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Volumn , Issue , 2008, Pages 53-76

Bluetongue virus replication and assembly

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EID: 85147083370     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012369368-6.50008-3     Document Type: Chapter
Times cited : (9)

References (80)
  • 1
    • 0031239832 scopus 로고    scopus 로고
    • Modification of cytoskeleton and prosome networks in relation to protein synthesis in influenza A virus-infected LLC-MK2 cells
    • M.C. Arcangeletti, F. Pinardi, S. Missorini, F. De Conto, G. Conti, P. Portincasa, K. Scherrer and C. Chezzi (1997) Modification of cytoskeleton and prosome networks in relation to protein synthesis in influenza A virus-infected LLC-MK2 cells. Virus Res. 51 19-34.
    • (1997) Virus Res. , vol.51 , pp. 19-34
    • Arcangeletti, M.C.1    Pinardi, F.2    Missorini, S.3    De Conto, F.4    Conti, G.5    Portincasa, P.6    Scherrer, K.7    Chezzi, C.8
  • 2
    • 0035845528 scopus 로고    scopus 로고
    • Structural features of an influenza virus promoter and their implications for viral RNA synthesis
    • S.H. Bae, H.K. Cheong, J.H. Lee, C. Cheong, M. Kainosho and B.S. Choi (2001) Structural features of an influenza virus promoter and their implications for viral RNA synthesis. Proc. Natl. Acad. Sci. USA. 98 10602-10607.
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , pp. 10602-10607
    • Bae, S.H.1    Cheong, H.K.2    Lee, J.H.3    Cheong, C.4    Kainosho, M.5    Choi, B.S.6
  • 3
    • 0014812498 scopus 로고
    • Transcription in vitro by reovirus associated ribonucleic acid-dependent polymerase
    • A.K. Bannerjee and A.J. Shatkin (1970) Transcription in vitro by reovirus associated ribonucleic acid-dependent polymerase. J. Virol. 6 1-11.
    • (1970) J. Virol. , vol.6 , pp. 1-11
    • Bannerjee, A.K.1    Shatkin, A.J.2
  • 4
    • 0031924404 scopus 로고    scopus 로고
    • Membrane organization of bluetongue virus non-structural glycoprotein NS3
    • O.B. Bansal, A. Stokes, A. Bansal, D.H.L. Bishop and P. Roy (1998) Membrane organization of bluetongue virus non-structural glycoprotein NS3. J. Virol. 72 3362-3369.
    • (1998) J. Virol. , vol.72 , pp. 3362-3369
    • Bansal, O.B.1    Stokes, A.2    Bansal, A.3    Bishop, D.H.L.4    Roy, P.5
  • 5
    • 0036235572 scopus 로고    scopus 로고
    • Cis-acting elements important for retroviral RNA packaging specificity
    • B.E. Beasley and W.S. Hu (2002) Cis-acting elements important for retroviral RNA packaging specificity. J. Virol. 76 4950-4960.
    • (2002) J. Virol. , vol.76 , pp. 4950-4960
    • Beasley, B.E.1    Hu, W.S.2
  • 6
    • 0036789972 scopus 로고    scopus 로고
    • The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release
    • A.R. Beaton, J. Rodriguez, Y.K. Reddy and P. Roy (2002) The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release. Proc. Natl. Acad. Sci. USA. 99 13154-13159.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 13154-13159
    • Beaton, A.R.1    Rodriguez, J.2    Reddy, Y.K.3    Roy, P.4
  • 7
    • 33846672647 scopus 로고    scopus 로고
    • Interaction between bluetongue virus outer capsid protein VP2 and vimentin is necessary for virus egress
    • B. Bhattacharya, R.J. Noad and P. Roy (2007) Interaction between bluetongue virus outer capsid protein VP2 and vimentin is necessary for virus egress. Virol. J. Jan 15; 4 7.
    • (2007) Virol. J. Jan 15; , vol.4 , pp. 7
    • Bhattacharya, B.1    Noad, R.J.2    Roy, P.3
  • 8
    • 0014112271 scopus 로고
    • Cytopathologic changes and development of inclusion bodies in cultured cells infected with bluetongue virus
    • J.G. Bowne and M.M. Jochim (1967) Cytopathologic changes and development of inclusion bodies in cultured cells infected with bluetongue virus. Am. J. Vet. Res. 28 1091-1105.
