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Volumn 309, Issue , 2006, Pages 117-167

Reovirus structure and morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED RNA; VIRUS PROTEIN;

EID: 33748121977     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/3-540-30773-7_5     Document Type: Review
Times cited : (28)

References (228)
  • 1
    • 0018831093 scopus 로고
    • Genetic variation during lytic reovirus infection: High-passage stocks of wild-type reovirus contain temperature-sensitive mutants
    • Ahmed R, Chakraborty PR, Fields BN (1980a) Genetic variation during lytic reovirus infection: high-passage stocks of wild-type reovirus contain temperature-sensitive mutants. J Virol 34:285-287
    • (1980) J Virol , vol.34 , pp. 285-287
    • Ahmed, R.1    Chakraborty, P.R.2    Fields, B.N.3
  • 2
    • 0018859414 scopus 로고
    • Genetic variation during persistent reovirus infection: Presence of extragenically suppressed temperature-sensitive lesions in wild-type virus isolated from persistently infected L cells
    • Ahmed R, Chakraborty PR, Graham AF, Ramig RF, Fields BN (1980b) Genetic variation during persistent reovirus infection: presence of extragenically suppressed temperature-sensitive lesions in wild-type virus isolated from persistently infected L cells. J Virol 34:383-389
    • (1980) J Virol , vol.34 , pp. 383-389
    • Ahmed, R.1    Chakraborty, P.R.2    Graham, A.F.3    Ramig, R.F.4    Fields, B.N.5
  • 3
    • 0026529484 scopus 로고
    • Reovirus genome segment assortment into progeny genomes studied by the use of monoclonal antibodies directed against reovirus proteins
    • Antczak JB, Joklik WK (1992) Reovirus genome segment assortment into progeny genomes studied by the use of monoclonal antibodies directed against reovirus proteins. Virology 187:760-776
    • (1992) Virology , vol.187 , pp. 760-776
    • Antczak, J.B.1    Joklik, W.K.2
  • 5
    • 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)
    • Attoui H, Fang Q, Jaafar FM, Cantaloube JF, Biagini P, de Micco P, deLamballerie X (2002) 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 83:1941-1951
    • (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    deLamballerie, X.7
  • 6
    • 0030999547 scopus 로고    scopus 로고
    • Mutations in reovirus outer-capsid protein sigma3 selected during persistent infections of L cells confer resistance to protease inhibitor E64
    • Baer GS, Dermody TS (1997) Mutations in reovirus outer-capsid protein sigma3 selected during persistent infections of L cells confer resistance to protease inhibitor E64. J Virol 71:4921-4928
    • (1997) J Virol , vol.71 , pp. 4921-4928
    • Baer, G.S.1    Dermody, T.S.2
  • 7
    • 0036635529 scopus 로고    scopus 로고
    • Evidence for segment-nonspecific packaging of the influenza A virus genome
    • Bancroft CT, Parslow TG (2002) Evidence for segment-nonspecific packaging of the influenza A virus genome. J Virol 76:7133-7139
    • (2002) J Virol , vol.76 , pp. 7133-7139
    • Bancroft, C.T.1    Parslow, T.G.2
  • 8
    • 0024110653 scopus 로고
    • The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1
    • Bartlett JA, Joklik WK (1988) The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1. Virology 167:31-37
    • (1988) Virology , vol.167 , pp. 31-37
    • Bartlett, J.A.1    Joklik, W.K.2
  • 11
    • 0025249289 scopus 로고
    • Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice
    • Bass DM, Bodkin D, Dambrauskas R, Trier JS, Fields BN, Wolf JL (1990) Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice. J Virol 64:1830-1833
    • (1990) J Virol , vol.64 , pp. 1830-1833
    • Bass, D.M.1    Bodkin, D.2    Dambrauskas, R.3    Trier, J.S.4    Fields, B.N.5    Wolf, J.L.6
  • 12
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E, Denzler KL, Tartaglia J, Perkus ME, Paoletti E, Jacobs BL (1995) Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J Virol 69:499-505
    • (1995) J Virol , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 14
    • 0037695004 scopus 로고    scopus 로고
    • Reovirus sigma NS and mu NS proteins form cytoplasmic inclusion structures in the absence of viral infection
    • Becker MM, Peters TR, Dermody TS (2003) Reovirus sigma NS and mu NS proteins form cytoplasmic inclusion structures in the absence of viral infection. J Virol 77:5948-5963
    • (2003) J Virol , vol.77 , pp. 5948-5963
    • Becker, M.M.1    Peters, T.R.2    Dermody, T.S.3
  • 15
    • 0032486592 scopus 로고    scopus 로고
    • Characterization of the thermosensitive ts453 reovirus mutant: Increased dsRNA binding of sigma 3 protein correlates with interferon resistance
    • Bergeron J, Mabrouk T, Garzon S, Lemay G (1998) Characterization of the thermosensitive ts453 reovirus mutant: increased dsRNA binding of sigma 3 protein correlates with interferon resistance. Virology 246:199-210
    • (1998) Virology , vol.246 , pp. 199-210
    • Bergeron, J.1    Mabrouk, T.2    Garzon, S.3    Lemay, G.4
  • 16
    • 0030613775 scopus 로고    scopus 로고
    • Characterization of the reovirus lambda1 protein RNA 5′-triphosphatase activity
    • Bisaillon M, Lemay G (1997a) Characterization of the reovirus lambda1 protein RNA 5′-triphosphatase activity. J Biol Chem 272:29954-29957
    • (1997) J Biol Chem , vol.272 , pp. 29954-29957
    • Bisaillon, M.1    Lemay, G.2
  • 17
    • 0031259835 scopus 로고    scopus 로고
    • Molecular dissection of the reovirus lambda1 protein nucleic acids binding site
    • Bisaillon M, Lemay G (1997b) Molecular dissection of the reovirus lambda1 protein nucleic acids binding site. Virus Res 51:231-237
    • (1997) Virus Res , vol.51 , pp. 231-237
    • Bisaillon, M.1    Lemay, G.2
  • 18
    • 0030800967 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein
    • Bisaillon M, Bergeron J, Lemay G (1997) Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein. J Biol Chem 272:18298-18303
    • (1997) J Biol Chem , vol.272 , pp. 18298-18303
    • Bisaillon, M.1    Bergeron, J.2    Lemay, G.3
  • 19
    • 0000956277 scopus 로고
    • Morphogenesis of the T4 head
    • Karam JD, Drake JW, Kreuzer KN, Mosig G, Hall D, Eiserling FA, Black LW, Kutter E, Spîcer E, Carlson K, Miller ES eds, T4. American Society for Microbiology, Washington, DC, pp
