메뉴 건너뛰기




Volumn 89, Issue 17, 2015, Pages 9029-9043

The nucleocapsid protein of coronaviruses acts as a viral suppressor of RNA silencing in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

ARGONAUTE 2 PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; NUCLEOCAPSID PROTEIN; RNA; SHORT HAIRPIN RNA; SMALL INTERFERING RNA; ARGONAUTE PROTEIN; DEAD BOX PROTEIN; DICER1 PROTEIN, MOUSE; EIF2C2 PROTEIN, MOUSE; NUCLEOCAPSID PROTEIN, CORONAVIRUS; RIBONUCLEASE III;

EID: 84938916581     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01331-15     Document Type: Article
Times cited : (151)

References (74)
  • 1
    • 60149088848 scopus 로고    scopus 로고
    • Origins and mechanisms of miRNAs and siRNAs
    • Carthew RW, Sontheimer EJ. 2009. Origins and mechanisms of miRNAs and siRNAs. Cell 136:642-655. http://dx.doi.org/10.1016/j.cell.2009.01.035.
    • (2009) Cell , vol.136 , pp. 642-655
    • Carthew, R.W.1    Sontheimer, E.J.2
  • 2
    • 77956170809 scopus 로고    scopus 로고
    • RNA-based antiviral immunity
    • Ding SW. 2010. RNA-based antiviral immunity. Nat Rev Immunol 10: 632-644. http://dx.doi.org/10.1038/nri2824.
    • (2010) Nat Rev Immunol , vol.10 , pp. 632-644
    • Ding, S.W.1
  • 3
    • 66149125689 scopus 로고    scopus 로고
    • The role of RNAi and microRNAs in animal virus replication and antiviral immunity
    • Umbach JL, Cullen BR. 2009. The role of RNAi and microRNAs in animal virus replication and antiviral immunity. Genes Dev 23:1151-1164. http://dx.doi.org/10.1101/gad.1793309.
    • (2009) Genes Dev , vol.23 , pp. 1151-1164
    • Umbach, J.L.1    Cullen, B.R.2
  • 4
    • 58049202272 scopus 로고    scopus 로고
    • Innate immunity to virus infection
    • Takeuchi O, Akira S. 2009. Innate immunity to virus infection. Immunol Rev 227:75-86. http://dx.doi.org/10.1111/j.1600-065X.2008.00737.x.
    • (2009) Immunol Rev , vol.227 , pp. 75-86
    • Takeuchi, O.1    Akira, S.2
  • 6
    • 84885635441 scopus 로고    scopus 로고
    • RNA interference functions as an antiviral immunity mechanism in mammals
    • Li Y, Lu J, Han Y, Fan X, Ding SW. 2013. RNA interference functions as an antiviral immunity mechanism in mammals. Science 342:231-234. http://dx.doi.org/10.1126/science.1241911.
    • (2013) Science , vol.342 , pp. 231-234
    • Li, Y.1    Lu, J.2    Han, Y.3    Fan, X.4    Ding, S.W.5
  • 8
    • 84885638182 scopus 로고    scopus 로고
    • Molecular biology: RNAi, antiviral after all
    • Sagan SM, Sarnow P. 2013. Molecular biology: RNAi, antiviral after all. Science 342:207-208. http://dx.doi.org/10.1126/science.1245475.
    • (2013) Science , vol.342 , pp. 207-208
    • Sagan, S.M.1    Sarnow, P.2
  • 9
    • 14344252157 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing: insights from viral infections
    • Voinnet O. 2005. Induction and suppression of RNA silencing: insights from viral infections. Nat Rev Genet 6:206-220. http://dx.doi.org/10.1038/nrg1555.
    • (2005) Nat Rev Genet , vol.6 , pp. 206-220
    • Voinnet, O.1
  • 10
    • 78650575533 scopus 로고    scopus 로고
    • Viral RNA silencing suppressors (RSS): novel strategy of viruses to ablate the host RNA interference (RNAi) defense system
    • Bivalkar-Mehla S, Vakharia J, Mehla R, Abreha M, Kanwar JR, Tikoo A, Chauhan A. 2011. Viral RNA silencing suppressors (RSS): novel strategy of viruses to ablate the host RNA interference (RNAi) defense system. Virus Res 155:1-9. http://dx.doi.org/10.1016/j.virusres.2010.10.003.
