메뉴 건너뛰기




Volumn 726, Issue , 2012, Pages 379-402

Assembly of large icosahedral double-stranded RNA viruses

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DNA POLYMERASE; DOUBLE STRANDED RNA; HELICASE; PENTAMER; POLYMER; PROTEIN P7; PROTEIN T13; PROTEIN T2; RNA CAPPING ENZYME; RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS PROTEIN;

EID: 84858221251     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-0980-9_17     Document Type: Article
Times cited : (41)

References (181)
  • 2
    • 0038730770 scopus 로고    scopus 로고
    • Do viruses form lineages across different domains of life?
    • DOI 10.1016/S0923-2508(03)00065-2
    • Bamford DH (2003) Do viruses form lineages across different domains of life? Res Microbiol 154:231-236 (Pubitemid 36645268)
    • (2003) Research in Microbiology , vol.154 , Issue.4 , pp. 231-236
    • Bamford, D.H.1
  • 3
    • 0019166535 scopus 로고
    • Electron microscopy of cells infected with nonsense mutants of bacteriophate φ6
    • DOI 10.1016/0042-6822(80)90287-1
    • Bamford DH, Mindich L (1980) Electron microscopy of cells infected with nonsense mutants of bacteriophage j 6. Virology 107:222-228 (Pubitemid 11226530)
    • (1980) Virology , vol.107 , Issue.1 , pp. 222-228
    • Bamford, D.H.1    Mindich, L.2
  • 4
    • 0023337259 scopus 로고
    • Membrane fusion in prokaryotes: Bacteriophage j 6 membrane fuses with the Pseudomonas syringae outer membrane
    • Bamford DH, Romantschuk M, Somerharju PJ (1987) Membrane fusion in prokaryotes: bacteriophage j 6 membrane fuses with the Pseudomonas syringae outer membrane. EMBO J 6:1467-1473
    • (1987) EMBO J , vol.6 , pp. 1467-1473
    • Bamford, D.H.1    Romantschuk, M.2    Somerharju, P.J.3
  • 5
    • 0027233089 scopus 로고
    • Structural studies of the enveloped dsRNA bacteriophage ∅6 of Pseudomonas syringae by Raman spectroscopy. II. Nucleocapsid structure and thermostability of the virion, nucleocapsid and polymerase complex
    • DOI 10.1006/jmbi.1993.1164
    • Bamford JK, Bamford DH, Li T, Thomas GJ Jr (1993) Structural studies of the enveloped dsRNA bacteriophage j 6 of Pseudomonas syringae by Raman spectroscopy. II. Nucleocapsid structure and thermostability of the virion, nucleocapsid and polymerase complex. J Mol Biol 230:473-482 (Pubitemid 23161357)
    • (1993) Journal of Molecular Biology , vol.230 , Issue.2 , pp. 473-482
    • Bamford, J.K.H.1    Bamford, D.H.2    Li, T.3    Thomas Jr., G.J.4
  • 6
    • 0014812498 scopus 로고
    • Transcription in vitro by reovirus-associated ribonucleic acid-dependent polymerase
    • Banerjee AK, Shatkin AJ (1970) Transcription in vitro by reovirus-associated ribonucleic acid-dependent polymerase. J Virol 6:1-11
    • (1970) J Virol , vol.6 , pp. 1-11
    • Banerjee, A.K.1    Shatkin, A.J.2
  • 7
    • 0026714394 scopus 로고
    • Preliminary crystallographic study of bluetongue virus capsid protein, VP7
    • DOI 10.1016/0022-2836(92)90850-J
    • Basak AK, Stuart DI, Roy P (1992) Preliminary crystallographic study of bluetongue virus capsid protein, VP7. J Mol Biol 228:687-689 (Pubitemid 23007584)
    • (1992) Journal of Molecular Biology , vol.228 , Issue.2 , pp. 687-689
    • Basak, A.K.1    Stuart, D.I.2    Roy, P.3
  • 8
    • 0037695004 scopus 로고    scopus 로고
    • Reovirus σNS and μNS proteins form cytoplasmic inclusion structures in the absence of viral infection
    • DOI 10.1128/JVI.77.10.5948-5963.2003
    • Becker MM, Peters TR, Dermody TS (2003) Reovirus s NS and m NS proteins form cytoplasmic inclusion structures in the absence of viral infection. J Virol 77:5948-5963 (Pubitemid 36538986)
    • (2003) Journal of Virology , vol.77 , Issue.10 , pp. 5948-5963
    • Becker, M.M.1    Peters, T.R.2    Dermody, T.S.3
  • 9
    • 0037044331 scopus 로고    scopus 로고
    • Characterization of subunit-specifi c interactions in a double-stranded RNA virus: Raman difference spectroscopy of the j 6 procapsid
    • Benevides JM, Juuti JT, Tuma R, Bamford DH, Thomas GJ Jr (2002) Characterization of subunit-specifi c interactions in a double-stranded RNA virus: Raman difference spectroscopy of the j 6 procapsid. Biochemistry 41:11946-11953
    • (2002) Biochemistry , vol.41 , pp. 11946-11953
    • Benevides, J.M.1    Juuti, J.T.2    Tuma, R.3    Bamford, D.H.4    Thomas, Jr.G.J.5
  • 10
    • 0037301362 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP5 interacts with major core protein VP2
    • DOI 10.1128/JVI.77.3.1757-1763.2003
    • Berois M, Sapin C, Erk I, Poncet D, Cohen J (2003) Rotavirus nonstructural protein NSP5 interacts with major core protein VP2. J Virol 77:1757-1763 (Pubitemid 36109987)
    • (2003) Journal of Virology , vol.77 , Issue.3 , pp. 1757-1763
    • Berois, M.1    Sapin, C.2    Erk, I.3    Poncet, D.4    Cohen, J.5
  • 11
    • 0019920358 scopus 로고
    • Purification and characterization of bovine rotavirus cores
    • Bican P, Cohen J, Charpilienne A, Scherrer R (1982) Purifi cation and characterization of bovine rotavirus cores. J Virol 43:1113-1117 (Pubitemid 12057970)
    • (1982) Journal of Virology , vol.43 , Issue.3 , pp. 1113-1117
    • Bican, P.1    Cohen, J.2    Charpilienne, A.3    Scherrer, R.4
  • 12
    • 0030800967 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus λ1 protein
    • DOI 10.1074/jbc.272.29.18298
    • Bisaillon M, Bergeron J, Lemay G (1997) Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus l 1 protein. J Biol Chem 272:18298-18303 (Pubitemid 27306420)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18298-18303
    • Bisaillon, M.1    Bergeron, J.2    Lemay, G.3
  • 14
    • 0027420113 scopus 로고
    • Characterization of virus inclusion bodies in bluetongue virus-infected cells
    • Brookes SM, Hyatt AD, Eaton BT (1993) Characterization of virus inclusion bodies in bluetongue virus-infected cells. J Gen Virol 74:525-530 (Pubitemid 23092909)
    • (1993) Journal of General Virology , vol.74 , Issue.3 , pp. 525-530
    • Brookes, S.M.1    Hyatt, A.D.2    Eaton, B.T.3
  • 15
    • 0027992057 scopus 로고
    • Purification and properties of virus particles, infectious subviral particles, cores and VP7 crystals of African horsesickness virus serotype 9
    • Burroughs JN, O'Hara RS, Smale CJ, Hamblin C, Walton A, Armstrong R, Mertens PP (1994) Purifi cation and properties of virus particles, infectious subviral particles, cores and VP7 crystals of African horsesickness virus serotype 9. J Gen Virol 75:1849-1857 (Pubitemid 24243063)
    • (1994) Journal of General Virology , vol.75 , Issue.8 , pp. 1849-1857
    • Burroughs, J.N.1    O'Hara, R.S.2    Smale, C.J.3    Hamblin, C.4    Walton, A.5    Armstrong, R.6    Mertens, P.P.C.7
  • 16
    • 77954218124 scopus 로고    scopus 로고
    • Insights into the role of the non-structural protein 2 (NS2) in Bluetongue virus morphogenesis
    • Butan C, Tucker P (2010) Insights into the role of the non-structural protein 2 (NS2) in Bluetongue virus morphogenesis. Virus Res 151:109-117
    • (2010) Virus Res , vol.151 , pp. 109-117
    • Butan, C.1    Tucker, P.2
  • 17
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double-stranded RNA virus φ6
    • DOI 10.1093/emboj/16.14.4477
    • Butcher SJ, Dokland T, Ojala PM, Bamford DH, Fuller SD (1997) Intermediates in the assembly pathway of the double-stranded RNA virus j 6. EMBO J 16:4477-4487 (Pubitemid 27298201)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4477-4487
    • Butcher, S.J.1    Dokland, T.2    Ojala, P.M.3    Bamford, D.H.4    Fuller, S.D.5
  • 18
    • 0035826258 scopus 로고    scopus 로고
    • A mechanism for initiating RNA-dependent RNA polymerization
    • DOI 10.1038/35065653
    • Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI (2001) A mechanism for initiating RNA-dependent RNA polymerization. Nature 410:235-240 (Pubitemid 32216599)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 235-240
    • Butcher, S.J.1    Grimes, J.M.2    Makeyev, E.V.3    Bamford, D.H.4    Stuart, D.I.5
  • 19
    • 0026043642 scopus 로고
    • Characterization of the VPg-dsRNA linkage of infectious pancreatic necrosis virus
    • Calvert JG, Nagy E, Soler M, Dobos P (1991) Characterization of the VPg-dsRNA linkage of infectious pancreatic necrosis virus. J Gen Virol 72:2563-2567
    • (1991) J Gen Virol , vol.72 , pp. 2563-2567
    • Calvert, J.G.1    Nagy, E.2    Soler, M.3    Dobos, P.4
  • 20
