메뉴 건너뛰기




Volumn , Issue , 2016, Pages 2797-2810

NF90 is a novel influenza A virus NS1-interacting protein that antagonizes the inhibitory role of NS1 on PKR phosphorylation

Author keywords

influenza A virus; NF90; nonstructural protein 1; protein kinase R phosphorylation; stress granules

Indexed keywords

INTERLEUKIN ENHANCER BINDING FACTOR 3; NONSTRUCTURAL PROTEIN 1; PROTEIN KINASE R;

EID: 84983458210     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12311     Document Type: Article
Times cited : (20)

References (69)
  • 1
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale BG, Randall RE, Ortin J and Jackson D (2008) The multifunctional NS1 protein of influenza A viruses. J Gen Virol 89 (Pt 10), 2359–2376.
    • (2008) J Gen Virol , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 2
    • 0033560753 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3’-end processing machinery
    • Chen Z, Li Y and Krug RM (1999) Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3’-end processing machinery. EMBO J 18, 2273–2283.
    • (1999) EMBO J , vol.18 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 3
    • 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 ME, Barabino SM, Li Y, Keller W and Krug RM (1998) Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol Cell 1, 991–1000.
    • (1998) Mol Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 4
    • 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 and Krug RM (2003) 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 307, 386–395.
    • (2003) Virology , vol.307 , pp. 386-395
    • Noah, D.L.1    Twu, K.Y.2    Krug, R.M.3
  • 7
    • 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 YK, Liu Q, Tikoo SK, Babiuk LA and Zhou Y (2007) 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 88 (Pt 1), 13–18.
    • (2007) J Gen Virol , vol.88 , pp. 13-18
    • Shin, Y.K.1    Liu, Q.2    Tikoo, S.K.3    Babiuk, L.A.4    Zhou, Y.5
  • 8
    • 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, Planz O, Beermann W, Bode JG, Schmolke M and Ludwig S (2007) Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses. J Virol 81, 3058–3067.
    • (2007) J Virol , vol.81 , pp. 3058-3067
    • Ehrhardt, C.1    Wolff, T.2    Pleschka, S.3    Planz, O.4    Beermann, W.5    Bode, J.G.6    Schmolke, M.7    Ludwig, S.8
  • 9
    • 33749004778 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling
    • Hale BG, Jackson D, Chen YH, Lamb RA and Randall RE (2006) Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling. Proc Natl Acad Sci USA 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
  • 10
    • 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, Carrasco L, Ortin J and Nieto A (2000) Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol Cell Biol 20, 6259–6268.
    • (2000) Mol Cell Biol , vol.20 , pp. 6259-6268
    • Aragon, T.1    de la Luna, S.2    Novoa, I.3    Carrasco, L.4    Ortin, J.5    Nieto, A.6
  • 11
    • 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 and Nieto A (2003) PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes. J Gen Virol 84 (Pt 12), 3263–3274.
    • (2003) J Gen Virol , vol.84 , pp. 3263-3274
    • Burgui, I.1    Aragon, T.2    Ortin, J.3    Nieto, A.4
  • 12
    • 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 and 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 USA 103, 7100–7105.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7100-7105
    • Min, J.Y.1    Krug, R.M.2
  • 13
    • 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 MG and Krug RM (1995) 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 214, 222–228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 14
    • 0032980412 scopus 로고    scopus 로고
    • Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells
    • Hatada E, Saito S and Fukuda R (1999) Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J Virol 73, 2425–2433.
    • (1999) J Virol , vol.73 , pp. 2425-2433
    • Hatada, E.1    Saito, S.2    Fukuda, R.3
  • 15
    • 0023656671 scopus 로고
    • Autophosphorylation of the protein kinase dependent on double-stranded RNA
    • Galabru J and Hovanessian A (1987) Autophosphorylation of the protein kinase dependent on double-stranded RNA. J Biol Chem 262, 15538–15544.