    • (2011) Virus Res , vol.155 , pp. 1-9
    • Bivalkar-Mehla, S.1    Vakharia, J.2    Mehla, R.3    Abreha, M.4    Kanwar, J.R.5    Tikoo, A.6    Chauhan, A.7
  • 11
    • 34250895710 scopus 로고    scopus 로고
    • The NS3 protein of Rice hoja blanca tenuivirus suppresses RNA silencing in plant and insect hosts by efficiently binding both siRNAs and miRNAs
    • Hemmes H, Lakatos L, Goldbach R, Burgyan J, Prins M. 2007. The NS3 protein of Rice hoja blanca tenuivirus suppresses RNA silencing in plant and insect hosts by efficiently binding both siRNAs and miRNAs. RNA 13:1079-1089. http://dx.doi.org/10.1261/rna.444007.
    • (2007) RNA , vol.13 , pp. 1079-1089
    • Hemmes, H.1    Lakatos, L.2    Goldbach, R.3    Burgyan, J.4    Prins, M.5
  • 13
    • 1842614300 scopus 로고    scopus 로고
    • Molecular mechanism of RNA silencing suppression mediated by p19 protein of tombusviruses
    • Lakatos L, Szittya G, Silhavy D, Burgyan J. 2004. Molecular mechanism of RNA silencing suppression mediated by p19 protein of tombusviruses. EMBO J 23:876-884. http://dx.doi.org/10.1038/sj.emboj.7600096.
    • (2004) EMBO J , vol.23 , pp. 876-884
    • Lakatos, L.1    Szittya, G.2    Silhavy, D.3    Burgyan, J.4
  • 14
    • 49149130474 scopus 로고    scopus 로고
    • Nuclear import of CaMV P6 is required for infection and suppression of the RNA silencing factor DRB4
    • Haas G, Azevedo J, Moissiard G, Geldreich A, Himber C, Bureau M, Fukuhara T, Keller M, Voinnet O. 2008. Nuclear import of CaMV P6 is required for infection and suppression of the RNA silencing factor DRB4. EMBO J 27:2102-2112. http://dx.doi.org/10.1038/emboj.2008.129.
    • (2008) EMBO J , vol.27 , pp. 2102-2112
    • Haas, G.1    Azevedo, J.2    Moissiard, G.3    Geldreich, A.4    Himber, C.5    Bureau, M.6    Fukuhara, T.7    Keller, M.8    Voinnet, O.9
  • 15
    • 0037295079 scopus 로고    scopus 로고
    • Turnip crinkle virus coat protein mediates suppression of RNA silencing in Nicotiana benthamiana
    • Thomas CL, Leh V, Lederer C, Maule AJ. 2003. Turnip crinkle virus coat protein mediates suppression of RNA silencing in Nicotiana benthamiana. Virology 306:33-41. http://dx.doi.org/10.1016/S0042-6822(02)00018-1.
    • (2003) Virology , vol.306 , pp. 33-41
    • Thomas, C.L.1    Leh, V.2    Lederer, C.3    Maule, A.J.4
  • 17
    • 0037123630 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing by an animal virus
    • Li H, Li WX, Ding SW. 2002. Induction and suppression of RNA silencing by an animal virus. Science 296:1319-1321. http://dx.doi.org/10.1126/science.1070948.
    • (2002) Science , vol.296 , pp. 1319-1321
    • Li, H.1    Li, W.X.2    Ding, S.W.3
  • 18
    • 84860840233 scopus 로고    scopus 로고
    • Targeting of dicer-2 and RNA by a viral RNA silencing suppressor in Drosophila cells
    • Qi N, Zhang L, Qiu Y, Wang Z, Si J, Liu Y, Xiang X, Xie J, Qin CF, Zhou X, Hu Y. 2012. Targeting of dicer-2 and RNA by a viral RNA silencing suppressor in Drosophila cells. J Virol 86:5763-5773. http://dx.doi.org/10.1128/JVI.07229-11.
    • (2012) J Virol , vol.86 , pp. 5763-5773
    • Qi, N.1    Zhang, L.2    Qiu, Y.3    Wang, Z.4    Si, J.5    Liu, Y.6    Xiang, X.7    Xie, J.8    Qin, C.F.9    Zhou, X.10    Hu, Y.11
  • 19
    • 80052481402 scopus 로고    scopus 로고
    • RNA binding by a novel helical fold of b2 protein from Wuhan nodavirus mediates the suppression of RNA interference and promotes b2 dimerization
    • Qi N, Cai D, Qiu Y, Xie J, Wang Z, Si J, Zhang J, Zhou X, Hu Y. 2011. RNA binding by a novel helical fold of b2 protein from Wuhan nodavirus mediates the suppression of RNA interference and promotes b2 dimerization. J Virol 85:9543-9554. http://dx.doi.org/10.1128/JVI.00785-11.