    • Black LW, Showe MK, Steven AC (1994) Morphogenesis of the T4 head. In: Karam JD, Drake JW, Kreuzer KN, Mosig G, Hall D, Eiserling FA, Black LW, Kutter E, Spîcer E, Carlson K, Miller ES (eds) Molecular biology of bacteriophage T4. American Society for Microbiology, Washington, DC, pp 218-258
    • (1994) Molecular biology of bacteriophage , pp. 218-258
    • Black, L.W.1    Showe, M.K.2    Steven, A.C.3
  • 20
    • 0024418092 scopus 로고
    • Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice
    • Bodkin DK, Nibert ML, Fields BN (1989) Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice. J Virol 63:4676-4681
    • (1989) J Virol , vol.63 , pp. 4676-4681
    • Bodkin, D.K.1    Nibert, M.L.2    Fields, B.N.3
  • 21
    • 0035450448 scopus 로고    scopus 로고
    • Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing
    • Breun LA, Broering TJ, McCutcheon AM, Harrison SJ, Luongo CL, Nibert ML (2001) Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing. Virology 287:333-348
    • (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
  • 22
    • 0036316297 scopus 로고    scopus 로고
    • Mammalian reovirus nonstructural protein μNS forms large inclusions and colocalizes with reovirus microtubule-associated protein μ2 in transfected cells
    • Broering TJ, Parker JS, Joyce PL, Kim J, Nibert ML (2002) Mammalian reovirus nonstructural protein μNS forms large inclusions and colocalizes with reovirus microtubule-associated protein μ2 in transfected cells. J Virol 76:8285-8297
    • (2002) J Virol , vol.76 , pp. 8285-8297
    • Broering, T.J.1    Parker, J.S.2    Joyce, P.L.3    Kim, J.4    Nibert, M.L.5
  • 23
    • 0842304505 scopus 로고    scopus 로고
    • Reovirus nonstructural protein mu NS recruits viral core surface proteins and entering core particles to factory-like inclusions
    • Broering TJ, Kim J, Miller CL, Piggott CDS, Dinoso JB, Nibert ML, Parker JSL (2004) Reovirus nonstructural protein mu NS recruits viral core surface proteins and entering core particles to factory-like inclusions. J Virol 78:1882-1892
    • (2004) J Virol , vol.78 , pp. 1882-1892
    • Broering, T.J.1    Kim, J.2    Miller, C.L.3    Piggott, C.D.S.4    Dinoso, J.B.5    Nibert, M.L.6    Parker, J.S.L.7
  • 24
    • 18144383857 scopus 로고    scopus 로고
    • Carboxyl-proximal regions of reovirus nonstructural protein mu NS necessary and sufficient for forming factory-like inclusions
    • Broering TJ, Arnold MM, Miller CL, Hurt JA, Joyce PL, Nibert ML (2005) Carboxyl-proximal regions of reovirus nonstructural protein mu NS necessary and sufficient for forming factory-like inclusions. J Virol 79:6194-6206
    • (2005) J Virol , vol.79 , pp. 6194-6206
    • Broering, T.J.1    Arnold, M.M.2    Miller, C.L.3    Hurt, J.A.4    Joyce, P.L.5    Nibert, M.L.6
  • 25
    • 0033614130 scopus 로고    scopus 로고
    • Self-assembly of tobacco mosaic virus: The role of an intermediate aggregate in generating both specificity and speed
    • Butler PJ (1999) Self-assembly of tobacco mosaic virus: the role of an intermediate aggregate in generating both specificity and speed. Phil Trans R Soc Lond B Biol Sci 354:537-550
    • (1999) Phil Trans R Soc Lond B Biol Sci , vol.354 , pp. 537-550
    • Butler, P.J.1
  • 26
    • 0020694127 scopus 로고
    • Ammonium chloride prevents lytic growth of reovirus and helps to establish persistent infection in mouse L cells
    • Canning WM, Fields BN (1983) Ammonium chloride prevents lytic growth of reovirus and helps to establish persistent infection in mouse L cells. Science 219:987-988
    • (1983) Science , vol.219 , pp. 987-988
    • Canning, W.M.1    Fields, B.N.2
  • 27
    • 0031964230 scopus 로고    scopus 로고
    • Protease cleavage of reovirus capsid protein mu1/mu1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle
    • Chandran K, Nibert ML (1998) Protease cleavage of reovirus capsid protein mu1/mu1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle. J Virol 72:467-475
    • (1998) J Virol , vol.72 , pp. 467-475
    • Chandran, K.1    Nibert, M.L.2
  • 28
    • 0032899595 scopus 로고    scopus 로고
    • In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins mu1 and sigma3
    • Chandran K, Walker SB, Chen Y, Contreras CM, Schiff LA, Baker TS, Nibert ML (1999) In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins mu1 and sigma3. J Virol 73:3941-3950
    • (1999) J Virol , vol.73 , pp. 3941-3950
    • Chandran, K.1    Walker, S.B.2    Chen, Y.3    Contreras, C.M.4    Schiff, L.A.5    Baker, T.S.6    Nibert, M.L.7
  • 29
    • 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
    • Chandran K, Zhang X, Olson NH, Walker SB, Chappell JD, Dermody TS, Baker TS, Nibert ML (2001) Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J Virol 75:5335-5342
    • (2001) J Virol , vol.75 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 30
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: A hydrophobic conformer of the reovirus membrane penetration protein mu 1 mediates membrane disruption
    • Chandran K, Farsetta DL, Nibert ML (2002) Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein mu 1 mediates membrane disruption. J Virol 76:9920-9933
    • (2002) J Virol , vol.76 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 31
    • 0345166984 scopus 로고    scopus 로고
    • The delta region of outer-capsid protein mu 1 undergoes conformational change and release from reovirus particles during cell entry
    • Chandran K, Parker JSL, Ehrlich M, Kirchhausen T, Nibert ML (2003) The delta region of outer-capsid protein mu 1 undergoes conformational change and release from reovirus particles during cell entry. J Virol 77:13361-13375
    • (2003) J Virol , vol.77 , pp. 13361-13375
    • Chandran, K.1    Parker, J.S.L.2    Ehrlich, M.3    Kirchhausen, T.4    Nibert, M.L.5
  • 32
    • 0015166005 scopus 로고
    • Fate of parental reovirus in infected cell
    • Chang CT, Zweerink HJ (1971) Fate of parental reovirus in infected cell. Virology 46:544-555
    • (1971) Virology , vol.46 , pp. 544-555
    • Chang, C.T.1    Zweerink, H.J.2
  • 33
    • 0035800739 scopus 로고    scopus 로고
    • Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells
    • Charpilienne A, Nejmeddine M, Berios M, Parez N, Neumann E, Hewat E, Trugnan G, Cohen J (2001) Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells. J Biol Chem 276:29361-29367
    • (2001) J Biol Chem , vol.276 , pp. 29361-29367
    • Charpilienne, A.1    Nejmeddine, M.2    Berios, M.3    Parez, N.4    Neumann, E.5    Hewat, E.6    Trugnan, G.7    Cohen, J.8
  • 34
    • 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
    • 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
    • (2002) J Virol , vol.76 , pp. 7822-7831
    • Charpilienne, A.1    Lepault, J.2    Rey, F.3    Cohen, J.4
  • 35
    • 0027185672 scopus 로고
    • Rescue of infectivity by in vitro transcapsidation of rotavirus single-shelled particles
    • Chen D, Ramig RF (1993a) Rescue of infectivity by in vitro transcapsidation of rotavirus single-shelled particles. Virology 192:422-429
    • (1993) Virology , vol.192 , pp. 422-429
    • Chen, D.1    Ramig, R.F.2
  • 36
    • 0027325343 scopus 로고
    • Rescue of infectivity by sequential in vitro transcapsidation of rotavirus core particles with inner capsid and outer capsid proteins
    • Chen D, Ramig RF (1993b) Rescue of infectivity by sequential in vitro transcapsidation of rotavirus core particles with inner capsid and outer capsid proteins. Virology 192:743-751
    • (1993) Virology , vol.192 , pp. 743-751
    • Chen, D.1    Ramig, R.F.2
  • 37
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein sigma 1 reveals evolutionary relationship to adenovirus fiber
    • Chappell JD, Prota AE, Dermody TS, Stehle T (2002) Crystal structure of reovirus attachment protein sigma 1 reveals evolutionary relationship to adenovirus fiber. EMBO J 21:1-11
    • (2002) EMBO J , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 38
    • 20744460868 scopus 로고    scopus 로고
    • Effects of a temperature sensitivity mutation in the J1R protein component of a complex required for vaccinia virus assembly
    • Chiu WL, Szajner P, Moss B, Chang W (2005) Effects of a temperature sensitivity mutation in the J1R protein component of a complex required for vaccinia virus assembly. J Virol 79:8046-8056
    • (2005) J Virol , vol.79 , pp. 8046-8056
    • Chiu, W.L.1    Szajner, P.2    Moss, B.3    Chang, W.4
  • 39
    • 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
    • (1986) J Virol , vol.60 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 40
    • 0030000103 scopus 로고    scopus 로고
    • - reovirus temperature-sensitive mutant defective in minor core protein mu2
    • - reovirus temperature-sensitive mutant defective in minor core protein mu2. J Virol 70:4237-4245
    • (1996) J Virol , vol.70 , pp. 4237-4245
    • Coombs, K.M.1
  • 41
    • 0032579850 scopus 로고    scopus 로고
    • Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles
    • Coombs KM (1998a) Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles. Virology 243:218-228
    • (1998) Virology , vol.243 , pp. 218-228
    • Coombs, K.M.1
  • 42
    • 0031926250 scopus 로고    scopus 로고
    • Temperature-sensitive mutants of reovirus
    • Coombs KM (1998b) Temperature-sensitive mutants of reovirus. Curr Top Microbiol Immunol 233:69-107
    • (1998) Curr Top Microbiol Immunol , vol.233 , pp. 69-107
    • Coombs, K.M.1
  • 43
    • 0028078574 scopus 로고
    • Studies of the major reovirus core protein sigma 2: Reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn
    • Coombs KM, Mak SC, Petrycky-Cox LD (1994) Studies of the major reovirus core protein sigma 2: reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn. J Virol 68:177-186
    • (1994) J Virol , vol.68 , pp. 177-186
    • Coombs, K.M.1    Mak, S.C.2    Petrycky-Cox, L.D.3
  • 44
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton TE (1990) Protein folding. Biochem J 270:1-16
    • (1990) Biochem J , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 45
    • 0015440085 scopus 로고
    • Temperature-sensitive mutants of reovirus type 3: Studies on the synthesis of viral RNA
    • Cross RK, Fields BN (1972) Temperature-sensitive mutants of reovirus type 3: studies on the synthesis of viral RNA. Virology 50:799-809
    • (1972) Virology , vol.50 , pp. 799-809
    • Cross, R.K.1    Fields, B.N.2
  • 46
    • 0344651935 scopus 로고
    • Replication of animal viruses as studied by electron microscopy
    • Dales S (1965) Replication of animal viruses as studied by electron microscopy. Am J Med 38:699-715
    • (1965) Am J Med , vol.38 , pp. 699-715
    • Dales, S.1
  • 47
    • 0026786353 scopus 로고
    • Further characterization of the ts453 mutant of mammalian orthoreovirus serotype 3 and nucleotide sequence of the mutated S4 gene
    • Danis C, Garzon S, Lemay G (1992) Further characterization of the ts453 mutant of mammalian orthoreovirus serotype 3 and nucleotide sequence of the mutated S4 gene. Virology 190:494-498
    • (1992) Virology , vol.190 , pp. 494-498
    • Danis, C.1    Garzon, S.2    Lemay, G.3
  • 48
    • 34548617946 scopus 로고    scopus 로고
    • DeLano WL (2004) The PyMOL molecular graphics system. (http://www.pymol.org)
    • (2004)
    • DeLano, W.L.1
  • 49
    • 0028106465 scopus 로고
    • Site-directed mutagenic analysis of reovirus sigma 3 protein binding to dsRNA
    • Denzler KL, Jacobs BL (1994) Site-directed mutagenic analysis of reovirus sigma 3 protein binding to dsRNA. Virology 204:190-199
    • (1994) Virology , vol.204 , pp. 190-199
    • Denzler, K.L.1    Jacobs, B.L.2
  • 50
    • 0025134429 scopus 로고
    • Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains
    • Dermody TS, Nibert ML, Bassel-Duby R, Fields BN (1990) Sequence diversity in S1 genes and S1 translation products of 11 serotype 3 reovirus strains. J Virol 64:4842-4850
    • (1990) J Virol , vol.64 , pp. 4842-4850
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 51
    • 0025931308 scopus 로고
    • The S2 gene nucleotide sequences of prototype strains of the three reovirus serotypes: Characterization of reovirus core protein sigma 2