    • 74849086825 scopus 로고    scopus 로고
    • Ratification vote on taxonomic proposals to the international committee on taxonomy of viruses 2009
    • Carstens EB (2010) Ratifi cation vote on taxonomic proposals to the International Committee on Taxonomy of Viruses (2009). Arch Virol 155:133-146
    • (2010) Arch Virol , vol.155 , pp. 133-146
    • Carstens, E.B.1
  • 21
    • 0042850598 scopus 로고    scopus 로고
    • Three-dimensional structure of Penicillium chrysogenum virus: A double-stranded RNA virus with a genuine T=1 capsid
    • DOI 10.1016/S0022-2836(03)00695-8
    • Caston JR, Ghabrial SA, Jiang D, Rivas G, Alfonso C, Roca R, Luque D, Carrascosa JL (2003) Three-dimensional structure of Penicillium chrysogenum virus: a double-stranded RNA virus with a genuine T = 1 capsid. J Mol Biol 331:417-431 (Pubitemid 36904026)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.2 , pp. 417-431
    • Caston, J.R.1    Ghabrial, S.A.2    Jiang, D.3    Rivas, G.4    Alfonso, C.5    Roca, R.6    Luque, D.7    Carrascosa, J.L.8
  • 22
    • 0030666069 scopus 로고    scopus 로고
    • Picobirnavirus, a novel group of undescribed viruses of mammals and birds: A minireview
    • Chandra R (1997) Picobirnavirus, a novel group of undescribed viruses of mammals and birds: a minireview. Acta Virol 41:59-62 (Pubitemid 27463617)
    • (1997) Acta Virologica , vol.41 , Issue.1 , pp. 59-62
    • Chandra, R.1
  • 24
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber
    • DOI 10.1093/emboj/21.1.1
    • Chappell JD, Prota AE, Dermody TS, Stehle T (2002) Crystal structure of reovirus attachment protein s 1 reveals evolutionary relationship to adenovirus fiber. EMBO J 21:1-11 (Pubitemid 34087069)
    • (2002) EMBO Journal , vol.21 , Issue.1-2 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 25
    • 0036317769 scopus 로고    scopus 로고
    • Identification of rotavirus VP6 residues located at the interface with VP2 that are essential for capsid assembly and transcriptase activity
    • DOI 10.1128/JVI.76.15.7822-7831.2002
    • Charpilienne A, Lepault J, Rey F, Cohen J (2002) Identification of rotavirus VP6 residues located at the interface with VP2 that are essential for capsid assembly and transcriptase activity. J Virol 76:7822-7831 (Pubitemid 34761004)
    • (2002) Journal of Virology , vol.76 , Issue.15 , pp. 7822-7831
    • Charpilienne, A.1    Lepault, J.2    Rey, F.3    Cohen, J.4
  • 26
    • 0033527897 scopus 로고    scopus 로고
    • Rotavirus open cores catalyze 5'-capping and methylation of exogenous RNA: Evidence that VP3 is a methyltransferase
    • DOI 10.1006/viro.1999.0029
    • Chen D, Luongo CL, Nibert ML, Patton JT (1999) Rotavirus open cores catalyze 5 ¢ -capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase. Virology 265:120-130 (Pubitemid 30012391)
    • (1999) Virology , vol.265 , Issue.1 , pp. 120-130
    • Chen, D.1    Luongo, C.L.2    Nibert, M.L.3    Patton, J.T.4
  • 28
    • 77649336015 scopus 로고    scopus 로고
    • Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics
    • Cheng L, Zhu J, Hui WH, Zhang X, Honig B, Fang Q, Zhou ZH (2010) Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics. J Mol Biol 397:852-863
    • (2010) J Mol Biol , vol.397 , pp. 852-863
    • Cheng, L.1    Zhu, J.2    Hui, W.H.3    Zhang, X.4    Honig, B.5    Fang, Q.6    Zh, Z.7
  • 29
    • 0022478937 scopus 로고
    • Reovirus guanylyltransferase is L2 gene product lambda 2
    • Cleveland DR, Zarbl H, Millward S (1986) Reovirus guanylyltransferase is L2 gene product lambda 2. J Virol 60:307-311 (Pubitemid 16003176)
    • (1986) Journal of Virology , vol.60 , Issue.1 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 30
    • 0030000103 scopus 로고    scopus 로고
    • - reovirus temperature-sensitive mutant defective in minor core protein μ2
    • Coombs KM (1996) Identification and characterization of a double-stranded RNA reovirus temperature-sensitive mutant defective in minor core protein m 2. J Virol 70:4237-4245 (Pubitemid 26187424)
    • (1996) Journal of Virology , vol.70 , Issue.7 , pp. 4237-4245
    • Coombs, K.M.1
  • 31
    • 17644376907 scopus 로고    scopus 로고
    • The birnavirus crystal structure reveals structural relationships among icosahedral viruses
    • DOI 10.1016/j.cell.2005.01.009
    • Coulibaly F, Chevalier C, Gutsche I, Pous J, Navaza J, Bressanelli S, Delmas B, Rey FA (2005) The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell 120:761-772 (Pubitemid 40568795)
    • (2005) Cell , vol.120 , Issue.6 , pp. 761-772
    • Coulibaly, F.1    Chevalier, C.2    Gutsche, I.3    Pous, J.4    Navaza, J.5    Bressanelli, S.6    Delmas, B.7    Rey, F.A.8
  • 33
    • 75449090774 scopus 로고    scopus 로고
    • Crystal structure of an Aquabirnavirus particle: Insights into antigenic diversity and virulence determinism
    • Coulibaly F, Chevalier C, Delmas B, Rey FA (2010) Crystal structure of an Aquabirnavirus particle: insights into antigenic diversity and virulence determinism. J Virol 84:1792-1799
    • (2010) J Virol , vol.84 , pp. 1792-1799
    • Coulibaly, F.1    Chevalier, C.2    Delmas, B.3    Rey, F.A.4
  • 34
    • 77955292770 scopus 로고    scopus 로고
    • Phospholipids act as secondary receptor during the entry of the enveloped, double-stranded RNA bacteriophage phi6
    • Cvirkaite-Krupovic V, Poranen MM, Bamford DH (2010) Phospholipids act as secondary receptor during the entry of the enveloped, double-stranded RNA bacteriophage phi6. J Gen Virol 91:2116-2120
    • (2010) J Gen Virol , vol.91 , pp. 2116-2120
    • Cvirkaite-Krupovic, V.1    Poranen, M.M.2    Bamford, D.H.3
  • 35
    • 0033607480 scopus 로고    scopus 로고
    • A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage j 6
    • de Haas F, Paatero AO, Mindich L, Bamford DH, Fuller SD (1999) A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage j 6. J Mol Biol 294:357-372
    • (1999) J Mol Biol , vol.294 , pp. 357-372
    • De Haas, F.1    Paatero, A.O.2    Mindich, L.3    Bamford, D.H.4    Fuller, S.D.5
  • 38
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden KA, Wang G, Yeager M, Nibert ML, Coombs KM, Furlong DB, Fields BN, Baker TS (1993) Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J Cell Biol 122:1023-1041 (Pubitemid 23254171)
    • (1993) Journal of Cell Biology , vol.122 , Issue.5 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 39
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • DOI 10.1006/viro.1998.9146
    • Dryden KA, Farsetta DL, Wang G, Keegan JM, Fields BN, Baker TS, Nibert ML (1998) Internal/structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245:33-46 (Pubitemid 28384075)
    • (1998) Virology , vol.245 , Issue.1 , pp. 33-46
    • Dryden, K.A.1    Farsetta, D.L.2    Wang, G.3    Keegan, J.M.4    Fields, B.N.5    Baker, T.S.6    Nibert, M.L.7
  • 41
    • 0024059749 scopus 로고
    • In vitro replication and transcription of the segmented double-stranded RNA bacteriophage j 6
    • Ewen ME, Revel HR (1988) In vitro replication and transcription of the segmented double-stranded RNA bacteriophage j 6. Virology 165:489-498
    • (1988) Virology , vol.165 , pp. 489-498
    • Ewen, M.E.1    Revel, H.R.2
  • 42
    • 0025129528 scopus 로고
    • RNA-protein complexes responsible for replication and transcription of the double-stranded RNA bacteriophage ∅6
    • DOI 10.1016/0042-6822(90)90348-U
    • Ewen ME, Revel HR (1990) RNA-protein complexes responsible for replication and transcription of the doublestranded RNA bacteriophage j 6. Virology 178:509-519 (Pubitemid 20349888)
    • (1990) Virology , vol.178 , Issue.2 , pp. 509-519
    • Ewen, M.E.1    Revel, H.R.2
  • 43
    • 0032970118 scopus 로고    scopus 로고
    • Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo
    • Fabbretti E, Afrikanova I, Vascotto F, Burrone OR (1999) Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo . J Gen Virol 80:333-339 (Pubitemid 29095192)
    • (1999) Journal of General Virology , vol.80 , Issue.2 , pp. 333-339
    • Fabbretti, E.1    Afrikanova, I.2    Vascotto, F.3    Burrone, O.R.4
  • 44
    • 0025372616 scopus 로고
    • Molecular structure of the cell-attachment protein of reovirus: Correlation of computer-processed electron micrographs with sequence-based predictions