    • (2011) J Virol , vol.85 , pp. 9543-9554
    • Qi, N.1    Cai, D.2    Qiu, Y.3    Xie, J.4    Wang, Z.5    Si, J.6    Zhang, J.7    Zhou, X.8    Hu, Y.9
  • 21
    • 1842832222 scopus 로고    scopus 로고
    • The influenza A virus NS1 protein binds small interfering RNAs and suppresses RNA silencing in plants
    • Bucher E, Hemmes H, de Haan P, Goldbach R, Prins M. 2004. The influenza A virus NS1 protein binds small interfering RNAs and suppresses RNA silencing in plants. J Gen Virol 85:983-991. http://dx.doi.org/10.1099/vir.0.19734-0.
    • (2004) J Gen Virol , vol.85 , pp. 983-991
    • Bucher, E.1    Hemmes, H.2    de Haan, P.3    Goldbach, R.4    Prins, M.5
  • 23
    • 19944420154 scopus 로고    scopus 로고
    • A virus-encoded inhibitor that blocks RNA interference in mammalian cells
    • Sullivan CS, Ganem D. 2005. A virus-encoded inhibitor that blocks RNA interference in mammalian cells. J Virol 79:7371-7379. http://dx.doi.org/10.1128/JVI.79.12.7371-7379.2005.
    • (2005) J Virol , vol.79 , pp. 7371-7379
    • Sullivan, C.S.1    Ganem, D.2
  • 24
    • 19344370167 scopus 로고    scopus 로고
    • Evidence that HIV-1 encodes an siRNA and a suppressor of RNA silencing
    • Bennasser Y, Le SY, Benkirane M, Jeang KT. 2005. Evidence that HIV-1 encodes an siRNA and a suppressor of RNA silencing. Immunity 22:607-619. http://dx.doi.org/10.1016/j.immuni.2005.03.010.
    • (2005) Immunity , vol.22 , pp. 607-619
    • Bennasser, Y.1    Le, S.Y.2    Benkirane, M.3    Jeang, K.T.4
  • 25
    • 41049095100 scopus 로고    scopus 로고
    • HCV core protein interacts with Dicer to antagonize RNA silencing
    • Chen W, Zhang Z, Chen J, Zhang J, Zhang J, Wu Y, Huang Y, Cai X, Huang A. 2008. HCV core protein interacts with Dicer to antagonize RNA silencing. Virus Res 133:250-258. http://dx.doi.org/10.1016/j.virusres.2008.01.011.
    • (2008) Virus Res , vol.133 , pp. 250-258
    • Chen, W.1    Zhang, Z.2    Chen, J.3    Zhang, J.4    Zhang, J.5    Wu, Y.6    Huang, Y.7    Cai, X.8    Huang, A.9
  • 27
    • 0030928832 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR
    • Brand SR, Kobayashi R, Mathews MB. 1997. The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. J Biol Chem 272:8388-8395. http://dx.doi.org/10.1074/jbc.272.13.8388.
    • (1997) J Biol Chem , vol.272 , pp. 8388-8395
    • Brand, S.R.1    Kobayashi, R.2    Mathews, M.B.3
  • 28
    • 0036678864 scopus 로고    scopus 로고
    • Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: the role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza
    • Geiss GK, Salvatore M, Tumpey TM, Carter VS, Wang X, Basler CF, Taubenberger JK, Bumgarner RE, Palese P, Katze MG, Garcia-Sastre A. 2002. Cellular transcriptional profiling in influenza A virus-infected lung epithelial cells: the role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. Proc Natl Acad SciUSA99:10736-10741. http://dx.doi.org/10.1073/pnas.112338099.
    • (2002) Proc Natl Acad SciUSA , vol.99 , pp. 10736-10741
    • Geiss, G.K.1    Salvatore, M.2    Tumpey, T.M.3    Carter, V.S.4    Wang, X.5    Basler, C.F.6    Taubenberger, J.K.7    Bumgarner, R.E.8    Palese, P.9    Katze, M.G.10    Garcia-Sastre, A.11
  • 29
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: update on repli-cation and pathogenesis
    • Perlman S, Netland J. 2009. Coronaviruses post-SARS: update on repli-cation and pathogenesis. Nat Rev Microbiol 7:439-450. http://dx.doi.org/10.1038/nrmicro2147.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 31
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber F, Wagner V, Rasmussen SB, Hartmann R, Paludan SR. 2006. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J Virol 80:5059-5064. http://dx.doi.org/10.1128/JVI.80.10.5059-5064.2006.