    • (1967) Am. J. Vet. Res. , vol.28 , pp. 1091-1105
    • Bowne, J.G.1    Jochim, M.M.2
  • 9
    • 50149089970 scopus 로고    scopus 로고
    • A Reverse genetics system for Bluetongue virus
    • M. Boyce, C.C. Celma and P. Roy (2008) A Reverse genetics system for Bluetongue virus. J. Virol. 82 8339-8348.
    • (2008) J. Virol. , vol.82 , pp. 8339-8348
    • Boyce, M.1    Celma, C.C.2    Roy, P.3
  • 10
    • 33847228746 scopus 로고    scopus 로고
    • Recovery of infectious bluetongue virus from RNA
    • M. Boyce and P. Roy (2007) Recovery of infectious bluetongue virus from RNA. J. Virol. 81 2179-2186.
    • (2007) J. Virol. , vol.81 , pp. 2179-2186
    • Boyce, M.1    Roy, P.2
  • 11
    • 1842536809 scopus 로고    scopus 로고
    • Purified recombinant bluetongue virus VP1 exhibits RNA replicase activity
    • M. Boyce, J. Wehrfritz, R. Noad and P. Roy (2004) Purified recombinant bluetongue virus VP1 exhibits RNA replicase activity. J. Virol. 78 3994-4002.
    • (2004) J. Virol. , vol.78 , pp. 3994-4002
    • Boyce, M.1    Wehrfritz, J.2    Noad, R.3    Roy, P.4
  • 12
    • 4444295304 scopus 로고    scopus 로고
    • Structure and assembly of the RNA binding domain of bluetongue virus non-structural protein 2
    • C. Butan, H. Van Der Zandt and P.A. Tucker (2004) Structure and assembly of the RNA binding domain of bluetongue virus non-structural protein 2. J. Biol. Chem. 279 37613-37621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37613-37621
    • Butan, C.1    Van Der Zandt, H.2    Tucker, P.A.3
  • 13
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • C.E. Creutz (1992) The annexins and exocytosis. Science 258 924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 14
    • 0024853528 scopus 로고
    • The site of bluetongue virus attachment to glycophorins from a number of animal erythrocytes
    • B.T. Eaton and G.S. Crameri (1989) The site of bluetongue virus attachment to glycophorins from a number of animal erythrocytes. J. Gen. Virol. 70 3347-3353.
    • (1989) J. Gen. Virol. , vol.70 , pp. 3347-3353
    • Eaton, B.T.1    Crameri, G.S.2
  • 16
    • 0036138056 scopus 로고    scopus 로고
    • Localization of the single-stranded RNA-binding domains of bluetongue virus nonstructural protein NS2
    • G.C. Fillmore, H. Lin and J.K.K. Li (2002) Localization of the single-stranded RNA-binding domains of bluetongue virus nonstructural protein NS2. J. Virol. 76 499-506.
    • (2002) J. Virol. , vol.76 , pp. 499-506
    • Fillmore, G.C.1    Lin, H.2    Li, J.K.K.3
  • 17
    • 34247609683 scopus 로고    scopus 로고
    • Bluetongue virus entry into cells
    • M. Forzan, M. Marsh and P. Roy (2007) Bluetongue virus entry into cells. J Virol. 81 4819-4827.
    • (2007) J Virol. , vol.81 , pp. 4819-4827
    • Forzan, M.1    Marsh, M.2    Roy, P.3
  • 18
    • 1242319267 scopus 로고    scopus 로고
    • A capsid protein of nonenveloped bluetongue virus exhibits membrane fusion activity
    • M. Forzan, C. Wirblich and P. Roy (2004) A capsid protein of nonenveloped bluetongue virus exhibits membrane fusion activity. Proc. Natl. Acad. Sci. USA. 101 2100-2105.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 2100-2105
    • Forzan, M.1    Wirblich, C.2    Roy, P.3
  • 19
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • E.O. Freed (2002) Viral late domains. J. Virol. 76 4679-4687.
