메뉴 건너뛰기




Volumn 343, Issue 1, 2005, Pages 25-35

Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction

Author keywords

Electron cryomicroscopy; Orthoreovirus; Reoviridae; Reovirus; Virus structure

Indexed keywords

CAPSID PROTEIN; VIRUS PROTEIN;

EID: 27644594455     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2005.08.002     Document Type: Article
Times cited : (63)

References (68)
  • 1
    • 0023139089 scopus 로고
    • Isolation of a reovirus from the snake, Python regius
    • W. Ahne, I. Thomsen, and J. Winton Isolation of a reovirus from the snake, Python regius Brief Report Arch. Virol. 94 1987 135 139
    • (1987) Arch. Virol. , vol.94 , pp. 135-139
    • Ahne, W.1    Thomsen, I.2    Winton, J.3
  • 2
    • 0036324190 scopus 로고    scopus 로고
    • Common evolutionary origin of aquareoviruses and orthoreoviruses revealed by genome characterization of Golden shiner reovirus, Grass carp reovirus, Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family Reoviridae)
    • H. Attoui, Q. Fang, F.M. Jaafar, J.F. Cantaloube, P. Biagini, P. De Micco, and X. De Lamballerie Common evolutionary origin of aquareoviruses and orthoreoviruses revealed by genome characterization of Golden shiner reovirus, Grass carp reovirus, Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family Reoviridae) J. Gen. Virol. 83 2002 1941 1951
    • (2002) J. Gen. Virol. , vol.83 , pp. 1941-1951
    • Attoui, H.1    Fang, Q.2    Jaafar, F.M.3    Cantaloube, J.F.4    Biagini, P.5    De Micco, P.6    De Lamballerie, X.7
  • 3
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryo-electron microscopy
    • T.S. Baker, and R.H. Cheng A model-based approach for determining orientations of biological macromolecules imaged by cryo-electron microscopy J. Struct. Biol. 116 1996 120 130
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 4
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • T.S. Baker, N.H. Olson, and S.D. Fuller Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs Microbiol. Mol. Biol. Rev. 63 1999 862 922
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 5
    • 0036889348 scopus 로고    scopus 로고
    • An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons
    • V.D. Bowman, E.S. Chase, A.W.E. Franz, P.R. Chipman, X. Zhang, K.L. Perry, T.S. Baker, and T.J. Smith An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons J. Virol. 76 2002 12250 12258
    • (2002) J. Virol. , vol.76 , pp. 12250-12258
    • Bowman, V.D.1    Chase, E.S.2    Franz, A.W.E.3    Chipman, P.R.4    Zhang, X.5    Perry, K.L.6    Baker, T.S.7    Smith, T.J.8
  • 6
    • 0035450448 scopus 로고    scopus 로고
    • Mammalian reovirus L2 gene and λ2 core spike protein sequences and pangenomic comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing
    • L.A. Breun, T.J. Broering, A.M. McCutcheon, S.J. Harrison, C.L. Luongo, and M.L. Nibert Mammalian reovirus L2 gene and λ2 core spike protein sequences and pangenomic comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing Virology 287 2001 333 348
    • (2001) Virology , vol.287 , pp. 333-348
    • Breun, L.A.1    Broering, T.J.2    McCutcheon, A.M.3    Harrison, S.J.4    Luongo, C.L.5    Nibert, M.L.6
  • 7
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • K. Chandran, X. Zhang, N.O. Olson, S.B. Walker, J.D. Chappell, T.S. Dermody, T.S. Baker, and M.L. Nibert Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein J. Virol. 75 2001 5335 5342
    • (2001) J. Virol. , vol.75 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.O.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 8