    • (2006) J Virol , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5
  • 32
    • 77956855860 scopus 로고    scopus 로고
    • The 7a accessory protein of severe acute respiratory syndrome coronavirus acts as an RNA silencing suppressor
    • Karjee S, Minhas A, Sood V, Ponia SS, Banerjea AC, Chow VT, Mukherjee SK, Lal SK. 2010. The 7a accessory protein of severe acute respiratory syndrome coronavirus acts as an RNA silencing suppressor. J Virol 84:10395-10401. http://dx.doi.org/10.1128/JVI.00748-10.
    • (2010) J Virol , vol.84 , pp. 10395-10401
    • Karjee, S.1    Minhas, A.2    Sood, V.3    Ponia, S.S.4    Banerjea, A.C.5    Chow, V.T.6    Mukherjee, S.K.7    Lal, S.K.8
  • 33
    • 27744472746 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice
    • Yount B, Roberts RS, Sims AC, Deming D, Frieman MB, Sparks J, Denison MR, Davis N, Baric RS. 2005. Severe acute respiratory syndrome coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice. J Virol 79:14909-14922. http://dx.doi.org/10.1128/JVI.79.23.14909-14922.2005.
    • (2005) J Virol , vol.79 , pp. 14909-14922
    • Yount, B.1    Roberts, R.S.2    Sims, A.C.3    Deming, D.4    Frieman, M.B.5    Sparks, J.6    Denison, M.R.7    Davis, N.8    Baric, R.S.9
  • 34
    • 33748467621 scopus 로고    scopus 로고
    • Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus
    • Tan YJ, Lim SG, Hong W. 2006. Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus. Antivir Res 72:78-88. http://dx.doi.org/10.1016/j.antiviral.2006.05.010.
    • (2006) Antivir Res , vol.72 , pp. 78-88
    • Tan, Y.J.1    Lim, S.G.2    Hong, W.3
  • 35
    • 20144388640 scopus 로고    scopus 로고
    • Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses
    • Tang TK, Wu MP, Chen ST, Hou MH, Hong MH, Pan FM, Yu HM, Chen JH, Yao CW, Wang AH. 2005. Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses. Proteomics 5:925-937. http://dx.doi.org/10.1002/pmic.200401204.
    • (2005) Proteomics , vol.5 , pp. 925-937
    • Tang, T.K.1    Wu, M.P.2    Chen, S.T.3    Hou, M.H.4    Hong, M.H.5    Pan, F.M.6    Yu, H.M.7    Chen, J.H.8    Yao, C.W.9    Wang, A.H.10
  • 36
    • 45649085737 scopus 로고    scopus 로고
    • Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAILNMR method
    • Takeda M, Chang CK, Ikeya T, Guntert P, Chang YH, Hsu YL, Huang TH, Kainosho M. 2008. Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAILNMR method. J Mol Biol 380:608-622. http://dx.doi.org/10.1016/j.jmb.2007.11.093.
    • (2008) J Mol Biol , vol.380 , pp. 608-622
    • Takeda, M.1    Chang, C.K.2    Ikeya, T.3    Guntert, P.4    Chang, Y.H.5    Hsu, Y.L.6    Huang, T.H.7    Kainosho, M.8
  • 37
    • 0023714871 scopus 로고
    • Interactions between coronavirus nucleocapsid protein and viral RNAs: implications for viral transcription
    • Baric RS, Nelson GW, Fleming JO, Deans RJ, Keck JG, Casteel N, Stohlman SA. 1988. Interactions between coronavirus nucleocapsid protein and viral RNAs: implications for viral transcription. J Virol 62:4280-4287.
    • (1988) J Virol , vol.62 , pp. 4280-4287
    • Baric, R.S.1    Nelson, G.W.2    Fleming, J.O.3    Deans, R.J.4    Keck, J.G.5    Casteel, N.6    Stohlman, S.A.7
  • 38
    • 70350728646 scopus 로고    scopus 로고
    • Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes
    • Grossoehme NE, Li L, Keane SC, Liu P, Dann CE, III, Leibowitz JL, Giedroc DP. 2009. Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes. J Mol Biol 394:544-557. http://dx.doi.org/10.1016/j.jmb.2009.09.040.