    • (1987) J Biol Chem , vol.262 , pp. 15538-15544
    • Galabru, J.1    Hovanessian, A.2
  • 16
    • 0032480017 scopus 로고    scopus 로고
    • PACT, a protein activator of the interferon-induced protein kinase, PKR
    • Patel RC and Sen GC (1998) PACT, a protein activator of the interferon-induced protein kinase, PKR. EMBO J 17, 4379–4390.
    • (1998) EMBO J , vol.17 , pp. 4379-4390
    • Patel, R.C.1    Sen, G.C.2
  • 17
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey JW (1991) Translational control in mammalian cells. Annu Rev Biochem 60, 717–755.
    • (1991) Annu Rev Biochem , vol.60 , pp. 717-755
    • Hershey, J.W.1
  • 18
    • 84876453384 scopus 로고    scopus 로고
    • Regulation of stress granules and P-bodies during RNA virus infection
    • Lloyd RE (2013) Regulation of stress granules and P-bodies during RNA virus infection. Wiley Interdiscip Rev RNA 4, 317–331.
    • (2013) Wiley Interdiscip Rev RNA , vol.4 , pp. 317-331
    • Lloyd, R.E.1
  • 19
    • 85016938715 scopus 로고    scopus 로고
    • Cytoplasmic RNA granules and viral infection
    • Tsai WC and Lloyd RE (2014) Cytoplasmic RNA granules and viral infection. Annu Rev Virol 1, 147–170.
    • (2014) Annu Rev Virol , vol.1 , pp. 147-170
    • Tsai, W.C.1    Lloyd, R.E.2
  • 20
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan JR and Parker R (2009) Eukaryotic stress granules: the ins and outs of translation. Mol Cell 36, 932–941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 21
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B
    • Kumar A, Haque J, Lacoste J, Hiscott J and Williams BR (1994) Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B. Proc Natl Acad Sci USA 91, 6288–6292.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6288-6292
    • Kumar, A.1    Haque, J.2    Lacoste, J.3    Hiscott, J.4    Williams, B.R.5
  • 22
    • 0022617764 scopus 로고
    • Translational control by influenza virus: suppression of the kinase that phosphorylates the alpha subunit of initiation factor eIF-2 and selective translation of influenza viral mRNAs
    • Katze MG, Detjen BM, Safer B and Krug RM (1986) Translational control by influenza virus: suppression of the kinase that phosphorylates the alpha subunit of initiation factor eIF-2 and selective translation of influenza viral mRNAs. Mol Cell Biol 6, 1741–1750.
    • (1986) Mol Cell Biol , vol.6 , pp. 1741-1750
    • Katze, M.G.1    Detjen, B.M.2    Safer, B.3    Krug, R.M.4
  • 23
    • 0031670374 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase
    • Tan SL and Katze MG (1998) Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase. J Interferon Cytokine Res 18, 757–766.
    • (1998) J Interferon Cytokine Res , vol.18 , pp. 757-766
    • Tan, S.L.1    Katze, M.G.2
  • 24
    • 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 JY, Krug RM and Sen GC (2006) Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology 349, 13–21.
    • (2006) Virology , vol.349 , pp. 13-21
    • Li, S.1    Min, J.Y.2    Krug, R.M.3    Sen, G.C.4
  • 25
    • 34247566514 scopus 로고    scopus 로고
    • A site on the influenza A virus NS1 protein mediates both inhibition of PKR activation and temporal regulation of viral RNA synthesis
    • Min JY, Li S, Sen GC and Krug RM (2007) A site on the influenza A virus NS1 protein mediates both inhibition of PKR activation and temporal regulation of viral RNA synthesis. Virology 363, 236–243.