    • 0000080575 scopus 로고    scopus 로고
    • Structural refinement of the DNA-containing capsid of canine parvovirus using RSRef, a resolution-dependent stereochemically restrained real-space refinement method
    • M.S. Chapman Structural refinement of the DNA-containing capsid of canine parvovirus using RSRef, a resolution-dependent stereochemically restrained real-space refinement method Acta Crystallogr., Sect. D: Biol. Crystallogr. 52 1996 129 142
    • (1996) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.52 , pp. 129-142
    • Chapman, M.S.1
  • 9
    • 0032579850 scopus 로고    scopus 로고
    • Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles
    • K.M. Coombs Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles Virology 243 1998 218 228
    • (1998) Virology , vol.243 , pp. 218-228
    • Coombs, K.M.1
  • 10
    • 1842483912 scopus 로고    scopus 로고
    • Reptilian reovirus utilizes a small type III protein with an external myristoylated amino terminus to mediate cell-cell fusion
    • J.A. Corcoran, and R. Duncan Reptilian reovirus utilizes a small type III protein with an external myristoylated amino terminus to mediate cell-cell fusion J. Virol. 78 2004 4342 4351
    • (2004) J. Virol. , vol.78 , pp. 4342-4351
    • Corcoran, J.A.1    Duncan, R.2
  • 11
    • 0036171070 scopus 로고    scopus 로고
    • The S4 genome segment of baboon reovirus is bicistronic and encodes a novel fusion-associated small transmembrane protein
    • S. Dawe, and R. Duncan The S4 genome segment of baboon reovirus is bicistronic and encodes a novel fusion-associated small transmembrane protein J. Virol. 76 2002 2131 2140
    • (2002) J. Virol. , vol.76 , pp. 2131-2140
    • Dawe, S.1    Duncan, R.2
  • 12
    • 0037164412 scopus 로고    scopus 로고
    • Isolation and identification of a reovirus from a lizard, Uromastyx hardwickii, in the United Kingdom
    • S.E. Drury, R.E. Gough, and B. Welchman Dde Isolation and identification of a reovirus from a lizard, Uromastyx hardwickii, in the United Kingdom Vet. Rec. 151 2002 637 638
    • (2002) Vet. Rec. , vol.151 , pp. 637-638
    • Drury, S.E.1    Gough, R.E.2    Welchman Dde, B.3
  • 13
    • 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
    • K.A. Dryden, G. Wang, M. Yeager, M.L. Nibert, K.M. Coombs, D.B. Furlong, B.N. Fields, and T.S. Baker 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 1993 1023 1041
    • (1993) J. Cell Biol. , vol.122 , 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
  • 14
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • K.A. Dryden, D.L. Farsetta, G. Wang, J.M. Keegan, B.N. Fields, T.S. Baker, and M.L. Nibert Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus Virology 245 1998 33 46
    • (1998) Virology , vol.245 , 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
  • 15
    • 0030008825 scopus 로고    scopus 로고
    • The low pH-dependent entry of avian reovirus is accompanied by two specific cleavages of the major outer capsid protein μ2C
    • R. Duncan The low pH-dependent entry of avian reovirus is accompanied by two specific cleavages of the major outer capsid protein μ2C Virology 219 1996 179 189
    • (1996) Virology , vol.219 , pp. 179-189
    • Duncan, R.1
  • 16
    • 0033179264 scopus 로고    scopus 로고
    • Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: A species proposal
    • R. Duncan Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: a species proposal Virology 260 1999 316 328
    • (1999) Virology , vol.260 , pp. 316-328
    • Duncan, R.1
  • 17
    • 0032566915 scopus 로고    scopus 로고
