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Volumn 96, Issue 9, 2015, Pages 2483-2500

Alphavirus RNA synthesis and non-structural protein functions

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CIS ACTING ELEMENT; GENOMIC RNA; HOST FACTOR; NONSTRUCTURAL PROTEIN 1; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4; NUCLEOSIDE TRIPHOSPHATASE; POLYPROTEIN; PROTEINASE; RNA DIRECTED RNA POLYMERASE; RNA TRIPHOSPHATASE; UNCLASSIFIED DRUG; VIRUS RNA; VIRAL PROTEIN;

EID: 84941595490     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/jgv.0.000249     Document Type: Article
Times cited : (190)

References (199)
  • 1
    • 78751701774 scopus 로고    scopus 로고
    • Lineage replacement accompanying duplication and rapid fixation of an RNA element in the nsP3 gene in a species of alphavirus
    • Aaskov, J., Jones, A., Choi, W., Lowry, K. & Stewart, E. (2011). Lineage replacement accompanying duplication and rapid fixation of an RNA element in the nsP3 gene in a species of alphavirus. Virology 410, 353–359.
    • (2011) Virology , vol.410 , pp. 353-359
    • Aaskov, J.1    Jones, A.2    Choi, W.3    Lowry, K.4    Stewart, E.5
  • 2
    • 0028833053 scopus 로고
    • Reaction in alphavirus mRNA capping: Formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP
    • Ahola, T. & Kääriäinen, L. (1995). Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP. Proc Natl Acad Sci U S A 92, 507–511.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 507-511
    • Ahola, T.1    Kääriäinen, L.2
  • 3
    • 84926610921 scopus 로고    scopus 로고
    • Sequence analysis reveals a conserved extension in the capping enzyme of the alphavirus supergroup, and a homologous domain in nodaviruses
    • Ahola, T. & Karlin, D. G. (2015). Sequence analysis reveals a conserved extension in the capping enzyme of the alphavirus supergroup, and a homologous domain in nodaviruses. Biol Direct 10, 16.
    • (2015) Biol Direct , vol.10 , pp. 16
    • Ahola, T.1    Karlin, D.G.2
  • 4
    • 0031060112 scopus 로고    scopus 로고
    • Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities
    • Ahola, T., Laakkonen, P., Vihinen, H. & Kääriäinen, L. (1997). Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities. J Virol 71, 392–397.
    • (1997) J Virol , vol.71 , pp. 392-397
    • Ahola, T.1    Laakkonen, P.2    Vihinen, H.3    Kääriäinen, L.4
  • 5
    • 0033152498 scopus 로고    scopus 로고
    • Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity
    • Ahola, T., Lampio, A., Auvinen, P. & Kääriäinen, L. (1999). Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity. EMBO J 18, 3164–3172.
    • (1999) EMBO J , vol.18 , pp. 3164-3172
    • Ahola, T.1    Lampio, A.2    Auvinen, P.3    Kääriäinen, L.4
  • 7
    • 84864122222 scopus 로고    scopus 로고
    • Evasion of the innate immune response: The Old World alphavirus nsP2 protein induces rapid degradation of Rpb1, a catalytic subunit of RNA polymerase II
    • Akhrymuk, I., Kulemzin, S. V. & Frolova, E. I. (2012). Evasion of the innate immune response: the Old World alphavirus nsP2 protein induces rapid degradation of Rpb1, a catalytic subunit of RNA polymerase II. J Virol 86, 7180–7191.
    • (2012) J Virol , vol.86 , pp. 7180-7191
    • Akhrymuk, I.1    Kulemzin, S.V.2    Frolova, E.I.3
  • 8
    • 0038047136 scopus 로고    scopus 로고
    • The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A
    • Allen, M. D., Buckle, A. M., Cordell, S. C., Löwe, J. & Bycroft, M. (2003). The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A. J Mol Biol 330, 503–511.
    • (2003) J Mol Biol , vol.330 , pp. 503-511
    • Allen, M.D.1    Buckle, A.M.2    Cordell, S.C.3    Löwe, J.4    Bycroft, M.5
  • 9
    • 34248359925 scopus 로고    scopus 로고
    • Development of Sindbis viruses encoding nsP2/GFP chimeric proteins and their application for studying nsP2 functioning
    • Atasheva, S., Gorchakov, R., English, R., Frolov, I. & Frolova, E. (2007). Development of Sindbis viruses encoding nsP2/GFP chimeric proteins and their application for studying nsP2 functioning. J Virol 81, 5046–5057.
    • (2007) J Virol , vol.81 , pp. 5046-5057
    • Atasheva, S.1    Gorchakov, R.2    English, R.3    Frolov, I.4    Frolova, E.5
  • 10
    • 0026028278 scopus 로고
    • Solubilization and immunoprecipitation of alphavirus replication complexes
    • Barton, D. J., Sawicki, S. G. & Sawicki, D. L. (1991). Solubilization and immunoprecipitation of alphavirus replication complexes. J Virol 65, 1496–1506.
    • (1991) J Virol , vol.65 , pp. 1496-1506
    • Barton, D.J.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 11
    • 84941582017 scopus 로고    scopus 로고
    • ICTVdB-The Universal Virus Database, version 4. Online: Columbia University, New York, USA
    • Büchen-Osmond, C. E. (2006). In: ICTVdB-The Universal Virus Database, version 4. Online: Columbia University, New York, USA. http://www.ncbi.nlm.nih.gov/ICTVdb/Ictv/fs_index.htm.
    • (2006)
    • Büchen-Osmond, C.E.1
  • 12
    • 34548679613 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonuclear protein K interacts with Sindbis virus nonstructural proteins and viral subgenomic mRNA
    • Burnham, A. J., Gong, L. & Hardy, R. W. (2007). Heterogeneous nuclear ribonuclear protein K interacts with Sindbis virus nonstructural proteins and viral subgenomic mRNA. Virology 367, 212–221.
    • (2007) Virology , vol.367 , pp. 212-221
    • Burnham, A.J.1    Gong, L.2    Hardy, R.W.3
  • 13
    • 84883340196 scopus 로고    scopus 로고
    • Chikungunya virus 39 untranslated region: Adaptation to mosquitoes and a population bottleneck as major evolutionary forces
    • Chen, R., Wang, E., Tsetsarkin, K. A. & Weaver, S. C. (2013). Chikungunya virus 39 untranslated region: adaptation to mosquitoes and a population bottleneck as major evolutionary forces. PLoS Pathog 9, e1003591.
    • (2013) Plos Pathog , vol.9
    • Chen, R.1    Wang, E.2    Tsetsarkin, K.A.3    Weaver, S.C.4
  • 15
    • 77349125350 scopus 로고    scopus 로고
    • Frameshifting in alphaviruses: A diversity of 39 stimulatory structures
    • Chung, B. Y., Firth, A. E. & Atkins, J. F. (2010). Frameshifting in alphaviruses: a diversity of 39 stimulatory structures. J Mol Biol 397, 448–456.
    • (2010) J Mol Biol , vol.397 , pp. 448-456
    • Chung, B.Y.1    Firth, A.E.2    Atkins, J.F.3
  • 17
    • 77953320616 scopus 로고    scopus 로고
    • Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: Role for G3BP1 and G3BP2 in virus replication
    • Cristea, I. M., Rozjabek, H., Molloy, K. R., Karki, S., White, L. L., Rice, C. M., Rout, M. P., Chait, B. T. & MacDonald, M. R. (2010). Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3BP2 in virus replication. J Virol 84, 6720–6732.
    • (2010) J Virol , vol.84 , pp. 6720-6732
    • Cristea, I.M.1    Rozjabek, H.2    Molloy, K.R.3    Karki, S.4    White, L.L.5    Rice, C.M.6    Rout, M.P.7    Chait, B.T.8    Macdonald, M.R.9
  • 18
    • 0021086810 scopus 로고
    • Identification of a unique guanine-7-methyltransferase in Semliki Forest virus (SFV) infected cell extracts
    • Cross, R. K. (1983). Identification of a unique guanine-7-methyltransferase in Semliki Forest virus (SFV) infected cell extracts. Virology 130, 452–463.
    • (1983) Virology , vol.130 , pp. 452-463
    • Cross, R.K.1
  • 21
    • 84896884405 scopus 로고    scopus 로고
    • Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity
    • Das, P. K., Merits, A. & Lulla, A. (2014). Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity. J Biol Chem 289, 5635–5653.
    • (2014) J Biol Chem , vol.289 , pp. 5635-5653
    • Das, P.K.1    Merits, A.2    Lulla, A.3
  • 22
    • 0024403231 scopus 로고
    • In vitro synthesis of infectious venezuelan equine encephalitis virus RNA from a cDNA clone: Analysis of a viable deletion mutant
    • Davis, N. L., Willis, L. V., Smith, J. F. & Johnston, R. E. (1989). In vitro synthesis of infectious venezuelan equine encephalitis virus RNA from a cDNA clone: analysis of a viable deletion mutant. Virology 171, 189–204.
    • (1989) Virology , vol.171 , pp. 189-204
    • Davis, N.L.1    Willis, L.V.2    Smith, J.F.3    Johnston, R.E.4
  • 23
    • 0029881285 scopus 로고    scopus 로고
    • Sindbis virus RNAnegative mutants that fail to convert from minus-strand to plusstrand synthesis: Role of the nsP2 protein
    • Dé, I., Sawicki, S. G. & Sawicki, D. L. (1996). Sindbis virus RNAnegative mutants that fail to convert from minus-strand to plusstrand synthesis: role of the nsP2 protein. J Virol 70, 2706–2719.
    • (1996) J Virol , vol.70 , pp. 2706-2719
    • Dé, I.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 24
    • 0345599124 scopus 로고    scopus 로고
    • Functional analysis of nsP3 phosphoprotein mutants of Sindbis virus
    • Dé, I., Fata-Hartley, C., Sawicki, S. G. & Sawicki, D. L. (2003). Functional analysis of nsP3 phosphoprotein mutants of Sindbis virus. J Virol 77, 13106–13116.
    • (2003) J Virol , vol.77 , pp. 13106-13116
    • Dé, I.1    Fata-Hartley, C.2    Sawicki, S.G.3    Sawicki, D.L.4
  • 25
    • 0025352629 scopus 로고
    • Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo
    • de Groot, R. J., Hardy, W. R., Shirako, Y. & Strauss, J. H. (1990). Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo. EMBO J 9, 2631–2638.
    • (1990) EMBO J , vol.9 , pp. 2631-2638
    • de Groot, R.J.1    Hardy, W.R.2    Shirako, Y.3    Strauss, J.H.4
  • 28
    • 0036338445 scopus 로고    scopus 로고
    • Alphavirus minusstrand RNA synthesis: Identification of a role for Arg183 of the nsP4 polymerase
    • Fata, C. L., Sawicki, S. G. & Sawicki, D. L. (2002a). Alphavirus minusstrand RNA synthesis: identification of a role for Arg183 of the nsP4 polymerase. J Virol 76, 8632–8640.
    • (2002) J Virol , vol.76 , pp. 8632-8640
    • Fata, C.L.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 29
    • 0036333797 scopus 로고    scopus 로고
    • Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant
    • Fata, C. L., Sawicki, S. G. & Sawicki, D. L. (2002b). Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant. J Virol 76, 8641–8649.
