메뉴 건너뛰기
Journal of Virology
Volumn 88, Issue 19, 2014, Pages 11154-11165
Inhibition of antiviral innate immunity by birnavirus VP3 protein via blockage of viral double-stranded RNA binding to the host cytoplasmic RNA detector MDA5
Author keywords

[No Author keywords available]
Indexed keywords

BETA INTERFERON; DOUBLE STRANDED RNA; INTERFERON; PATTERN RECOGNITION RECEPTOR; PROTEIN MDA5; PROTEIN VP3; UNCLASSIFIED DRUG; AVIAN PROTEIN; DEAD BOX PROTEIN; VIRUS PROTEIN; VIRUS RNA; VP3 PROTEIN, INFECTIOUS BURSAL DISEASE VIRUS;
EID: 84906968604     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01115-14     Document Type: Article
Times cited : (54)
References (49)
  • 1
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M. 2006. Intracellular pattern recognition receptors in the host response. Nature 442:39-44. http://dx.doi.org/10.1038/nature04946.
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 2
    • 69949108452 scopus 로고    scopus 로고
    • RIG-I-like receptors: sensing and responding toRNAvirus infection
    • Nakhaei P, Genin P, Civas A, Hiscott J. 2009. RIG-I-like receptors: sensing and responding toRNAvirus infection. Semin. Immunol. 21:215-222. http://dx.doi.org/10.1016/j.smim.2009.05.001.
    • (2009) Semin. Immunol. , vol.21 , pp. 215-222
    • Nakhaei, P.1    Genin, P.2    Civas, A.3    Hiscott, J.4
  • 3
    • 80052143412 scopus 로고    scopus 로고
    • RIG-I-like receptors: cytoplasmic sensors for non-self RNA
    • Kato H, Takahasi K, Fujita T. 2011. RIG-I-like receptors: cytoplasmic sensors for non-self RNA. Immunol. Rev. 243:91-98. http://dx.doi.org/10.1111/j.1600-065X.2011.01052.x.
    • (2011) Immunol. Rev. , vol.243 , pp. 91-98
    • Kato, H.1    Takahasi, K.2    Fujita, T.3
  • 4
    • 77957997708 scopus 로고    scopus 로고
    • Preference of RIG-I for short viralRNAmolecules in infected cells revealed by next-generation sequencing
    • Baum A, Sachidanandam R, Garcia-Sastre A. 2010. Preference of RIG-I for short viralRNAmolecules in infected cells revealed by next-generation sequencing. Proc. Natl. Acad. Sci. U. S. A. 107:16303-16308. http://dx.doi.org/10.1073/pnas.1005077107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16303-16308
    • Baum, A.1    Sachidanandam, R.2    Garcia-Sastre, A.3
  • 5
    • 68049089651 scopus 로고    scopus 로고
    • Recognition of 5= triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus
    • Schlee M, Roth A, Hornung V, Hagmann CA, Wimmenauer V, Barchet W, Coch C, Janke M, Mihailovic A, Wardle G. 2009. Recognition of 5= triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 31:25-34. http://dx.doi.org/10.1016/j.immuni.2009.05.008.
    • (2009) Immunity , vol.31 , pp. 25-34
    • Schlee, M.1    Roth, A.2    Hornung, V.3    Hagmann, C.A.4    Wimmenauer, V.5    Barchet, W.6    Coch, C.7    Janke, M.8    Mihailovic, A.9    Wardle, G.10
  • 7
    • 79955533131 scopus 로고    scopus 로고
    • Characterization of chicken Mda5 activity: regulation of IFN-beta in the absence of RIG-I functionality
    • Karpala AJ, Stewart C, McKay J, Lowenthal JW, Bean AG. 2011. Characterization of chicken Mda5 activity: regulation of IFN-beta in the absence of RIG-I functionality. J. Immunol. 186:5397-5405. http://dx.doi.org/10.4049/jimmunol.1003712.