    • (2007) Virology , vol.363 , pp. 236-243
    • Min, J.Y.1    Li, S.2    Sen, G.C.3    Krug, R.M.4
  • 26
    • 84983426932 scopus 로고    scopus 로고
    • Robust expression of vault RNAs induced by influenza A virus plays a critical role in suppression of PKR-mediated innate immunity
    • Li F, Chen Y, Zhang Z, Ouyang J, Wang Y, Yan R, Huang S, Gao GF, Guo G and Chen JL (2015) Robust expression of vault RNAs induced by influenza A virus plays a critical role in suppression of PKR-mediated innate immunity. Nucleic Acids Res 43, 10321–10337.
    • (2015) Nucleic Acids Res , vol.43 , pp. 10321-10337
    • Li, F.1    Chen, Y.2    Zhang, Z.3    Ouyang, J.4    Wang, Y.5    Yan, R.6    Huang, S.7    Gao, G.F.8    Guo, G.9    Chen, J.L.10
  • 27
    • 84869218756 scopus 로고    scopus 로고
    • The NS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infection
    • Mok BW, Song W, Wang P, Tai H, Chen Y, Zheng M, Wen X, Lau SY, Wu WL and Matsumoto K (2012) The NS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infection. J Virol 86, 12695–12707.
    • (2012) J Virol , vol.86 , pp. 12695-12707
    • Mok, B.W.1    Song, W.2    Wang, P.3    Tai, H.4    Chen, Y.5    Zheng, M.6    Wen, X.7    Lau, S.Y.8    Wu, W.L.9    Matsumoto, K.10
  • 28
    • 84860900591 scopus 로고    scopus 로고
    • Influenza A virus inhibits cytoplasmic stress granule formation
    • Khaperskyy DA, Hatchette TF and McCormick C (2012) Influenza A virus inhibits cytoplasmic stress granule formation. FASEB J 26, 1629–1639.
    • (2012) FASEB J , vol.26 , pp. 1629-1639
    • Khaperskyy, D.A.1    Hatchette, T.F.2    McCormick, C.3
  • 29
    • 0035943647 scopus 로고    scopus 로고
    • Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR
    • Saunders LR, Perkins DJ, Balachandran S, Michaels R, Ford R, Mayeda A and Barber GN (2001) Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR. J Biol Chem 276, 32300–32312.
    • (2001) J Biol Chem , vol.276 , pp. 32300-32312
    • Saunders, L.R.1    Perkins, D.J.2    Balachandran, S.3    Michaels, R.4    Ford, R.5    Mayeda, A.6    Barber, G.N.7
  • 30
    • 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, Erme SM, Williams BR and Sen GC (1999) DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR. J Biol Chem 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    Erme, S.M.6    Williams, B.R.7    Sen, G.C.8
  • 31
    • 0035980011 scopus 로고    scopus 로고
    • Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase
    • Parker LM, Fierro-Monti I and Mathews MB (2001) Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase. J Biol Chem 276, 32522–32530.
    • (2001) J Biol Chem , vol.276 , pp. 32522-32530
    • Parker, L.M.1    Fierro-Monti, I.2    Mathews, M.B.3
  • 33
    • 0033545970 scopus 로고    scopus 로고
    • Nuclear factor-90 of activated T-cells: a double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR
    • Langland JO, Kao PN and Jacobs BL (1999) Nuclear factor-90 of activated T-cells: a double-stranded RNA-binding protein and substrate for the double-stranded RNA-dependent protein kinase, PKR. Biochemistry 38, 6361–6368.
    • (1999) Biochemistry , vol.38 , pp. 6361-6368
    • Langland, J.O.1    Kao, P.N.2    Jacobs, B.L.3
  • 35
    • 0028088479 scopus 로고
    • Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90
    • Kao PN, Chen L, Brock G, Ng J, Kenny J, Smith AJ and Corthesy B (1994) Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90. J Biol Chem 269, 20691–20699.
    • (1994) J Biol Chem , vol.269 , pp. 20691-20699
    • Kao, P.N.1    Chen, L.2    Brock, G.3    Ng, J.4    Kenny, J.5    Smith, A.J.6    Corthesy, B.7
  • 36
    • 34249063242 scopus 로고    scopus 로고
    • NF90 regulates inducible IL-2 gene expression in T cells
    • Shi L, Godfrey WR, Lin J, Zhao G and Kao PN (2007) NF90 regulates inducible IL-2 gene expression in T cells. J Exp Med 204, 971–977.