    • (2002) J Virol , vol.76 , pp. 8641-8649
    • Fata, C.L.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 30
    • 2342623475 scopus 로고    scopus 로고
    • Changes of the secondary structure of the 59 end of the Sindbis virus genome inhibit virus growth in mosquito cells and lead to accumulation of adaptive mutations
    • Fayzulin, R. & Frolov, I. (2004). Changes of the secondary structure of the 59 end of the Sindbis virus genome inhibit virus growth in mosquito cells and lead to accumulation of adaptive mutations. J Virol 78, 4953–4964.
    • (2004) J Virol , vol.78 , pp. 4953-4964
    • Fayzulin, R.1    Frolov, I.2
  • 31
    • 54049148146 scopus 로고    scopus 로고
    • Discovery of frameshifting in Alphavirus 6K resolves a 20-year enigma
    • Firth, A. E., Chung, B. Y., Fleeton, M. N. & Atkins, J. F. (2008). Discovery of frameshifting in Alphavirus 6K resolves a 20-year enigma. Virol J 5, 108.
    • (2008) Virol J , vol.5 , pp. 108
    • Firth, A.E.1    Chung, B.Y.2    Fleeton, M.N.3    Atkins, J.F.4
  • 32
    • 80055074497 scopus 로고    scopus 로고
    • Stimulation of stop codon readthrough: Frequent presence of an extended 39 RNA structural element
    • Firth, A. E., Wills, N. M., Gesteland, R. F. & Atkins, J. F. (2011). Stimulation of stop codon readthrough: frequent presence of an extended 39 RNA structural element. Nucleic Acids Res 39, 6679–6691.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6679-6691
    • Firth, A.E.1    Wills, N.M.2    Gesteland, R.F.3    Atkins, J.F.4
  • 34
    • 84873855984 scopus 로고    scopus 로고
    • Hypervariable domains of nsP3 proteins of New World and Old World alphaviruses mediate formation of distinct, virus-specific protein complexes
    • Foy, N. J., Akhrymuk, M., Akhrymuk, I., Atasheva, S., Bopda-Waffo, A., Frolov, I. & Frolova, E. I. (2013a). Hypervariable domains of nsP3 proteins of New World and Old World alphaviruses mediate formation of distinct, virus-specific protein complexes. J Virol 87, 1997–2010.
    • (2013) J Virol , vol.87 , pp. 1997-2010
    • Foy, N.J.1    Akhrymuk, M.2    Akhrymuk, I.3    Atasheva, S.4    Bopda-Waffo, A.5    Frolov, I.6    Frolova, E.I.7
  • 35
    • 84880388487 scopus 로고    scopus 로고
    • Hypervariable domain of nonstructural protein nsP3 of Venezuelan equine encephalitis virus determines cell-specific mode of virus replication
    • Foy, N. J., Akhrymuk, M., Shustov, A. V., Frolova, E. I. & Frolov, I. (2013b). Hypervariable domain of nonstructural protein nsP3 of Venezuelan equine encephalitis virus determines cell-specific mode of virus replication. J Virol 87, 7569–7584.
    • (2013) J Virol , vol.87 , pp. 7569-7584
    • Foy, N.J.1    Akhrymuk, M.2    Shustov, A.V.3    Frolova, E.I.4    Frolov, I.5
  • 36
    • 0018667611 scopus 로고
    • Biophysical studies on circle formation by Sindbis virus 49 S RNA
    • Frey, T. K., Gard, D. L. & Strauss, J. H. (1979). Biophysical studies on circle formation by Sindbis virus 49 S RNA. J Mol Biol 132, 1–18.
    • (1979) J Mol Biol , vol.132 , pp. 1-18
    • Frey, T.K.1    Gard, D.L.2    Strauss, J.H.3
  • 37
    • 0015395328 scopus 로고
    • Membrane-associated replication complex in arbovirus infection
    • Friedman, R. M., Levin, J. G., Grimley, P. M. & Berezesky, I. K. (1972). Membrane-associated replication complex in arbovirus infection. J Virol 10, 504–515.
    • (1972) J Virol , vol.10 , pp. 504-515
    • Friedman, R.M.1    Levin, J.G.2    Grimley, P.M.3    Berezesky, I.K.4
  • 38
    • 0030068269 scopus 로고    scopus 로고
    • Translation of Sindbis virus mRNA: Analysis of sequences downstream of the initiating AUG codon that enhance translation
    • Frolov, I. & Schlesinger, S. (1996). Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation. J Virol 70, 1182–1190.
    • (1996) J Virol , vol.70 , pp. 1182-1190
    • Frolov, I.1    Schlesinger, S.2
  • 39
    • 0032924734 scopus 로고    scopus 로고
    • Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells
    • Frolov, I., Agapov, E., Hoffman, T. A., Jr, Prágai, B. M., Lippa, M., Schlesinger, S. & Rice, C. M. (1999). Selection of RNA replicons capable of persistent noncytopathic replication in mammalian cells. J Virol 73, 3854–3865.
    • (1999) J Virol , vol.73 , pp. 3854-3865
    • Frolov, I.1    Agapov, E.2    Hoffman, T.A.3    Prágai, B.M.4    Lippa, M.5    Schlesinger, S.6    Rice, C.M.7
  • 40
    • 0035175362 scopus 로고    scopus 로고
    • Cis-acting RNA elements at the 59 end of Sindbis virus genome RNA regulate minus-and plus-strand RNA synthesis
    • Frolov, I., Hardy, R. & Rice, C. M. (2001). Cis-acting RNA elements at the 59 end of Sindbis virus genome RNA regulate minus-and plus-strand RNA synthesis. RNA 7, 1638–1651.
    • (2001) RNA , vol.7 , pp. 1638-1651
    • Frolov, I.1    Hardy, R.2    Rice, C.M.3
  • 41
    • 0031060528 scopus 로고    scopus 로고
    • Packaging signals in alphaviruses
    • Frolova, E., Frolov, I. & Schlesinger, S. (1997). Packaging signals in alphaviruses. J Virol 71, 248–258.
    • (1997) J Virol , vol.71 , pp. 248-258
    • Frolova, E.1    Frolov, I.2    Schlesinger, S.3
  • 42
    • 33645779746 scopus 로고    scopus 로고
    • Formation of nsP3-specific protein complexes during Sindbis virus replication
    • Frolova, E., Gorchakov, R., Garmashova, N., Atasheva, S., Vergara, L. A. & Frolov, I. (2006). Formation of nsP3-specific protein complexes during Sindbis virus replication. J Virol 80, 4122–4134.
    • (2006) J Virol , vol.80 , pp. 4122-4134
    • Frolova, E.1    Gorchakov, R.2    Garmashova, N.3    Atasheva, S.4    Vergara, L.A.5    Frolov, I.6
  • 43
    • 78049491884 scopus 로고    scopus 로고
    • Functional Sindbis virus replicative complexes are formed at the plasma membrane
    • Frolova, E. I., Gorchakov, R., Pereboeva, L., Atasheva, S. & Frolov, I. (2010). Functional Sindbis virus replicative complexes are formed at the plasma membrane. J Virol 84, 11679–11695.
    • (2010) J Virol , vol.84 , pp. 11679-11695
    • Frolova, E.I.1    Gorchakov, R.2    Pereboeva, L.3    Atasheva, S.4    Frolov, I.5
  • 44
    • 84869049624 scopus 로고    scopus 로고
    • Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci
    • Fros, J. J., Domeradzka, N. E., Baggen, J., Geertsema, C., Flipse, J., Vlak, J. M. & Pijlman, G. P. (2012). Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci. J Virol 86, 10873–10879.
    • (2012) J Virol , vol.86 , pp. 10873-10879
    • Fros, J.J.1    Domeradzka, N.E.2    Baggen, J.3    Geertsema, C.4    Flipse, J.5    Vlak, J.M.6    Pijlman, G.P.7
  • 45
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer, S., Kartenbeck, J. & Helenius, A. (1988). Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes. J Cell Biol 107, 2075–2086.
    • (1988) J Cell Biol , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 46
    • 33645538734 scopus 로고    scopus 로고
    • Deletions in the hypervariable domain of the nsP3 gene attenuate Semliki Forest virus virulence
    • Galbraith, S. E., Sheahan, B. J. & Atkins, G. J. (2006). Deletions in the hypervariable domain of the nsP3 gene attenuate Semliki Forest virus virulence. J Gen Virol 87, 937–947.
    • (2006) J Gen Virol , vol.87 , pp. 937-947
    • Galbraith, S.E.1    Sheahan, B.J.2    Atkins, G.J.3
  • 47
    • 33744937066 scopus 로고    scopus 로고
    • Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription
    • Garmashova, N., Gorchakov, R., Frolova, E. & Frolov, I. (2006). Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription. J Virol 80, 5686–5696.
    • (2006) J Virol , vol.80 , pp. 5686-5696
    • Garmashova, N.1    Gorchakov, R.2    Frolova, E.3    Frolov, I.4
  • 48
    • 33847199327 scopus 로고    scopus 로고
    • The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff
    • Garmashova, N., Gorchakov, R., Volkova, E., Paessler, S., Frolova, E. & Frolov, I. (2007). The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff. J Virol 81, 2472–2484.
    • (2007) J Virol , vol.81 , pp. 2472-2484
    • Garmashova, N.1    Gorchakov, R.2    Volkova, E.3    Paessler, S.4    Frolova, E.5    Frolov, I.6
  • 49
    • 37849019535 scopus 로고    scopus 로고
    • The 39 untranslated region of sindbis virus represses deadenylation of viral transcripts in mosquito and mammalian cells
    • Garneau, N. L., Sokoloski, K. J., Opyrchal, M., Neff, C. P., Wilusz, C. J. & Wilusz, J. (2008). The 39 untranslated region of sindbis virus represses deadenylation of viral transcripts in mosquito and mammalian cells. J Virol 82, 880–892.
    • (2008) J Virol , vol.82 , pp. 880-892
    • Garneau, N.L.1    Sokoloski, K.J.2    Opyrchal, M.3    Neff, C.P.4    Wilusz, C.J.5    Wilusz, J.6
  • 50
    • 0033809466 scopus 로고    scopus 로고
    • Alphavirus RNA genome repair and evolution: Molecular characterization of infectious sindbis virus isolates lacking a known conserved motif at the 39 end of the genome
    • George, J. & Raju, R. (2000). Alphavirus RNA genome repair and evolution: molecular characterization of infectious sindbis virus isolates lacking a known conserved motif at the 39 end of the genome. J Virol 74, 9776–9785.
    • (2000) J Virol , vol.74 , pp. 9776-9785
    • George, J.1    Raju, R.2
  • 51
    • 0019304039 scopus 로고
    • Semliki Forest virus replication complex capable of synthesizing 42S and 26S nascent RNA chains
    • Gomatos, P. J., Kääriäinen, L., Keränen, S., Ranki, M. & Sawicki, D. L. (1980). Semliki Forest virus replication complex capable of synthesizing 42S and 26S nascent RNA chains. J Gen Virol 49, 61–69.