    • Dermody TS, Schiff LA, Nibert ML, Coombs KM, Fields BN (1991) The S2 gene nucleotide sequences of prototype strains of the three reovirus serotypes: characterization of reovirus core protein sigma 2. J Virol 65:5721-5731
    • (1991) J Virol , vol.65 , pp. 5721-5731
    • Dermody, T.S.1    Schiff, L.A.2    Nibert, M.L.3    Coombs, K.M.4    Fields, B.N.5
  • 52
    • 0020079241 scopus 로고
    • Activation and characterization of the reovirus transcriptase: Genetic analysis
    • Drayna D, Fields BN (1982a) Activation and characterization of the reovirus transcriptase: genetic analysis. J Virol 41:110-118
    • (1982) J Virol , vol.41 , pp. 110-118
    • Drayna, D.1    Fields, B.N.2
  • 53
    • 0020467144 scopus 로고
    • Biochemical studies on the mechanism of chemical and physical inactivation of reovirus
    • Drayna D, Fields BN (1982b) Biochemical studies on the mechanism of chemical and physical inactivation of reovirus. J Gen Virol 63:161-170
    • (1982) J Gen Virol , vol.63 , pp. 161-170
    • Drayna, D.1    Fields, B.N.2
  • 54
    • 0020365482 scopus 로고
    • Genetic studies on the mechanism of chemical and physical inactivation of reovirus
    • Drayna D, Fields BN (1982c) Genetic studies on the mechanism of chemical and physical inactivation of reovirus. J Gen Virol 63:149-159
    • (1982) J Gen Virol , vol.63 , pp. 149-159
    • Drayna, D.1    Fields, B.N.2
  • 55
    • 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
    • (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
  • 56
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • 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
    • (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
  • 57
    • 0033179264 scopus 로고    scopus 로고
    • Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: A species proposal
    • Duncan R (1999) Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: a species proposal. Virology 260:316-328
    • (1999) Virology , vol.260 , pp. 316-328
    • Duncan, R.1
  • 58
    • 0035101193 scopus 로고    scopus 로고
    • Adaptation of reovirus to growth in the presence of protease inhibitor E64 segregates with a mutation in the carboxy terminus of viral outer-capsid protein sigma3
    • Ebert DH, Wetzel JD, Brumbaugh DE, Chance SR, Stobie LE, Baer GS, Dermody TS (2001) Adaptation of reovirus to growth in the presence of protease inhibitor E64 segregates with a mutation in the carboxy terminus of viral outer-capsid protein sigma3. J Virol 75:3197-3206
    • (2001) J Virol , vol.75 , pp. 3197-3206
    • Ebert, D.H.1    Wetzel, J.D.2    Brumbaugh, D.E.3    Chance, S.R.4    Stobie, L.E.5    Baer, G.S.6    Dermody, T.S.7
  • 59
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert DH, Deussing J, Peters C, Dermody TS (2002) Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J Biol Chem 277:24609-24617
    • (2002) J Biol Chem , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 60
    • 0025951699 scopus 로고
    • An influenza virus containing 9 different RNA segments
    • Enami M, Sharma G, Benham C, Palese P (1991) An influenza virus containing 9 different RNA segments. Virology 185:291-298
    • (1991) Virology , vol.185 , pp. 291-298
    • Enami, M.1    Sharma, G.2    Benham, C.3    Palese, P.4
  • 61
    • 0001581287 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Estes MK (2001) Rotaviruses and their replication. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1747-1785
    • (2001) Fields virology , pp. 1747-1785
    • Estes, M.K.1
  • 62
    • 34548631307 scopus 로고
    • The structure of vaccine bodies in isolated cells
    • Ewing J (1905) The structure of vaccine bodies in isolated cells. J Med Res 13:233-251
    • (1905) J Med Res , vol.13 , pp. 233-251
    • Ewing, J.1
  • 63
    • 0025320720 scopus 로고
    • Active site localization in a viral mRNA capping enzyme
    • Fausnaugh J, Shatkin AJ (1990) Active site localization in a viral mRNA capping enzyme. J Biol Chem 265:7669-7672
    • (1990) J Biol Chem , vol.265 , pp. 7669-7672
    • Fausnaugh, J.1    Shatkin, A.J.2
  • 64
    • 0014483713 scopus 로고
    • Isolation and preliminary genetic and biochemical characterization of temperature-sensitive mutants of reovirus
    • Fields BN, Joklik WK (1969) Isolation and preliminary genetic and biochemical characterization of temperature-sensitive mutants of reovirus. Virology 37:335-342
    • (1969) Virology , vol.37 , pp. 335-342
    • Fields, B.N.1    Joklik, W.K.2
  • 65
    • 0015022708 scopus 로고
    • Temperature-sensitive mutants of reovirus type 3: Defects in viral maturation as studied by immunofluorescence and electron microscopy
    • Fields BN, Raine CS, Baum SG (1971) Temperature-sensitive mutants of reovirus type 3: defects in viral maturation as studied by immunofluorescence and electron microscopy. Virology 43:569-578
    • (1971) Virology , vol.43 , pp. 569-578
    • Fields, B.N.1    Raine, C.S.2    Baum, S.G.3
  • 66
    • 0015419242 scopus 로고
    • Temperature-sensitive mutants of reovirus type 3: Studies on the synthesis of viral peptides
    • Fields BN, Laskov R, Scharff MD (1972) Temperature-sensitive mutants of reovirus type 3: studies on the synthesis of viral peptides. Virology 50:209-215
    • (1972) Virology , vol.50 , pp. 209-215
    • Fields, B.N.1    Laskov, R.2    Scharff, M.D.3
  • 67
    • 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
    • (1990) J Virol , vol.64 , pp. 2990-3000
    • Fraser, R.D.1    Furlong, D.B.2    Trus, B.L.3    Nibert, M.L.4    Fields, B.N.5    Steven, A.C.6
  • 69
    • 0016442397 scopus 로고
    • Reovirus messenger RNA contains amethylated, blocked 5′-terminal structure: M-7G(5′)ppp(5′)G-MpCp-
    • Furuichi Y, Morgan M, Muthukrishnan S, Shatkin AJ (1975) Reovirus messenger RNA contains amethylated, blocked 5′-terminal structure: m-7G(5′)ppp(5′)G-MpCp-. Proc Natl Acad Sci U S A 72:362-366
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 362-366
    • Furuichi, Y.1    Morgan, M.2    Muthukrishnan, S.3    Shatkin, A.J.4
  • 70
    • 0024318804 scopus 로고
    • Stimulation of chloramphenicol acetyltransferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected COS cells
    • Giantini M, Shatkin AJ (1989) Stimulation of chloramphenicol acetyltransferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected COS cells. J Virol 63:2415-2421