    • (2007) J Exp Med , vol.204 , pp. 971-977
    • Shi, L.1    Godfrey, W.R.2    Lin, J.3    Zhao, G.4    Kao, P.N.5
  • 37
    • 0036924040 scopus 로고    scopus 로고
    • Nuclear export of NF90 is required for interleukin-2 mRNA stabilization
    • Shim J, Lim H, Yates JR and Karin M (2002) Nuclear export of NF90 is required for interleukin-2 mRNA stabilization. Mol Cell 10, 1331–1344.
    • (2002) Mol Cell , vol.10 , pp. 1331-1344
    • Shim, J.1    Lim, H.2    Yates, J.R.3    Karin, M.4
  • 38
    • 78649855245 scopus 로고    scopus 로고
    • Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense
    • Harashima A, Guettouche T and Barber GN (2010) Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense. Genes Dev 24, 2640–2653.
    • (2010) Genes Dev , vol.24 , pp. 2640-2653
    • Harashima, A.1    Guettouche, T.2    Barber, G.N.3
  • 39
    • 84910675034 scopus 로고    scopus 로고
    • NF90 isoforms, a new family of cellular proteins involved in viral replication?
    • Patino C, Haenni AL and Urcuqui-Inchima S (2015) NF90 isoforms, a new family of cellular proteins involved in viral replication? Biochimie 108, 20–24.
    • (2015) Biochimie , vol.108 , pp. 20-24
    • Patino, C.1    Haenni, A.L.2    Urcuqui-Inchima, S.3
  • 40
    • 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, Lai A, Smith GJ, Zhang J, Lin T and Guan Y (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    Song, W.2    Mok, B.W.3    Zhao, P.4    Qin, K.5    Lai, A.6    Smith, G.J.7    Zhang, J.8    Lin, T.9    Guan, Y.10
  • 43
    • 79960363657 scopus 로고    scopus 로고
    • HIV-1 replication and latency are regulated by translational control of cyclin T1
    • Hoque M, Shamanna RA, Guan D, Pe'ery T and Mathews MB (2011) HIV-1 replication and latency are regulated by translational control of cyclin T1. J Mol Biol 410, 917–932.
    • (2011) J Mol Biol , vol.410 , pp. 917-932
    • Hoque, M.1    Shamanna, R.A.2    Guan, D.3    Pe'ery, T.4    Mathews, M.B.5
  • 44
    • 33645229489 scopus 로고    scopus 로고
    • Cell-type-specific repression of internal ribosome entry site activity by double-stranded RNA-binding protein 76
    • Merrill MK, Dobrikova EY and Gromeier M (2006) Cell-type-specific repression of internal ribosome entry site activity by double-stranded RNA-binding protein 76. J Virol 80, 3147–3156.
    • (2006) J Virol , vol.80 , pp. 3147-3156
    • Merrill, M.K.1    Dobrikova, E.Y.2    Gromeier, M.3
  • 45
    • 33745778659 scopus 로고    scopus 로고
    • The double-stranded RNA binding protein 76:NF45 heterodimer inhibits translation initiation at the rhinovirus type 2 internal ribosome entry site
    • Merrill MK and Gromeier M (2006) The double-stranded RNA binding protein 76:NF45 heterodimer inhibits translation initiation at the rhinovirus type 2 internal ribosome entry site. J Virol 80, 6936–6942.
    • (2006) J Virol , vol.80 , pp. 6936-6942
    • Merrill, M.K.1    Gromeier, M.2
  • 46
    • 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 and Gehrke L (2011) NF90 binds the dengue virus RNA 3’ terminus and is a positive regulator of dengue virus replication. PLoS One 6, e16687.