    • Characterization of two avian reoviruses that exhibit strain-specific quantitative differences in their syncytium-inducing and pathogenic capabilities
    • R. Duncan, and K. Sullivan Characterization of two avian reoviruses that exhibit strain-specific quantitative differences in their syncytium-inducing and pathogenic capabilities Virology 250 1998 263 272
    • (1998) Virology , vol.250 , pp. 263-272
    • Duncan, R.1    Sullivan, K.2
  • 18
    • 1242270680 scopus 로고    scopus 로고
    • Reptilian reovirus: A new fusogenic orthoreovirus species
    • R. Duncan, J. Corcoran, J. Shou, and D. Stoltz Reptilian reovirus: a new fusogenic orthoreovirus species Virology 319 2004 131 140
    • (2004) Virology , vol.319 , pp. 131-140
    • Duncan, R.1    Corcoran, J.2    Shou, J.3    Stoltz, D.4
  • 19
    • 0002880402 scopus 로고
    • Studies on chronic respiratory disease of chickens: II. Isolation of a virus
    • J.E. Fahey, and J.F. Crawley Studies on chronic respiratory disease of chickens: II. Isolation of a virus Can. J. Comp. Med. 18 1954 13 21
    • (1954) Can. J. Comp. Med. , vol.18 , pp. 13-21
    • Fahey, J.E.1    Crawley, J.F.2
  • 20
    • 0023945392 scopus 로고
    • Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles
    • D.B. Furlong, M.L. Nibert, and B.N. Fields Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles J. Virol. 62 1988 246 256
    • (1988) J. Virol. , vol.62 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 22
    • 0015891913 scopus 로고
    • Characterization of two reoviruses isolated from turkeys with infectious enteritis
    • A. Gershowitz, and R.E. Wooley Characterization of two reoviruses isolated from turkeys with infectious enteritis Avian Dis. 17 1973 406 414
    • (1973) Avian Dis. , vol.17 , pp. 406-414
    • Gershowitz, A.1    Wooley, R.E.2
  • 24
    • 0036297716 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of avian reovirus guanylyltransferase
    • J. Hsiao, J. Martinez-Costas, J. Benavente, and V.N. Vakharia Cloning, expression, and characterization of avian reovirus guanylyltransferase Virology 296 2002 288 299
    • (2002) Virology , vol.296 , pp. 288-299
    • Hsiao, J.1    Martinez-Costas, J.2    Benavente, J.3    Vakharia, V.N.4
  • 25
    • 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
    • J. Jané-Valbuena, M.L. Nibert, S.M. Spencer, S.B. Walker, T.S. Baker, Y. Chen, V.E. Centonze, and L.A. Schiff Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: an approach for analyzing σ3 functions during virus entry J. Virol. 73 1999 2963 2973
    • (1999) J. Virol. , vol.73 , pp. 2963-2973
    • Jané-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
  • 26
    • 1042289782 scopus 로고    scopus 로고
    • Nucleoside and RNA triphosphatase activities of Orthoreovirus transcriptase cofactor μ2
    • J. Kim, J.S.L. Parker, K.E. Murray, and M.L. Nibert Nucleoside and RNA triphosphatase activities of Orthoreovirus transcriptase cofactor μ2 J. Biol. Chem. 279 2004 4394 4403
    • (2004) J. Biol. Chem. , vol.279 , pp. 4394-4403
    • Kim, J.1    Parker, J.S.L.2    Murray, K.E.3    Nibert, M.L.4
  • 27
    • 1542268897 scopus 로고    scopus 로고
    • Orthoreovirus and Aquareovirus core proteins: Conserved enzymatic surfaces, but not protein-protein interfaces
    • J. Kim, Y. Tao, K.M. Reinisch, S.C. Harrison, and M.L. Nibert Orthoreovirus and Aquareovirus core proteins: conserved enzymatic surfaces, but not protein-protein interfaces Virus Res. 101 2004 15 28
    • (2004) Virus Res. , vol.101 , pp. 15-28
    • Kim, J.1    Tao, Y.2    Reinisch, K.M.3    Harrison, S.C.4    Nibert, M.L.5