    • (2011) J. Immunol. , vol.186 , pp. 5397-5405
    • Karpala, A.J.1    Stewart, C.2    McKay, J.3    Lowenthal, J.W.4    Bean, A.G.5
  • 8
    • 41549087403 scopus 로고    scopus 로고
    • Proteomics analysis of host cells infected with infectious bursal disease virus
    • Zheng X, Hong L, Shi L, Guo J, Sun Z, Zhou J. 2008. Proteomics analysis of host cells infected with infectious bursal disease virus. Mol. Cell. Proteomics 7:612-625. http://dx.doi.org/10.1074/mcp.M700396-MCP200.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 612-625
    • Zheng, X.1    Hong, L.2    Shi, L.3    Guo, J.4    Sun, Z.5    Zhou, J.6
  • 9
    • 0034715855 scopus 로고    scopus 로고
    • VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane and induces cell lysis
    • Lombardo E, Maraver A, Espinosa I, Ferna´ndez-Arias A, Rodriguez JF. 2000. VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane and induces cell lysis. Virology 277:345-357. http://dx.doi.org/10.1006/viro.2000.0595.
    • (2000) Virology , vol.277 , pp. 345-357
    • Lombardo, E.1    Maraver, A.2    Espinosa, I.3    Ferna´ndez-Arias, A.4    Rodriguez, J.F.5
  • 10
    • 76149130046 scopus 로고    scopus 로고
    • The VP5 protein of infectious bursal disease virus promotes virion release from infected cells and is not involved in cell death
    • Wu Y, Hong L, Ye J, Huang Z, Zhou J. 2009. The VP5 protein of infectious bursal disease virus promotes virion release from infected cells and is not involved in cell death. Arch. Virol. 154:1873-1882. http://dx.doi.org/10.1007/s00705-009-0524-4.
    • (2009) Arch. Virol. , vol.154 , pp. 1873-1882
    • Wu, Y.1    Hong, L.2    Ye, J.3    Huang, Z.4    Zhou, J.5
  • 11
    • 0036168067 scopus 로고    scopus 로고
    • The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids
    • Chevalier C, Lepault J, Erk I, Da Costa B, Delmas B. 2002. The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids. J. Virol. 76:2384-2392. http://dx.doi.org/10.1128/jvi.76.5.2384-2392.2002.
    • (2002) J. Virol. , vol.76 , pp. 2384-2392
    • Chevalier, C.1    Lepault, J.2    Erk, I.3    Da Costa, B.4    Delmas, B.5
  • 12
    • 0036173429 scopus 로고    scopus 로고
    • The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2
    • Da Costa B, Chevalier C, Henry C, Huet J-C, Petit S, Lepault J, Boot H, Delmas B. 2002. The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2. J. Virol. 76:2393-2402. http://dx.doi.org/10.1128/jvi.76.5.2393-2402.2002.
    • (2002) J. Virol. , vol.76 , pp. 2393-2402
    • Da Costa, B.1    Chevalier, C.2    Henry, C.3    Huet, J.-C.4    Petit, S.5    Lepault, J.6    Boot, H.7    Delmas, B.8
  • 15
    • 33645465215 scopus 로고    scopus 로고
    • Infectious bursal disease virus: strains that differ in virulence differentially modulate the innate immune response to infection in the chicken bursa
    • Eldaghayes I, Rothwell L, Williams A, Withers D, Balu S, Davison F, Kaiser P. 2006. Infectious bursal disease virus: strains that differ in virulence differentially modulate the innate immune response to infection in the chicken bursa. Viral Immunol. 19:83-91. http://dx.doi.org/10.1089/vim.2006.19.83.
    • (2006) Viral Immunol , vol.19 , pp. 83-91
    • Eldaghayes, I.1    Rothwell, L.2    Williams, A.3    Withers, D.4    Balu, S.5    Davison, F.6    Kaiser, P.7
  • 16
    • 84871995488 scopus 로고    scopus 로고
    • Critical roles of glucocorticoid-induced leucine zipper in infectious bursal disease virus (IBDV)-induced suppression of type I interferon expression and enhancement of IBDV growth in host cells via interaction with VP4
    • Li Z, Wang Y, Li X, Li X, Cao H, Zheng SJ. 2013. Critical roles of glucocorticoid-induced leucine zipper in infectious bursal disease virus (IBDV)-induced suppression of type I interferon expression and enhancement of IBDV growth in host cells via interaction with VP4. J. Virol. 87:1221-1231. http://dx.doi.org/10.1128/JVI.02421-12.