    • (1989) J Virol , vol.63 , pp. 2415-2421
    • Giantini, M.1    Shatkin, A.J.2
  • 71
    • 0021752428 scopus 로고
    • Reovirus type 3 genome segment S4: Nucleotide sequence of the gene encoding a major virion surface protein
    • Giantini M, Seliger LS, Furuichi Y, Shatkin AJ (1984) Reovirus type 3 genome segment S4: nucleotide sequence of the gene encoding a major virion surface protein. J Virology 52:984-987
    • (1984) J Virology , vol.52 , pp. 984-987
    • Giantini, M.1    Seliger, L.S.2    Furuichi, Y.3    Shatkin, A.J.4
  • 72
    • 0032484483 scopus 로고    scopus 로고
    • Amino terminus of reovirus nonstructural protein sigma NS is important for ssRNA binding and nucleoprotein complex formation
    • Gillian AL, Nibert ML (1998) Amino terminus of reovirus nonstructural protein sigma NS is important for ssRNA binding and nucleoprotein complex formation. Virology 240:1-11
    • (1998) Virology , vol.240 , pp. 1-11
    • Gillian, A.L.1    Nibert, M.L.2
  • 73
    • 0033625344 scopus 로고    scopus 로고
    • Reovirus protein sigmaNS binds in multiple copies to single-stranded RNA and shares properties with single-stranded DNA binding proteins
    • Gillian AL, Schmechel SC, Livny J, Schiff LA, Nibert ML (2000) Reovirus protein sigmaNS binds in multiple copies to single-stranded RNA and shares properties with single-stranded DNA binding proteins. J Virol 74:5939-5948
    • (2000) J Virol , vol.74 , pp. 5939-5948
    • Gillian, A.L.1    Schmechel, S.C.2    Livny, J.3    Schiff, L.A.4    Nibert, M.L.5
  • 75
    • 0018928388 scopus 로고
    • Small reovirus-specific particle with polycytidylate-dependent RNA polymerase activity
    • Gomatos PJ, Stamatos NM, Sarkar NH (1980) Small reovirus-specific particle with polycytidylate-dependent RNA polymerase activity. J Virol 36:556-565
    • (1980) J Virol , vol.36 , pp. 556-565
    • Gomatos, P.J.1    Stamatos, N.M.2    Sarkar, N.H.3
  • 76
    • 0019391135 scopus 로고
    • Small reovirus particle composed solely of sigma NS with specificity for binding different nucleic acids
    • Gomatos PJ, Prakash O, Stamatos NM (1981) Small reovirus particle composed solely of sigma NS with specificity for binding different nucleic acids. J Virol 39:115-124
    • (1981) J Virol , vol.39 , pp. 115-124
    • Gomatos, P.J.1    Prakash, O.2    Stamatos, N.M.3
  • 77
    • 34548236387 scopus 로고
    • Recherches sur la pathologie et étiologie de l'infection vaccinique et varioleuse
    • Guarnieri G (1893) Recherches sur la pathologie et étiologie de l'infection vaccinique et varioleuse. Arch Ital Biol 19:195-209
    • (1893) Arch Ital Biol , vol.19 , pp. 195-209
    • Guarnieri, G.1
  • 78
    • 0028924754 scopus 로고
    • Genetic mapping of reovirus virulence and organ tropism in severe combined immunodeficient mice: Organ-specific virulence genes
    • Haller BL, Barkon ML, Vogler GP, Virgin HW (1995) Genetic mapping of reovirus virulence and organ tropism in severe combined immunodeficient mice: organ-specific virulence genes. J Virol 69:357-364
    • (1995) J Virol , vol.69 , pp. 357-364
    • Haller, B.L.1    Barkon, M.L.2    Vogler, G.P.3    Virgin, H.W.4
  • 79
    • 0033602711 scopus 로고    scopus 로고
    • Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein
    • Harrison SJ, Farsetta DL, Kim J, Noble S, Broering TJ, Nibert ML (1999) Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda1 protein. Virology 258:54-64
    • (1999) Virology , vol.258 , pp. 54-64
    • Harrison, S.J.1    Farsetta, D.L.2    Kim, J.3    Noble, S.4    Broering, T.J.5    Nibert, M.L.6
  • 80
    • 0028899793 scopus 로고
    • The reovirus mutant tsA279 has temperature-sensitive lesions in the M2 and L2 genes: The M2 gene is associated with decreased viral protein production and blockade in transmembrane transport
    • Hazelton PR, Coombs KM (1995) The reovirus mutant tsA279 has temperature-sensitive lesions in the M2 and L2 genes: the M2 gene is associated with decreased viral protein production and blockade in transmembrane transport. Virology 207:46-58
    • (1995) Virology , vol.207 , pp. 46-58
    • Hazelton, P.R.1    Coombs, K.M.2
  • 81
    • 0033045992 scopus 로고    scopus 로고
    • The reovirus mutant tsA279 L2 gene is associated with generation of a spikeless core particle: Implications for capsid assembly
    • Hazelton PR, Coombs KM (1999) The reovirus mutant tsA279 L2 gene is associated with generation of a spikeless core particle: implications for capsid assembly. J Virol 73:2298-2308
    • (1999) J Virol , vol.73 , pp. 2298-2308
    • Hazelton, P.R.1    Coombs, K.M.2
  • 82
    • 0017253105 scopus 로고
    • Reovirus-coded polypeptides in infected cells: Isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively
    • Huismans H, Joklik WK (1976) Reovirus-coded polypeptides in infected cells: isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively. Virology 70:411-424
    • (1976) Virology , vol.70 , pp. 411-424
    • Huismans, H.1    Joklik, W.K.2
  • 83
    • 0021915811 scopus 로고
    • Genome rearrangements of bovine rotavirus after serial passage at high multiplicity of infection
    • Hundley F, Biryahwaho B, Gow M, Desselberger U (1985) Genome rearrangements of bovine rotavirus after serial passage at high multiplicity of infection. Virology 143:88-103
    • (1985) Virology , vol.143 , pp. 88-103
    • Hundley, F.1    Biryahwaho, B.2    Gow, M.3    Desselberger, U.4
  • 84
    • 0014351107 scopus 로고
    • Temperature-sensitive conditional-lethal mutants of reovirus 3. I. Isolation and characterization
    • Ikegami N, Gomatos PJ (1968) Temperature-sensitive conditional-lethal mutants of reovirus 3. I. Isolation and characterization. Virology 36:447-458
    • (1968) Virology , vol.36 , pp. 447-458
    • Ikegami, N.1    Gomatos, P.J.2
  • 85
    • 0000588762 scopus 로고
    • Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein
    • Imani F, Jacobs BL (1988) Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein. Proc Natl Acad Sci U S A 85:7887-7891
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 7887-7891
    • Imani, F.1    Jacobs, B.L.2