  • 28
    • 0032848446 scopus 로고    scopus 로고
    • Isolation and experimental transmission of a reovirus pathogenic in ratsnakes (Elaphe species)
    • E.W. Lamirande, D.K. Nichols, J.W. Owens, J.M. Gaskin, and E.R. Jacobson Isolation and experimental transmission of a reovirus pathogenic in ratsnakes (Elaphe species) Virus Res. 63 1999 135 141
    • (1999) Virus Res. , vol.63 , pp. 135-141
    • Lamirande, E.W.1    Nichols, D.K.2    Owens, J.W.3    Gaskin, J.M.4    Jacobson, E.R.5
  • 30
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration, μ1, in a complex with its protector protein, σ3
    • S. Liemann, K. Chandran, T.S. Baker, M.L. Nibert, and S.C. Harrison Structure of the reovirus membrane-penetration, μ1, in a complex with its protector protein, σ3 Cell 108 2002 283 295
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 31
    • 0036346029 scopus 로고    scopus 로고
    • Loss of activities for mRNA synthesis accompanies loss of λ2 spikes from reovirus cores: An effect of λ2 on λ1 shell structure
    • C.L. Luongo, X. Zhang, S.B. Walker, Y. Chen, T.J. Broering, D.L. Farsetta, V.D. Bowman, T.S. Baker, and M.L. Nibert Loss of activities for mRNA synthesis accompanies loss of λ2 spikes from reovirus cores: an effect of λ2 on λ1 shell structure Virology 296 2002 24 38
    • (2002) Virology , vol.296 , pp. 24-38
    • Luongo, C.L.1    Zhang, X.2    Walker, S.B.3    Chen, Y.4    Broering, T.J.5    Farsetta, D.L.6    Bowman, V.D.7    Baker, T.S.8    Nibert, M.L.9
  • 33
    • 0028853290 scopus 로고
    • Endogenous enzymatic activities of the avian reovirus S1133: Identification of the viral capping enzyme
    • J. Martinez-Costas, R. Varela, and J. Benavente Endogenous enzymatic activities of the avian reovirus S1133: identification of the viral capping enzyme Virology 206 1995 1017 1026
    • (1995) Virology , vol.206 , pp. 1017-1026
    • Martinez-Costas, J.1    Varela, R.2    Benavente, J.3
  • 34
    • 0031060494 scopus 로고    scopus 로고
    • Protein architecture of avian reovirus S1133 and identification of the cell attachment protein
    • J. Martinez-Costas, A. Grande, R. Varela, C. Garcia-Martinez, and J. Benavente Protein architecture of avian reovirus S1133 and identification of the cell attachment protein J. Virol. 71 1997 59 64
    • (1997) J. Virol. , vol.71 , pp. 59-64
    • Martinez-Costas, J.1    Grande, A.2    Varela, R.3    Garcia-Martinez, C.4    Benavente, J.5
  • 35
    • 0016976783 scopus 로고
    • Isolation of adenoviruses and reoviruses from avian species other than domestic fowl
    • J.B. McFerran, T.J. Connor, and R.M. McCracken Isolation of adenoviruses and reoviruses from avian species other than domestic fowl Avian Dis. 20 1976 519 524
    • (1976) Avian Dis. , vol.20 , pp. 519-524
    • McFerran, J.B.1    Connor, T.J.2    McCracken, R.M.3
  • 36
    • 1542328804 scopus 로고    scopus 로고
    • The dsRNA viruses
    • P. Mertens The dsRNA viruses Virus Res. 101 2004 3 13
    • (2004) Virus Res. , vol.101 , pp. 3-13
    • Mertens, P.1
  • 37
    • 0020028581 scopus 로고
    • The symmetry of the reovirus outer shell
    • P. Metcalf The symmetry of the reovirus outer shell J. Ultrastruct. Res. 78 1982 292 301
    • (1982) J. Ultrastruct. Res. , vol.78 , pp. 292-301
    • Metcalf, P.1
  • 38
    • 0026072563 scopus 로고
    • The three-dimensional structure of reovirus obtained by cryo-electron microscopy
    • P. Metcalf, M. Cyrklaff, and M. Adrian The three-dimensional structure of reovirus obtained by cryo-electron microscopy EMBO J. 10 1991 3129 3136