    • (2013) J. Virol. , vol.87 , pp. 1221-1231
    • Li, Z.1    Wang, Y.2    Li, X.3    Li, X.4    Cao, H.5    Zheng, S.J.6
  • 17
    • 0037386822 scopus 로고    scopus 로고
    • Characterization of the RNA-binding activity of VP3, a major structural protein of infectious bursal disease virus
    • Kochan G, Gonzalez D, Rodriguez J. 2003. Characterization of the RNA-binding activity of VP3, a major structural protein of infectious bursal disease virus. Arch. Virol. 148:723-744. http://dx.doi.org/10.1007/s00705-002-0949-5.
    • (2003) Arch. Virol. , vol.148 , pp. 723-744
    • Kochan, G.1    Gonzalez, D.2    Rodriguez, J.3
  • 18
    • 84866657279 scopus 로고    scopus 로고
    • The VP3 factor from viruses of Birnaviridae family suppresses RNA silencing by binding both long and small RNA duplexes
    • Valli A, Busnadiego I, Maliogka V, Ferrero D, Casto´n JR, Rodri´guez JF, Garci´a JA. 2012. The VP3 factor from viruses of Birnaviridae family suppresses RNA silencing by binding both long and small RNA duplexes. PLoS One 7:e45957. http://dx.doi.org/10.1371/journal.pone.0045957.
    • (2012) PLoS One , vol.7 , pp. e45957
    • Valli, A.1    Busnadiego, I.2    Maliogka, V.3    Ferrero, D.4    Casto´n, J.R.5    Rodri´guez, J.F.6    Garci´a, J.A.7
  • 19
    • 84867319379 scopus 로고    scopus 로고
    • The infectious bursal disease virus RNA-binding VP3 polypeptide inhibits PKR-mediated apoptosis
    • Busnadiego I, Maestre AM, Rodri´guez D, Rodri´guez JF. 2012. The infectious bursal disease virus RNA-binding VP3 polypeptide inhibits PKR-mediated apoptosis. PLoS One 7:e46768. http://dx.doi.org/10.1371/journal.pone.0046768.
    • (2012) PLoS One , vol.7 , pp. e46768
    • Busnadiego, I.1    Maestre, A.M.2    Rodri´guez, D.3    Rodri´guez, J.F.4
  • 20
    • 0036828149 scopus 로고    scopus 로고
    • Infectious bursal disease virus capsid protein VP3 interacts both with VP1, the RNA-dependent RNA polymerase, and with viral double-stranded RNA
    • Tacken MG, Peeters BP, Thomas AA, Rottier PJ, Boot HJ. 2002. Infectious bursal disease virus capsid protein VP3 interacts both with VP1, the RNA-dependent RNA polymerase, and with viral double-stranded RNA. J. Virol. 76:11301-11311. http://dx.doi.org/10.1128/JVI.76.22.11301-11311.2002.
    • (2002) J. Virol. , vol.76 , pp. 11301-11311
    • Tacken, M.G.1    Peeters, B.P.2    Thomas, A.A.3    Rottier, P.J.4    Boot, H.J.5
  • 22
    • 15944407299 scopus 로고    scopus 로고
    • Antigenic and molecular characterization of infectious bursal disease virus in China from layer chicken flocks
    • Zhou J, Ye J, Ye W, Chen Q, Zheng X, Guo J. 2005. Antigenic and molecular characterization of infectious bursal disease virus in China from layer chicken flocks. Prog. Biochem. Biophys. 32:37-45. http://dx.doi.org/10.3321/j.issn:1000-3282.2005.01.007.