    • Fraser RD, Furlong DB, Trus BL, Nibert ML, Fields BN, Steven AC (1990) Molecular structure of the cell-attachment protein of reovirus: correlation of computer-processed electron micrographs with sequence-based predictions. J Virol 64:2990-3000 (Pubitemid 20171291)
    • (1990) Journal of Virology , vol.64 , Issue.6 , pp. 2990-3000
    • Fraser, R.D.B.1    Furlong, D.B.2    Trus, B.L.3    Nibert, M.L.4    Fields, B.N.5    Steven, A.C.6
  • 46
    • 0025215056 scopus 로고
    • Synthesis of bluetongue virus (BTV) corelike particles by a recombinant baculovirus expressing the two major structural core proteins of BTV
    • French TJ, Roy P (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 (Pubitemid 20104888)
    • (1990) Journal of Virology , vol.64 , Issue.4 , pp. 1530-1536
    • French, T.J.1    Roy, P.2
  • 47
    • 0028928032 scopus 로고
    • In vitro packaging of the single-stranded RNA genomic precursors of the segmented double-stranded RNA bacteriophage j 6: The three segments modulate each other's packaging effi ciency
    • Frilander M, Bamford DH (1995) In vitro packaging of the single-stranded RNA genomic precursors of the segmented double-stranded RNA bacteriophage j 6: the three segments modulate each other's packaging effi ciency. J Mol Biol 246:418-428
    • (1995) J Mol Biol , vol.246 , pp. 418-428
    • Frilander, M.1    Bamford, D.H.2
  • 48
    • 0026627864 scopus 로고
    • Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage j 6
    • Frilander M, Gottlieb P, Strassman J, Bamford DH, Mindich L (1992) Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage j 6. J Virol 66:5013-5017
    • (1992) J Virol , vol.66 , pp. 5013-5017
    • Frilander, M.1    Gottlieb, P.2    Strassman, J.3    Bamford, D.H.4    Mindich, L.5
  • 49
    • 0029330856 scopus 로고
    • The large genome segment of dsRNA bacteriophage j 6 is the key regulator in the in vitro minus and plus strand synthesis
    • Frilander M, Poranen M, Bamford DH (1995) The large genome segment of dsRNA bacteriophage j 6 is the key regulator in the in vitro minus and plus strand synthesis. RNA 1:510-518
    • (1995) RNA , vol.1 , pp. 510-518
    • Frilander, M.1    Poranen, M.2    Bamford, D.H.3
  • 50
    • 0022212617 scopus 로고
    • Biochemical evidence for the oligomeric (possibly trimeric) structure of the major inner capsid polypeptide (45K) of rotaviruses
    • Gorziglia M, Larrea C, Liprandi F, Esparza J (1985) Biochemical evidence for the oligomeric (possibly trimeric) structure of the major inner capsid polypeptide (45K) of rotaviruses. J Gen Virol 66:1889-1900 (Pubitemid 16251091)
    • (1985) Journal of General Virology , vol.66 , Issue.9 , pp. 1889-1900
    • Gorziglia, M.1    Larrea, C.2    Liprandi, F.3    Esparza, J.4
  • 51
    • 0023841702 scopus 로고
    • Nucleotide sequence of the middle dsRNA segment of bacteriophage φ6: Placement of the genes of membrane-associated proteins
    • DOI 10.1016/0042-6822(88)90245-0
    • Gottlieb P, Metzger S, Romantschuk M, Carton J, Strassman J, Bamford DH, Kalkkinen N, Mindich L (1988a) Nucleotide sequence of the middle dsRNA segment of bacteriophage j 6: placement of the genes of membraneassociated proteins. Virology 163:183-190 (Pubitemid 18088727)
    • (1988) Virology , vol.163 , Issue.1 , pp. 183-190
    • Gottlieb, P.1    Metzger, S.2    Romantschuk, M.3    Carton, J.4    Strassman, J.5    Bambord, D.H.6    Kalkkinen, N.7    Mindich, L.8
  • 52
    • 0023675432 scopus 로고
    • Production of a polyhedral particle in Escherichia coli from a cDNA copy of the large genomic segment of bacteriophage j 6
    • Gottlieb P, Strassman J, Bamford DH, Mindich L (1988b) Production of a polyhedral particle in Escherichia coli from a cDNA copy of the large genomic segment of bacteriophage j 6. J Virol 62:181-187
    • (1988) J Virol , vol.62 , pp. 181-187
    • Gottlieb, P.1    Strassman, J.2    Bamford, D.H.3    Mindich, L.4
  • 53
    • 0026560654 scopus 로고
    • In vitro packaging and replication of individual genomic segments of bacteriophage j 6 RNA
    • Gottlieb P, Strassman J, Qiao X, Frilander M, Frucht A, Mindich L (1992) In vitro packaging and replication of individual genomic segments of bacteriophage j 6 RNA. J Virol 66:2611-2616
    • (1992) J Virol , vol.66 , pp. 2611-2616
    • Gottlieb, P.1    Strassman, J.2    Qiao, X.3    Frilander, M.4    Frucht, A.5    Mindich, L.6
  • 54
    • 0028222195 scopus 로고
    • Identification of the packaging regions within the genomic RNA segments of bacteriophage Φ6
    • DOI 10.1006/viro.1994.1160
    • Gottlieb P, Qiao X, Strassman J, Frilander M, Mindich L (1994) Identification of the packaging regions within the genomic RNA segments of bacteriophage j 6. Virology 200:42-47 (Pubitemid 24170452)
    • (1994) Virology , vol.200 , Issue.1 , pp. 42-47
    • Gottlieb, P.1    Qiao, X.2    Strassman, J.3    Frilander, M.4    Mindich, L.5
  • 55
    • 0036349164 scopus 로고    scopus 로고
    • Characterization of j 12, a bacteriophage related to j 6: Nucleotide sequence of the small and middle double-stranded RNA
    • Gottlieb P, Wei H, Potgieter C, Toporovsky I (2002) Characterization of j 12, a bacteriophage related to j 6: nucleotide sequence of the small and middle double-stranded RNA. Virology 293:118-124
    • (2002) Virology , vol.293 , pp. 118-124
    • Gottlieb, P.1    Wei, H.2    Potgieter, C.3    Toporovsky, I.4
  • 56
    • 0033553535 scopus 로고    scopus 로고
    • The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography
    • DOI 10.1016/S0092-8674(00)80758-8
    • Gouet P, Diprose JM, Grimes JM, Malby R, Burroughs JN, Zientara S, Stuart DI, Mertens PP (1999) The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell 97:481-490 (Pubitemid 29231171)
    • (1999) Cell , vol.97 , Issue.4 , pp. 481-490
    • Gouet, P.1    Diprose, J.M.2    Grimes, J.M.3    Malby, R.4    Burroughs, J.N.5    Zientara, S.6    Stuart, D.I.7    Mertens, P.P.C.8
  • 57
    • 0028874050 scopus 로고
    • The crystal structure of bluetongue virus VP7
    • Grimes J, Basak AK, Roy P, Stuart D (1995) The crystal structure of bluetongue virus VP7. Nature 373:167-170
    • (1995) Nature , vol.373 , pp. 167-170
    • Grimes, J.1    Basak, A.K.2    Roy, P.3    Stuart, D.4
  • 59
    • 77953312059 scopus 로고    scopus 로고
    • Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome
    • Guglielmi KM, McDonald SM, Patton JT (2010) Mechanism of intraparticle synthesis of the rotavirus double-stranded RNA genome. J Biol Chem 285:18123-18128
    • (2010) J Biol Chem , vol.285 , pp. 18123-18128
    • Guglielmi, K.M.1    McDonald, S.M.2    Patton, J.T.3
  • 60
    • 0037384087 scopus 로고    scopus 로고
    • Assembly of single-shelled cores and double-shelled virus-like particles after baculovirus expression of major structural proteins P3, P7 and P8 of Rice dwarf virus
    • DOI 10.1099/vir.0.18904-0
    • Hagiwara K, Higashi T, Namba K, Uehara-Ichiki T, Omura T (2003) Assembly of single-shelled cores and doubleshelled virus-like particles after baculovirus expression of major structural proteins P3, P7 and P8 of Rice dwarf virus . J Gen Virol 84:981-984 (Pubitemid 36432230)
    • (2003) Journal of General Virology , vol.84 , Issue.4 , pp. 981-984
    • Hagiwara, K.1    Higashi, T.2    Namba, K.3    Uehara-Ichiki, T.4    Omura, T.5
  • 61
    • 0024059552 scopus 로고
    • Chemical crosslinking of bacteriophage j 6 nucleocapsid proteins
    • Hantula J, Bamford DH (1988) Chemical crosslinking of bacteriophage j 6 nucleocapsid proteins. Virology 165:482-488
    • (1988) Virology , vol.165 , pp. 482-488
    • Hantula, J.1    Bamford, D.H.2
  • 62
    • 0032710383 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP2 protein: Role in cell entry
    • Hassan SS, Roy P (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.S.1    Roy, P.2
  • 63
    • 0034892675 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP5 protein: Role in cellular permeabilization
    • DOI 10.1128/JVI.75.18.8356-8367.2001
    • Hassan SH, Wirblich C, Forzan M, Roy P (2001) Expression and functional characterization of bluetongue virus VP5 protein: role in cellular permeabilization. J Virol 75:8356-8367 (Pubitemid 32768940)
    • (2001) Journal of Virology , vol.75 , Issue.18 , pp. 8356-8367
    • Hassan, S.H.1    Wirblich, C.2    Forzan, M.3    Roy, P.4
  • 64
    • 0026719673 scopus 로고
    • Three-dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy
    • Hewat EA, Booth TF, Loudon PT, Roy P (1992) Three-dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy. Virology 189:10-20
    • (1992) Virology , vol.189 , pp. 10-20
    • Hewat, E.A.1    Booth, T.F.2    Loudon, P.T.3    Roy, P.4
  • 66
    • 0034690810 scopus 로고    scopus 로고
    • Characterization of Φ8, a bacteriophage containing three double- stranded RNA genomic segments and distantly related to Φ6
    • DOI 10.1006/viro.2000.0374
    • Hoogstraten D, Qiao X, Sun Y, Hu A, Onodera S, Mindich L (2000) Characterization of j 8, a bacteriophage containing three double-stranded RNA genomic segments and distantly related to j 6. Virology 272:218-224 (Pubitemid 30429445)
    • (2000) Virology , vol.272 , Issue.1 , pp. 218-224
    • Hoogstraten, D.1    Qiao, X.2    Sun, Y.3    Hu, A.4    Onodera, S.5    Mindich, L.6
  • 67
    • 0036297716 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of avian reovirus guanylyltransferase
    • DOI 10.1006/viro.2002.1427
    • Hsiao J, Martinez-Costas J, Benavente J, Vakharia VN (2002) Cloning, expression, and characterization of avian reovirus guanylyltransferase. Virology 296:288-299 (Pubitemid 34713268)
    • (2002) Virology , vol.296 , Issue.2 , pp. 288-299
    • Hsiao, J.1    Martinez-Costas, J.2    Benavente, J.3    Vakharia, V.N.4
  • 68
    • 33744821066 scopus 로고    scopus 로고
    • Structure of the Bacteriophage φ{symbol}6 Nucleocapsid Suggests a Mechanism for Sequential RNA Packaging
    • DOI 10.1016/j.str.2006.03.018, PII S096921260600219X
    • Huiskonen JT, de Haas F, Bubeck D, Bamford DH, Fuller SD, Butcher SJ (2006) Structure of the bacteriophage j 6 nucleocapsid suggests a mechanism for sequential RNA packaging. Structure 14:1039-1048 (Pubitemid 43831662)
    • (2006) Structure , vol.14 , Issue.6 , pp. 1039-1048
    • Huiskonen, J.T.1    De Haas, F.2    Bubeck, D.3    Bamford, D.H.4    Fuller, S.D.5    Butcher, S.J.6
  • 69
    • 34248171243 scopus 로고    scopus 로고
    • Structure of a hexameric RNA packaging motor in a viral polymerase complex
    • DOI 10.1016/j.jsb.2006.08.021, PII S1047847706003066, Structural Analysis of Supramolecular Assembles by Hybrid Methods
    • Huiskonen JT, Jaalinoja HT, Briggs JA, Fuller SD, Butcher SJ (2007) Structure of a hexameric RNA packaging motor in a viral polymerase complex. J Struct Biol 158:156-164 (Pubitemid 46719988)
    • (2007) Journal of Structural Biology , vol.158 , Issue.2 , pp. 156-164
    • Huiskonen, J.T.1    Jaalinoja, H.T.2    Briggs, J.A.G.3    Fuller, S.D.4    Butcher, S.J.5
  • 71
    • 33846785442 scopus 로고    scopus 로고
    • Electron Cryomicroscopy Comparison of the Architectures of the Enveloped Bacteriophages φ{symbol}6 and φ{symbol}8
    • DOI 10.1016/j.str.2006.12.004, PII S0969212607000263
    • Jaalinoja HT, Huiskonen JT, Butcher SJ (2007) Electron cryomicroscopy comparison of the architectures of the enveloped bacteriophages j 6 and j 8. Structure 15:157-167 (Pubitemid 46209812)
    • (2007) Structure , vol.15 , Issue.2 , pp. 157-167
    • Jaalinoja, H.T.1    Huiskonen, J.T.2    Butcher, S.J.3
  • 72
    • 0345196599 scopus 로고    scopus 로고
    • Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: An approach for analyzing σ3 functions during virus entry
    • Jane-Valbuena J, Nibert ML, Spencer SM, Walker SB, Baker TS, Chen Y, Centonze VE, Schiff LA (1999) Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed s 3 protein: an approach for analyzing s 3 functions during virus entry. J Virol 73:2963-2973 (Pubitemid 29135685)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 2963-2973
    • Jane-Valbuena, J.1    Nibert, M.L.2    Spencer, S.M.3    Walker, S.B.4    Baker, T.S.5    Chen, Y.6    Centonze, V.E.7    Schiff, L.A.8
  • 73
    • 0037118101 scopus 로고    scopus 로고
    • Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold
    • DOI 10.1038/417311a
    • Jayaram H, Taraporewala Z, Patton JT, Prasad BV (2002) Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold. Nature 417:311-315 (Pubitemid 34534716)
    • (2002) Nature , vol.417 , Issue.6886 , pp. 311-315
    • Jayaram, H.1    Taraporewala, Z.2    Patton, J.T.3    Prasad, B.V.V.4
  • 74
    • 0029060842 scopus 로고
    • RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage j 6
    • Juuti JT, Bamford DH (1995) RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage j 6. J Mol Biol 249:545-554
    • (1995) J Mol Biol , vol.249 , pp. 545-554
    • Juuti, J.T.1    Bamford, D.H.2
  • 75
    • 0031567131 scopus 로고    scopus 로고
    • Protein P7 of phage Φ6 RNA polymerase complex, acquiring of RNA packaging activity by in vitro assembly of the purified protein onto deficient particles
    • DOI 10.1006/jmbi.1996.0817
    • Juuti JT, Bamford DH (1997) Protein P7 of phage j 6 RNA polymerase complex, acquiring of RNA packaging activity by in vitro assembly of the purifi ed protein onto defi cient particles. J Mol Biol 266:891-900 (Pubitemid 27122596)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.5 , pp. 891-900
    • Juuti, J.T.1    Bamford, D.H.2
  • 76
    • 0032486109 scopus 로고    scopus 로고
    • Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage φ6
    • DOI 10.1006/jmbi.1998.1772
    • Juuti JT, Bamford DH, Tuma R, Thomas GJ Jr (1998) Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage j 6. J Mol Biol 279:347-359 (Pubitemid 28263975)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.2 , pp. 347-359
    • Juuti, J.T.1    Bamford, D.H.2    Tuma, R.3    Thomas Jr., G.J.4
  • 77
    • 0037427447 scopus 로고    scopus 로고
    • Conserved intermediates on the assembly pathway of double-stranded RNA bacteriophages
    • DOI 10.1016/S0022-2836(03)00322-X
    • Kainov DE, Butcher SJ, Bamford DH, Tuma R (2003a) Conserved intermediates on the assembly pathway of doublestranded RNA bacteriophages. J Mol Biol 328:791-804 (Pubitemid 36506887)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.4 , pp. 791-804
    • Kainov, D.E.1    Butcher, S.J.2    Bamford, D.H.3    Tuma, R.4
  • 79
    • 3142702664 scopus 로고    scopus 로고
    • Packaging motor from double-stranded RNA bacteriophage Φ12 acts as an obligatory passive conduit during transcription
    • DOI 10.1093/nar/gkh680
    • Kainov DE, Lisal J, Bamford DH, Tuma R (2004) Packaging motor from double-stranded RNA bacteriophage j 12 acts as an obligatory passive conduit during transcription. Nucleic Acids Res 32:3515-3521 (Pubitemid 39157701)
    • (2004) Nucleic Acids Research , vol.32 , Issue.12 , pp. 3515-3521
    • Kainov, D.E.1    Lisal, J.2    Bamford, D.H.3    Tuma, R.4
  • 80
    • 0142060906 scopus 로고    scopus 로고
    • Defining the structure-function relationships of bluetongue virus helicase protein VP6
    • DOI 10.1128/JVI.77.21.11347-11356.2003
    • Kar AK, Roy P (2003) Defi ning the structure-function relationships of bluetongue virus helicase protein VP6. J Virol 77:11347-11356 (Pubitemid 37271633)
    • (2003) Journal of Virology , vol.77 , Issue.21 , pp. 11347-11356
    • Kar, A.K.1    Roy, P.2
  • 81
    • 2942709880 scopus 로고    scopus 로고
    • Mapping the assembly pathway of Bluetongue virus scaffolding protein VP3
    • DOI 10.1016/j.virol.2004.04.018, PII S0042682204002594
    • Kar AK, Ghosh M, Roy P (2004) Mapping the assembly pathway of Bluetongue virus scaffolding protein VP3. Virology 324:387-399 (Pubitemid 38797855)
    • (2004) Virology , vol.324 , Issue.2 , pp. 387-399
    • Kar, A.K.1    Ghosh, M.2    Roy, P.3
  • 82
    • 0036889158 scopus 로고    scopus 로고
    • The hydrophilic amino-terminal arm of reovirus core shell protein λ1 is dispensable for particle assembly
    • DOI 10.1128/JVI.76.23.12211-12222.2002
    • Kim J, Zhang X, Centonze VE, Bowman VD, Noble S, Baker TS, Nibert ML (2002) The hydrophilic amino-terminal arm of reovirus core shell protein l 1 is dispensable for particle assembly. J Virol 76:12211-12222 (Pubitemid 35304318)
    • (2002) Journal of Virology , vol.76 , Issue.23 , pp. 12211-12222
    • Kim, J.1    Zhang, X.2    Centonze, V.E.3    Bowman, V.D.4    Noble, S.5    Baker, T.S.6    Nibert, M.L.7
  • 83
    • 1042289782 scopus 로고    scopus 로고
    • Nucleoside and RNA Triphosphatase Activities of Orthoreovirus Transcriptase Cofactor μ2
    • DOI 10.1074/jbc.M308637200
    • Kim J, Parker JS, Murray KE, Nibert ML (2004) Nucleoside and RNA triphosphatase activities of orthoreovirus transcriptase cofactor m 2. J Biol Chem 279:4394-4403 (Pubitemid 38199028)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4394-4403