    • (1991) EMBO J. , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 39
    • 0021771537 scopus 로고
    • Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral cell attachment protein σ1
    • L. Nagata, S.A. Masri, D.C. Mah, and P.W.K. Lee Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral cell attachment protein σ1 Nucleic Acids Res. 12 1984 8699 8710
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8699-8710
    • Nagata, L.1    Masri, S.A.2    Mah, D.C.3    Lee, P.W.K.4
  • 40
    • 0033919812 scopus 로고    scopus 로고
    • Trypsin-induced structural transformation in aquareovirus
    • E.L. Nason, S.K. Samal, and B.V.V. Prasad Trypsin-induced structural transformation in aquareovirus J. Virol. 74 2000 6546 6555
    • (2000) J. Virol. , vol.74 , pp. 6546-6555
    • Nason, E.L.1    Samal, S.K.2    Prasad, B.V.V.3
  • 41
    • 0034990083 scopus 로고    scopus 로고
    • A monoclonal antibody specific for reovirus outer-capsid protein σ3 inhibits σ1-mediated hemagglutination by steric hindrance
    • E.L. Nason, J.D. Wetzel, S.K. Mukherjee, E.S. Barton, B.V.V. Prasad, and T.S. Dermody A monoclonal antibody specific for reovirus outer-capsid protein σ3 inhibits σ1-mediated hemagglutination by steric hindrance J. Virol. 75 2001 6625 6634
    • (2001) J. Virol. , vol.75 , pp. 6625-6634
    • Nason, E.L.1    Wetzel, J.D.2    Mukherjee, S.K.3    Barton, E.S.4    Prasad, B.V.V.5    Dermody, T.S.6
  • 42
    • 32344445136 scopus 로고    scopus 로고
    • Sequences of avian reovirus M1, M2, and M3 genes and structure/function of the encoded Âμ proteins
    • in press.
    • Noad, L., Shou, J., Coombs, K.M., Duncan, R., in press. Sequences of avian reovirus M1, M2, and M3 genes and structure/function of the encoded Âμ proteins. Virus Res.
    • Virus Res.
    • Noad, L.1    Shou, J.2    Coombs, K.M.3    Duncan, R.4
  • 43
    • 0035038930 scopus 로고    scopus 로고
    • Avian reovirus major m-class outer capsid protein influences efficiency of productive macrophage infection in a virus strain-specific manner
    • D. O'Hara, M. Patrick, D. Cepica, K.M. Coombs, and R. Duncan Avian reovirus major m-class outer capsid protein influences efficiency of productive macrophage infection in a virus strain-specific manner J. Virol. 75 2001 5027 5035
    • (2001) J. Virol. , vol.75 , pp. 5027-5035
    • O'Hara, D.1    Patrick, M.2    Cepica, D.3    Coombs, K.M.4    Duncan, R.5
  • 44
    • 0037404548 scopus 로고    scopus 로고
    • Disulfide bonding among μ1 trimers in mammalian reovirus outer capsid: A late and reversible step in virion morphogenesis
    • A.L. Odegard, K. Chandran, S. Liemann, S.C. Harrison, and M.L. Nibert Disulfide bonding among μ1 trimers in mammalian reovirus outer capsid: a late and reversible step in virion morphogenesis J. Virol. 77 2003 5389 5400
    • (2003) J. Virol. , vol.77 , pp. 5389-5400
    • Odegard, A.L.1    Chandran, K.2    Liemann, S.3    Harrison, S.C.4    Nibert, M.L.5
  • 45
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution
    • A.M. Olland, J. Jané-Valbuena, L.A. Schiff, M.L. Nibert, and S.C. Harrison Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution EMBO J. 20 2001 979 989
    • (2001) EMBO J. , vol.20 , pp. 979-989
    • Olland, A.M.1    Jané-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 46
    • 0035947373 scopus 로고    scopus 로고
    • Generation and genetic characterization of avian reovirus temperature-sensitive mutants
    • M. Patrick, R. Duncan, and K.M. Coombs Generation and genetic characterization of avian reovirus temperature-sensitive mutants Virology 284 2001 113 122
    • (2001) Virology , vol.284 , pp. 113-122