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 20
    • 9644252807 scopus 로고    scopus 로고
    • Mechanisms of enveloped virus release
    • E.O. Freed (2004) Mechanisms of enveloped virus release. Virus Res. 106 85-86.
    • (2004) Virus Res. , vol.106 , pp. 85-86
    • Freed, E.O.1
  • 21
    • 0024390981 scopus 로고
    • Expression of two related nonstructural proteins of bluetongue virus (BTV) type 10 in insect cells by a recombinant baculovirus: production of polyclonal ascitic fluid and characterization of the gene product in BTV-infected BHK cells
    • T.J. French, S. Inumaru and P. Roy (1989) Expression of two related nonstructural proteins of bluetongue virus (BTV) type 10 in insect cells by a recombinant baculovirus: production of polyclonal ascitic fluid and characterization of the gene product in BTV-infected BHK cells. J. Virol. 63 3270-3278.
    • (1989) J. Virol. , vol.63 , pp. 3270-3278
    • French, T.J.1    Inumaru, S.2    Roy, P.3
  • 22
    • 0025225427 scopus 로고
    • Assembly of double-shelled, virus-like particles of bluetongue virus by the simultaneous expression of four structural proteins
    • T.J. French, J.J. Marshall and P. Roy (1990) Assembly of double-shelled, virus-like particles of bluetongue virus by the simultaneous expression of four structural proteins. J. Virol. 64 5695-5700.
    • (1990) J. Virol. , vol.64 , pp. 5695-5700
    • French, T.J.1    Marshall, J.J.2    Roy, P.3
  • 23
    • 0025215056 scopus 로고
    • Synthesis of bluetongue virus (BTV) corelike particles by a recombinant baculovirus expressing the two major structural core proteins of BTV
    • T.J. French and P. Roy (1990) Synthesis of bluetongue virus (BTV) corelike particles by a recombinant baculovirus expressing the two major structural core proteins of BTV. J. Virol. 64 1530-1536.
    • (1990) J. Virol. , vol.64 , pp. 1530-1536
    • French, T.J.1    Roy, P.2
  • 26
    • 0029106664 scopus 로고
    • Adaptation of bluetongue virus in mosquito cells results in overexpression of NS3 proteins and release of virus particles
    • F. Guirakhoo, J.A. Catalan and T.P. Monath (1995) Adaptation of bluetongue virus in mosquito cells results in overexpression of NS3 proteins and release of virus particles. Arch. Virol. 140 967-974.
    • (1995) Arch. Virol. , vol.140 , pp. 967-974
    • Guirakhoo, F.1    Catalan, J.A.2    Monath, T.P.3
  • 27
    • 5644221347 scopus 로고    scopus 로고
    • The NS3 protein of bluetongue virus exhibits viroporin-like properties
    • Z. Han and R.N. Harty (2004) The NS3 protein of bluetongue virus exhibits viroporin-like properties. J. Biol. Chem. 279 43092-43097.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43092-43097
    • Han, Z.1    Harty, R.N.2
  • 28
    • 0032710383 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP2 protein: role in cell entry
    • S.H. Hassan and P. Roy (1999) Expression and functional characterization of bluetongue virus VP2 protein: role in cell entry. J. Virol. 73 9832-9842.
    • (1999) J. Virol. , vol.73 , pp. 9832-9842
    • Hassan, S.H.1    Roy, P.2
  • 29
    • 0034892675 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP5 protein: role in cellular permeabilization
    • S.H. Hassan, C. Wirblich, M. Forzan and P. Roy (2001) Expression and functional characterization of bluetongue virus VP5 protein: role in cellular permeabilization. J. Virol. 75 8356-8367.
    • (2001) J. Virol. , vol.75 , pp. 8356-8367
    • Hassan, S.H.1    Wirblich, C.2    Forzan, M.3    Roy, P.4
  • 30
    • 0027008546 scopus 로고
    • Structure of bluetongue virus particles by cryoelectron microscopy
    • E.A. Hewat, T.F. Booth and P. Roy (1992) Structure of bluetongue virus particles by cryoelectron microscopy. J. Struct. Biol. 109 61-69.