    • (2005) Prog. Biochem. Biophys. , vol.32 , pp. 37-45
    • Zhou, J.1    Ye, J.2    Ye, W.3    Chen, Q.4    Zheng, X.5    Guo, J.6
  • 23
    • 67649559816 scopus 로고    scopus 로고
    • Competitive replication of different genotypes of infectious bursal disease virus on chicken embryo fibroblasts
    • Shi L, Li H, Ma G, Zhou J, Hong L, Zheng X, Wu Y, Wang Y, Yan Y. 2009. Competitive replication of different genotypes of infectious bursal disease virus on chicken embryo fibroblasts. Virus Genes 39:46-52. http://dx.doi.org/10.1007/s11262-008-0313-2.
    • (2009) Virus Genes , vol.39 , pp. 46-52
    • Shi, L.1    Li, H.2    Ma, G.3    Zhou, J.4    Hong, L.5    Zheng, X.6    Wu, Y.7    Wang, Y.8    Yan, Y.9
  • 24
    • 84862874910 scopus 로고    scopus 로고
    • Proteome dynamics in primary target organ of infectious bursal disease virus
    • Wu Y, Peng C, Xu L, Zheng X, Liao M, Yan Y, Jin Y, Zhou J. 2012. Proteome dynamics in primary target organ of infectious bursal disease virus. Proteomics 12:1844 -1859. http://dx.doi.org/10.1002/pmic.201100479.
    • (2012) Proteomics , vol.12 , pp. 1844-1859
    • Wu, Y.1    Peng, C.2    Xu, L.3    Zheng, X.4    Liao, M.5    Yan, Y.6    Jin, Y.7    Zhou, J.8
  • 25
    • 33845298265 scopus 로고    scopus 로고
    • In vitro expression and monoclonal antibody of RNA-dependent RNA polymerase for infectious bursal disease virus
    • Zheng X, Hong L, Li Y, Guo J, Zhang G, Zhou J. 2006. In vitro expression and monoclonal antibody of RNA-dependent RNA polymerase for infectious bursal disease virus. DNA Cell Biol. 25:646-653. http://dx.doi.org/10.1089/dna.2006.25.646.
    • (2006) DNA Cell Biol , vol.25 , pp. 646-653
    • Zheng, X.1    Hong, L.2    Li, Y.3    Guo, J.4    Zhang, G.5    Zhou, J.6
  • 26
    • 67349249346 scopus 로고    scopus 로고
    • Antibody to VP4 protein is an indicator discriminating pathogenic and nonpathogenic IBDV infection
    • Wang Y, Wu X, Li H, Wu Y, Shi L, Zheng X, Luo M, Yan Y, Zhou J. 2009. Antibody to VP4 protein is an indicator discriminating pathogenic and nonpathogenic IBDV infection. Mol. Immunol. 46:1964-1969. http://dx.doi.org/10.1016/j.molimm.2009.03.011.
    • (2009) Mol. Immunol. , vol.46 , pp. 1964-1969
    • Wang, Y.1    Wu, X.2    Li, H.3    Wu, Y.4    Shi, L.5    Zheng, X.6    Luo, M.7    Yan, Y.8    Zhou, J.9
  • 27
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed LJ, Muench H. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 28
    • 0032540360 scopus 로고    scopus 로고
    • Promoter structures and differential responses to viral and nonviral inducers of chicken type I interferon genes
    • Sick C, Schultz U, Munster U, Meier J, Kaspers B, Staeheli P. 1998. Promoter structures and differential responses to viral and nonviral inducers of chicken type I interferon genes. J. Biol. Chem. 273:9749-9754. http://dx.doi.org/10.1074/jbc.273.16.9749.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9749-9754
    • Sick, C.1    Schultz, U.2    Munster, U.3    Meier, J.4    Kaspers, B.5    Staeheli, P.6
  • 29
    • 84880377810 scopus 로고    scopus 로고
    • Cellular chaperonin CCT_ contributes to rabies virus replication during infection
    • Zhang J, Wu X, Zan J, Wu Y, Ye C, Ruan X, Zhou J. 2013. Cellular chaperonin CCT_ contributes to rabies virus replication during infection. J. Virol. 87:7608-7621. http://dx.doi.org/10.1128/JVI.03186-12.