    • (1980) J Gen Virol , vol.49 , pp. 61-69
    • Gomatos, P.J.1    Kääriäinen, L.2    Keränen, S.3    Ranki, M.4    Sawicki, D.L.5
  • 53
    • 0023705613 scopus 로고
    • A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination
    • Gorbalenya, A. E., Koonin, E. V., Donchenko, A. P. & Blinov, V. M. (1988). A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett 235, 16–24.
    • (1988) FEBS Lett , vol.235 , pp. 16-24
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 54
    • 0346365303 scopus 로고    scopus 로고
    • Selection of functional 59 cis-acting elements promoting efficient sindbis virus genome replication
    • Gorchakov, R., Hardy, R., Rice, C. M. & Frolov, I. (2004). Selection of functional 59 cis-acting elements promoting efficient sindbis virus genome replication. J Virol 78, 61–75.
    • (2004) J Virol , vol.78 , pp. 61-75
    • Gorchakov, R.1    Hardy, R.2    Rice, C.M.3    Frolov, I.4
  • 55
    • 22544443363 scopus 로고    scopus 로고
    • Inhibition of transcription and translation in Sindbis virus-infected cells
    • Gorchakov, R., Frolova, E. & Frolov, I. (2005). Inhibition of transcription and translation in Sindbis virus-infected cells. J Virol 79, 9397–9409.
    • (2005) J Virol , vol.79 , pp. 9397-9409
    • Gorchakov, R.1    Frolova, E.2    Frolov, I.3
  • 56
    • 45749090147 scopus 로고    scopus 로고
    • A new role for ns polyprotein cleavage in Sindbis virus replication
    • Gorchakov, R., Frolova, E., Sawicki, S., Atasheva, S., Sawicki, D. & Frolov, I. (2008a). A new role for ns polyprotein cleavage in Sindbis virus replication. J Virol 82, 6218–6231.
    • (2008) J Virol , vol.82 , pp. 6218-6231
    • Gorchakov, R.1    Frolova, E.2    Sawicki, S.3    Atasheva, S.4    Sawicki, D.5    Frolov, I.6
  • 57
    • 53749083590 scopus 로고    scopus 로고
    • Different types of nsP3-containing protein complexes in Sindbis virus-infected cells
    • Gorchakov, R., Garmashova, N., Frolova, E. & Frolov, I. (2008b). Different types of nsP3-containing protein complexes in Sindbis virus-infected cells. J Virol 82, 10088–10101.
    • (2008) J Virol , vol.82 , pp. 10088-10101
    • Gorchakov, R.1    Garmashova, N.2    Frolova, E.3    Frolov, I.4
  • 58
    • 0014350984 scopus 로고
    • Cytoplasmic structures associated with an arbovirus infection: Loci of viral ribonucleic acid synthesis
    • Grimley, P. M., Berezesky, I. K. & Friedman, R. M. (1968). Cytoplasmic structures associated with an arbovirus infection: loci of viral ribonucleic acid synthesis. J Virol 2, 1326–1338.
    • (1968) J Virol , vol.2 , pp. 1326-1338
    • Grimley, P.M.1    Berezesky, I.K.2    Friedman, R.M.3
  • 59
    • 77954666312 scopus 로고    scopus 로고
    • HnRNP A1 interacts with the genomic and subgenomic RNA promoters of Sindbis virus and is required for the synthesis of G and SG RNA
    • Gui, H., Lu, C.-W., Adams, S., Stollar, V. & Li, M.-L. (2010). hnRNP A1 interacts with the genomic and subgenomic RNA promoters of Sindbis virus and is required for the synthesis of G and SG RNA. J Biomed Sci 17, 59.
    • (2010) J Biomed Sci , vol.17 , pp. 59
    • Gui, H.1    Lu, C.-W.2    Adams, S.3    Stollar, V.4    Li, M.-L.5
  • 60
    • 0024582528 scopus 로고
    • Mapping of RNA–temperature-sensitive mutants of Sindbis virus: Complementation group F mutants have lesions in nsP4
    • Hahn, Y. S., Grakoui, A., Rice, C. M., Strauss, E. G. & Strauss, J. H. (1989a). Mapping of RNA–temperature-sensitive mutants of Sindbis virus: complementation group F mutants have lesions in nsP4. J Virol 63, 1194–1202.
    • (1989) J Virol , vol.63 , pp. 1194-1202
    • Hahn, Y.S.1    Grakoui, A.2    Rice, C.M.3    Strauss, E.G.4    Strauss, J.H.5
  • 61
    • 0024358586 scopus 로고
    • Mapping of RNA–temperature-sensitive mutants of Sindbis virus: Assignment of complementation groups A, B, and G to nonstructural proteins
    • Hahn, Y. S., Strauss, E. G. & Strauss, J. H. (1989b). Mapping of RNA–temperature-sensitive mutants of Sindbis virus: assignment of complementation groups A, B, and G to nonstructural proteins. J Virol 63, 3142–3150.
    • (1989) J Virol , vol.63 , pp. 3142-3150
    • Hahn, Y.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 62
    • 31944440868 scopus 로고    scopus 로고
    • The role of the 39 terminus of the Sindbis virus genome in minus-strand initiation site selection
    • Hardy, R. W. (2006). The role of the 39 terminus of the Sindbis virus genome in minus-strand initiation site selection. Virology 345, 520–531.
    • (2006) Virology , vol.345 , pp. 520-531
    • Hardy, R.W.1
  • 63
    • 16244413640 scopus 로고    scopus 로고
    • Requirements at the 39 end of the sindbis virus genome for efficient synthesis of minus-strand RNA
    • Hardy, R. W. & Rice, C. M. (2005). Requirements at the 39 end of the sindbis virus genome for efficient synthesis of minus-strand RNA. J Virol 79, 4630–4639.
    • (2005) J Virol , vol.79 , pp. 4630-4639
    • Hardy, R.W.1    Rice, C.M.2
  • 64
    • 0024421374 scopus 로고
    • Processing the nonstructural polyproteins of sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans
    • Hardy, W. R. & Strauss, J. H. (1989). Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans. J Virol 63, 4653–4664.
    • (1989) J Virol , vol.63 , pp. 4653-4664
    • Hardy, W.R.1    Strauss, J.H.2
  • 65
    • 0025277442 scopus 로고
    • Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus
    • Hardy, W. R., Hahn, Y. S., de Groot, R. J., Strauss, E. G. & Strauss, J. H. (1990). Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus. Virology 177, 199–208.
    • (1990) Virology , vol.177 , pp. 199-208
    • Hardy, W.R.1    Hahn, Y.S.2    de Groot, R.J.3    Strauss, E.G.4    Strauss, J.H.5
  • 66
    • 0016872716 scopus 로고
    • 59 Nucleotide sequence of sindbis viral RNA
    • Hefti, E., Bishop, D. H., Dubin, D. T. & Stollar, V. (1975). 59 Nucleotide sequence of sindbis viral RNA. J Virol 17, 149–159173879.
    • (1975) J Virol , vol.17
    • Hefti, E.1    Bishop, D.H.2    Dubin, D.T.3    Stollar, V.4
  • 67
    • 0035265836 scopus 로고    scopus 로고
    • Poliovirus RNA replication requires genome circularization through a protein-protein bridge
    • Herold, J. & Andino, R. (2001). Poliovirus RNA replication requires genome circularization through a protein-protein bridge. Mol Cell 7, 581–591.
    • (2001) Mol Cell , vol.7 , pp. 581-591
    • Herold, J.1    Andino, R.2
  • 68
    • 0026556707 scopus 로고
    • Utilization of heterologous alphavirus junction sequences as promoters by Sindbis virus
    • Hertz, J. M. & Huang, H. V. (1992). Utilization of heterologous alphavirus junction sequences as promoters by Sindbis virus. J Virol 66, 857–864.
    • (1992) J Virol , vol.66 , pp. 857-864
    • Hertz, J.M.1    Huang, H.V.2
  • 69
    • 0030933213 scopus 로고    scopus 로고
    • RNA–RNA recombination in Sindbis virus: Roles of the 39 conserved motif, poly(A) tail, and nonviral sequences of template RNAs in polymerase recognition and template switching
    • Hill, K. R., Hajjou, M., Hu, J. Y. & Raju, R. (1997). RNA–RNA recombination in Sindbis virus: roles of the 39 conserved motif, poly(A) tail, and nonviral sequences of template RNAs in polymerase recognition and template switching. J Virol 71, 2693–2704.
    • (1997) J Virol , vol.71 , pp. 2693-2704
    • Hill, K.R.1    Hajjou, M.2    Hu, J.Y.3    Raju, R.4
  • 71
    • 35548943206 scopus 로고    scopus 로고
    • Efficient replication, and evolution of Sindbis virus genomes with non-canonical 39A/U-rich elements (NC3ARE) in neonatal mice
    • James, F. D., Hietala, K. A., Eldar, D., Guess, T. E., Cone, C., Mundell, N. A., Barnett, J. V. & Raju, R. (2007). Efficient replication, and evolution of Sindbis virus genomes with non-canonical 39A/U-rich elements (NC3ARE) in neonatal mice. Virus Genes 35, 651–662.
    • (2007) Virus Genes , vol.35 , pp. 651-662
    • James, F.D.1    Hietala, K.A.2    Eldar, D.3    Guess, T.E.4    Cone, C.5    Mundell, N.A.6    Barnett, J.V.7    Raju, R.8
  • 73
    • 0036371127 scopus 로고    scopus 로고
    • Functions of alphavirus nonstructural proteins in RNA replication
    • Kääriäinen, L. & Ahola, T. (2002). Functions of alphavirus nonstructural proteins in RNA replication. Prog Nucleic Acid Res Mol Biol 71, 187–222.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 187-222
    • Kääriäinen, L.1    Ahola, T.2
  • 74
    • 84881231721 scopus 로고    scopus 로고
    • Template RNA length determines the size of replication complex spherules for Semliki Forest virus
    • Kallio, K., Hellström, K., Balistreri, G., Spuul, P., Jokitalo, E. & Ahola, T. (2013). Template RNA length determines the size of replication complex spherules for Semliki Forest virus. J Virol 87, 9125–9134.
    • (2013) J Virol , vol.87 , pp. 9125-9134
    • Kallio, K.1    Hellström, K.2    Balistreri, G.3    Spuul, P.4    Jokitalo, E.5    Ahola, T.6
  • 75
    • 77957271801 scopus 로고    scopus 로고
    • The infection of mammalian and insect cells with SFV bearing nsP1 palmitoylation mutations
    • Karo-Astover, L., Sarova, O., Merits, A. & Zusinaite, E. (2010). The infection of mammalian and insect cells with SFV bearing nsP1 palmitoylation mutations. Virus Res 153, 277–287.
    • (2010) Virus Res , vol.153 , pp. 277-287
    • Karo-Astover, L.1    Sarova, O.2    Merits, A.3    Zusinaite, E.4
  • 76
    • 2542484464 scopus 로고    scopus 로고
    • Regulation of Semliki Forest virus RNA replication: A model for the control of alphavirus pathogenesis in invertebrate hosts
    • Kim, K. H., Rümenapf, T., Strauss, E. G. & Strauss, J. H. (2004). Regulation of Semliki Forest virus RNA replication: a model for the control of alphavirus pathogenesis in invertebrate hosts. Virology 323, 153–163.