    • Kim, J.1    Parker, J.S.L.2    Murray, K.E.3    Nibert, M.L.4
  • 85
    • 3242665450 scopus 로고    scopus 로고
    • The origin of phospholipids of the enveloped bacteriophage phi6
    • DOI 10.1016/j.virol.2004.05.021, PII S004268220400371X
    • Laurinavicius S, Kakela R, Bamford DH, Somerharju P (2004) The origin of phospholipids of the enveloped bacteriophage phi6. Virology 326:182-190 (Pubitemid 38943017)
    • (2004) Virology , vol.326 , Issue.1 , pp. 182-190
    • Laurinavicius, S.1    Kakela, R.2    Bamford, D.H.3    Somerharju, P.4
  • 86
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • DOI 10.1038/nsb0297-118
    • Lawton JA, Estes MK, Prasad BV (1997a) Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat Struct Biol 4:118-121 (Pubitemid 27066386)
    • (1997) Nature Structural Biology , vol.4 , Issue.2 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.V.3
  • 87
    • 0030768785 scopus 로고    scopus 로고
    • Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: Implications for the architecture of the VP2 capsid layer
    • Lawton JA, Zeng CQ, Mukherjee SK, Cohen J, Estes MK, Prasad BV (1997b) Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer. J Virol 71:7353-7360 (Pubitemid 27391674)
    • (1997) Journal of Virology , vol.71 , Issue.10 , pp. 7353-7360
    • Lawton, J.A.1    Zeng, C.Q.-Y.2    Mukherjee, S.K.3    Cohen, J.4    Estes, M.K.5    Venkataram Prasad, B.V.6
  • 88
    • 0026778224 scopus 로고
    • The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus
    • Le Blois H, French T, Mertens PP, Burroughs JN, Roy P (1992) The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus. Virology 189:757-761
    • (1992) Virology , vol.189 , pp. 757-761
    • Le Blois, H.1    French, T.2    Mertens, P.P.3    Burroughs, J.N.4    Roy, P.5
  • 90
  • 91
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3
    • DOI 10.1016/S0092-8674(02)00612-8
    • Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein, m 1, in a complex with its protector protein, s 3. Cell 108:283-295 (Pubitemid 34161147)
    • (2002) Cell , vol.108 , Issue.2 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 92
    • 0026766537 scopus 로고
    • Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity
    • Liu M, Mattion NM, Estes MK (1992) Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity. Virology 188:77-84
    • (1992) Virology , vol.188 , pp. 77-84
    • Liu, M.1    Mattion, N.M.2    Estes, M.K.3
  • 93
    • 0026785734 scopus 로고
    • Interaction of nucleic acids with core-like and subcore-like particles of bluetongue virus
    • Loudon PT, Roy P (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
  • 98
    • 0035794638 scopus 로고    scopus 로고
    • Atomic structure of the major capsid protein of rotavirus: Implications for the architecture of the virion
    • DOI 10.1093/emboj/20.7.1485
    • Mathieu M, Petitpas I, Navaza J, Lepault J, Kohli E, Pothier P, Prasad BV, Cohen J, Rey FA (2001) Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion. EMBO J 20:1485-1497 (Pubitemid 32299386)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1485-1497
    • Mathieu, M.1    Petitpas, I.2    Navaza, J.3    Lepault, J.4    Kohli, E.5    Pothier, P.6    Prasad, B.V.V.7    Cohen, J.8    Rey, F.A.9
  • 99
    • 69249202488 scopus 로고    scopus 로고
    • Bluetongue virus VP6 acts early in the replication cycle and can form the basis of chimeric virus formation
    • Matsuo E, Roy P (2009) Bluetongue virus VP6 acts early in the replication cycle and can form the basis of chimeric virus formation. J Virol 83:8842-8848
    • (2009) J Virol , vol.83 , pp. 8842-8848
    • Matsuo, E.1    Roy, P.2
  • 100
    • 77349116567 scopus 로고    scopus 로고
    • X-ray crystal structure of the rotavirus inner capsid particle at 3.8 Å resolution
    • McClain B, Settembre E, Temple BR, Bellamy AR, Harrison SC (2010) X-ray crystal structure of the rotavirus inner capsid particle at 3.8 Å resolution. J Mol Biol 397:587-599
    • (2010) J Mol Biol , vol.397 , pp. 587-599
    • McClain, B.1    Settembre, E.2    Temple, B.R.3    Bellamy, A.R.4    Harrison, S.C.5
  • 101
    • 43049118630 scopus 로고    scopus 로고
    • Conformational changes accompany activation of reovirus RNA-dependent RNA transcription
    • Mendez II, Weiner SG, She YM, Yeager M, Coombs KM (2008) Conformational changes accompany activation of reovirus RNA-dependent RNA transcription. J Struct Biol 162:277-289
    • (2008) J Struct Biol , vol.162 , pp. 277-289
    • Mendez, I.I.1    Weiner, S.G.2    She, Y.M.3    Yeager, M.4    Coombs, K.M.5
  • 102
    • 1542328804 scopus 로고    scopus 로고
    • The dsRNA viruses
    • DOI 10.1016/j.virusres.2003.12.002, PII S0168170203003666
    • Mertens P (2004) The dsRNA viruses. Virus Res 101:3-13 (Pubitemid 38317105)
    • (2004) Virus Research , vol.101 , Issue.1 , pp. 3-13
    • Mertens, P.1
  • 103
    • 73849150681 scopus 로고    scopus 로고
    • Localization of mammalian orthoreovirus proteins to cytoplasmic factory-like structures via nonoverlapping regions of NS
    • Miller CL, Arnold MM, Broering TJ, Hastings CE, Nibert ML (2010) Localization of mammalian orthoreovirus proteins to cytoplasmic factory-like structures via nonoverlapping regions of NS. J Virol 84:867-882
    • (2010) J Virol , vol.84 , pp. 867-882
    • Miller, C.L.1    Arnold, M.M.2    Broering, T.J.3    Hastings, C.E.4    Nibert, M.L.5
  • 104
    • 0018386121 scopus 로고
    • Cell wall lysin as a component of the bacteriophage 6 virion
    • Mindich L, Lehman J (1979) Cell wall lysin as a component of the bacteriophage j 6 virion. J Virol 30:489-496 (Pubitemid 9165244)
    • (1979) Journal of Virology , vol.30 , Issue.2 , pp. 489-496
    • Mindich, L.1    Lehman, J.2
  • 105
    • 0027978133 scopus 로고
    • RNA structural requirements for stability and minus-strand synthesis in the dsRNA bacteriophage φ6
    • DOI 10.1006/viro.1994.1341
    • Mindich L, Qiao X, Onodera S, Gottlieb P, Frilander M (1994) RNA structural requirements for stability and minusstrand synthesis in the dsRNA bacteriophage j 6. Virology 202:258-263 (Pubitemid 24241997)
    • (1994) Virology , vol.202 , Issue.1 , pp. 258-263
    • Mindich, L.1    Qiao, X.2    Onodera, S.3    Gottlieb, P.4    Frilander, M.5
  • 108
    • 0028261073 scopus 로고
    • Subcore- and core-like particles of Broadhaven virus (BRDV), a tick-borne orbivirus, synthesized from baculovirus expressed VP2 and VP7, the major core proteins of BRDV
    • DOI 10.1016/0168-1702(94)90088-4
    • Moss SR, Nuttall PA (1994) Subcore- and core-like particles of Broadhaven virus (BRDV), a tick-borne orbivirus, synthesized from baculovirus expressed VP2 and VP7, the major core proteins of BRDV. Virus Res 32:401-407 (Pubitemid 24164045)
    • (1994) Virus Research , vol.32 , Issue.3 , pp. 401-407
    • Moss, S.R.1    Nuttall, P.A.2
  • 109
    • 0036785914 scopus 로고    scopus 로고
    • L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism
    • Naitow H, Tang J, Canady M, Wickner RB, Johnson JE (2002) L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism. Nat Struct Biol 9:725-728
    • (2002) Nat Struct Biol , vol.9 , pp. 725-728
    • Naitow, H.1    Tang, J.2    Canady, M.3    Wickner, R.B.4    Johnson, J.E.5
  • 111
    • 0033919812 scopus 로고    scopus 로고
    • Trypsin-induced structural transformation in aquareovirus
    • DOI 10.1128/JVI.74.14.6546-6555.2000
    • Nason EL, Samal SK, Venkataram Prasad BV (2000) Trypsin-induced structural transformation in aquareovirus. J Virol 74:6546-6555 (Pubitemid 30429823)
    • (2000) Journal of Virology , vol.74 , Issue.14 , pp. 6546-6555
    • Nason, E.L.1    Samal, S.K.2    Prasad, B.V.V.3
  • 113
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein m 1/m 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration
    • Nibert ML, Fields BN (1992) A carboxy-terminal fragment of protein m 1/m 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J Virol 66:6408-6418
    • (1992) J Virol , vol.66 , pp. 6408-6418
    • Nibert, M.L.1    Fields, B.N.2
  • 114
    • 9644268149 scopus 로고    scopus 로고
    • Putative autocleavage of reovirus μ1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization
    • DOI 10.1016/j.jmb.2004.10.026, PII S002228360401318X