    • (1992) J. Struct. Biol. , vol.109 , pp. 61-69
    • Hewat, E.A.1    Booth, T.F.2    Roy, P.3
  • 31
    • 0018393054 scopus 로고
    • Characterization of the tubules associated with the replication of three different orbiviruses
    • H. Huismans and H.J. Els (1979) Characterization of the tubules associated with the replication of three different orbiviruses. Virology 92 397-406.
    • (1979) Virology , vol.92 , pp. 397-406
    • Huismans, H.1    Els, H.J.2
  • 32
    • 0019579977 scopus 로고
    • Identification of the serotype-specific and group-specific antigens of bluetongue virus
    • H. Huismans and B.J. Erasmus (1981) Identification of the serotype-specific and group-specific antigens of bluetongue virus. Onderstepoort J. Vet. Res. 48 51-58.
    • (1981) Onderstepoort J. Vet. Res. , vol.48 , pp. 51-58
    • Huismans, H.1    Erasmus, B.J.2
  • 33
    • 0024450255 scopus 로고
    • The release of bluetongue virus from infected cells and their superinfection by progeny virus
    • A.D. Hyatt, B.T. Eaton and S.M. Brookes (1989) The release of bluetongue virus from infected cells and their superinfection by progeny virus. Virology 173 21-34.
    • (1989) Virology , vol.173 , pp. 21-34
    • Hyatt, A.D.1    Eaton, B.T.2    Brookes, S.M.3
  • 34
    • 0025775558 scopus 로고
    • Localization of the non-structural protein NS3 in bluetongue virus-infected cells
    • A.D. Hyatt, A.R. Gould, B. Coupar and B.T. Eaton (1991) Localization of the non-structural protein NS3 in bluetongue virus-infected cells. J. Gen. Virol. 72 2263-2267.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2263-2267
    • Hyatt, A.D.1    Gould, A.R.2    Coupar, B.3    Eaton, B.T.4
  • 35
    • 0027193489 scopus 로고
    • Release of bluetongue virus-like particles from insect cells is mediated by BTV nonstructural protein NS3/NS3A
    • A.D. Hyatt, Y. Zhao and P. Roy (1993) Release of bluetongue virus-like particles from insect cells is mediated by BTV nonstructural protein NS3/NS3A. Virology 193 592-603.
    • (1993) Virology , vol.193 , pp. 592-603
    • Hyatt, A.D.1    Zhao, Y.2    Roy, P.3
  • 36
    • 0021060414 scopus 로고
    • Molecular basis of bluetongue virus neutralization
    • J. Kahlon, K. Sugiyama and P. Roy (1983) Molecular basis of bluetongue virus neutralization. J. Virol. 48 627-632.
    • (1983) J. Virol. , vol.48 , pp. 627-632
    • Kahlon, J.1    Sugiyama, K.2    Roy, P.3
  • 37
    • 33846925536 scopus 로고    scopus 로고
    • Bluetongue virus RNA binding protein NS2 is a modulator of viral replication and assembly
    • A.K. Kar, B. Bhattacharya and P. Roy (2007) Bluetongue virus RNA binding protein NS2 is a modulator of viral replication and assembly. BMC Mol. Biol. 8 4.
    • (2007) BMC Mol. Biol. , vol.8 , pp. 4
    • Kar, A.K.1    Bhattacharya, B.2    Roy, P.3
  • 38
    • 2942709880 scopus 로고    scopus 로고
    • Mapping the assembly of bluetongue virus scaffolding protein VP3
    • A.K. Kar, M. Ghosh and P. Roy (2004) Mapping the assembly of bluetongue virus scaffolding protein VP3. Virology 324 387-399.
    • (2004) Virology , vol.324 , pp. 387-399
    • Kar, A.K.1    Ghosh, M.2    Roy, P.3
  • 39
    • 0142060906 scopus 로고    scopus 로고
    • Defining the structure-function relationships of bluetongue virus helicase protein VP6
    • A.K. Kar and P. Roy (2003) Defining the structure-function relationships of bluetongue virus helicase protein VP6. J. Virol. 77 11347-11356.