    • (2004) Virology , vol.323 , pp. 153-163
    • Kim, K.H.1    Rümenapf, T.2    Strauss, E.G.3    Strauss, J.H.4
  • 77
    • 79961205984 scopus 로고    scopus 로고
    • Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution
    • Kim, D. Y., Firth, A. E., Atasheva, S., Frolova, E. I. & Frolov, I. (2011). Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution. J Virol 85, 8022–8036.
    • (2011) J Virol , vol.85 , pp. 8022-8036
    • Kim, D.Y.1    Firth, A.E.2    Atasheva, S.3    Frolova, E.I.4    Frolov, I.5
  • 78
    • 0027474358 scopus 로고
    • Attenuation of Venezuelan equine encephalitis virus strain TC-83 is encoded by the 59-noncoding region and the E2 envelope glycoprotein
    • Kinney, R. M., Chang, G. J., Tsuchiya, K. R., Sneider, J. M., Roehrig, J. T., Woodward, T. M. & Trent, D. W. (1993). Attenuation of Venezuelan equine encephalitis virus strain TC-83 is encoded by the 59-noncoding region and the E2 envelope glycoprotein. J Virol 67, 1269–1277.
    • (1993) J Virol , vol.67 , pp. 1269-1277
    • Kinney, R.M.1    Chang, G.J.2    Tsuchiya, K.R.3    Sneider, J.M.4    Roehrig, J.T.5    Woodward, T.M.6    Trent, D.W.7
  • 79
    • 0025255251 scopus 로고
    • Mutagenesis of the 39 nontranslated region of Sindbis virus RNA
    • Kuhn, R. J., Hong, Z. & Strauss, J. H. (1990). Mutagenesis of the 39 nontranslated region of Sindbis virus RNA. J Virol 64, 1465–1476.
    • (1990) J Virol , vol.64 , pp. 1465-1476
    • Kuhn, R.J.1    Hong, Z.2    Strauss, J.H.3
  • 80
    • 0026443665 scopus 로고
    • Attenuation of Sindbis virus neurovirulence by using defined mutations in nontranslated regions of the genome RNA
    • Kuhn, R. J., Griffin, D. E., Zhang, H., Niesters, H. G. & Strauss, J. H. (1992). Attenuation of Sindbis virus neurovirulence by using defined mutations in nontranslated regions of the genome RNA. J Virol 66, 7121–7127.
    • (1992) J Virol , vol.66 , pp. 7121-7127
    • Kuhn, R.J.1    Griffin, D.E.2    Zhang, H.3    Niesters, H.G.4    Strauss, J.H.5
  • 82
    • 69249212445 scopus 로고    scopus 로고
    • Structural and functional elements of the promoter encoded by the 59 untranslated region of the Venezuelan equine encephalitis virus genome
    • Kulasegaran-Shylini, R., Atasheva, S., Gorenstein, D. G. & Frolov, I. (2009a). Structural and functional elements of the promoter encoded by the 59 untranslated region of the Venezuelan equine encephalitis virus genome. J Virol 83, 8327–8339.
    • (2009) J Virol , vol.83 , pp. 8327-8339
    • Kulasegaran-Shylini, R.1    Atasheva, S.2    Gorenstein, D.G.3    Frolov, I.4
  • 83
    • 63549096251 scopus 로고    scopus 로고
    • The 59UTR-specific mutation in VEEV TC-83 genome has a strong effect on RNA replication and subgenomic RNA synthesis, but not on translation of the encoded proteins
    • Kulasegaran-Shylini, R., Thiviyanathan, V., Gorenstein, D. G. & Frolov, I. (2009b). The 59UTR-specific mutation in VEEV TC-83 genome has a strong effect on RNA replication and subgenomic RNA synthesis, but not on translation of the encoded proteins. Virology 387, 211–221.
    • (2009) Virology , vol.387 , pp. 211-221
    • Kulasegaran-Shylini, R.1    Thiviyanathan, V.2    Gorenstein, D.G.3    Frolov, I.4
  • 85
    • 0028173041 scopus 로고
    • Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli
    • Laakkonen, P., Hyvönen, M., Peränen, J. & Kääriäinen, L. (1994). Expression of Semliki Forest virus nsP1-specific methyltransferase in insect cells and in Escherichia coli. J Virol 68, 7418–7425.
    • (1994) J Virol , vol.68 , pp. 7418-7425
    • Laakkonen, P.1    Hyvönen, M.2    Peränen, J.3    Kääriäinen, L.4
  • 86
    • 0029956554 scopus 로고    scopus 로고
    • The effects of palmitoylation on membrane association of Semliki forest virus RNA capping enzyme
    • Laakkonen, P., Ahola, T. & Kääriäinen, L. (1996). The effects of palmitoylation on membrane association of Semliki forest virus RNA capping enzyme. J Biol Chem 271, 28567–28571.
    • (1996) J Biol Chem , vol.271 , pp. 28567-28571
    • Laakkonen, P.1    Ahola, T.2    Kääriäinen, L.3
  • 87
    • 0031775227 scopus 로고    scopus 로고
    • Alphavirus replicase protein NSP1 induces filopodia and rearrangement of actin filaments
    • Laakkonen, P., Auvinen, P., Kujala, P. & Kääriäinen, L. (1998). Alphavirus replicase protein NSP1 induces filopodia and rearrangement of actin filaments. J Virol 72, 10265–10269.
    • (1998) J Virol , vol.72 , pp. 10265-10269
    • Laakkonen, P.1    Auvinen, P.2    Kujala, P.3    Kääriäinen, L.4
  • 89
    • 0028142238 scopus 로고
    • Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: Effects on phosphorylation and on virus replication in vertebrate and invertebrate cells
    • LaStarza, M. W., Grakoui, A. & Rice, C. M. (1994a). Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: effects on phosphorylation and on virus replication in vertebrate and invertebrate cells. Virology 202, 224–232.
    • (1994) Virology , vol.202 , pp. 224-232
    • Lastarza, M.W.1    Grakoui, A.2    Rice, C.M.3
  • 90
    • 0027935902 scopus 로고
    • Genetic analysis of the nsP3 region of Sindbis virus: Evidence for roles in minus-strand and subgenomic RNA synthesis
    • LaStarza, M. W., Lemm, J. A. & Rice, C. M. (1994b). Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesis. J Virol 68, 5781–5791.
    • (1994) J Virol , vol.68 , pp. 5781-5791
    • Lastarza, M.W.1    Lemm, J.A.2    Rice, C.M.3
  • 91
    • 0027463085 scopus 로고
    • Assembly of functional Sindbis virus RNA replication complexes: Requirement for coexpression of P123 and P34
    • Lemm, J. A. & Rice, C. M. (1993). Assembly of functional Sindbis virus RNA replication complexes: requirement for coexpression of P123 and P34. J Virol 67, 1905–1915.
    • (1993) J Virol , vol.67 , pp. 1905-1915
    • Lemm, J.A.1    Rice, C.M.2
  • 92
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional Sindbis virus replication complexes: A model for the temporal regulation of minus-and plus-strand RNA synthesis
    • Lemm, J. A., Rümenapf, T., Strauss, E. G., Strauss, J. H. & Rice, C. M. (1994). Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus-and plus-strand RNA synthesis. EMBO J 13, 2925–2934.
    • (1994) EMBO J , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rümenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 93
    • 0031878237 scopus 로고    scopus 로고
    • Template-dependent initiation of Sindbis virus RNA replication in vitro
    • Lemm, J. A., Bergqvist, A., Read, C. M. & Rice, C. M. (1998). Template-dependent initiation of Sindbis virus RNA replication in vitro. J Virol 72, 6546–6553.
    • (1998) J Virol , vol.72 , pp. 6546-6553
    • Lemm, J.A.1    Bergqvist, A.2    Read, C.M.3    Rice, C.M.4
  • 94
    • 0025268737 scopus 로고
    • Complete sequence of the genomic RNA of O’nyong-nyong virus and its use in the construction of alphavirus phylogenetic trees
    • Levinson, R. S., Strauss, J. H. & Strauss, E. G. (1990). Complete sequence of the genomic RNA of O’nyong-nyong virus and its use in the construction of alphavirus phylogenetic trees. Virology 175, 110–123.
    • (1990) Virology , vol.175 , pp. 110-123
    • Levinson, R.S.1    Strauss, J.H.2    Strauss, E.G.3
  • 95
    • 0025213983 scopus 로고
    • Promoter for Sindbis virus RNA-dependent subgenomic RNA transcription
    • Levis, R., Schlesinger, S. & Huang, H. V. (1990). Promoter for Sindbis virus RNA-dependent subgenomic RNA transcription. J Virol 64, 1726–1733.
    • (1990) J Virol , vol.64 , pp. 1726-1733
    • Levis, R.1    Schlesinger, S.2    Huang, H.V.3
  • 96
    • 0027313140 scopus 로고
    • The signal for translational readthrough of a UGA codon in Sindbis virus RNA involves a single cytidine residue immediately downstream of the termination codon
    • Li, G. & Rice, C. M. (1993). The signal for translational readthrough of a UGA codon in Sindbis virus RNA involves a single cytidine residue immediately downstream of the termination codon. J Virol 67, 5062–5067.
    • (1993) J Virol , vol.67 , pp. 5062-5067
    • Li, G.1    Rice, C.M.2
  • 97
    • 3042601257 scopus 로고    scopus 로고
    • Identification of the amino acid sequence in Sindbis virus nsP4 that binds to the promoter for the synthesis of the subgenomic RNA
    • Li, M.-L. & Stollar, V. (2004). Identification of the amino acid sequence in Sindbis virus nsP4 that binds to the promoter for the synthesis of the subgenomic RNA. Proc Natl Acad Sci U S A 101, 9429–9434.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9429-9434
    • Li, M.-L.1    Stollar, V.2
  • 98
    • 34247143367 scopus 로고    scopus 로고
    • Distinct sites on the Sindbis virus RNAdependent RNA polymerase for binding to the promoters for the synthesis of genomic and subgenomic RNA
    • Li, M.-L. & Stollar, V. (2007). Distinct sites on the Sindbis virus RNAdependent RNA polymerase for binding to the promoters for the synthesis of genomic and subgenomic RNA. J Virol 81, 4371–4373.
    • (2007) J Virol , vol.81 , pp. 4371-4373
    • Li, M.-L.1    Stollar, V.2
  • 99
    • 0025045885 scopus 로고
    • Phosphorylation of Sindbis virus nsP3 in vivo and in vitro
    • Li, G. P., La Starza, M. W., Hardy, W. R., Strauss, J. H. & Rice, C. M. (1990). Phosphorylation of Sindbis virus nsP3 in vivo and in vitro. Virology 179, 416–427.
    • (1990) Virology , vol.179 , pp. 416-427
    • Li, G.P.1    La Starza, M.W.2    Hardy, W.R.3    Strauss, J.H.4    Rice, C.M.5
  • 100
    • 77649121708 scopus 로고    scopus 로고
    • In vitro synthesis of Sindbis virus genomic and subgenomic RNAs: Influence of nsP4 mutations and nucleoside triphosphate concentrations
    • Li, M.-L., Wang, H. & Stollar, V. (2010). In vitro synthesis of Sindbis virus genomic and subgenomic RNAs: influence of nsP4 mutations and nucleoside triphosphate concentrations. J Virol 84, 2732–2739.