    • Patrick, M.1    Duncan, R.2    Coombs, K.M.3
  • 48
    • 0034901402 scopus 로고    scopus 로고
    • Molecular characterization and expression of the M6 gene of grass carp hemorrhage virus (GCHV), an aquareovirus
    • T. Qiu, R.H. Lu, J. Zhang, and Z.Y. Zhu Molecular characterization and expression of the M6 gene of grass carp hemorrhage virus (GCHV), an aquareovirus Arch. Virol. 146 2001 1391 1397
    • (2001) Arch. Virol. , vol.146 , pp. 1391-1397
    • Qiu, T.1    Lu, R.H.2    Zhang, J.3    Zhu, Z.Y.4
  • 49
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • K.M. Reinisch, M.L. Nibert, and S.C. Harrison Structure of the reovirus core at 3.6 Å resolution Nature 404 2000 960 967
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 50
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 51
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • M.F. Sanner Python: a programming language for software integration and development J. Mol. Graphics Mod. 17 1999 57 61
    • (1999) J. Mol. Graphics Mod. , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 53
    • 0019918321 scopus 로고
    • Avian reovirus polypeptides: Analysis of intracellular virus specified products, virions, top component, and cores
    • T. Schnitzer, T. Ramos, and V. Gouvea Avian reovirus polypeptides: analysis of intracellular virus specified products, virions, top component, and cores J. Virol. 43 1982 1006 1014
    • (1982) J. Virol. , vol.43 , pp. 1006-1014
    • Schnitzer, T.1    Ramos, T.2    Gouvea, V.3
  • 55
    • 0034161496 scopus 로고    scopus 로고
    • A new class of fusion-associated small transmembrane (FAST) proteins encoded by the nonenveloped fusogenic reoviruses
    • M. Shmulevitz, and R. Duncan A new class of fusion-associated small transmembrane (FAST) proteins encoded by the nonenveloped fusogenic reoviruses EMBO J. 19 2000 902 912
    • (2000) EMBO J. , vol.19 , pp. 902-912
    • Shmulevitz, M.1    Duncan, R.2
  • 56
    • 0036138025 scopus 로고    scopus 로고
    • Sequential partially overlapping gene arrangement in the tricistronic S1 genome segments of avian reovirus and Nelson Bay reovirus: Implications for translation initiation
    • M. Shmulevitz, Z. Yameen, S. Dawe, J. Shou, D. O'Hara, I. Holmes, and R. Duncan Sequential partially overlapping gene arrangement in the tricistronic S1 genome segments of avian reovirus and Nelson Bay reovirus: implications for translation initiation J. Virol. 76 2002 609 618
    • (2002) J. Virol. , vol.76 , pp. 609-618
    • Shmulevitz, M.1    Yameen, Z.2    Dawe, S.3    Shou, J.4    O'Hara, D.5    Holmes, I.6    Duncan, R.7
  • 57
    • 2442671553 scopus 로고    scopus 로고
    • Cell-cell fusion induced by the avian reovirus membrane fusion protein is regulated by protein degradation
    • M. Shmulevitz, J. Corcoran, J. Salsman, and R. Duncan Cell-cell fusion induced by the avian reovirus membrane fusion protein is regulated by protein degradation J. Virol. 78 2004 5996 6004
    • (2004) J. Virol. , vol.78 , pp. 5996-6004
    • Shmulevitz, M.1    Corcoran, J.2    Salsman, J.3    Duncan, R.4
  • 58
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • L.J. Sturzenbecker, M. Nibert, D. Furlong, and B.N. Fields Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle J. Virol. 61 1987 2351 2361
    • (1987) J. Virol. , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 59
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-Structural studies of the reovirus polymerase λ3
    • Y. Tao, D.L. Farsetta, M.L. Nibert, and S.C. Harrison RNA synthesis in a cage-Structural studies of the reovirus polymerase λ3 Cell 111 2002 733 745