    • Nibert ML, Odegard AL, Agosto MA, Chandran K, Schiff LA (2005) Putative autocleavage of reovirus m 1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization. J Mol Biol 345:461-474 (Pubitemid 39575917)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.3 , pp. 461-474
    • Nibert, M.L.1    Odegard, A.L.2    Agosto, M.A.3    Chandran, K.4    Schiff, L.A.5
  • 116
    • 0025892607 scopus 로고
    • Generation of infectious nucleocapsids by in vitro assembly of the shell protein on to the polymerase complex of the dsRNA bacteriophage φ6
    • Olkkonen VM, Ojala PM, Bamford DH (1991) Generation of infectious nucleocapsids by in vitro assembly of the shell protein on to the polymerase complex of the dsRNA bacteriophage j 6. J Mol Biol 218:569-581 (Pubitemid 121003961)
    • (1991) Journal of Molecular Biology , vol.218 , Issue.3 , pp. 569-581
    • Olkkonen, V.M.1    Ojala, P.M.2    Bamford, D.H.3
  • 117
    • 0031774382 scopus 로고    scopus 로고
    • Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage φ6
    • Paatero AO, Mindich L, Bamford DH (1998) Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage j 6. J Virol 72:10058-10065 (Pubitemid 28520875)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 10058-10065
    • Paatero, A.O.1    Mindich, L.2    Bamford, D.H.3
  • 120
    • 0025281467 scopus 로고
    • Rotavirus RNA replication: Single-stranded RNA extends from the replicase particle
    • Patton JT, Gallegos CO (1990) Rotavirus RNA replication: single-stranded RNA extends from the replicase particle. J Gen Virol 71:1087-1094 (Pubitemid 20174348)
    • (1990) Journal of General Virology , vol.71 , Issue.5 , pp. 1087-1094
    • Patton, J.T.1    Gallegos, C.O.2
  • 121
    • 0034715823 scopus 로고    scopus 로고
    • Genome replication and packaging of segmented double-stranded RNA viruses
    • Patton JT, Spencer E (2000) Genome replication and packaging of segmented double-stranded RNA viruses. Virology 277:217-225
    • (2000) Virology , vol.277 , pp. 217-225
    • Patton, J.T.1    Spencer, E.2
  • 123
    • 0034041604 scopus 로고    scopus 로고
    • RNA secondary structures of the bacteriophage π6 packaging regions
    • DOI 10.1017/S1355838200992598
    • Pirttimaa MJ, Bamford DH (2000) RNA secondary structures of the bacteriophage j 6 packaging regions. RNA 6:880-889 (Pubitemid 30396028)
    • (2000) RNA , vol.6 , Issue.6 , pp. 880-889
    • Pirttimaa, M.J.T.1    Bamford, D.H.2
  • 124
    • 0036786440 scopus 로고    scopus 로고
    • Nonspecific nucleoside triphosphatase P4 of double-stranded RNA bacteriophage j 6 is required for single-stranded RNA packaging and transcription
    • Pirttimaa MJ, Paatero AO, Frilander MJ, Bamford DH (2002) Nonspecifi c nucleoside triphosphatase P4 of double-stranded RNA bacteriophage j 6 is required for single-stranded RNA packaging and transcription. J Virol 76:10122-10127
    • (2002) J Virol , vol.76 , pp. 10122-10127
    • Pirttimaa, M.J.1    Paatero, A.O.2    Frilander, M.J.3    Bamford, D.H.4
  • 125
    • 0032978372 scopus 로고    scopus 로고
    • Packaging and replication regulation revealed by chimeric genome segments of double-stranded RNA bacteriophage φ6
    • DOI 10.1017/S1355838299981876
    • Poranen MM, Bamford DH (1999) Packaging and replication regulation revealed by chimeric genome segments of double-stranded RNA bacteriophage j 6. RNA 5:446-454 (Pubitemid 29125003)
    • (1999) RNA , vol.5 , Issue.3 , pp. 446-454
    • Poranen, M.M.1    Bamford, D.H.2
  • 126
    • 84858270802 scopus 로고    scopus 로고
    • Cystovirus cystoviridae
    • 2011 Tidona C, Darai G (eds) 2nd edn. Springer, New York
    • Poranen MM, Bamford DH (2011) Cystovirus, cystoviridae. In: Tidona C, Darai G (eds) Springer index of viruses, 2nd edn. Springer, New York
    • Springer Index of Viruses
    • Poranen, M.M.1    Bamford, D.H.2
  • 127
    • 0344339712 scopus 로고    scopus 로고
    • A novel virus-host cell membrane interaction. Membrane voltage-dependent endocytic-like entry of bacteriophage straight j 6 nucleocapsid
    • Poranen MM, Daugelavicius R, Ojala PM, Hess MW, Bamford DH (1999) A novel virus-host cell membrane interaction. Membrane voltage-dependent endocytic-like entry of bacteriophage straight j 6 nucleocapsid. J Cell Biol 147:671-682
    • (1999) J Cell Biol , vol.147 , pp. 671-682
    • Poranen, M.M.1    Daugelavicius, R.2    Ojala, P.M.3    Hess, M.W.4    Bamford, D.H.5
  • 128
    • 0035002345 scopus 로고    scopus 로고
    • Self-assembly of a viral molecular machine from purified protein and RNA constituents
    • DOI 10.1016/S1097-2765(01)00228-3
    • Poranen MM, Paatero AO, Tuma R, Bamford DH (2001) Self-assembly of a viral molecular machine from purifi ed protein and RNA constituents. Mol Cell 7:845-854 (Pubitemid 32436444)
    • (2001) Molecular Cell , vol.7 , Issue.4 , pp. 845-854
    • Poranen, M.M.1    Paatero, A.O.2    Tuma, R.3    Bamford, D.H.4
  • 130
    • 26944486944 scopus 로고    scopus 로고
    • Assembly of double-stranded RNA bacteriophages
    • DOI 10.1016/S0065-3527(05)64002-X, PII S006535270564002X, Virus Structure and Assembly
    • Poranen MM, Tuma R, Bamford DH (2005b) Assembly of double-stranded RNA bacteriophages. Adv Virus Res 64:15-43 (Pubitemid 43591147)
    • (2005) Advances in Virus Research , vol.64 , pp. 15-43
    • Poranen, M.M.1    Tuma, R.2    Bamford, D.H.3
  • 131
    • 53149140981 scopus 로고    scopus 로고
    • Roles of the minor capsid protein P7 in the assembly and replication of double-stranded RNA bacteriophage j 6
    • Poranen MM, Butcher SJ, Simonov VM, Laurinmaki P, Bamford DH (2008) Roles of the minor capsid protein P7 in the assembly and replication of double-stranded RNA bacteriophage j 6. J Mol Biol 383:529-538
    • (2008) J Mol Biol , vol.383 , pp. 529-538
    • Poranen, M.M.1    Butcher, S.J.2    Simonov, V.M.3    Laurinmaki, P.4    Bamford, D.H.5
  • 133
    • 0025178591 scopus 로고
    • Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy
    • Prasad BV, Burns JW, Marietta E, Estes MK, Chiu W (1990) Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Nature 343:476-479
    • (1990) Nature , vol.343 , pp. 476-479
    • Prasad, B.V.1    Burns, J.W.2    Marietta, E.3    Estes, M.K.4    Chiu, W.5
  • 134
    • 0029839752 scopus 로고    scopus 로고
    • Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus
    • Prasad BV, Rothnagel R, Zeng CQ, Jakana J, Lawton JA, Chiu W, Estes MK (1996) Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature 382:471-473
    • (1996) Nature , vol.382 , pp. 471-473
    • Prasad, B.V.1    Rothnagel, R.2    Zeng, C.Q.3    Jakana, J.4    Lawton, J.A.5    Chiu, W.6    Estes, M.K.7
  • 135
    • 0028916125 scopus 로고
    • In vitro packaging of individual genomic segments of bacteriophage j 6, RNA: Serial dependence relationships
    • Qiao X, Casini G, Qiao J, Mindich L (1995) In vitro packaging of individual genomic segments of bacteriophage j 6, RNA: serial dependence relationships. J Virol 69:2926-2931
    • (1995) J Virol , vol.69 , pp. 2926-2931
    • Qiao, X.1    Casini, G.2    Qiao, J.3    Mindich, L.4
  • 136
    • 0142245619 scopus 로고    scopus 로고
    • Analysis of Specific Binding Involved in Genomic Packaging of the Double-Stranded-RNA Bacteriophage φ6
    • DOI 10.1128/JB.185.21.6409-6414.2003
    • Qiao X, Qiao J, Mindich L (2003) Analysis of specifi c binding involved in genomic packaging of the double-stranded- RNA bacteriophage j 6. J Bacteriol 185:6409-6414 (Pubitemid 37305541)
    • (2003) Journal of Bacteriology , vol.185 , Issue.21 , pp. 6409-6414
    • Qiao, X.1    Qiao, J.2    Mindich, L.3
  • 137
    • 77649332889 scopus 로고    scopus 로고
    • Characterization of j 2954, a newly isolated bacteriophage containing three dsRNA genomic segments
    • Qiao X, Sun Y, Qiao J, Di Sanzo F, Mindich L (2010) Characterization of j 2954, a newly isolated bacteriophage containing three dsRNA genomic segments. BMC Microbiol 10:55
    • (2010) BMC Microbiol , vol.10 , pp. 55
    • Qiao, X.1    Sun, Y.2    Qiao, J.3    Di Sanzo, F.4    Mindich, L.5
  • 139
    • 0031901745 scopus 로고    scopus 로고
    • A leucine zipper-like domain is essential for dimerization and encapsidation of bluetongue virus nucleocapsid protein VP4
    • Ramadevi N, Rodriguez J, Roy P (1998b) A leucine zipper-like domain is essential for dimerization and encapsidation of bluetongue virus nucleocapsid protein VP4. J Virol 72:2983-2990 (Pubitemid 28175537)