    • (2010) J Virol , vol.84 , pp. 2732-2739
    • Li, M.-L.1    Wang, H.2    Stollar, V.3
  • 101
    • 66149116780 scopus 로고    scopus 로고
    • HnRNP A1 interacts with the 59 untranslated regions of enterovirus 71 and Sindbis virus RNA and is required for viral replication
    • Lin, J.-Y., Shih, S.-R., Pan, M., Li, C., Lue, C.-F., Stollar, V. & Li, M.-L. (2009). hnRNP A1 interacts with the 59 untranslated regions of enterovirus 71 and Sindbis virus RNA and is required for viral replication. J Virol 83, 6106–6114.
    • (2009) J Virol , vol.83 , pp. 6106-6114
    • Lin, J.-Y.1    Shih, S.-R.2    Pan, M.3    Li, C.4    Lue, C.-F.5    Stollar, V.6    Li, M.-L.7
  • 102
    • 33646721756 scopus 로고    scopus 로고
    • Molecular determinants of substrate specificity for Semliki Forest virus nonstructural protease
    • Lulla, A., Lulla, V., Tints, K., Ahola, T. & Merits, A. (2006). Molecular determinants of substrate specificity for Semliki Forest virus nonstructural protease. J Virol 80, 5413–5422.
    • (2006) J Virol , vol.80 , pp. 5413-5422
    • Lulla, A.1    Lulla, V.2    Tints, K.3    Ahola, T.4    Merits, A.5
  • 103
    • 50949102677 scopus 로고    scopus 로고
    • Molecular defects caused by temperature-sensitive mutations in Semliki Forest virus nsP1
    • Lulla, V., Sawicki, D. L., Sawicki, S. G., Lulla, A., Merits, A. & Ahola, T. (2008). Molecular defects caused by temperature-sensitive mutations in Semliki Forest virus nsP1. J Virol 82, 9236–9244.
    • (2008) J Virol , vol.82 , pp. 9236-9244
    • Lulla, V.1    Sawicki, D.L.2    Sawicki, S.G.3    Lulla, A.4    Merits, A.5    Ahola, T.6
  • 104
    • 84855936001 scopus 로고    scopus 로고
    • Macromolecular assemblydriven processing of the 2/3 cleavage site in the alphavirus replicase polyprotein
    • Lulla, A., Lulla, V. & Merits, A. (2012). Macromolecular assemblydriven processing of the 2/3 cleavage site in the alphavirus replicase polyprotein. J Virol 86, 553–565.
    • (2012) J Virol , vol.86 , pp. 553-565
    • Lulla, A.1    Lulla, V.2    Merits, A.3
  • 105
    • 84883309644 scopus 로고    scopus 로고
    • Presentation overrides specificity: Probing the plasticity of alphaviral proteolytic activity through mutational analysis
    • Lulla, V., Karo-Astover, L., Rausalu, K., Merits, A. & Lulla, A. (2013). Presentation overrides specificity: probing the plasticity of alphaviral proteolytic activity through mutational analysis. J Virol 87, 10207–10220.
    • (2013) J Virol , vol.87 , pp. 10207-10220
    • Lulla, V.1    Karo-Astover, L.2    Rausalu, K.3    Merits, A.4    Lulla, A.5
  • 106
    • 67449102614 scopus 로고    scopus 로고
    • The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket
    • Malet, H., Coutard, B., Jamal, S., Dutartre, H., Papageorgiou, N., Neuvonen, M., Ahola, T., Forrester, N., Gould, E. A. & other authors (2009). The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket. J Virol 83, 6534–6545.
    • (2009) J Virol , vol.83 , pp. 6534-6545
    • Malet, H.1    Coutard, B.2    Jamal, S.3    Dutartre, H.4    Papageorgiou, N.5    Neuvonen, M.6    Ahola, T.7    Forrester, N.8    Gould, E.A.9
  • 107
    • 0036917889 scopus 로고    scopus 로고
    • SAM (Dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin, J. L. & McMillan, F. M. (2002). SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12, 783–793.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 109
    • 23044475941 scopus 로고    scopus 로고
    • Importance of eIF2alpha phosphorylation and stress granule assembly in alphavirus translation regulation
    • McInerney, G. M., Kedersha, N. L., Kaufman, R. J., Anderson, P. & Liljeström, P. (2005). Importance of eIF2alpha phosphorylation and stress granule assembly in alphavirus translation regulation. Mol Biol Cell 16, 3753–3763.
    • (2005) Mol Biol Cell , vol.16 , pp. 3753-3763
    • McInerney, G.M.1    Kedersha, N.L.2    Kaufman, R.J.3    Erson, P.4    Liljeström, P.5
  • 110
    • 0035057147 scopus 로고    scopus 로고
    • Proteolytic processing of Semliki Forest virus-specific non-structural polyprotein by nsP2 protease
    • Merits, A., Vasiljeva, L., Ahola, T., Kääriäinen, L. & Auvinen, P. (2001). Proteolytic processing of Semliki Forest virus-specific non-structural polyprotein by nsP2 protease. J Gen Virol 82, 765–773.
    • (2001) J Gen Virol , vol.82 , pp. 765-773
    • Merits, A.1    Vasiljeva, L.2    Ahola, T.3    Kääriäinen, L.4    Auvinen, P.5
  • 111
    • 0025193991 scopus 로고
    • Both amino acid changes in nsP1 of Sindbis virusLM21 contribute to and are required for efficient expression of the mutant phenotype
    • Mi, S. & Stollar, V. (1990). Both amino acid changes in nsP1 of Sindbis virusLM21 contribute to and are required for efficient expression of the mutant phenotype. Virology 178, 429–434.
    • (1990) Virology , vol.178 , pp. 429-434
    • Mi, S.1    Stollar, V.2
  • 112
    • 0025851067 scopus 로고
    • Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli
    • Mi, S. & Stollar, V. (1991). Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli. Virology 184, 423–427.
    • (1991) Virology , vol.184 , pp. 423-427
    • Mi, S.1    Stollar, V.2
  • 113
    • 34247602505 scopus 로고    scopus 로고
    • Adaptation of Venezuelan equine encephalitis virus lacking 51-nt conserved sequence element to replication in mammalian and mosquito cells
    • Michel, G., Petrakova, O., Atasheva, S. & Frolov, I. (2007). Adaptation of Venezuelan equine encephalitis virus lacking 51-nt conserved sequence element to replication in mammalian and mosquito cells. Virology 362, 475–487.
    • (2007) Virology , vol.362 , pp. 475-487
    • Michel, G.1    Petrakova, O.2    Atasheva, S.3    Frolov, I.4
  • 115
  • 116
    • 84920842317 scopus 로고    scopus 로고
    • Eilat virus host range restriction is present at multiple levels of the virus life cycle
    • Nasar, F., Gorchakov, R. V., Tesh, R. B. & Weaver, S. C. (2015). Eilat virus host range restriction is present at multiple levels of the virus life cycle. J Virol 89, 1404–1418.
    • (2015) J Virol , vol.89 , pp. 1404-1418
    • Nasar, F.1    Gorchakov, R.V.2    Tesh, R.B.3    Weaver, S.C.4
  • 117
    • 81755182978 scopus 로고    scopus 로고
    • SH3 domain-mediated recruitment of host cell amphiphysins by alphavirus nsP3 promotes viral RNA replication
    • Neuvonen, M., Kazlauskas, A., Martikainen, M., Hinkkanen, A., Ahola, T. & Saksela, K. (2011). SH3 domain-mediated recruitment of host cell amphiphysins by alphavirus nsP3 promotes viral RNA replication. PLoS Pathog 7, e1002383.
    • (2011) Plos Pathog , vol.7
    • Neuvonen, M.1    Kazlauskas, A.2    Martikainen, M.3    Hinkkanen, A.4    Ahola, T.5    Saksela, K.6
  • 118
    • 36549060100 scopus 로고    scopus 로고
    • Structural and functional analyses of stem-loop 1 of the Sindbis virus genome
    • Nickens, D. G. & Hardy, R. W. (2008). Structural and functional analyses of stem-loop 1 of the Sindbis virus genome. Virology 370, 158–172.
    • (2008) Virology , vol.370 , pp. 158-172
    • Nickens, D.G.1    Hardy, R.W.2
  • 119
    • 0025047017 scopus 로고
    • Defined mutations in the 59 nontranslated sequence of Sindbis virus RNA
    • Niesters, H. G. & Strauss, J. H. (1990a). Defined mutations in the 59 nontranslated sequence of Sindbis virus RNA. J Virol 64, 4162–4168.
    • (1990) J Virol , vol.64 , pp. 4162-4168
    • Niesters, H.G.1    Strauss, J.H.2
  • 120
    • 0025212683 scopus 로고
    • Mutagenesis of the conserved 51-nucleotide region of Sindbis virus
    • Niesters, H. G. & Strauss, J. H. (1990b). Mutagenesis of the conserved 51-nucleotide region of Sindbis virus. J Virol 64, 1639–1647.
    • (1990) J Virol , vol.64 , pp. 1639-1647
    • Niesters, H.G.1    Strauss, J.H.2
  • 121
    • 84884689115 scopus 로고    scopus 로고
    • RIG-I and MDA-5 detection of viral RNA-dependent RNA polymerase activity restricts positive-strand RNA virus replication
    • Nikonov, A., Mölder, T., Sikut, R., Kiiver, K., Männik, A., Toots, U., Lulla, A., Lulla, V., Utt, A. & other authors (2013). RIG-I and MDA-5 detection of viral RNA-dependent RNA polymerase activity restricts positive-strand RNA virus replication. PLoS Pathog 9, e1003610.
    • (2013) Plos Pathog , vol.9
    • Nikonov, A.1    Mölder, T.2    Sikut, R.3    Kiiver, K.4    Männik, A.5    Toots, U.6    Lulla, A.7    Lulla, V.8    Utt, A.9
  • 122
    • 0032567393 scopus 로고    scopus 로고
    • Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure
    • O’Reilly, E. K. & Kao, C. C. (1998). Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure. Virology 252, 287–303.
    • (1998) Virology , vol.252 , pp. 287-303
    • O’Reilly, E.K.1    Kao, C.C.2
  • 123
    • 0029955552 scopus 로고    scopus 로고
    • Complete sequence of Venezuelan equine encephalitis virus subtype IE reveals conserved and hypervariable domains within the C terminus of nsP3
    • Oberste, M. S., Parker, M. D. & Smith, J. F. (1996). Complete sequence of Venezuelan equine encephalitis virus subtype IE reveals conserved and hypervariable domains within the C terminus of nsP3. Virology 219, 314–320.
    • (1996) Virology , vol.219 , pp. 314-320
    • Oberste, M.S.1    Parker, M.D.2    Smith, J.F.3
  • 124
    • 0019424413 scopus 로고
    • Comparative studies of the 39-terminal sequences of several alpha virus RNAs
    • Ou, J. H., Strauss, E. G. & Strauss, J. H. (1981). Comparative studies of the 39-terminal sequences of several alpha virus RNAs. Virology 109, 281–289.