    • (2003) J. Virol. , vol.77 , pp. 11347-11356
    • Kar, A.K.1    Roy, P.2
  • 40
    • 0022980090 scopus 로고
    • Nucleotide sequence of a cDNA clone of RNA segment 10 of bluetongue virus (serotype 10)
    • J.W. Lee and P. Roy (1986) Nucleotide sequence of a cDNA clone of RNA segment 10 of bluetongue virus (serotype 10). J. Gen. Virol. 67 2833-2837.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2833-2837
    • Lee, J.W.1    Roy, P.2
  • 41
    • 0141453603 scopus 로고    scopus 로고
    • Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch
    • C.K. Limn and P. Roy (2003) Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch. J. Virol. 77 1111-1124.
    • (2003) J. Virol. , vol.77 , pp. 1111-1124
    • Limn, C.K.1    Roy, P.2
  • 42
    • 0033851585 scopus 로고    scopus 로고
    • Functional dissection of the major structural protein of bluetongue virus: identification of key residues within VP7 essential for capsid assembly
    • C.H. Limn, N. Staeuber, K. Monastyrskaya, P. Gouet and P. Roy (2000) Functional dissection of the major structural protein of bluetongue virus: identification of key residues within VP7 essential for capsid assembly. J. Virol. 74 8658-8669.
    • (2000) J. Virol. , vol.74 , pp. 8658-8669
    • Limn, C.H.1    Staeuber, N.2    Monastyrskaya, K.3    Gouet, P.4    Roy, P.5
  • 43
    • 0026785734 scopus 로고
    • Interaction of nucleic acids with core-like and subcore-like particles of bluetongue virus
    • P.T. Loudon and P. Roy (1992) Interaction of nucleic acids with core-like and subcore-like particles of bluetongue virus. Virology 191 231-236.
    • (1992) Virology , vol.191 , pp. 231-236
    • Loudon, P.T.1    Roy, P.2
  • 44
    • 33747889837 scopus 로고    scopus 로고
    • Specific binding of bluetongue virus NS2 to different viral plus-strand RNAs
    • K. Lymperopoulos, R. Noad, S. Tosi, S. Nethisinghe, I. Brierley and P. Roy (2006) Specific binding of bluetongue virus NS2 to different viral plus-strand RNAs. Virology 353 17-26.
    • (2006) Virology , vol.353 , pp. 17-26
    • Lymperopoulos, K.1    Noad, R.2    Tosi, S.3    Nethisinghe, S.4    Brierley, I.5    Roy, P.6
  • 45
    • 0041355333 scopus 로고    scopus 로고
    • Sequence specificity in the interaction of bluetongue virus non-structural protein 2 (NS2) with viral RNA
    • K. Lymperopoulos, C. Wirblich, I. Brierley and P. Roy (2003) Sequence specificity in the interaction of bluetongue virus non-structural protein 2 (NS2) with viral RNA. J. Biol. Chem. 278 31722-31730.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31722-31730
    • Lymperopoulos, K.1    Wirblich, C.2    Brierley, I.3    Roy, P.4
  • 46
    • 8444227378 scopus 로고    scopus 로고
    • Segment specific inverted repeat sequences in bluetongue virus mRNA are required for interaction with the virus non structural protein NS2
    • W. Markotter, J. Theron and L.H. Nel (2004) Segment specific inverted repeat sequences in bluetongue virus mRNA are required for interaction with the virus non structural protein NS2. Virus Res. 105 1-9.
    • (2004) Virus Res. , vol.105 , pp. 1-9
    • Markotter, W.1    Theron, J.2    Nel, L.H.3
  • 47
    • 0032584782 scopus 로고    scopus 로고
    • 0-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus
    • J. Martinez Costas, G. Sutton, N. Ramadevi and P. Roy (1998) Guanylyltransferase and RNA 50-triphosphatase activities of the purified expressed VP4 protein of bluetongue virus. J. Mol. Biol. 280 859-866.