    • (2009) J Mol Biol , vol.394 , pp. 544-557
    • Grossoehme, N.E.1    Li, L.2    Keane, S.C.3    Liu, P.4    Dann, C.E.5    Leibowitz, J.L.6    Giedroc, D.P.7
  • 40
    • 7644242097 scopus 로고    scopus 로고
    • The nucleoprotein is required for efficient coronavirus genome replication
    • Almazan F, Galan C, Enjuanes L. 2004. The nucleoprotein is required for efficient coronavirus genome replication. J Virol 78:12683-12688. http://dx.doi.org/10.1128/JVI.78.22.12683-12688.2004.
    • (2004) J Virol , vol.78 , pp. 12683-12688
    • Almazan, F.1    Galan, C.2    Enjuanes, L.3
  • 41
    • 79960315021 scopus 로고    scopus 로고
    • SARS-CoV nucleocapsid protein antagonizes IFN-beta response by targeting initial step of IFN-beta induction pathway, and its C-terminal region is critical for the antagonism
    • Lu X, Pan J, Tao J, Guo D. 2011. SARS-CoV nucleocapsid protein antagonizes IFN-beta response by targeting initial step of IFN-beta induction pathway, and its C-terminal region is critical for the antagonism. Virus Genes 42:37-45. http://dx.doi.org/10.1007/s11262-010-0544-x.
    • (2011) Virus Genes , vol.42 , pp. 37-45
    • Lu, X.1    Pan, J.2    Tao, J.3    Guo, D.4
  • 44
    • 27944468304 scopus 로고    scopus 로고
    • SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization
    • Luo H, Ye F, Chen K, Shen X, Jiang H. 2005. SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization. Biochemistry 44:15351-15358. http://dx.doi.org/10.1021/bi051122c.
    • (2005) Biochemistry , vol.44 , pp. 15351-15358
    • Luo, H.1    Ye, F.2    Chen, K.3    Shen, X.4    Jiang, H.5
  • 45
    • 33749367362 scopus 로고    scopus 로고
    • Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: selfassociation analysis and nucleic acid binding characterization
    • Luo H, Chen J, Chen K, Shen X, Jiang H. 2006. Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: selfassociation analysis and nucleic acid binding characterization. Biochemistry 45:11827-11835. http://dx.doi.org/10.1021/bi0609319.
    • (2006) Biochemistry , vol.45 , pp. 11827-11835
    • Luo, H.1    Chen, J.2    Chen, K.3    Shen, X.4    Jiang, H.5
  • 46
    • 34147113199 scopus 로고    scopus 로고
    • Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA
    • Chen CY, Chang CK, Chang YW, Sue SC, Bai HI, Riang L, Hsiao CD, Huang TH. 2007. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J Mol Biol 368:1075-1086. http://dx.doi.org/10.1016/j.jmb.2007.02.069.
    • (2007) J Mol Biol , vol.368 , pp. 1075-1086
    • Chen, C.Y.1    Chang, C.K.2    Chang, Y.W.3    Sue, S.C.4    Bai, H.I.5    Riang, L.6    Hsiao, C.D.7    Huang, T.H.8
  • 47
    • 84897568235 scopus 로고    scopus 로고
    • Hepatitis B virus polymerase suppresses NF-κB signaling by inhibiting the activity of IKKs via interaction with Hsp90β
    • Liu D, Wu A, Cui L, Hao R, Wang Y, He J, Guo D. 2014. Hepatitis B virus polymerase suppresses NF-κB signaling by inhibiting the activity of IKKs via interaction with Hsp90β. PLoS One 9:e91658. http://dx.doi.org/10.1371/journal.pone.0091658.
    • (2014) PLoS One , vol.9
    • Liu, D.1    Wu, A.2    Cui, L.3    Hao, R.4    Wang, Y.5    He, J.6    Guo, D.7
  • 48
    • 79952258054 scopus 로고    scopus 로고
    • Construction and genetic analysis of murine hepatitis virus strain A59 Nsp16 temperature-sensitive mutant and the revertant virus
    • Chang GH, Luo BJ, Lu P, Lin L, Wu XY, Li J, Hu Y, Zhu QY. 2011. Construction and genetic analysis of murine hepatitis virus strain A59 Nsp16 temperature-sensitive mutant and the revertant virus. Virol Sin 26:19-29. http://dx.doi.org/10.1007/s12250-011-3145-x.