    • (1981) Virology , vol.109 , pp. 281-289
    • Ou, J.H.1    Strauss, E.G.2    Strauss, J.H.3
  • 125
    • 0007440780 scopus 로고
    • Sequence studies of several alphavirus genomic RNAs in the region containing the start of the subgenomic RNA
    • Ou, J. H., Rice, C. M., Dalgarno, L., Strauss, E. G. & Strauss, J. H. (1982a). Sequence studies of several alphavirus genomic RNAs in the region containing the start of the subgenomic RNA. Proc Natl Acad Sci U S A 79, 5235–5239.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 5235-5239
    • Ou, J.H.1    Rice, C.M.2    Dalgarno, L.3    Strauss, E.G.4    Strauss, J.H.5
  • 126
    • 0020490544 scopus 로고
    • The 39-non-coding regions of alphavirus RNAs contain repeating sequences
    • Ou, J. H., Trent, D. W. & Strauss, J. H. (1982b). The 39-non-coding regions of alphavirus RNAs contain repeating sequences. J Mol Biol 156, 719–730.
    • (1982) J Mol Biol , vol.156 , pp. 719-730
    • Ou, J.H.1    Trent, D.W.2    Strauss, J.H.3
  • 127
    • 0026584175 scopus 로고
    • Cellular proteins bind to the 39 end of Sindbis virus minus-strand RNA
    • Pardigon, N. & Strauss, J. H. (1992). Cellular proteins bind to the 39 end of Sindbis virus minus-strand RNA. J Virol 66, 1007–1015.
    • (1992) J Virol , vol.66 , pp. 1007-1015
    • Pardigon, N.1    Strauss, J.H.2
  • 128
    • 0030060397 scopus 로고    scopus 로고
    • Mosquito homolog of the La autoantigen binds to Sindbis virus RNA
    • Pardigon, N. & Strauss, J. H. (1996). Mosquito homolog of the La autoantigen binds to Sindbis virus RNA. J Virol 70, 1173–1181.
    • (1996) J Virol , vol.70 , pp. 1173-1181
    • Pardigon, N.1    Strauss, J.H.2
  • 129
    • 67349175974 scopus 로고    scopus 로고
    • The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice
    • Park, E. & Griffin, D. E. (2009). The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice. Virology 388, 305–314.
    • (2009) Virology , vol.388 , pp. 305-314
    • Park, E.1    Griffin, D.E.2
  • 130
    • 0032526621 scopus 로고    scopus 로고
    • Evolutionary conservation of histone macroH2A subtypes and domains
    • Pehrson, J. R. & Fuji, R. N. (1998). Evolutionary conservation of histone macroH2A subtypes and domains. Nucleic Acids Res 26, 2837–2842.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2837-2842
    • Pehrson, J.R.1    Fuji, R.N.2
  • 131
    • 0023731901 scopus 로고
    • Semliki Forest virus-specific non-structural protein nsP3 is a phosphoprotein
    • Peränen, J., Takkinen, K., Kalkkinen, N. & Kääriäinen, L. (1988). Semliki Forest virus-specific non-structural protein nsP3 is a phosphoprotein. J Gen Virol 69, 2165–2178.
    • (1988) J Gen Virol , vol.69 , pp. 2165-2178
    • Peränen, J.1    Takkinen, K.2    Kalkkinen, N.3    Kääriäinen, L.4
  • 132
    • 0029060940 scopus 로고
    • The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles
    • Peränen, J., Laakkonen, P., Hyvönen, M. & Kääriäinen, L. (1995). The alphavirus replicase protein nsP1 is membrane-associated and has affinity to endocytic organelles. Virology 208, 610–620.
    • (1995) Virology , vol.208 , pp. 610-620
    • Peränen, J.1    Laakkonen, P.2    Hyvönen, M.3    Kääriäinen, L.4
  • 134
    • 0025784087 scopus 로고
    • Analysis of Sindbis virus promoter recognition in vivo, using novel vectors with two subgenomic mRNA promoters
    • Raju, R. & Huang, H. V. (1991). Analysis of Sindbis virus promoter recognition in vivo, using novel vectors with two subgenomic mRNA promoters. J Virol 65, 2501–2510.
    • (1991) J Virol , vol.65 , pp. 2501-2510
    • Raju, R.1    Huang, H.V.2
  • 135
    • 0033023884 scopus 로고    scopus 로고
    • In vivo addition of poly(A) tail and AU-rich sequences to the 39 terminus of the Sindbis virus RNA genome: A novel 39-end repair pathway
    • Raju, R., Hajjou, M., Hill, K. R., Botta, V. & Botta, S. (1999). In vivo addition of poly(A) tail and AU-rich sequences to the 39 terminus of the Sindbis virus RNA genome: a novel 39-end repair pathway. J Virol 73, 2410–2419.
    • (1999) J Virol , vol.73 , pp. 2410-2419
    • Raju, R.1    Hajjou, M.2    Hill, K.R.3    Botta, V.4    Botta, S.5
  • 137
    • 0030011522 scopus 로고    scopus 로고
    • Functional significance of the nuclear-targeting and NTP-binding motifs of Semliki Forest virus nonstructural protein nsP2
    • Rikkonen, M. (1996). Functional significance of the nuclear-targeting and NTP-binding motifs of Semliki Forest virus nonstructural protein nsP2. Virology 218, 352–361.
    • (1996) Virology , vol.218 , pp. 352-361
    • Rikkonen, M.1
  • 138
    • 0028018141 scopus 로고
    • ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2
    • Rikkonen, M., Peränen, J. & Kääriäinen, L. (1994). ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. J Virol 68, 5804–5810.
    • (1994) J Virol , vol.68 , pp. 5804-5810
    • Rikkonen, M.1    Peränen, J.2    Kääriäinen, L.3
  • 139
    • 0026793857 scopus 로고
    • Conservation of the putative methyltransferase domain: A hallmark of the’Sindbis-like’ supergroup of positive-strand RNA viruses
    • Rozanov, M. N., Koonin, E. V. & Gorbalenya, A. E. (1992). Conservation of the putative methyltransferase domain: a hallmark of the’Sindbis-like’ supergroup of positive-strand RNA viruses. J Gen Virol 73, 2129–2134.
    • (1992) J Gen Virol , vol.73 , pp. 2129-2134
    • Rozanov, M.N.1    Koonin, E.V.2    Gorbalenya, A.E.3
  • 140
    • 58549095054 scopus 로고    scopus 로고
    • Characterization of purified Sindbis virus nsP4 RNA-dependent RNA polymerase activity in vitro
    • Rubach, J. K., Wasik, B. R., Rupp, J. C., Kuhn, R. J., Hardy, R. W. & Smith, J. L. (2009). Characterization of purified Sindbis virus nsP4 RNA-dependent RNA polymerase activity in vitro. Virology 384, 201–208.
    • (2009) Virology , vol.384 , pp. 201-208
    • Rubach, J.K.1    Wasik, B.R.2    Rupp, J.C.3    Kuhn, R.J.4    Hardy, R.W.5    Smith, J.L.6
  • 141
    • 0028181666 scopus 로고
    • Subgenomic mRNA of Aura alphavirus is packaged into virions
    • Rümenapf, T., Strauss, E. G. & Strauss, J. H. (1994). Subgenomic mRNA of Aura alphavirus is packaged into virions. J Virol 68, 56–62.
    • (1994) J Virol , vol.68 , pp. 56-62
    • Rümenapf, T.1    Strauss, E.G.2    Strauss, J.H.3
  • 142
    • 79952596574 scopus 로고    scopus 로고
    • Requirement for the amino-terminal domain of sindbis virus nsP4 during virus infection
    • Rupp, J. C., Jundt, N. & Hardy, R. W. (2011). Requirement for the amino-terminal domain of sindbis virus nsP4 during virus infection. J Virol 85, 3449–3460.
    • (2011) J Virol , vol.85 , pp. 3449-3460
    • Rupp, J.C.1    Jundt, N.2    Hardy, R.W.3
  • 143
    • 33748304343 scopus 로고    scopus 로고
    • The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease
    • Russo, A. T., White, M. A. & Watowich, S. J. (2006). The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease. Structure 14, 1449–1458.
    • (2006) Structure , vol.14 , pp. 1449-1458
    • Russo, A.T.1    White, M.A.2    Watowich, S.J.3
  • 144
    • 0037301423 scopus 로고    scopus 로고
    • Properly folded nonstructural polyprotein directs the semliki forest virus replication complex to the endosomal compartment
    • Salonen, A., Vasiljeva, L., Merits, A., Magden, J., Jokitalo, E. & Kääriäinen, L. (2003). Properly folded nonstructural polyprotein directs the semliki forest virus replication complex to the endosomal compartment. J Virol 77, 1691–1702.
    • (2003) J Virol , vol.77 , pp. 1691-1702
    • Salonen, A.1    Vasiljeva, L.2    Merits, A.3    Magden, J.4    Jokitalo, E.5    Kääriäinen, L.6
  • 145
    • 5644258600 scopus 로고    scopus 로고
    • Viral RNA replication in association with cellular membranes
    • Salonen, A., Ahola, T. & Kääriäinen, L. (2005). Viral RNA replication in association with cellular membranes. Curr Top Microbiol Immunol 285, 139–173.
    • (2005) Curr Top Microbiol Immunol , vol.285 , pp. 139-173
    • Salonen, A.1    Ahola, T.2    Kääriäinen, L.3
  • 146
    • 0017105708 scopus 로고
    • Replication of semliki forest virus: Polyadenylate in plus-strand RNA and polyuridylate in minus-strand RNA
    • Sawicki, D. L. & Gomatos, P. J. (1976). Replication of semliki forest virus: polyadenylate in plus-strand RNA and polyuridylate in minus-strand RNA. J Virol 20, 446–464.
    • (1976) J Virol , vol.20 , pp. 446-464
    • Sawicki, D.L.1    Gomatos, P.J.2
  • 147
    • 0018851365 scopus 로고
    • Short-lived minus-strand polymerase for Semliki Forest virus
    • Sawicki, D. L. & Sawicki, S. G. (1980). Short-lived minus-strand polymerase for Semliki Forest virus. J Virol 34, 108–118.
    • (1980) J Virol , vol.34 , pp. 108-118
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 148
    • 0022007185 scopus 로고
    • Functional analysis of the A complementation group mutants of Sindbis HR virus
    • Sawicki, D. L. & Sawicki, S. G. (1985). Functional analysis of the A complementation group mutants of Sindbis HR virus. Virology 144, 20–34.
    • (1985) Virology , vol.144 , pp. 20-34
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 149
    • 0027166774 scopus 로고
    • A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis
    • Sawicki, D. L. & Sawicki, S. G. (1993). A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis. J Virol 67, 3605–3610.
    • (1993) J Virol , vol.67 , pp. 3605-3610
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 150
    • 0028319950 scopus 로고
    • Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes
    • Sawicki, D. L. & Sawicki, S. G. (1994). Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes. Arch Virol Suppl 9, 393–405.