  • 86
    • 0015413504 scopus 로고    scopus 로고
    • Ito Y, Joklik WK (1972) Temperature-sensitive mutants of reovirus. I. Patterns of gene expression by mutants of groups C, D, and E. Virology 50:189-201
    • Ito Y, Joklik WK (1972) Temperature-sensitive mutants of reovirus. I. Patterns of gene expression by mutants of groups C, D, and E. Virology 50:189-201
  • 87
    • 0345196599 scopus 로고    scopus 로고
    • Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed sigma3 protein: An approach for analyzing sigma3 functions during virus entry
    • Jané-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 sigma3 protein: an approach for analyzing sigma3 functions during virus entry. J Virol 73:2963-2973
    • (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
  • 88
    • 0036233299 scopus 로고    scopus 로고
    • Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma 3
    • Jané-Valbuena J, Breun LA, Schiff LA, Nibert ML (2002) Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma 3. J Virol 76:5184-5197
    • (2002) J Virol , vol.76 , pp. 5184-5197
    • Jané-Valbuena, J.1    Breun, L.A.2    Schiff, L.A.3    Nibert, M.L.4
  • 89
    • 1542328802 scopus 로고    scopus 로고
    • Emerging themes in rotavirus cell entry, genome organization, transcription and replication
    • Jayaram H, Estes MK, Prasad BVV (2004) Emerging themes in rotavirus cell entry, genome organization, transcription and replication. Virus Res 101:67-81
    • (2004) Virus Res , vol.101 , pp. 67-81
    • Jayaram, H.1    Estes, M.K.2    Prasad, B.V.V.3
  • 90
    • 0023991762 scopus 로고
    • Complete nucleotide sequence of the M2 gene segment of reovirus type 3 Dearing and analysis of its protein product mu 1
    • Jayasuriya AK, Nibert ML, Fields BN (1988) Complete nucleotide sequence of the M2 gene segment of reovirus type 3 Dearing and analysis of its protein product mu 1. Virology 163:591-602
    • (1988) Virology , vol.163 , pp. 591-602
    • Jayasuriya, A.K.1    Nibert, M.L.2    Fields, B.N.3
  • 92
    • 0022330997 scopus 로고
    • Recent progress in reovirus research
    • Joklik WK (1985) Recent progress in reovirus research. Annu Rev Genet 19:537-575
    • (1985) Annu Rev Genet , vol.19 , pp. 537-575
    • Joklik, W.K.1
  • 93
    • 0031900710 scopus 로고    scopus 로고
    • Assembly of the reovirus genome
    • Joklik WK (1998) Assembly of the reovirus genome. Curr Top Microbiol Immunol 233:57-68
    • (1998) Curr Top Microbiol Immunol , vol.233 , pp. 57-68
    • Joklik, W.K.1
  • 94
    • 0028926921 scopus 로고
    • What reassorts when reovirus genome segments reassort?
    • Joklik WK, Roner MR (1995) What reassorts when reovirus genome segments reassort? J Biol Chem 270:4181-4184
    • (1995) J Biol Chem , vol.270 , pp. 4181-4184
    • Joklik, W.K.1    Roner, M.R.2
  • 95
    • 0029687561 scopus 로고    scopus 로고
    • Molecular recognition in the assembly of the segmented reovirus genome
    • Joklik WK, Roner MR (1996) Molecular recognition in the assembly of the segmented reovirus genome. Prog Nucleic Acids Res Mol Biol 53:249-281
    • (1996) Prog Nucleic Acids Res Mol Biol , vol.53 , pp. 249-281
    • Joklik, W.K.1    Roner, M.R.2
  • 96
    • 0037427447 scopus 로고    scopus 로고
    • Conserved intermediates on the assembly pathway of double-stranded RNA bacteriophages
    • Kainov DE, Butcher SJ, Bamford DH, Tuma R (2003) Conserved intermediates on the assembly pathway of double-stranded RNA bacteriophages. J Mol Biol 328:791-804
    • (2003) J Mol Biol , vol.328 , pp. 791-804
    • Kainov, D.E.1    Butcher, S.J.2    Bamford, D.H.3    Tuma, R.4
  • 97
    • 0001659603 scopus 로고    scopus 로고
    • Rotaviruses
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Kapikian AZ, Hoshino Y, Chanock RM (2001) Rotaviruses. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1787-1833
    • (2001) Fields virology , pp. 1787-1833
    • Kapikian, A.Z.1    Hoshino, Y.2    Chanock, R.M.3
  • 98
    • 0028961363 scopus 로고
    • Comparative sequence analysis of the reovirus S4 genes from 13 serotype 1 and serotype 3 field isolates
    • Kedl R, Schmechel S, Schiff L (1995) Comparative sequence analysis of the reovirus S4 genes from 13 serotype 1 and serotype 3 field isolates. J Virol 69:552-559
    • (1995) J Virol , vol.69 , pp. 552-559
    • Kedl, R.1    Schmechel, S.2    Schiff, L.3
  • 99
    • 0036889158 scopus 로고    scopus 로고
    • The hydrophilic amino-terminal arm of reovirus core shell protein lambda1 is dispensable for particle assembly
    • 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 lambda1 is dispensable for particle assembly. J Virol 76:12211-12222
    • (2002) J Virol , vol.76 , 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
  • 100
    • 1542268897 scopus 로고    scopus 로고
    • Orthoreovirus and aquareovirus core proteins: Conserved enzymatic surfaces, but not protein-protein interfaces
    • Kim J, Tao Y, Reinisch KM, Harrison SC, Nibert ML (2004) Orthoreovirus and aquareovirus core proteins: conserved enzymatic surfaces, but not protein-protein interfaces. Virus Res 101:15-28
    • (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
  • 101
    • 0024314726 scopus 로고
    • Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relationship to positive strand RNA viral polymerases
    • Koonin EV, Gorbalenya AE, Chumakov KM (1989) Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relationship to positive strand RNA viral polymerases. FEBS Lett 252:42-46
    • (1989) FEBS Lett , vol.252 , pp. 42-46
    • Koonin, E.V.1    Gorbalenya, A.E.2    Chumakov, K.M.3
  • 102
    • 0001178029 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Lamb RA, Krug RM (2001) Orthomyxoviridae: the viruses and their replication. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1487-1531
    • (2001) Fields virology , pp. 1487-1531
    • Lamb, R.A.1    Krug, R.M.2
  • 103
    • 0028200822 scopus 로고
    • Reovirus exists in the form of 13 particle species that differ in their content of protein sigma 1
    • Larson SM, Antczak JB, Joklik WK (1994) Reovirus exists in the form of 13 particle species that differ in their content of protein sigma 1. Virology 201:303-311