    • (1998) J. Mol. Biol. , vol.280 , pp. 859-866
    • Martinez Costas, J.1    Sutton, G.2    Ramadevi, N.3    Roy, P.4
  • 48
    • 0023145305 scopus 로고
    • Purification and properties of virus particles, infectious subviral particles, and cores of bluetongue virus serotypes 1 and 4
    • P.P. Mertens, J.N. Burroughs and J. Anderson (1987) Purification and properties of virus particles, infectious subviral particles, and cores of bluetongue virus serotypes 1 and 4. Virology 157 375-386.
    • (1987) Virology , vol.157 , pp. 375-386
    • Mertens, P.P.1    Burroughs, J.N.2    Anderson, J.3
  • 49
    • 34250779119 scopus 로고    scopus 로고
    • Orbivirus, Reoviridae
    • C.M. Fauquet, M.A. Mayo, J. Maniloff, U. Desselberger, L.A. Ball (Eds), London: Elsevier/Acadamic Press
    • P.P.C. Mertens, S. Maan, A. Samuel and H. Attoui (2005) Orbivirus, Reoviridae. C.M. Fauquet, M.A. Mayo, J. Maniloff, U. Desselberger, L.A. Ball (Eds) Virus Taxonomy, VIIIth Report of the ICTV London: Elsevier/Acadamic Press 466-483.
    • (2005) Virus Taxonomy, VIIIth Report of the ICTV , pp. 466-483
    • Mertens, P.P.C.1    Maan, S.2    Samuel, A.3    Attoui, H.4
  • 51
    • 22544470304 scopus 로고    scopus 로고
    • Phosphorylation of bluetongue virus nonstructural protein 2 is essential for formation of viral inclusion bodies
    • J. Modrof, K. Lymperopoulos and P. Roy (2005) Phosphorylation of bluetongue virus nonstructural protein 2 is essential for formation of viral inclusion bodies. J. Virol. 79 10023-10031.
    • (2005) J. Virol. , vol.79 , pp. 10023-10031
    • Modrof, J.1    Lymperopoulos, K.2    Roy, P.3
  • 54
    • 2642540746 scopus 로고    scopus 로고
    • Role of an arbovirus nonstructural protein in cellular pathogenesis and virus release
    • R. Owens and P. Roy (2004) Role of an arbovirus nonstructural protein in cellular pathogenesis and virus release. J. Virol. 78 6649-6656.
    • (2004) J. Virol. , vol.78 , pp. 6649-6656
    • Owens, R.1    Roy, P.2
  • 55
    • 0029843594 scopus 로고    scopus 로고
    • 0 end of viral mRNA, but the interaction is not sufficient to initiate minus-strand synthesis
    • J.T. Patton (1996) Rotavirus VP1 alone specifically binds to the 30 end of viral mRNA, but the interaction is not sufficient to initiate minus-strand synthesis. J. Virol. 70 7940-7947.
    • (1996) J. Virol. , vol.70 , pp. 7940-7947
    • Patton, J.T.1
  • 56
    • 0030831560 scopus 로고    scopus 로고
    • Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome
    • J.T. Patton, M.T. Jones, A.N. Kalbach, Y.W. He and J. Xiaobo (1997) Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome. J. Virol. 71 9618-9626.
    • (1997) J. Virol. , vol.71 , pp. 9618-9626
    • Patton, J.T.1    Jones, M.T.2    Kalbach, A.N.3    He, Y.W.4    Xiaobo, J.5
  • 57
    • 0027285762 scopus 로고
    • 0 end consensus sequence of viral mRNAs in infected cells
    • D. Poncet, C. Aponte and J. Cohen (1993) Rotavirus protein NSP3 (NS34) is bound to the 30 end consensus sequence of viral mRNAs in infected cells. J. Virol. 67 3159-3165.