    • (1994) Arch Virol Suppl , vol.9 , pp. 393-405
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 151
    • 0017843190 scopus 로고
    • Mechanism for control of synthesis of Semliki Forest virus 26S and 42S RNA
    • Sawicki, D. L., Kääriäinen, L., Lambek, C. & Gomatos, P. J. (1978). Mechanism for control of synthesis of Semliki Forest virus 26S and 42S RNA. J Virol 25, 19–27.
    • (1978) J Virol , vol.25 , pp. 19-27
    • Sawicki, D.L.1    Kääriäinen, L.2    Lambek, C.3    Gomatos, P.J.4
  • 152
    • 0037302340 scopus 로고    scopus 로고
    • Alphavirus minus-strand synthesis and persistence in mouse embryo fibroblasts derived from mice lacking RNase L and protein kinase R
    • Sawicki, D. L., Silverman, R. H., Williams, B. R. & Sawicki, S. G. (2003). Alphavirus minus-strand synthesis and persistence in mouse embryo fibroblasts derived from mice lacking RNase L and protein kinase R. J Virol 77, 1801–1811.
    • (2003) J Virol , vol.77 , pp. 1801-1811
    • Sawicki, D.L.1    Silverman, R.H.2    Williams, B.R.3    Sawicki, S.G.4
  • 153
    • 33645972603 scopus 로고    scopus 로고
    • Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells
    • Sawicki, D. L., Perri, S., Polo, J. M. & Sawicki, S. G. (2006). Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells. J Virol 80, 360–371.
    • (2006) J Virol , vol.80 , pp. 360-371
    • Sawicki, D.L.1    Perri, S.2    Polo, J.M.3    Sawicki, S.G.4
  • 155
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. & Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27, 157–162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 156
    • 0025752329 scopus 로고
    • Mutations that confer resistance to mycophenolic acid and ribavirin on Sindbis virus map to the nonstructural protein nsP1
    • Scheidel, L. M. & Stollar, V. (1991). Mutations that confer resistance to mycophenolic acid and ribavirin on Sindbis virus map to the nonstructural protein nsP1. Virology 181, 490–499.
    • (1991) Virology , vol.181 , pp. 490-499
    • Scheidel, L.M.1    Stollar, V.2
  • 157
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier, G., O’Gara, M., Saenger, W. & Cheng, X. (1995). Universal catalytic domain structure of AdoMet-dependent methyltransferases. J Mol Biol 247, 16–20.
    • (1995) J Mol Biol , vol.247 , pp. 16-20
    • Schluckebier, G.1    O’Gara, M.2    Saenger, W.3    Cheng, X.4
  • 158
    • 84925386816 scopus 로고    scopus 로고
    • Stress granule components G3BP1 and G3BP2 play a proviral role early in Chikungunya virus replication
    • Scholte, F. E., Tas, A., Albulescu, I. C., Zˇ usinaite, E., Merits, A., Snijder, E. J. & van Hemert, M. J. (2015). Stress granule components G3BP1 and G3BP2 play a proviral role early in Chikungunya virus replication. J Virol 89, 4457–4469.
    • (2015) J Virol , vol.89 , pp. 4457-4469
    • Scholte, F.E.1    Tas, A.2    Albulescu, I.C.3    Zˇ Usinaite, E.4    Merits, A.5    Snijder, E.J.6    van Hemert, M.J.7
  • 159
    • 84867391808 scopus 로고    scopus 로고
    • Structural and functional insights into alphavirus polyprotein processing and pathogenesis
    • Shin, G., Yost, S. A., Miller, M. T., Elrod, E. J., Grakoui, A. & Marcotrigiano, J. (2012). Structural and functional insights into alphavirus polyprotein processing and pathogenesis. Proc Natl Acad Sci U S A 109, 16534–16539.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 16534-16539
    • Shin, G.1    Yost, S.A.2    Miller, M.T.3    Elrod, E.J.4    Grakoui, A.5    Marcotrigiano, J.6
  • 160
    • 0025336486 scopus 로고
    • Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123
    • Shirako, Y. & Strauss, J. H. (1990). Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123. Virology 177, 54–64.
    • (1990) Virology , vol.177 , pp. 54-64
    • Shirako, Y.1    Strauss, J.H.2
  • 161
    • 0027979138 scopus 로고
    • Regulation of Sindbis virus RNA replication: Uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis
    • Shirako, Y. & Strauss, J. H. (1994). Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis. J Virol 68, 1874–1885.
    • (1994) J Virol , vol.68 , pp. 1874-1885
    • Shirako, Y.1    Strauss, J.H.2
  • 162
    • 0031937629 scopus 로고    scopus 로고
    • Requirement for an aromatic amino acid or histidine at the N terminus of Sindbis virus RNA polymerase
    • Shirako, Y. & Strauss, J. H. (1998). Requirement for an aromatic amino acid or histidine at the N terminus of Sindbis virus RNA polymerase. J Virol 72, 2310–2315.
    • (1998) J Virol , vol.72 , pp. 2310-2315
    • Shirako, Y.1    Strauss, J.H.2
  • 163
    • 0037289824 scopus 로고    scopus 로고
    • Modification of the 59 terminus of Sindbis virus genomic RNA allows nsP4 RNA polymerases with nonaromatic amino acids at the N terminus to function in RNA replication
    • Shirako, Y., Strauss, E. G. & Strauss, J. H. (2003). Modification of the 59 terminus of Sindbis virus genomic RNA allows nsP4 RNA polymerases with nonaromatic amino acids at the N terminus to function in RNA replication. J Virol 77, 2301–2309.
    • (2003) J Virol , vol.77 , pp. 2301-2309
    • Shirako, Y.1    Strauss, E.G.2    Strauss, J.H.3
  • 164
    • 0015527746 scopus 로고
    • Replication of Sindbis virus. I. Relative size and genetic content of 26 s and 49 s RNA
    • Simmons, D. T. & Strauss, J. H. (1972a). Replication of Sindbis virus. I. Relative size and genetic content of 26 s and 49 s RNA. J Mol Biol 71, 599–613.
    • (1972) J Mol Biol , vol.71 , pp. 599-613
    • Simmons, D.T.1    Strauss, J.H.2
  • 165
    • 0015527731 scopus 로고
    • Replication of Sindbis virus. II. Multiple forms of double-stranded RNA isolated from infected cells
    • Simmons, D. T. & Strauss, J. H. (1972b). Replication of Sindbis virus. II. Multiple forms of double-stranded RNA isolated from infected cells. J Mol Biol 71, 615–631.
    • (1972) J Mol Biol , vol.71 , pp. 615-631
    • Simmons, D.T.1    Strauss, J.H.2
  • 166
    • 77956312311 scopus 로고    scopus 로고
    • Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells
    • Sokoloski, K. J., Dickson, A. M., Chaskey, E. L., Garneau, N. L., Wilusz, C. J. & Wilusz, J. (2010). Sindbis virus usurps the cellular HuR protein to stabilize its transcripts and promote productive infections in mammalian and mosquito cells. Cell Host Microbe 8, 196–207.
    • (2010) Cell Host Microbe , vol.8 , pp. 196-207
    • Sokoloski, K.J.1    Dickson, A.M.2    Chaskey, E.L.3    Garneau, N.L.4    Wilusz, C.J.5    Wilusz, J.6
  • 167
  • 168
    • 33846052318 scopus 로고    scopus 로고
    • Role of the amphipathic peptide of Semliki forest virus replicase protein nsP1 in membrane association and virus replication
    • Spuul, P., Salonen, A., Merits, A., Jokitalo, E., Kääriäinen, L. & Ahola, T. (2007). Role of the amphipathic peptide of Semliki forest virus replicase protein nsP1 in membrane association and virus replication. J Virol 81, 872–883.
    • (2007) J Virol , vol.81 , pp. 872-883
    • Spuul, P.1    Salonen, A.2    Merits, A.3    Jokitalo, E.4    Kääriäinen, L.5    Ahola, T.6
  • 169
    • 77954505687 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest Virus replication complexes from the plasma membrane to modified lysosomes
    • Spuul, P., Balistreri, G., Kääriäinen, L. & Ahola, T. (2010). Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest Virus replication complexes from the plasma membrane to modified lysosomes. J Virol 84, 7543–7557.
    • (2010) J Virol , vol.84 , pp. 7543-7557
    • Spuul, P.1    Balistreri, G.2    Kääriäinen, L.3    Ahola, T.4
  • 170
    • 79955426289 scopus 로고    scopus 로고
    • Assembly of alphavirus replication complexes from RNA and protein components in a novel trans-replication system in mammalian cells
    • Spuul, P., Balistreri, G., Hellström, K., Golubtsov, A. V., Jokitalo, E. & Ahola, T. (2011). Assembly of alphavirus replication complexes from RNA and protein components in a novel trans-replication system in mammalian cells. J Virol 85, 4739–4751.
    • (2011) J Virol , vol.85 , pp. 4739-4751
    • Spuul, P.1    Balistreri, G.2    Hellström, K.3    Golubtsov, A.V.4    Jokitalo, E.5    Ahola, T.6
  • 172
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss, J. H. & Strauss, E. G. (1994). The alphaviruses: gene expression, replication, and evolution. Microbiol Rev 58, 491–562.
    • (1994) Microbiol Rev , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 173
    • 0020826410 scopus 로고
    • Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon
    • Strauss, E. G., Rice, C. M. & Strauss, J. H. (1983). Sequence coding for the alphavirus nonstructural proteins is interrupted by an opal termination codon. Proc Natl Acad Sci U S A 80, 5271–5275.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 5271-5275
    • Strauss, E.G.1    Rice, C.M.2    Strauss, J.H.3
  • 174
    • 0021319456 scopus 로고
    • Complete nucleotide sequence of the genomic RNA of Sindbis virus
    • Strauss, E. G., Rice, C. M. & Strauss, J. H. (1984). Complete nucleotide sequence of the genomic RNA of Sindbis virus. Virology 133, 92–110.
    • (1984) Virology , vol.133 , pp. 92-110
    • Strauss, E.G.1    Rice, C.M.2    Strauss, J.H.3
  • 175
    • 0031985086 scopus 로고    scopus 로고
    • Regulation of alphavirus 26S mRNA transcription by replicase component nsP2
    • Suopanki, J., Sawicki, D. L., Sawicki, S. G. & Kääriäinen, L. (1998). Regulation of alphavirus 26S mRNA transcription by replicase component nsP2. J Gen Virol 79, 309–319.
    • (1998) J Gen Virol , vol.79 , pp. 309-319
    • Suopanki, J.1    Sawicki, D.L.2    Sawicki, S.G.3    Kääriäinen, L.4
  • 176
    • 33749473615 scopus 로고    scopus 로고
    • Catalytic core of alphavirus nonstructural protein nsP4 possesses terminal adenylyltransferase activity
    • Tomar, S., Hardy, R. W., Smith, J. L. & Kuhn, R. J. (2006). Catalytic core of alphavirus nonstructural protein nsP4 possesses terminal adenylyltransferase activity. J Virol 80, 9962–9969.