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 60
    • 1242338230 scopus 로고    scopus 로고
    • Avian reovirus nonstructural protein mNS forms viroplasm-like inclusions and recruits protein SNS to these structures
    • F. Touris-Otero, J. Martinez-Costas, V.N. Vakharia, and J. Benavente Avian reovirus nonstructural protein mNS forms viroplasm-like inclusions and recruits protein SNS to these structures Virology 319 2004 94 106
    • (2004) Virology , vol.319 , pp. 94-106
    • Touris-Otero, F.1    Martinez-Costas, J.2    Vakharia, V.N.3    Benavente, J.4
  • 61
    • 0033831623 scopus 로고    scopus 로고
    • The history of avian reovirus
    • L. van der Heide The history of avian reovirus Avian Dis. 44 2000 638 641
    • (2000) Avian Dis. , vol.44 , pp. 638-641
    • Van Der Heide, L.1
  • 62
    • 0027936370 scopus 로고
    • Protein coding assignment of avian reovirus strain S1133
    • R. Varela, and J. Benavente Protein coding assignment of avian reovirus strain S1133 J. Virol. 68 1994 6775 6777
    • (1994) J. Virol. , vol.68 , pp. 6775-6777
    • Varela, R.1    Benavente, J.2
  • 63
    • 0024477475 scopus 로고
    • The sequences of the reovirus serotype 1, 2, and 3 L1 genome segments and analysis of the mode of divergence of the reovirus serotypes
    • J.R. Wiener, and W.K. Joklik The sequences of the reovirus serotype 1, 2, and 3 L1 genome segments and analysis of the mode of divergence of the reovirus serotypes Virology 169 1989 194 203
    • (1989) Virology , vol.169 , pp. 194-203
    • Wiener, J.R.1    Joklik, W.K.2
  • 64
    • 4644319640 scopus 로고    scopus 로고
    • Avian reovirus temperature-sensitive mutant tsA12 has a lesion in major core protein σa and is defective in assembly
    • W. Xu, M.K. Patrick, P.R. Hazelton, and K.M. Coombs Avian reovirus temperature-sensitive mutant tsA12 has a lesion in major core protein σA and is defective in assembly J. Virol. 78 2004 11142 11151
    • (2004) J. Virol. , vol.78 , pp. 11142-11151
    • Xu, W.1    Patrick, M.K.2    Hazelton, P.R.3    Coombs, K.M.4
  • 66
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å
    • X. Zhang, S.B. Walker, P.R. Chipman, M.L. Nibert, and T.S. Baker Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å Nat. Struct. Biol. 10 2003 1011 1018
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 67
    • 26444511104 scopus 로고    scopus 로고
    • Features of Reovirus Outer-capsid Protein μ1 Revealed by Electron Cryomicroscopy and Image Reconstruction of the Virion at 7.0-Å Resolution
    • in press
    • Zhang, X., Ji, Y., Zhang, L., Harrison, S.C., Marinescu, D.C., Nibert, M. L., Baker, T.S., in press. Features of Reovirus Outer-capsid Protein μ1 Revealed by Electron Cryomicroscopy and Image Reconstruction of the Virion at 7.0-Å Resolution. Structure. 13.
    • Structure , pp. 13
    • Zhang, X.1    Ji, Y.2    Zhang, L.3    Harrison, S.C.4    Marinescu, D.C.5    Nibert, M.L.6    Baker, T.S.7
  • 68
    • 0141960927 scopus 로고    scopus 로고
    • Cytoplasmic polyhedrosis virus structure at 8 Å by electron cryomicroscopy: Structural basis of capsid stability and mRNA processing regulation
    • Z.H. Zhou, H. Zhang, J. Jakana, X.Y. Lu, and J.Q. Zhang Cytoplasmic polyhedrosis virus structure at 8 Å by electron cryomicroscopy: structural basis of capsid stability and mRNA processing regulation Structure 11 2003 651 663
    • (2003) Structure , vol.11 , pp. 651-663
    • Zhou, Z.H.1    Zhang, H.2    Jakana, J.3    Lu, X.Y.4    Zhang, J.Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.