    • (1993) J. Virol. , vol.67 , pp. 3159-3165
    • Poncet, D.1    Aponte, C.2    Cohen, J.3
  • 59
    • 0031689350 scopus 로고    scopus 로고
    • Bluetongue virus core protein VP4 has nucleoside triphosphate phosphohydrolase activity
    • N. Ramadevi and P. Roy (1998) Bluetongue virus core protein VP4 has nucleoside triphosphate phosphohydrolase activity. J. Gen. Virol. 79 2475-2480.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2475-2480
    • Ramadevi, N.1    Roy, P.2
  • 60
    • 0028324464 scopus 로고
    • Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • P. Raynal and H.B. Pollard (1994) Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta. 1197 63-93.
    • (1994) Biochim. Biophys. Acta. , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 61
    • 0027087184 scopus 로고
    • Bluetongue virus proteins
    • P. Roy (1992) Bluetongue virus proteins. J. Gen. Virol. 73 3051-3064.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3051-3064
    • Roy, P.1
  • 62
    • 50949126281 scopus 로고    scopus 로고
    • Bluetongue virus proteins and their role in virus entry, assembly and release
    • P. Roy (Eds), USA: Elsevier Academic Press, USA: Elsevier Academic Press.
    • P. Roy (2005) Bluetongue virus proteins and their role in virus entry, assembly and release. P. Roy (Eds) Virus Structure and Assembly USA: Elsevier Academic Press USA: Elsevier Academic Press.
    • (2005) Virus Structure and Assembly
    • Roy, P.1
  • 63
    • 0025347649 scopus 로고
    • Structure of the bluetongue virus genome and its encoded proteins
    • P. Roy, J.J. Marshall and T.J. French (1990) Structure of the bluetongue virus genome and its encoded proteins. Curr. Top. Microbiol. Immunol. 162 43-87.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.162 , pp. 43-87
    • Roy, P.1    Marshall, J.J.2    French, T.J.3
  • 64
    • 1842329184 scopus 로고    scopus 로고
    • Blue-tongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates
    • N. Stauber, J. Martinez-Costas, G. Sutton, K. Monastyrskaya and P. Roy (1997) Blue-tongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates. J. Virol. 71 7220-7226.
    • (1997) J. Virol. , vol.71 , pp. 7220-7226
    • Stauber, N.1    Martinez-Costas, J.2    Sutton, G.3    Monastyrskaya, K.4    Roy, P.5
  • 66
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-structural studies of reovirus polymerase lambda3
    • Y. Tao, D.L. Farsetta, M.L. Nibert and S.C. Harrison (2002) RNA synthesis in a cage-structural studies of reovirus polymerase lambda3. Cell 111 733-745.
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 67
    • 0031550798 scopus 로고    scopus 로고
    • Stable protein-RNA interaction involves the terminal domains of bluetongue virus mRNA, but not the terminally conserved sequences
    • J. Theron and L.H. Nel (1997) Stable protein-RNA interaction involves the terminal domains of bluetongue virus mRNA, but not the terminally conserved sequences. Virology 229 134-142.
    • (1997) Virology , vol.229 , pp. 134-142
    • Theron, J.1    Nel, L.H.2
  • 68
    • 0025144003 scopus 로고
    • Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: it binds the single-stranded RNA species
    • C.P. Thomas, T.F. Booth and P. Roy (1990) Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: it binds the single-stranded RNA species. J. Gen. Virol. 71 2073-2083.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2073-2083
    • Thomas, C.P.1    Booth, T.F.2    Roy, P.3
  • 69
    • 0025732463 scopus 로고
    • A comparison of the genes which encode non-structural protein NS3 of different orbiviruses
    • V. van Staden and H. Huismans (1991) A comparison of the genes which encode non-structural protein NS3 of different orbiviruses. J. Gen. Virol. 72 1073-1079.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1073-1079
    • van Staden, V.1    Huismans, H.2
  • 70
    • 0029108557 scopus 로고
    • Expression of nonstructural protein NS3 of African horse sickness virus (AHSV): evidence for a cytotoxic effect of NS3 in insect cells, and characterization of the gene products in AHSV infected vero cells
    • V. van Staden, M.A. Stoltz and H. Huismans (1995) Expression of nonstructural protein NS3 of African horse sickness virus (AHSV): evidence for a cytotoxic effect of NS3 in insect cells, and characterization of the gene products in AHSV infected vero cells. Arch. Virol. 140 289-306.