    • (2011) PLoS One , vol.6
    • Gomila, R.C.1    Martin, G.W.2    Gehrke, L.3
  • 47
    • 84958780009 scopus 로고    scopus 로고
    • NF45 and NF90 bind HIV-1 RNA and modulate HIV gene expression
    • Li Y and Belshan M (2016) NF45 and NF90 bind HIV-1 RNA and modulate HIV gene expression. Viruses 8, 47.
    • (2016) Viruses , vol.8 , pp. 47
    • Li, Y.1    Belshan, M.2
  • 48
    • 0036008607 scopus 로고    scopus 로고
    • Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA
    • Shin HJ, Kim SS, Cho YH, Lee SG and Rho HM (2002) Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA. Arch Virol 147, 471–491.
    • (2002) Arch Virol , vol.147 , pp. 471-491
    • Shin, H.J.1    Kim, S.S.2    Cho, Y.H.3    Lee, S.G.4    Rho, H.M.5
  • 50
    • 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 and Lemon SM (2014) hnRNP L and NF90 interact with hepatitis C virus 5’-terminal untranslated RNA and promote efficient replication. J Virol 88, 7199–7209.
    • (2014) J Virol , vol.88 , pp. 7199-7209
    • Li, Y.1    Masaki, T.2    Shimakami, T.3    Lemon, S.M.4
  • 51
    • 84886772094 scopus 로고    scopus 로고
    • Induction of p53, p21 and apoptosis by silencing the NF90/NF45 complex in human papilloma virus-transformed cervical carcinoma cells
    • Shamanna RA, Hoque M, Pe'ery T and Mathews MB (2013) Induction of p53, p21 and apoptosis by silencing the NF90/NF45 complex in human papilloma virus-transformed cervical carcinoma cells. Oncogene 32, 5176–5185.
    • (2013) Oncogene , vol.32 , pp. 5176-5185
    • Shamanna, R.A.1    Hoque, M.2    Pe'ery, T.3    Mathews, M.B.4
  • 52
    • 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, Lau SY, Wang P, Song W, Jin DY and Yuen KY (2014) NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells. J Immunol 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    Lau, S.Y.6    Wang, P.7    Song, W.8    Jin, D.Y.9    Yuen, K.Y.10
  • 53
    • 0032995665 scopus 로고    scopus 로고
    • RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids
    • Wang W, Riedel K, Lynch P, Chien CY, Montelione GT and Krug RM (1999) RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids. RNA 5, 195–205.
    • (1999) RNA , vol.5 , pp. 195-205
    • Wang, W.1    Riedel, K.2    Lynch, P.3    Chien, C.Y.4    Montelione, G.T.5    Krug, R.M.6
  • 54
    • 0345167006 scopus 로고    scopus 로고
    • A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice
    • Donelan NR, Basler CF and Garcia-Sastre A (2003) A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice. J Virol 77, 13257–13266.
    • (2003) J Virol , vol.77 , pp. 13257-13266
    • Donelan, N.R.1    Basler, C.F.2    Garcia-Sastre, A.3
  • 57
    • 0025298202 scopus 로고
    • Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon
    • Meurs E, Chong K, Galabru J, Thomas NS, Kerr IM, Williams BR and Hovanessian AG (1990) Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62, 379–390.
    • (1990) Cell , vol.62 , pp. 379-390
    • Meurs, E.1    Chong, K.2    Galabru, J.3    Thomas, N.S.4    Kerr, I.M.5    Williams, B.R.6    Hovanessian, A.G.7
  • 59
    • 78651488459 scopus 로고    scopus 로고
    • The role of protein kinase R in the interferon response
    • Pindel A and Sadler A (2011) The role of protein kinase R in the interferon response. J Interferon Cytokine Res 31, 59–70.
    • (2011) J Interferon Cytokine Res , vol.31 , pp. 59-70
    • Pindel, A.1    Sadler, A.2
  • 60
    • 0345164384 scopus 로고    scopus 로고
    • Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase
    • Gale M Jr and Katze MG (1998) Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase. Pharmacol Ther 78, 29–46.