    • (2006) J Virol , vol.80 , pp. 9962-9969
    • Tomar, S.1    Hardy, R.W.2    Smith, J.L.3    Kuhn, R.J.4
  • 177
    • 80051583576 scopus 로고    scopus 로고
    • Heterologous production, purification and characterization of enzymatically active Sindbis virus nonstructural protein nsP1
    • Tomar, S., Narwal, M., Harms, E., Smith, J. L. & Kuhn, R. J. (2011). Heterologous production, purification and characterization of enzymatically active Sindbis virus nonstructural protein nsP1. Protein Expr Purif 79, 277–284.
    • (2011) Protein Expr Purif , vol.79 , pp. 277-284
    • Tomar, S.1    Narwal, M.2    Harms, E.3    Smith, J.L.4    Kuhn, R.J.5
  • 178
    • 0037639148 scopus 로고    scopus 로고
    • Amino acid mutations in the replicase protein nsP3 of Semliki Forest virus cumulatively affect neurovirulence
    • Tuittila, M. & Hinkkanen, A. E. (2003). Amino acid mutations in the replicase protein nsP3 of Semliki Forest virus cumulatively affect neurovirulence. J Gen Virol 84, 1525–1533.
    • (2003) J Gen Virol , vol.84 , pp. 1525-1533
    • Tuittila, M.1    Hinkkanen, A.E.2
  • 179
    • 0033999561 scopus 로고    scopus 로고
    • Replicase complex genes of Semliki Forest virus confer lethal neurovirulence
    • Tuittila, M. T., Santagati, M. G., Röyttä, M., Määttä, J. A. & Hinkkanen, A. E. (2000). Replicase complex genes of Semliki Forest virus confer lethal neurovirulence. J Virol 74, 4579–4589.
    • (2000) J Virol , vol.74 , pp. 4579-4589
    • Tuittila, M.T.1    Santagati, M.G.2    Röyttä, M.3    Määttä, J.A.4    Hinkkanen, A.E.5
  • 180
    • 84883292987 scopus 로고    scopus 로고
    • Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus
    • Varjak, M., Saul, S., Arike, L., Lulla, A., Peil, L. & Merits, A. (2013). Magnetic fractionation and proteomic dissection of cellular organelles occupied by the late replication complexes of Semliki Forest virus. J Virol 87, 10295–10312.
    • (2013) J Virol , vol.87 , pp. 10295-10312
    • Varjak, M.1    Saul, S.2    Arike, L.3    Lulla, A.4    Peil, L.5    Merits, A.6
  • 181
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 59-triphosphatase activity of Nsp2
    • Vasiljeva, L., Merits, A., Auvinen, P. & Kääriäinen, L. (2000). Identification of a novel function of the alphavirus capping apparatus. RNA 59-triphosphatase activity of Nsp2. J Biol Chem 275, 17281–17287.
    • (2000) J Biol Chem , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3    Kääriäinen, L.4
  • 182
    • 0142211312 scopus 로고    scopus 로고
    • Regulation of the sequential processing of Semliki Forest virus replicase polyprotein
    • Vasiljeva, L., Merits, A., Golubtsov, A., Sizemskaja, V., Kääriäinen, L. & Ahola, T. (2003). Regulation of the sequential processing of Semliki Forest virus replicase polyprotein. J Biol Chem 278, 41636–41645.
    • (2003) J Biol Chem , vol.278 , pp. 41636-41645
    • Vasiljeva, L.1    Merits, A.2    Golubtsov, A.3    Sizemskaja, V.4    Kääriäinen, L.5    Ahola, T.6
  • 183
    • 29944433224 scopus 로고    scopus 로고
    • Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: A strategy to overcome the antiviral effect of protein kinase PKR
    • Ventoso, I., Sanz, M. A., Molina, S., Berlanga, J. J., Carrasco, L. & Esteban, M. (2006). Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR. Genes Dev 20, 87–100.
    • (2006) Genes Dev , vol.20 , pp. 87-100
    • Ventoso, I.1    Sanz, M.A.2    Molina, S.3    Berlanga, J.J.4    Carrasco, L.5    Esteban, M.6
  • 184
    • 0035937166 scopus 로고    scopus 로고
    • Elimination of phosphorylation sites of Semliki Forest virus replicase protein nsP3
    • Vihinen, H., Ahola, T., Tuittila, M., Merits, A. & Kääriäinen, L. (2001). Elimination of phosphorylation sites of Semliki Forest virus replicase protein nsP3. J Biol Chem 276, 5745–5752.
    • (2001) J Biol Chem , vol.276 , pp. 5745-5752
    • Vihinen, H.1    Ahola, T.2    Tuittila, M.3    Merits, A.4    Kääriäinen, L.5
  • 186
    • 0026086221 scopus 로고
    • Sindbis virus nsP1 functions in negative-strand RNA synthesis
    • Wang, Y. F., Sawicki, S. G. & Sawicki, D. L. (1991). Sindbis virus nsP1 functions in negative-strand RNA synthesis. J Virol 65, 985–988.
    • (1991) J Virol , vol.65 , pp. 985-988
    • Wang, Y.F.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 187
    • 0028040383 scopus 로고
    • Alphavirus nsP3 functions to form replication complexes transcribing negativestrand RNA
    • Wang, Y. F., Sawicki, S. G. & Sawicki, D. L. (1994). Alphavirus nsP3 functions to form replication complexes transcribing negativestrand RNA. J Virol 68, 6466–6475.
    • (1994) J Virol , vol.68 , pp. 6466-6475
    • Wang, Y.F.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 188
    • 0029879411 scopus 로고    scopus 로고
    • Mutagenesis of the Sindbis virus nsP1 protein: Effects on methyltransferase activity and viral infectivity
    • Wang, H. L., O’Rear, J. & Stollar, V. (1996). Mutagenesis of the Sindbis virus nsP1 protein: effects on methyltransferase activity and viral infectivity. Virology 217, 527–531.
    • (1996) Virology , vol.217 , pp. 527-531
    • Wang, H.L.1    O’Rear, J.2    Stollar, V.3
  • 189
    • 84899100887 scopus 로고    scopus 로고
    • Arrival of chikungunya virus in the new world: Prospects for spread and impact on public health
    • Weaver, S. C. (2014). Arrival of chikungunya virus in the new world: prospects for spread and impact on public health. PLoS Negl Trop Dis 8, e2921.
    • (2014) Plos Negl Trop Dis , vol.8
    • Weaver, S.C.1
  • 190
    • 84925400315 scopus 로고    scopus 로고
    • Chikungunya virus and the global spread of a mosquito-borne disease
    • Weaver, S. C. & Lecuit, M. (2015). Chikungunya virus and the global spread of a mosquito-borne disease. N Engl J Med 372, 1231–1239.
    • (2015) N Engl J Med , vol.372 , pp. 1231-1239
    • Weaver, S.C.1    Lecuit, M.2
  • 191
    • 0024428285 scopus 로고
    • Evidence for specificity in the encapsidation of Sindbis virus RNAs
    • Weiss, B., Nitschko, H., Ghattas, I., Wright, R. & Schlesinger, S. (1989). Evidence for specificity in the encapsidation of Sindbis virus RNAs. J Virol 63, 5310–5318.
    • (1989) J Virol , vol.63 , pp. 5310-5318
    • Weiss, B.1    Nitschko, H.2    Ghattas, I.3    Wright, R.4    Schlesinger, S.5
  • 192
    • 0028359402 scopus 로고
    • Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site
    • Weiss, B., Geigenmüller-Gnirke, U. & Schlesinger, S. (1994). Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site. Nucleic Acids Res 22, 780–786.
    • (1994) Nucleic Acids Res , vol.22 , pp. 780-786
    • Weiss, B.1    Geigenmüller-Gnirke, U.2    Schlesinger, S.3
  • 193
    • 0033541385 scopus 로고    scopus 로고
    • Salmon pancreas disease virus, an alphavirus infecting farmed Atlantic salmon, Salmo salar L
    • Weston, J. H., Welsh, M. D., McLoughlin, M. F. & Todd, D. (1999). Salmon pancreas disease virus, an alphavirus infecting farmed Atlantic salmon, Salmo salar L. Virology 256, 188–195.
    • (1999) Virology , vol.256 , pp. 188-195
    • Weston, J.H.1    Welsh, M.D.2    McLoughlin, M.F.3    Todd, D.4
  • 194
    • 0030830860 scopus 로고    scopus 로고
    • A novel viral RNA species in Sindbis virus-infected cells
    • Wielgosz, M. M. & Huang, H. V. (1997). A novel viral RNA species in Sindbis virus-infected cells. J Virol 71, 9108–9117.
    • (1997) J Virol , vol.71 , pp. 9108-9117
    • Wielgosz, M.M.1    Huang, H.V.2
  • 195
    • 0035078780 scopus 로고    scopus 로고
    • Sequence requirements for Sindbis virus subgenomic mRNA promoter function in cultured cells
    • Wielgosz, M. M., Raju, R. & Huang, H. V. (2001). Sequence requirements for Sindbis virus subgenomic mRNA promoter function in cultured cells. J Virol 75, 3509–3519.
    • (2001) J Virol , vol.75 , pp. 3509-3519
    • Wielgosz, M.M.1    Raju, R.2    Huang, H.V.3
  • 196
    • 0033585015 scopus 로고    scopus 로고
    • A novel in vitro replication system for Dengue virus. Initiation ofRNAsynthesis at the 39-end of exogenous viral RNA templates requires 59-and 39-terminal complementary sequence motifs of the viral RNA
    • You, S. & Padmanabhan, R. (1999). A novel in vitro replication system for Dengue virus. Initiation ofRNAsynthesis at the 39-end of exogenous viral RNA templates requires 59-and 39-terminal complementary sequence motifs of the viral RNA. J Biol Chem 274, 33714–33722.
    • (1999) J Biol Chem , vol.274 , pp. 33714-33722
    • You, S.1    Padmanabhan, R.2
  • 198
    • 57649089398 scopus 로고    scopus 로고
    • Molecular cloning, overproduction, purification and biochemical characterization of the p39 nsp2 protease domains encoded by three alphaviruses
    • Zhang, D., Tözsér, J. & Waugh, D. S. (2009). Molecular cloning, overproduction, purification and biochemical characterization of the p39 nsp2 protease domains encoded by three alphaviruses. Protein Expr Purif 64, 89–97.
    • (2009) Protein Expr Purif , vol.64 , pp. 89-97
    • Zhang, D.1    Tözsér, J.2    Waugh, D.S.3
  • 199
    • 34347366405 scopus 로고    scopus 로고
    • Mutations at the palmitoylation site of nonstructural protein nsP1 of Semliki Forest virus attenuate virus replication and cause accumulation of compensatory mutations
    • Zusinaite, E., Tints, K., Kiiver, K., Spuul, P., Karo-Astover, L., Merits, A. & Sarand, I. (2007). Mutations at the palmitoylation site of nonstructural protein nsP1 of Semliki Forest virus attenuate virus replication and cause accumulation of compensatory mutations. J Gen Virol 88, 1977–1985.
    • (2007) J Gen Virol , vol.88 , pp. 1977-1985
    • Zusinaite, E.1    Tints, K.2    Kiiver, K.3    Spuul, P.4    Karo-Astover, L.5    Merits, A.6    Sarand, I.7


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