    • (1995) Arch. Virol. , vol.140 , pp. 289-306
    • van Staden, V.1    Stoltz, M.A.2    Huismans, H.3
  • 72
    • 0014525402 scopus 로고
    • Purification and characterization of bluetongue virus
    • D.W. Verwoerd (1969) Purification and characterization of bluetongue virus. Virology 38 203-212.
    • (1969) Virology , vol.38 , pp. 203-212
    • Verwoerd, D.W.1
  • 74
    • 0015456790 scopus 로고
    • Studies on the in vitro and the in vivo transcription of the bluetongue virus genome
    • D.W. Verwoerd and H. Huismans (1972) Studies on the in vitro and the in vivo transcription of the bluetongue virus genome. Onderstepoort J. Vet. Res. 39 185-191.
    • (1972) Onderstepoort J. Vet. Res. , vol.39 , pp. 185-191
    • Verwoerd, D.W.1    Huismans, H.2
  • 75
    • 0014720914 scopus 로고
    • Characterization of bluetongue virus ribonucleic acid
    • D.W. Verwoerd, H. Louw and R.A. Oellermann (1970) Characterization of bluetongue virus ribonucleic acid. J. Virol. 5 1-7.
    • (1970) J. Virol. , vol.5 , pp. 1-7
    • Verwoerd, D.W.1    Louw, H.2    Oellermann, R.A.3
  • 76
    • 34248187983 scopus 로고    scopus 로고
    • Reconstitution of bluetongue virus polymerase activity from isolated domains based on a three-dimensional structural model
    • J.M. Wehrfritz, M. Boyce, S. Mirza and P. Roy (2007) Reconstitution of bluetongue virus polymerase activity from isolated domains based on a three-dimensional structural model. Biopolymers 86 83-94.
    • (2007) Biopolymers , vol.86 , pp. 83-94
    • Wehrfritz, J.M.1    Boyce, M.2    Mirza, S.3    Roy, P.4
  • 77
    • 33645991207 scopus 로고    scopus 로고
    • Nonstructural protein 3 of blue-tongue virus assists virus release by recruiting the ESCRT-I protein Tsg101
    • C. Wirblich, B. Bhattacharya and P. Roy (2006) Nonstructural protein 3 of blue-tongue virus assists virus release by recruiting the ESCRT-I protein Tsg101. J. Virol. 86 460-473.
    • (2006) J. Virol. , vol.86 , pp. 460-473
    • Wirblich, C.1    Bhattacharya, B.2    Roy, P.3
  • 78
    • 0026475758 scopus 로고
    • Multiple glycoproteins synthesized by the smallest RNA segment (S10) of bluetongue virus
    • X. Wu, S.Y. Chen, H. Iwata, R.W. Compans and P. Roy (1992) Multiple glycoproteins synthesized by the smallest RNA segment (S10) of bluetongue virus. J. Virol. 66 7104-7112.
    • (1992) J. Virol. , vol.66 , pp. 7104-7112
    • Wu, X.1    Chen, S.Y.2    Iwata, H.3    Compans, R.W.4    Roy, P.5
  • 79
    • 0035451226 scopus 로고    scopus 로고
    • A conserved helix-unfolding motif in the naturally unfolded proteins
    • C.R. Zetina (2001) A conserved helix-unfolding motif in the naturally unfolded proteins. Proteins 44 479-483.
    • (2001) Proteins , vol.44 , pp. 479-483
    • Zetina, C.R.1
  • 80
    • 0028265174 scopus 로고
    • Deletion and mutational analyses of bluetongue virus NS2 protein indicate that the amino but not the carboxy terminus of the protein is critical for RNA-protein interactions
    • Y. Zhao, C. Thomas, C. Bremer and P. Roy (1994) Deletion and mutational analyses of bluetongue virus NS2 protein indicate that the amino but not the carboxy terminus of the protein is critical for RNA-protein interactions. J. Virol. 68 2179-2185.
    • (1994) J. Virol. , vol.68 , pp. 2179-2185
    • Zhao, Y.1    Thomas, C.2    Bremer, C.3    Roy, P.4


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