    • (1998) Pharmacol Ther , vol.78 , pp. 29-46
    • Gale, M.1    Katze, M.G.2
  • 61
    • 84894501374 scopus 로고    scopus 로고
    • Evidence for a crucial role of a host non-coding RNA in influenza A virus replication
    • Winterling C, Koch M, Koeppel M, Garcia-Alcalde F, Karlas A and Meyer TF (2014) Evidence for a crucial role of a host non-coding RNA in influenza A virus replication. RNA Biol 11, 66–75.
    • (2014) RNA Biol , vol.11 , pp. 66-75
    • Winterling, C.1    Koch, M.2    Koeppel, M.3    Garcia-Alcalde, F.4    Karlas, A.5    Meyer, T.F.6
  • 63
    • 84910625872 scopus 로고    scopus 로고
    • NRAV, a long noncoding RNA, modulates antiviral responses through suppression of interferon-stimulated gene transcription
    • Ouyang J, Zhu X, Chen Y, Wei H, Chen Q, Chi X, Qi B, Zhang L, Zhao Y and Gao GF (2014) NRAV, a long noncoding RNA, modulates antiviral responses through suppression of interferon-stimulated gene transcription. Cell Host Microbe 16, 616–626.
    • (2014) Cell Host Microbe , vol.16 , pp. 616-626
    • Ouyang, J.1    Zhu, X.2    Chen, Y.3    Wei, H.4    Chen, Q.5    Chi, X.6    Qi, B.7    Zhang, L.8    Zhao, Y.9    Gao, G.F.10
  • 64
    • 44649110160 scopus 로고    scopus 로고
    • Viral and cellular microRNAs as determinants of viral pathogenesis and immunity
    • Gottwein E and Cullen BR (2008) Viral and cellular microRNAs as determinants of viral pathogenesis and immunity. Cell Host Microbe 3, 375–387.
    • (2008) Cell Host Microbe , vol.3 , pp. 375-387
    • Gottwein, E.1    Cullen, B.R.2
  • 66
    • 57749169511 scopus 로고    scopus 로고
    • X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus
    • Bornholdt ZA and Prasad BV (2008) X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus. Nature 456, 985–988.
    • (2008) Nature , vol.456 , pp. 985-988
    • Bornholdt, Z.A.1    Prasad, B.V.2
  • 67
    • 84871997466 scopus 로고    scopus 로고
    • Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1
    • Okonski KM and Samuel CE (2013) Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1. J Virol 87, 756–766.
    • (2013) J Virol , vol.87 , pp. 756-766
    • Okonski, K.M.1    Samuel, C.E.2
  • 68
    • 84863407268 scopus 로고    scopus 로고
    • Regulation of stress granules in virus systems
    • White JP and Lloyd RE (2012) Regulation of stress granules in virus systems. Trends Microbiol 20, 175–183.
    • (2012) Trends Microbiol , vol.20 , pp. 175-183
    • White, J.P.1    Lloyd, R.E.2
  • 69
    • 84925545570 scopus 로고    scopus 로고
    • Utilization of liquid chromatography mass spectrometry analyses to identify LKB1-APC interaction in modulating Wnt/beta-catenin pathway of lung cancer cells
    • Jian SF, Hsiao CC, Chen SY, Weng CC, Kuo TL, Wu DC, Hung WC and Cheng KH (2014) Utilization of liquid chromatography mass spectrometry analyses to identify LKB1-APC interaction in modulating Wnt/beta-catenin pathway of lung cancer cells. Mol Cancer Res 12, 622–635.
    • (2014) Mol Cancer Res , vol.12 , pp. 622-635
    • Jian, S.F.1    Hsiao, C.C.2    Chen, S.Y.3    Weng, C.C.4    Kuo, T.L.5    Wu, D.C.6    Hung, W.C.7    Cheng, K.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.