dis , vol.204 , pp. S904-S910
    • Shabman, R.S.1    Gulcicek, E.E.2    Stone, K.L.3    Basler, C.F.4
  • 32
    • 84869014044 scopus 로고    scopus 로고
    • YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules
    • Kawaguchi A, Matsumoto K, Nagata K. YB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules. J Virol 2012;86:11086-11095.
    • (2012) J Virol , vol.86 , pp. 11086-11095
    • Kawaguchi, A.1    Matsumoto, K.2    Nagata, K.3
  • 33
    • 84948953767 scopus 로고    scopus 로고
    • Influenza virus induces cholesterol-enriched endocytic recycling compartments for budozone formation via cell cycle-independent centrosome maturation
    • Kawaguchi A, Hirohama M, Harada Y, Osari S, Nagata K. Influenza virus induces cholesterol-enriched endocytic recycling compartments for budozone formation via cell cycle-independent centrosome maturation. PLoS Pathog 2015;11:e1005284.
    • (2015) PLoS Pathog , vol.11
    • Kawaguchi, A.1    Hirohama, M.2    Harada, Y.3    Osari, S.4    Nagata, K.5
  • 34
    • 84985945896 scopus 로고    scopus 로고
    • A second RNA-binding site in the NS1 protein of nfluenza B virus
    • Ma LC, Guan R, Hamilton K, Aramini JM, Mao L et al. A second RNA-binding site in the NS1 protein of nfluenza B virus. Structure 2016;24:1562-1572.
    • (2016) Structure , vol.24 , pp. 1562-1572
    • Ma, L.C.1    Guan, R.2    Hamilton, K.3    Aramini, J.M.4    Mao, L.5
  • 35
    • 84977561786 scopus 로고    scopus 로고
    • Robust Lys63-linked ubiquitination of RIG-I promotes cytokine eruption in early influenza B virus infection
    • Jiang J, Li J, Fan W, Zheng W, Yu M et al. Robust Lys63-linked ubiquitination of RIG-I promotes cytokine eruption in early influenza B virus infection. J Virol 2016;90:6263-6275.
    • (2016) J Virol , vol.90 , pp. 6263-6275
    • Jiang, J.1    Li, J.2    Fan, W.3    Zheng, W.4    Yu, M.5
  • 36
    • 77957658503 scopus 로고    scopus 로고
    • Heterocellular induction of interferon by negative-sense RNA viruses
    • Chen S, Short JA, Young DF, Killip MJ, Schneider M et al. Heterocellular induction of interferon by negative-sense RNA viruses. Virology 2010;407:247-255.
    • (2010) Virology , vol.407 , pp. 247-255
    • Chen, S.1    Short, J.A.2    Young, D.F.3    Killip, M.J.4    Schneider, M.5
  • 37
    • 84982949470 scopus 로고    scopus 로고
    • Spliceosome SNRNP200 promotes viral RNA sensing and IRF3 activation of antiviral response
    • Tremblay N, Baril M, Chatel-Chaix L, Es-Saad S, Park AY et al. Spliceosome SNRNP200 promotes viral RNA sensing and IRF3 activation of antiviral response. PLoS Pathog 2016;12:e1005772.
    • (2016) PLoS Pathog , vol.12
    • Tremblay, N.1    Baril, M.2    Chatel-Chaix, L.3    Es-Saad, S.4    Park, A.Y.5
  • 38
    • 80052576674 scopus 로고    scopus 로고
    • Hostand strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins
    • Bortz E, Westera L, Maamary J, Steel J, Albrecht RA et al. Hostand strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins. MBio 2011;2:e00151-11.
    • (2011) MBio , vol.2 , pp. e00151-e00211
    • Bortz, E.1    Westera, L.2    Maamary, J.3    Steel, J.4    Albrecht, R.A.5
  • 39
    • 67749127718 scopus 로고    scopus 로고
    • Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein
    • Wang P, Song W, Mok BW, Zhao P, Qin K et al. Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein. J Virol 2009;83:7850-7861.
    • (2009) J Virol , vol.83 , pp. 7850-7861
    • Wang, P.1    Song, W.2    Mok, B.W.3    Zhao, P.4    Qin, K.5
  • 40
    • 84898623891 scopus 로고    scopus 로고
    • NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells
    • Wen X, Huang X, Mok BW, Chen Y, Zheng M et al. NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells. J Immunol 2014;192:3753-3764.
    • (2014) J Immunol , vol.192 , pp. 3753-3764
    • Wen, X.1    Huang, X.2    Mok, B.W.3    Chen, Y.4    Zheng, M.5
  • 41
    • 34748885125 scopus 로고    scopus 로고
    • Nuclear factors are involved in hepatitis C virus RNA replication
    • Isken O, Baroth M, Grassmann CW, Weinlich S, Ostareck DH et al. Nuclear factors are involved in hepatitis C virus RNA replication. RNA 2007;13:1675-1692.
    • (2007) RNA , vol.13 , pp. 1675-1692
    • Isken, O.1    Baroth, M.2    Grassmann, C.W.3    Weinlich, S.4    Ostareck, D.H.5
  • 42
    • 0242473186 scopus 로고    scopus 로고
    • Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus
    • Isken O, Grassmann CW, Sarisky RT, Kann M, Zhang S et al. Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus. Embo J 2003;22:5655-5665.
    • (2003) Embo J , vol.22 , pp. 5655-5665
    • Isken, O.1    Grassmann, C.W.2    Sarisky, R.T.3    Kann, M.4    Zhang, S.5
  • 43
    • 79952223157 scopus 로고    scopus 로고
    • NF90 binds the dengue virus RNA 3' terminus and is a positive regulator of dengue virus replication
    • Gomila RC, Martin GW, Gehrke L. NF90 binds the dengue virus RNA 3' terminus and is a positive regulator of dengue virus replication. PLoS One 2011;6:e16687.
    • (2011) PLoS One , vol.6
    • Gomila, R.C.1    Martin, G.W.2    Gehrke, L.3
  • 44
    • 84901999765 scopus 로고    scopus 로고
    • hnRNP L and NF90 interact with hepatitis C virus 5'-terminal untranslated RNA and promote efficient replication
    • Li Y, Masaki T, Shimakami T, Lemon SM. hnRNP L and NF90 interact with hepatitis C virus 5'-terminal untranslated RNA and promote efficient replication. J Virol 2014;88:7199-7209.
    • (2014) J Virol , vol.88 , pp. 7199-7209
    • Li, Y.1    Masaki, T.2    Shimakami, T.3    Lemon, S.M.4
  • 45
    • 80054745749 scopus 로고    scopus 로고
    • DRBP76 associates with Ebola virus VP35 and suppresses viral polymerase function
    • Shabman RS, Leung DW, Johnson J, Glennon N, Gulcicek EE et al. DRBP76 associates with Ebola virus VP35 and suppresses viral polymerase function. J Infect Dis 2011;204:S911-S918.
    • (2011) J Infect Dis , vol.204 , pp. S911-S918
    • Shabman, R.S.1    Leung, D.W.2    Johnson, J.3    Glennon, N.4    Gulcicek, E.E.5
  • 46
    • 84910675034 scopus 로고    scopus 로고
    • NF90 isoforms, a new family of cellular proteins involved in viral replication?
    • Patiño C, Haenni AL, Urcuqui-Inchima S. NF90 isoforms, a new family of cellular proteins involved in viral replication? Biochimie 2015;108:20-24.
    • (2015) Biochimie , vol.108 , pp. 20-24
    • Patiño, C.1    Haenni, A.L.2    Urcuqui-Inchima, S.3


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