    • (2011) Virol Sin , vol.26 , pp. 19-29
    • Chang, G.H.1    Luo, B.J.2    Lu, P.3    Lin, L.4    Wu, X.Y.5    Li, J.6    Hu, Y.7    Zhu, Q.Y.8
  • 49
    • 80055066817 scopus 로고    scopus 로고
    • Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2=-Omethylation by nsp16/nsp10 protein complex
    • Chen Y, Su C, Ke M, Jin X, Xu L, Zhang Z, Wu A, Sun Y, Yang Z, Tien P, Ahola T, Liang Y, Liu X, Guo D. 2011. Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2=-Omethylation by nsp16/nsp10 protein complex. PLoS Pathog 7:e1002294. http://dx.doi.org/10.1371/journal.ppat.1002294.
    • (2011) PLoS Pathog , vol.7
    • Chen, Y.1    Su, C.2    Ke, M.3    Jin, X.4    Xu, L.5    Zhang, Z.6    Wu, A.7    Sun, Y.8    Yang, Z.9    Tien, P.10    Ahola, T.11    Liang, Y.12    Liu, X.13    Guo, D.14
  • 50
    • 33846104528 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists
    • Kopecky-Bromberg SA, Martinez-Sobrido L, Frieman M, Baric RA, Palese P. 2007. Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists. J Virol 81:548-557. http://dx.doi.org/10.1128/JVI.01782-06.
    • (2007) J Virol , vol.81 , pp. 548-557
    • Kopecky-Bromberg, S.A.1    Martinez-Sobrido, L.2    Frieman, M.3    Baric, R.A.4    Palese, P.5
  • 51
    • 40649115979 scopus 로고    scopus 로고
    • The mechanism of RNase III action: how dicer dices
    • Ji X. 2008. The mechanism of RNase III action: how dicer dices. Curr Top Microbiol Immunol 320:99-116.
    • (2008) Curr Top Microbiol Immunol , vol.320 , pp. 99-116
    • Ji, X.1
  • 52
    • 28544452860 scopus 로고    scopus 로고
    • The structure of the flock house virus B2 protein, a viral suppressor of RNA interference, shows a novel mode of double-stranded RNA recognition
    • Lingel A, Simon B, Izaurralde E, Sattler M. 2005. The structure of the flock house virus B2 protein, a viral suppressor of RNA interference, shows a novel mode of double-stranded RNA recognition. EMBO Rep 6:1149-1155. http://dx.doi.org/10.1038/sj.embor.7400583.
    • (2005) EMBO Rep , vol.6 , pp. 1149-1155
    • Lingel, A.1    Simon, B.2    Izaurralde, E.3    Sattler, M.4
  • 53
    • 60049100937 scopus 로고    scopus 로고
    • Multiple Nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging
    • Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. 2009. Multiple Nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. J Virol 83: 2255-2264. http://dx.doi.org/10.1128/JVI.02001-08.
    • (2009) J Virol , vol.83 , pp. 2255-2264
    • Chang, C.K.1    Hsu, Y.L.2    Chang, Y.H.3    Chao, F.A.4    Wu, M.C.5    Huang, Y.S.6    Hu, C.K.7    Huang, T.H.8
  • 54
    • 84905901545 scopus 로고    scopus 로고
    • The coronavirus nucleocapsid is a multifunctional protein
    • McBride R, van Zyl M, Fielding BC. 2014. The coronavirus nucleocapsid is a multifunctional protein. Viruses 6:2991-3018. http://dx.doi.org/10.3390/v6082991.
    • (2014) Viruses , vol.6 , pp. 2991-3018
    • McBride, R.1    van Zyl, M.2    Fielding, B.C.3
  • 55
    • 53249097514 scopus 로고    scopus 로고
    • Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication
    • Pan J, Peng X, Gao Y, Li Z, Lu X, Chen Y, Ishaq M, Liu D, Dediego ML, Enjuanes L, Guo D. 2008. Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication. PLoS One 3:e3299. http://dx.doi.org/10.1371/journal.pone.0003299.
    • (2008) PLoS One , vol.3
    • Pan, J.1    Peng, X.2    Gao, Y.3    Li, Z.4    Lu, X.5    Chen, Y.6    Ishaq, M.7    Liu, D.8    Dediego, M.L.9    Enjuanes, L.10    Guo, D.11
  • 56
    • 33947387099 scopus 로고    scopus 로고
    • Mouse hepatitis coronavirus A59 nucleocapsid protein is a type I interferon antagonist
    • Ye Y, Hauns K, Langland JO, Jacobs BL, Hogue BG. 2007. Mouse hepatitis coronavirus A59 nucleocapsid protein is a type I interferon antagonist. J Virol 81:2554-2563. http://dx.doi.org/10.1128/JVI.01634-06.