    • (2013) J. Virol. , vol.87 , pp. 7608-7621
    • Zhang, J.1    Wu, X.2    Zan, J.3    Wu, Y.4    Ye, C.5    Ruan, X.6    Zhou, J.7
  • 30
    • 70449381259 scopus 로고    scopus 로고
    • Differential proteome analysis of host cells infected with porcine circovirus type 2
    • Zhang X, Zhou J, Wu Y, Zheng X, Ma G, Wang Z, Jin Y, He J, Yan Y. 2009. Differential proteome analysis of host cells infected with porcine circovirus type 2. J. Proteome Res. 8:5111-5119. http://dx.doi.org/10.1021/pr900488q.
    • (2009) J. Proteome Res. , vol.8 , pp. 5111-5119
    • Zhang, X.1    Zhou, J.2    Wu, Y.3    Zheng, X.4    Ma, G.5    Wang, Z.6    Jin, Y.7    He, J.8    Yan, Y.9
  • 31
    • 78651227626 scopus 로고    scopus 로고
    • Novel inhibitor of influenza non-structural protein 1 blocks multi-cycle replication in an RNase L-dependent manner
    • Walkiewicz MP, Basu D, Jablonski JJ, Geysen HM, Engel DA. 2011. Novel inhibitor of influenza non-structural protein 1 blocks multi-cycle replication in an RNase L-dependent manner. J. Gen. Virol. 92:60-70. http://dx.doi.org/10.1099/vir.0.025015-0.
    • (2011) J. Gen. Virol. , vol.92 , pp. 60-70
    • Walkiewicz, M.P.1    Basu, D.2    Jablonski, J.J.3    Geysen, H.M.4    Engel, D.A.5
  • 33
    • 0033991450 scopus 로고    scopus 로고
    • Generation of full-length cDNA of the two genomic dsRNA segments of infectious bursal disease virus
    • Boot HJ, Ter Huurne AH, Peeters BP. 2000. Generation of full-length cDNA of the two genomic dsRNA segments of infectious bursal disease virus. J. Virol. Methods 84:49-58. http://dx.doi.org/10.1016/S0166-0934(99)00132-9.
    • (2000) J. Virol. Methods , vol.84 , pp. 49-58
    • Boot, H.J.1    Ter Huurne, A.H.2    Peeters, B.P.3
  • 34
    • 84863962538 scopus 로고    scopus 로고
    • LSm14A is a processing body-associated sensor of viral nucleic acids that initiates cellular antiviral response in the early phase of viral infection
    • Li Y, Chen R, Zhou Q, Xu Z, Li C, Wang S, Mao A, Zhang X, He W, Shu H-B. 2012. LSm14A is a processing body-associated sensor of viral nucleic acids that initiates cellular antiviral response in the early phase of viral infection. Proc. Natl. Acad. Sci. U. S. A. 109:11770-11775. http://dx.doi.org/10.1073/pnas.1203405109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 11770-11775
    • Li, Y.1    Chen, R.2    Zhou, Q.3    Xu, Z.4    Li, C.5    Wang, S.6    Mao, A.7    Zhang, X.8    He, W.9    Shu, H.-B.10
  • 35
    • 84863126126 scopus 로고    scopus 로고
    • Critical role for voltage-dependent anion channel 2 in infectious bursal disease virusinduced apoptosis in host cells via interaction with VP5
    • Li Z, Wang Y, Xue Y, Li X, Cao H, Zheng SJ. 2012. Critical role for voltage-dependent anion channel 2 in infectious bursal disease virusinduced apoptosis in host cells via interaction with VP5. J. Virol. 86:1328- 1338. http://dx.doi.org/10.1128/JVI.06104-11.
    • (2012) J. Virol. , vol.86 , pp. 1328-1338
    • Li, Z.1    Wang, Y.2    Xue, Y.3    Li, X.4    Cao, H.5    Zheng, S.J.6
  • 37
    • 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 J-Y, 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
  • 38
    • 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 J-Y, Li S, Sen GC, 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. http://dx.doi.org/10.1016/j.virol.2007.01.038.