    • (1998) Journal of Virology , vol.72 , Issue.4 , pp. 2983-2990
    • Ramadevi, N.1    Rodriguez, J.2    Roy, P.3
  • 140
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao VB, Feiss M (2008) The bacteriophage DNA packaging motor. Annu Rev Genet 42:647-681
    • (2008) Annu Rev Genet , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 141
    • 26944480834 scopus 로고    scopus 로고
    • Structure-derived insights into virus assembly
    • DOI 10.1016/S0065-3527(05)64003-1, PII S0065352705640031, Virus Structure and Assembly
    • Reddy VS, Johnson JE (2005) Structure-derived insights into virus assembly. Adv Virus Res 64:45-68 (Pubitemid 43574755)
    • (2005) Advances in Virus Research , vol.64 , pp. 45-68
    • Reddy, V.S.1    Johnson, J.E.2
  • 142
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 A resolution
    • DOI 10.1038/35010041
    • Reinisch KM, Nibert ML, Harrison SC (2000) Structure of the reovirus core at 3.6 Å resolution. Nature 404:960-967 (Pubitemid 30243583)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 143
    • 0022761960 scopus 로고
    • Polyhedrin structure
    • Rohrmann GF (1986) Polyhedrin structure. J Gen Virol 67:1499-1513
    • (1986) J Gen Virol , vol.67 , pp. 1499-1513
    • Rohrmann, G.F.1
  • 145
    • 26944501278 scopus 로고    scopus 로고
    • Bluetongue virus proteins and particles and their role in virus entry, assembly, and release
    • DOI 10.1016/S0065-3527(05)64004-3, PII S0065352705640043, Virus Structure and Assembly
    • Roy P (2005) Bluetongue virus proteins and particles and their role in virus entry, assembly, and release. Adv Virus Res 64:69-123 (Pubitemid 43574758)
    • (2005) Advances in virus research , vol.64 , pp. 69-123
    • Roy, P.1
  • 146
    • 0035971072 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes
    • Schuck P, Taraporewala Z, McPhie P, Patton JT (2001) Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes. J Biol Chem 276:9679-9687
    • (2001) J Biol Chem , vol.276 , pp. 9679-9687
    • Schuck, P.1    Taraporewala, Z.2    McPhie, P.3    Patton, J.T.4
  • 147
    • 45549097253 scopus 로고    scopus 로고
    • Initial location of the RNA-dependent RNA polymerase in the bacteriophage j 6 procapsid determined by cryo-electron microscopy
    • Sen A, Heymann JB, Cheng N, Qiao J, Mindich L, Steven AC (2008) Initial location of the RNA-dependent RNA polymerase in the bacteriophage j 6 procapsid determined by cryo-electron microscopy. J Biol Chem 283:12227-12231
    • (2008) J Biol Chem , vol.283 , pp. 12227-12231
    • Sen, A.1    Heymann, J.B.2    Cheng, N.3    Qiao, J.4    Mindich, L.5    Steven, A.C.6
  • 149
    • 0030586878 scopus 로고    scopus 로고
    • The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization
    • DOI 10.1016/S0969-2126(96)00102-5
    • Shaw AL, Samal SK, Subramanian K, Prasad BV (1996) The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization. Structure 4:957-967 (Pubitemid 26324707)
    • (1996) Structure , vol.4 , Issue.8 , pp. 957-967
    • Shaw, A.L.1    Samal, S.K.2    Subramanian, K.3    Prasad, B.V.V.4
  • 150
    • 57649171916 scopus 로고    scopus 로고
    • Silencing by RNAi of the gene for Pns12, a viroplasm matrix protein of Rice dwarf virus, results in strong resistance of transgenic rice plants to the virus
    • Shimizu T, Yoshii M, Wei T, Hirochika H, Omura T (2009) Silencing by RNAi of the gene for Pns12, a viroplasm matrix protein of Rice dwarf virus , results in strong resistance of transgenic rice plants to the virus. Plant Biotechnol J 7:24-32
    • (2009) Plant Biotechnol J , vol.7 , pp. 24-32
    • Shimizu, T.1    Yoshii, M.2    Wei, T.3    Hirochika, H.4    Omura, T.5
  • 151
    • 0030580588 scopus 로고    scopus 로고
    • Assembly of the reovirus outer capsid requires μ1/σ3 interactions which are prevented by misfolded σ3 protein in temperature-sensitive mutant tsG453
    • DOI 10.1016/S0168-1702(96)01372-X, PII S016817029601372X
    • Shing M, Coombs KM (1996) Assembly of the reovirus outer capsid requires m 1/s 3 interactions which are prevented by misfolded s 3 protein in temperature-sensitive mutant tsG453. Virus Res 46:19-29 (Pubitemid 27072708)
    • (1996) Virus Research , vol.46 , Issue.1-2 , pp. 19-29
    • Shing, M.1    Coombs, K.M.2
  • 152
    • 0023394736 scopus 로고
    • Properties of RNA polymerase activity associated with infectious bursal disease virus and characterization of its reaction products
    • Spies U, Muller H, Becht H (1987) Properties of RNA polymerase activity associated with infectious bursal disease virus and characterization of its reaction products. Virus Res 8:127-140
    • (1987) Virus Res , vol.8 , pp. 127-140
    • Spies, U.1    Muller, H.2    Becht, H.3
  • 153
    • 1842329184 scopus 로고    scopus 로고
    • Bluetongue 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
    • Stauber N, Martinez-Costas J, Sutton G, Monastyrskaya K, Roy P (1997) Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of doublestranded RNA substrates. J Virol 71:7220-7226 (Pubitemid 27391656)
    • (1997) Journal of Virology , vol.71 , Issue.10 , pp. 7220-7226
    • Stauber, N.1    Martinez-Costas, J.2    Sutton, G.3    Monastyrskaya, K.4    Roy, P.5
  • 154
    • 0037431315 scopus 로고    scopus 로고
    • Unique properties of the inner core of bacteriophage φ8, a virus with a segmented dsRNA genome
    • DOI 10.1016/S0042-6822(03)00013-8
    • Sun Y, Qiao X, Qiao J, Onodera S, Mindich L (2003) Unique properties of the inner core of bacteriophage j 8, a virus with a segmented dsRNA genome. Virology 308:354-361 (Pubitemid 36434241)
    • (2003) Virology , vol.308 , Issue.2 , pp. 354-361
    • Sun, Y.1    Qiao, X.2    Qiao, J.3    Onodera, S.4    Mindich, L.5
  • 155
    • 0035079190 scopus 로고    scopus 로고
    • RGD tripeptide of bluetongue virus VP7 protein is responsible for core attachment to Culicoides cells
    • Tan BH, Nason E, Staeuber N, Jiang W, Monastryrskaya K, Roy P (2001) RGD tripeptide of bluetongue virus VP7 protein is responsible for core attachment to Culicoides cells. J Virol 75:3937-3947
    • (2001) J Virol , vol.75 , pp. 3937-3947
    • Tan, B.H.1    Nason, E.2    Staeuber, N.3    Jiang, W.4    Monastryrskaya, K.5    Roy, P.6
  • 157
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage - Structural studies of reovirus polymerase λ3
    • DOI 10.1016/S0092-8674(02)01110-8
    • Tao Y, Farsetta DL, Nibert ML, Harrison SC (2002) RNA synthesis in a cage - structural studies of reovirus polymerase l 3. Cell 111:733-745 (Pubitemid 35452525)
    • (2002) Cell , vol.111 , Issue.5 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 158
    • 0035034563 scopus 로고    scopus 로고
    • Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2
    • DOI 10.1128/JVI.75.10.4519-4527.2001
    • Taraporewala ZF, Patton JT (2001) Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2. J Virol 75:4519-4527 (Pubitemid 32381494)
    • (2001) Journal of Virology , vol.75 , Issue.10 , pp. 4519-4527
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 159
    • 1542268891 scopus 로고    scopus 로고
    • Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae
    • DOI 10.1016/j.virusres.2003.12.006, PII S0168170203003708
    • Taraporewala ZF, Patton JT (2004) Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae. Virus Res 101:57-66 (Pubitemid 38317109)
    • (2004) Virus Research , vol.101 , Issue.1 , pp. 57-66
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 160
    • 0032759060 scopus 로고    scopus 로고
    • Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA
    • Taraporewala Z, Chen D, Patton JT (1999) Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity. J Virol 73:9934-9943
    • (1999) J Virol , vol.73 , pp. 9934-9943
    • Taraporewala, Z.1    Chen, D.2    Patton, J.T.3
  • 162
    • 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
    • Thomas CP, Booth TF, Roy P (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 (Pubitemid 20296451)
    • (1990) Journal of General Virology , vol.71 , Issue.9 , pp. 2073-2083
    • Thomas, C.P.1    Booth, T.F.2    Roy, P.3
  • 163
    • 0041856540 scopus 로고    scopus 로고
    • Template recognition and formation of initiation complexes by the replicase of a segmented double-stranded RNA virus
    • DOI 10.1074/jbc.M305358200