    • (2007) J Virol , vol.81 , pp. 2554-2563
    • Ye, Y.1    Hauns, K.2    Langland, J.O.3    Jacobs, B.L.4    Hogue, B.G.5
  • 57
    • 53749083591 scopus 로고    scopus 로고
    • Murine coronavirus mouse hepatitis virus is recognized by MDA5 and induces type I interferon in brain macrophages/microglia
    • Roth-Cross JK, Bender SJ, Weiss SR. 2008. Murine coronavirus mouse hepatitis virus is recognized by MDA5 and induces type I interferon in brain macrophages/microglia. J Virol 82:9829-9838. http://dx.doi.org/10.1128/JVI.01199-08.
    • (2008) J Virol , vol.82 , pp. 9829-9838
    • Roth-Cross, J.K.1    Bender, S.J.2    Weiss, S.R.3
  • 58
    • 34250836810 scopus 로고    scopus 로고
    • Inhibition of the alpha/beta interferon response by mouse hepatitis virus at multiple levels
    • Roth-Cross JK, Martinez-Sobrido L, Scott EP, Garcia-Sastre A, Weiss SR. 2007. Inhibition of the alpha/beta interferon response by mouse hepatitis virus at multiple levels. J Virol 81:7189-7199. http://dx.doi.org/10.1128/JVI.00013-07.
    • (2007) J Virol , vol.81 , pp. 7189-7199
    • Roth-Cross, J.K.1    Martinez-Sobrido, L.2    Scott, E.P.3    Garcia-Sastre, A.4    Weiss, S.R.5
  • 59
    • 77951994186 scopus 로고    scopus 로고
    • Murine coronavirus cell type dependent interaction with the type I interferon response
    • Rose KM, Weiss SR. 2009. Murine coronavirus cell type dependent interaction with the type I interferon response. Viruses 1:689-712. http://dx.doi.org/10.3390/v1030689.
    • (2009) Viruses , vol.1 , pp. 689-712
    • Rose, K.M.1    Weiss, S.R.2
  • 60
    • 33846070661 scopus 로고    scopus 로고
    • Mouse hepatitis virus does not induce beta interferon synthesis and does not inhibit its induction by double-stranded RNA
    • Zhou H, Perlman S. 2007. Mouse hepatitis virus does not induce beta interferon synthesis and does not inhibit its induction by double-stranded RNA. J Virol 81:568-574. http://dx.doi.org/10.1128/JVI.01512-06.
    • (2007) J Virol , vol.81 , pp. 568-574
    • Zhou, H.1    Perlman, S.2
  • 61
    • 34047266608 scopus 로고    scopus 로고
    • Group 2 coronaviruses prevent immediate-early interferon induction by protection of viral RNA from host cell recognition
    • Versteeg GA, Bredenbeek PJ, van den Worm SH, Spaan WJ. 2007. Group 2 coronaviruses prevent immediate-early interferon induction by protection of viral RNA from host cell recognition. Virology 361:18-26. http://dx.doi.org/10.1016/j.virol.2007.01.020.
    • (2007) Virology , vol.361 , pp. 18-26
    • Versteeg, G.A.1    Bredenbeek, P.J.2    van den Worm, S.H.3    Spaan, W.J.4
  • 62
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert R, Kanjanahaluethai A, Egger D, Bienz K, Baker SC. 2002. RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J Virol 76:3697-3708. http://dx.doi.org/10.1128/JVI.76.8.3697-3708.2002.
    • (2002) J Virol , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 63
    • 33744928372 scopus 로고    scopus 로고
    • Ultrastructure and origin of membrane vesicles associated with the severe acute respiratory syndrome coronavirus replication complex
    • Snijder EJ, van der Meer Y, Zevenhoven-Dobbe J, Onderwater JJ, van der Meulen J, Koerten HK, Mommaas AM. 2006. Ultrastructure and origin of membrane vesicles associated with the severe acute respiratory syndrome coronavirus replication complex. J Virol 80:5927-5940. http://dx.doi.org/10.1128/JVI.02501-05.
    • (2006) J Virol , vol.80 , pp. 5927-5940
    • Snijder, E.J.1    van der Meer, Y.2    Zevenhoven-Dobbe, J.3    Onderwater, J.J.4    van der Meulen, J.5    Koerten, H.K.6    Mommaas, A.M.7
  • 64
    • 62549159638 scopus 로고    scopus 로고
    • Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase
    • Chen Y, Cai H, Pan J, Xiang N, Tien P, Ahola T, Guo D. 2009. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc Natl Acad Sci U S A 106:3484-3489. http://dx.doi.org/10.1073/pnas.0808790106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3484-3489
    • Chen, Y.1    Cai, H.2    Pan, J.3    Xiang, N.4    Tien, P.5    Ahola, T.6    Guo, D.7
  • 65
    • 26944439528 scopus 로고    scopus 로고
    • Molecular interactions in the assembly of coronaviruses
    • de Haan CA, Rottier PJ. 2005. Molecular interactions in the assembly of coronaviruses. Adv Virus Res 64:165-230.