    • (1994) Virology , vol.201 , pp. 303-311
    • Larson, S.M.1    Antczak, J.B.2    Joklik, W.K.3
  • 104
    • 0019510736 scopus 로고
    • Characterization of anti-reovirus immunoglobulins secreted by cloned hybridoma cell lines
    • Lee PW, Hayes EC, Joklik WK (1981a) Characterization of anti-reovirus immunoglobulins secreted by cloned hybridoma cell lines. Virology 108:134-146
    • (1981) Virology , vol.108 , pp. 134-146
    • Lee, P.W.1    Hayes, E.C.2    Joklik, W.K.3
  • 105
    • 0019522275 scopus 로고
    • Protein sigma 1 is the reovirus cell attachment protein
    • Lee PW, Hayes EC, Joklik WK (1981b) Protein sigma 1 is the reovirus cell attachment protein. Virology 108:156-163
    • (1981) Virology , vol.108 , pp. 156-163
    • Lee, P.W.1    Hayes, E.C.2    Joklik, W.K.3
  • 106
    • 0028173555 scopus 로고
    • Reovirus lambda 1 protein: Affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif
    • Lemay G, Danis C (1994) Reovirus lambda 1 protein: affinity for double-stranded nucleic acids by a small amino-terminal region of the protein independent from the zinc finger motif. J Gen Virol 75:3261-3266
    • (1994) J Gen Virol , vol.75 , pp. 3261-3266
    • Lemay, G.1    Danis, C.2
  • 107
    • 0021275359 scopus 로고
    • mRNA discrimination in extracts from uninfected and reovirus-infected L-cells
    • Lemieux R, Zarbl H, Millward S (1984) mRNA discrimination in extracts from uninfected and reovirus-infected L-cells. J Virol 51:215-222
    • (1984) J Virol , vol.51 , pp. 215-222
    • Lemieux, R.1    Zarbl, H.2    Millward, S.3
  • 108
    • 0023280220 scopus 로고
    • The viral protein sigma 3 participates in translation of late viral mRNA in reovirus-infected L cells
    • Lemieux R, Lemay G, Millward S (1987) The viral protein sigma 3 participates in translation of late viral mRNA in reovirus-infected L cells. J Virol 61:2472-2479
    • (1987) J Virol , vol.61 , pp. 2472-2479
    • Lemieux, R.1    Lemay, G.2    Millward, S.3
  • 110
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, mu1, in a complex with is protector protein, Sigma3
    • Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein, mu1, in a complex with is protector protein, Sigma3. Cell 108:283-295
    • (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
  • 111
    • 0027296972 scopus 로고
    • Reovirus M2 gene is associated with chromium release from mouse L cells
    • Lucia-Jandris P, Hooper JW, Fields BN (1993) Reovirus M2 gene is associated with chromium release from mouse L cells. J Virol 67:5339-5345
    • (1993) J Virol , vol.67 , pp. 5339-5345
    • Lucia-Jandris, P.1    Hooper, J.W.2    Fields, B.N.3
  • 113
    • 0036296501 scopus 로고    scopus 로고
    • Mutational analysis of a mammalian reovirus mRNA capping enzyme
    • Luongo CL (2002) Mutational analysis of a mammalian reovirus mRNA capping enzyme. Biochem Biophys Res Commun 291:932-938
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 932-938
    • Luongo, C.L.1
  • 114
    • 0032508690 scopus 로고    scopus 로고
    • Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus lambda2 protein. Evidence for activities in mRNA cap methylation
    • Luongo CL, Contreras CM, Farsetta DL, Nibert ML (1998) Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus lambda2 protein. Evidence for activities in mRNA cap methylation. J Biol Chem 273:23773-23780
    • (1998) J Biol Chem , vol.273 , pp. 23773-23780
    • Luongo, C.L.1    Contreras, C.M.2    Farsetta, D.L.3    Nibert, M.L.4
  • 115
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2
    • Luongo CL, Reinisch KM, Harrison SC, Nibert ML (2000) Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2. J Biol Chem 275:2804-2810
    • (2000) J Biol Chem , vol.275 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 116
    • 0036346029 scopus 로고    scopus 로고
    • Loss of activities for mRNA synthesis accompanies loss of lambda2 spikes from reovirus cores: An effect of lambda2 on lambda1 shell structure
    • Luongo CL, Zhang X, Walker SB, Chen Y, Broering TJ, Farsetta DL, Bowman VD, Baker TS, Nibert ML (2002) Loss of activities for mRNA synthesis accompanies loss of lambda2 spikes from reovirus cores: an effect of lambda2 on lambda1 shell structure. Virology 296:24-38
    • (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
  • 117
    • 0041355333 scopus 로고    scopus 로고
    • Sequence specificity in the interaction of Bluetongue virus non-structural protein 2 (NS2) with viral RNA
    • Lymperopoulos K, Wirblich C, Brierley I, Roy P (2003) Sequence specificity in the interaction of Bluetongue virus non-structural protein 2 (NS2) with viral RNA. J Biol Chem 278:31722-31730
    • (2003) J Biol Chem , vol.278 , pp. 31722-31730
    • Lymperopoulos, K.1    Wirblich, C.2    Brierley, I.3    Roy, P.4
  • 118
    • 0028339916 scopus 로고
    • Mutations in a CCHC zinc-binding motif of the reovirus sigma 3 protein decrease its intracellular stability
    • Mabrouk T, Lemay G (1994) Mutations in a CCHC zinc-binding motif of the reovirus sigma 3 protein decrease its intracellular stability. J Virol 68:5287-5290
    • (1994) J Virol , vol.68 , pp. 5287-5290
    • Mabrouk, T.1    Lemay, G.2
  • 119
    • 0029264544 scopus 로고
    • Two basic motifs of reovirus sigma 3 protein are involved in double-stranded RNA binding
    • Mabrouk T, Danis C, Lemay G (1995) Two basic motifs of reovirus sigma 3 protein are involved in double-stranded RNA binding. Biochem Cell Biol 73:137-145
    • (1995) Biochem Cell Biol , vol.73 , pp. 137-145
    • Mabrouk, T.1    Danis, C.2    Lemay, G.3
  • 120
    • 0027136089 scopus 로고
    • The reovirus M1 gene determines the relative capacity of growth of reovirus in cultured bovine aortic endothelial cells
    • Matoba Y, Colucci WS, Fields BN, Smith TW (1993) The reovirus M1 gene determines the relative capacity of growth of reovirus in cultured bovine aortic endothelial cells. J Clin Invest 92:2883-2888
    • (1993) J Clin Invest , vol.92 , pp. 2883-2888
    • Matoba, Y.1    Colucci, W.S.2    Fields, B.N.3    Smith, T.W.4
  • 121
    • 0016159315 scopus 로고
    • Temperature-sensitive mutants of reovirus. V. Studies on the nature of the temperature-sensitive lesion of the group C mutant ts447