    • Tortorici MA, Broering TJ, Nibert ML, Patton JT (2003) Template recognition and formation of initiation complexes by the replicase of a segmented double-stranded RNA virus. J Biol Chem 278:32673-32682 (Pubitemid 37055706)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 32673-32682
    • Tortorici, M.A.1    Broering, T.J.2    Nibert, M.L.3    Patton, J.T.4
  • 164
    • 29844450783 scopus 로고    scopus 로고
    • A base-specific recognition signal in the 5′ consensus sequence of rotavirus plus-strand RNAs promotes replication of the double-stranded RNA genome segments
    • DOI 10.1261/rna.2122606
    • Tortorici MA, Shapiro BA, Patton JT (2006) A base-specifi c recognition signal in the 5 ¢ consensus sequence of rotavirus plus-strand RNAs promotes replication of the double-stranded RNA genome segments. RNA 12:133-146 (Pubitemid 43037461)
    • (2006) RNA , vol.12 , Issue.1 , pp. 133-146
    • Tortorici, M.A.1    Shapiro, B.A.2    Patton, J.T.3
  • 165
    • 0030779747 scopus 로고    scopus 로고
    • Hypothesis on particle structure and assembly of rice dwarf phytoreovirus: Interactions among multiple structural proteins
    • Ueda S, Masuta C, Uyeda I (1997) Hypothesis on particle structure and assembly of rice dwarf phytoreovirus: interactions among multiple structural proteins. J Gen Virol 78:3135-3140 (Pubitemid 27511301)
    • (1997) Journal of General Virology , vol.78 , Issue.12 , pp. 3135-3140
    • Ueda, S.1    Masuta, C.2    Uyeda, I.3
  • 166
    • 0018906889 scopus 로고
    • Displacement of parental RNA strands during in vitro transcription by bacteriophage Φ6 nucleocapsids
    • Usala SJ, Brownstein BH, Haselkorn R (1980) Displacement of parental RNA strands during in vitro transcription by bacteriophage j 6 nucleocapsids. Cell 19:855-862 (Pubitemid 10155220)
    • (1980) Cell , vol.19 , Issue.4 , pp. 855-862
    • Usala, S.J.1    Brownstein, B.H.2    Haselkorn, R.3
  • 167
    • 31644432215 scopus 로고    scopus 로고
    • Pns12 protein of Rice dwarf virus is essential for formation of viroplasms and nucleation of viral-assembly complexes
    • DOI 10.1099/vir.0.81425-0
    • Wei T, Shimizu T, Hagiwara K, Kikuchi A, Moriyasu Y, Suzuki N, Chen H, Omura T (2006) Pns12 protein of Rice dwarf virus is essential for formation of viroplasms and nucleation of viral-assembly complexes. J Gen Virol 87:429-438 (Pubitemid 43169271)
    • (2006) Journal of General Virology , vol.87 , Issue.2 , pp. 429-438
    • Wei, T.1    Shimizu, T.2    Hagiwara, K.3    Kikuchi, A.4    Moriyasu, Y.5    Suzuki, N.6    Chen, H.7    Omura, T.8
  • 168
    • 70149112989 scopus 로고    scopus 로고
    • Three-dimensional structure of the enveloped bacteriophage j 12: An incomplete T = 13 lattice is superposed on an enclosed T = 1 shell
    • Wei H, Cheng RH, Berriman J, Rice WJ, Stokes DL, Katz A, Morgan DG, Gottlieb P (2009) Three-dimensional structure of the enveloped bacteriophage j 12: an incomplete T = 13 lattice is superposed on an enclosed T = 1 shell. PLoS One 4:e6850
    • (2009) PLoS One , vol.4
    • Wei, H.1    Cheng, R.H.2    Berriman, J.3    Rice, W.J.4    Stokes, D.L.5    Katz, A.6    Morgan, D.G.7    Gottlieb, P.8
  • 169
    • 0034713358 scopus 로고    scopus 로고
    • Phytoreovirus T = 1 core plays critical roles in organizing the outer capsid of T = 13 quasi-equivalence
    • DOI 10.1006/viro.2000.0300
    • Wu B, Hammar L, Xing L, Markarian S, Yan J, Iwasaki K, Fujiyoshi Y, Omura T, Cheng RH (2000) Phytoreovirus T = 1 core plays critical roles in organizing the outer capsid of T = 13 quasi-equivalence. Virology 271:18-25 (Pubitemid 30341510)
    • (2000) Virology , vol.271 , Issue.1 , pp. 18-25
    • Wu, B.1    Hammar, L.2    Xing, L.3    Markarian, S.4    Yan, J.5    Iwasaki, K.6    Fujiyoshi, Y.7    Omura, T.8    Cheng, R.H.9
  • 170
    • 0027432147 scopus 로고
    • Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2
    • Xu P, Miller SE, Joklik WK (1993) Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genome segments L1, L2, L3, and S2. Virology 197:726-731
    • (1993) Virology , vol.197 , pp. 726-731
    • Xu, P.1    Miller, S.E.2    Joklik, W.K.3
  • 171
    • 0030798963 scopus 로고    scopus 로고
    • VP7: An attachment protein of bluetongue virus for cellular receptors in Culicoides variipennis
    • Xu G, Wilson W, Mecham J, Murphy K, Zhou EM, Tabachnick W (1997) VP7: an attachment protein of bluetongue virus for cellular receptors in Culicoides variipennis . J Gen Virol 78:1617-1623 (Pubitemid 27343101)
    • (1997) Journal of General Virology , vol.78 , Issue.7 , pp. 1617-1623
    • Xu, G.1    Wilson, W.2    Mecham, J.3    Murphy, K.4    Zhou, E.-M.5    Tabachnick, W.6
  • 172
    • 0030588318 scopus 로고    scopus 로고
    • P2 protein encoded by genome segment S2 of rice dwarf phytoreovirus is essential for virus infection
    • DOI 10.1006/viro.1996.0560
    • Yan J, Tomaru M, Takahashi A, Kimura I, Hibino H, Omura T (1996) P2 protein encoded by genome segment S2 of rice dwarf phytoreovirus is essential for virus infection. Virology 224:539-541 (Pubitemid 26364501)
    • (1996) Virology , vol.224 , Issue.2 , pp. 539-541
    • Yan, J.1    Tomaru, M.2    Takahashi, A.3    Kimura, I.4    Hibino, H.5    Omura, T.6
  • 173
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • DOI 10.1038/nature06893, PII NATURE06893
    • Yu X, Jin L, Zhou ZH (2008) 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 453:415-419 (Pubitemid 351693126)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 174
    • 0029998886 scopus 로고    scopus 로고
    • Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants
    • Zeng CQ, Wentz MJ, Cohen J, Estes MK, Ramig RF (1996) Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants. J Virol 70:2736-2742
    • (1996) J Virol , vol.70 , pp. 2736-2742
    • Zeng, C.Q.1    Wentz, M.J.2    Cohen, J.3    Estes, M.K.4    Ramig, R.F.5
  • 175
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A
    • DOI 10.1038/nsb1009
    • Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS (2003) Reovirus polymerase l 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å. Nat Struct Biol 10:1011-1018 (Pubitemid 37500493)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 176
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141:472-482
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zh, Z.5
  • 177
    • 77950907290 scopus 로고    scopus 로고
    • Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins
    • Zhang X, Boyce M, Bhattacharya B, Schein S, Roy P, Zhou ZH (2011) Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins. Proc Natl Acad Sci USA 107:6292-6297
    • (2011) Proc Natl Acad Sci USA , vol.107 , pp. 6292-6297
    • Zhang, X.1    Boyce, M.2    Bhattacharya, B.3    Schein, S.4    Roy, P.5    Zh, Z.6
  • 178
    • 0033819795 scopus 로고    scopus 로고
    • Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus
    • Zheng H, Yu L, Wei C, Hu D, Shen Y, Chen Z, Li Y (2000) Assembly of double-shelled, virus-like particles in transgenic rice plants expressing two major structural proteins of rice dwarf virus. J Virol 74:9808-9810
    • (2000) J Virol , vol.74 , pp. 9808-9810
    • Zheng, H.1    Yu, L.2    Wei, C.3    Hu, D.4    Shen, Y.5    Chen, Z.6    Li, Y.7
  • 180
    • 37649002522 scopus 로고    scopus 로고
    • The P2 capsid protein of the nonenveloped rice dwarf phytoreovirus induces membrane fusion in insect host cells
    • Zhou F, Pu Y, Wei T, Liu H, Deng W, Wei C, Ding B, Omura T, Li Y (2007) The P2 capsid protein of the nonenveloped rice dwarf phytoreovirus induces membrane fusion in insect host cells. Proc Natl Acad Sci USA 104:19547-19552
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19547-19552
    • Zhou, F.1    Pu, Y.2    Wei, T.3    Liu, H.4    Deng, W.5    Wei, C.6    Ding, B.7    Omura, T.8    Li, Y.9
  • 181
    • 0030802761 scopus 로고    scopus 로고
    • Details of the arrangement of the outer capsid of rice dwarf phytoreovirus, as visualized by two-dimensional crystallography
    • Zhu Y, Hemmings AM, Iwasaki K, Fujiyoshi Y, Zhong B, Yan J, Isogai M, Omura T (1997) Details of the arrangement of the outer capsid of rice dwarf phytoreovirus, as visualized by two-dimensional crystallography. J Virol 71:8899-8901 (Pubitemid 27446479)
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8899-8901
    • Zhu, Y.1    Hemmings, A.M.2    Iwasaki, K.3    Fujiyoshi, Y.4    Zhong, B.5    Yan, J.6    Isogai, M.7    Omura, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.