    • (2005) Adv Virus Res , vol.64 , pp. 165-230
    • de Haan, C.A.1    Rottier, P.J.2
  • 66
    • 33746317830 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Masters PS. 2006. The molecular biology of coronaviruses. Adv Virus Res 66:193-292.
    • (2006) Adv Virus Res , vol.66 , pp. 193-292
    • Masters, P.S.1
  • 68
    • 27644584130 scopus 로고    scopus 로고
    • Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent
    • Hsieh PK, Chang SC, Huang CC, Lee TT, Hsiao CW, Kou YH, Chen IY, Chang CK, Huang TH, Chang MF. 2005. Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent. J Virol 79:13848-13855. http://dx.doi.org/10.1128/JVI.79.22.13848-13855.2005.
    • (2005) J Virol , vol.79 , pp. 13848-13855
    • Hsieh, P.K.1    Chang, S.C.2    Huang, C.C.3    Lee, T.T.4    Hsiao, C.W.5    Kou, Y.H.6    Chen, I.Y.7    Chang, C.K.8    Huang, T.H.9    Chang, M.F.10
  • 69
    • 0026469390 scopus 로고
    • Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus
    • Masters PS. 1992. Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus. Arch Virol 125: 141-160. http://dx.doi.org/10.1007/BF01309634.
    • (1992) Arch Virol , vol.125 , pp. 141-160
    • Masters, P.S.1
  • 70
    • 84881243429 scopus 로고    scopus 로고
    • Characterization of a critical interaction between the coronavirus nucleocapsid protein and nonstructural protein 3 of the viral replicase-transcriptase complex
    • Hurst KR, Koetzner CA, Masters PS. 2013. Characterization of a critical interaction between the coronavirus nucleocapsid protein and nonstructural protein 3 of the viral replicase-transcriptase complex. J Virol 87: 9159-9172. http://dx.doi.org/10.1128/JVI.01275-13.
    • (2013) J Virol , vol.87 , pp. 9159-9172
    • Hurst, K.R.1    Koetzner, C.A.2    Masters, P.S.3
  • 71
    • 84897014398 scopus 로고    scopus 로고
    • Recognition of the murine coronavirus genomic RNA packaging signal depends on the second RNA-binding domain of the nucleocapsid protein
    • Kuo L, Koetzner CA, Hurst KR, Masters PS. 2014. Recognition of the murine coronavirus genomic RNA packaging signal depends on the second RNA-binding domain of the nucleocapsid protein. J Virol 88:4451-4465. http://dx.doi.org/10.1128/JVI.03866-13.
    • (2014) J Virol , vol.88 , pp. 4451-4465
    • Kuo, L.1    Koetzner, C.A.2    Hurst, K.R.3    Masters, P.S.4
  • 73
    • 60549089450 scopus 로고    scopus 로고
    • Type I IFN-mediated protection of macrophages and dendritic cells secures control of murine coronavirus infection
    • Cervantes-Barragan L, Kalinke U, Zust R, Konig M, Reizis B, Lopez-Macias C, Thiel V, Ludewig B. 2009. Type I IFN-mediated protection of macrophages and dendritic cells secures control of murine coronavirus infection. J Immunol 182:1099-1106. http://dx.doi.org/10.4049/jimmunol.182.2.1099.
    • (2009) J Immunol , vol.182 , pp. 1099-1106
    • Cervantes-Barragan, L.1    Kalinke, U.2    Zust, R.3    Konig, M.4    Reizis, B.5    Lopez-Macias, C.6    Thiel, V.7    Ludewig, B.8
  • 74
    • 18744366350 scopus 로고    scopus 로고
    • Selective replication of coronavirus genomes that express nucleocapsid protein
    • Schelle B, Karl N, Ludewig B, Siddell SG, Thiel V. 2005. Selective replication of coronavirus genomes that express nucleocapsid protein. J Virol 79:6620-6630. http://dx.doi.org/10.1128/JVI.79.11.6620-6630.2005.
    • (2005) J Virol , vol.79 , pp. 6620-6630
    • Schelle, B.1    Karl, N.2    Ludewig, B.3    Siddell, S.G.4    Thiel, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.