    • (2007) Virology , vol.363 , pp. 236-243
    • Min, J.-Y.1    Li, S.2    Sen, G.C.3    Krug, R.M.4
  • 39
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1. 8 A˚ resolution
    • Olland AM, Jane´-Valbuena J, Schiff LA, Nibert ML, Harrison SC. 2001. Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 A˚ resolution. EMBO J. 20:979-989. http://dx.doi.org/10.1093/emboj/20.5.979.
    • (2001) EMBO J , vol.20 , pp. 979-989
    • Olland, A.M.1    Jane´-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 40
    • 70349234222 scopus 로고    scopus 로고
    • Rotavirus and reovirus modulation of the interferon response
    • Sherry B. 2009. Rotavirus and reovirus modulation of the interferon response. J. Interferon Cytokine Res. 29:559-567. http://dx.doi.org/10.1089/jir.2009.0072.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 559-567
    • Sherry, B.1
  • 42
    • 84873523444 scopus 로고    scopus 로고
    • Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling
    • Motz C, Schuhmann KM, Kirchhofer A, Moldt M, Witte G, Conzelmann K-K, Hopfner K-P. 2013. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science 339: 690-693. http://dx.doi.org/10.1126/science.1230949.
    • (2013) Science , vol.339 , pp. 690-693
    • Motz, C.1    Schuhmann, K.M.2    Kirchhofer, A.3    Moldt, M.4    Witte, G.5    Conzelmann, K.-K.6    Hopfner, K.-P.7
  • 43
    • 33845728488 scopus 로고    scopus 로고
    • The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR
    • Feng Z, Cerveny M, Yan Z, He B. 2007. The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR. J. Virol. 81:182-192. http://dx.doi.org/10.1128/JVI.01006-06.
    • (2007) J. Virol. , vol.81 , pp. 182-192
    • Feng, Z.1    Cerveny, M.2    Yan, Z.3    He, B.4
  • 44
    • 21644460103 scopus 로고    scopus 로고
    • Human cytomegalovirus TRS1 and IRS1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection
    • Cassady KA. 2005. Human cytomegalovirus TRS1 and IRS1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection. J. Virol. 79:8707- 8715. http://dx.doi.org/10.1128/JVI.79.14.8707-8715.2005.
    • (2005) J. Virol. , vol.79 , pp. 8707-8715
    • Cassady, K.A.1
  • 45
    • 19944372421 scopus 로고    scopus 로고
    • Double-stranded RNA binding by human cytomegalovirus pTRS1
    • Hakki M, Geballe AP. 2005. Double-stranded RNA binding by human cytomegalovirus pTRS1. J. Virol. 79:7311-7318. http://dx.doi.org/10.1128/JVI.79.12.7311-7318.2005.
    • (2005) J. Virol. , vol.79 , pp. 7311-7318
    • Hakki, M.1    Geballe, A.P.2
  • 46
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu B, Peisley A, Richards C, Yao H, Zeng X, Lin C, Chu F, Walz T, Hur S. 2013. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 152:276-289. http://dx.doi.org/10.1016/j.cell.2012.11.048.
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6    Chu, F.7    Walz, T.8    Hur, S.9
  • 47
    • 67650510680 scopus 로고    scopus 로고
    • Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors
    • Takahasi K, Kumeta H, Tsuduki N, Narita R, Shigemoto T, Hirai R, Yoneyama M, Horiuchi M, Ogura K, Fujita T. 2009. Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. J. Biol. Chem. 284:17465-17474. http://dx.doi.org/10.1074/jbc.M109.007179.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17465-17474
    • Takahasi, K.1    Kumeta, H.2    Tsuduki, N.3    Narita, R.4    Shigemoto, T.5    Hirai, R.6    Yoneyama, M.7    Horiuchi, M.8    Ogura, K.9    Fujita, T.10
  • 48
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth RB, Sun L, Ea CK, Chen ZJ. 2005. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 122:669-682. http://dx.doi.org/10.1016/j.cell.2005.08.012.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 49
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ. 2011. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146:448-461. http://dx.doi.org/10.1016/j.cell.2011.06.041.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.