    • Matsuhisa T, Joklik WK (1974) Temperature-sensitive mutants of reovirus. V. Studies on the nature of the temperature-sensitive lesion of the group C mutant ts447. Virology 60:380-389
    • (1974) Virology , vol.60 , pp. 380-389
    • Matsuhisa, T.1    Joklik, W.K.2
  • 122
    • 0034690808 scopus 로고    scopus 로고
    • Reovirus mu2 protein determines strain-specific differences in the rate of viral inclusion formation in L929 cells
    • Mbisa JL, Becker MM, Zou S, Dermody TS, Brown EG (2000) Reovirus mu2 protein determines strain-specific differences in the rate of viral inclusion formation in L929 cells. Virology 272:16-26
    • (2000) Virology , vol.272 , pp. 16-26
    • Mbisa, J.L.1    Becker, M.M.2    Zou, S.3    Dermody, T.S.4    Brown, E.G.5
  • 123
    • 14744276061 scopus 로고    scopus 로고
    • The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging
    • McCown MF, Pekosz A (2005) The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging. J Virol 79:3595-3605
    • (2005) J Virol , vol.79 , pp. 3595-3605
    • McCown, M.F.1    Pekosz, A.2
  • 124
    • 0018083729 scopus 로고
    • The nature of the polypeptide encoded by each of the 10 double-stranded RNA segments of reovirus type 3
    • McCrae MA, Joklik WK (1978) The nature of the polypeptide encoded by each of the 10 double-stranded RNA segments of reovirus type 3. Virology 89:578-593
    • (1978) Virology , vol.89 , pp. 578-593
    • McCrae, M.A.1    Joklik, W.K.2
  • 125
    • 0021187586 scopus 로고
    • Extragenic suppression of temperature-sensitive phenotype in reovirus: Mapping suppressor mutations
    • McPhillips TH, Ramig RF (1984) Extragenic suppression of temperature-sensitive phenotype in reovirus: mapping suppressor mutations. Virology 135:428-439
    • (1984) Virology , vol.135 , pp. 428-439
    • McPhillips, T.H.1    Ramig, R.F.2
  • 126
    • 0038045776 scopus 로고    scopus 로고
    • Mendez II, She Y-M, Ens W, Coombs KM (2003) Digestion pattern of reovirus outer capsid protein sigma3 determined by mass spectrometry. Virology 311:289-304
    • Mendez II, She Y-M, Ens W, Coombs KM (2003) Digestion pattern of reovirus outer capsid protein sigma3 determined by mass spectrometry. Virology 311:289-304
  • 128
    • 0026072563 scopus 로고
    • The three-dimensional structure of reovirus obtained by cryo-electron microscopy
    • Metcalf P, Cyrklaff M, Adrian M (1991) The three-dimensional structure of reovirus obtained by cryo-electron microscopy. EMBO J 10:3129-3136
    • (1991) EMBO J , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 129
    • 0036149374 scopus 로고    scopus 로고
    • Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein mu1
    • Middleton JK, Severson TF, Chandran K, Gillian AL, Yin J, Nibert ML (2002) Thermostability of reovirus disassembly intermediates (ISVPs) correlates with genetic, biochemical, and thermodynamic properties of major surface protein mu1. J Virol 76:1051-1061
    • (2002) J Virol , vol.76 , pp. 1051-1061
    • Middleton, J.K.1    Severson, T.F.2    Chandran, K.3    Gillian, A.L.4    Yin, J.5    Nibert, M.L.6
  • 130
    • 0037383448 scopus 로고    scopus 로고
    • Reovirus sigma NS protein localizes to inclusions through an association requiring the mu NS amino terminus
    • Miller CL, Broering TJ, Parker JS, Arnold MM, Nibert ML (2003) Reovirus sigma NS protein localizes to inclusions through an association requiring the mu NS amino terminus. J Virol 77:4566-4576
    • (2003) J Virol , vol.77 , pp. 4566-4576
    • Miller, C.L.1    Broering, T.J.2    Parker, J.S.3    Arnold, M.M.4    Nibert, M.L.5
  • 131
    • 4544281312 scopus 로고    scopus 로고
    • Increased ubiquitination and other covariant phenotypes attributed to a strain- and temperature-dependent defect of reovirus core protein mu 2
    • Miller CL, Parker JSL, Dinoso JB, Piggott CDS, Perron MJ, Nibert ML (2004) Increased ubiquitination and other covariant phenotypes attributed to a strain- and temperature-dependent defect of reovirus core protein mu 2. J Virol 78:10291-10302
    • (2004) J Virol , vol.78 , pp. 10291-10302
    • Miller, C.L.1    Parker, J.S.L.2    Dinoso, J.B.3    Piggott, C.D.S.4    Perron, M.J.5    Nibert, M.L.6
  • 132
    • 0024831457 scopus 로고
    • The function of reovirus proteins during the reovirus multiplication cycle: Analysis using monoreassortants
    • Moody MD, Joklik WK (1989) The function of reovirus proteins during the reovirus multiplication cycle: analysis using monoreassortants. Virology 173:437-446
    • (1989) Virology , vol.173 , pp. 437-446
    • Moody, M.D.1    Joklik, W.K.2
  • 133
    • 0016146228 scopus 로고
    • Reovirus morphogenesis. Corelike particles in cells infected at 39 degrees with wild-type reovirus and temperature- sensitive mutants of groups B and G
    • Morgan EM, Zweerink HJ (1974) Reovirus morphogenesis. Corelike particles in cells infected at 39 degrees with wild-type reovirus and temperature- sensitive mutants of groups B and G. Virology 59:556-565
    • (1974) Virology , vol.59 , pp. 556-565
    • Morgan, E.M.1    Zweerink, H.J.2
  • 134
    • 0016799069 scopus 로고
    • Characterization of transcriptase and replicase particles isolated from reovirus-infected cells
    • Morgan EM, Zweerink HJ (1975) Characterization of transcriptase and replicase particles isolated from reovirus-infected cells. Virology 68:455-466
    • (1975) Virology , vol.68 , pp. 455-466
    • Morgan, E.M.1    Zweerink, H.J.2
  • 135
    • 0024401164 scopus 로고
    • A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses
    • Morozov SY (1989) A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses. Nucleic Acids Res 17:5394
    • (1989) Nucleic Acids Res , vol.17 , pp. 5394
    • Morozov, S.Y.1
  • 136
    • 0017872929 scopus 로고
    • A genetic map of reovirus. III. Assignment of the double-stranded RNA-positive mutant groups A, B, and G to genome segments
    • Mustoe TA, Ramig RF, Sharpe AH, Fields BN (1978) A genetic map of reovirus. III. Assignment of the double-stranded RNA-positive mutant groups A, B, and G to genome segments. Virology 85:545-556
    • (1978) Virology , vol.85 , pp. 545-556
    • Mustoe, T.A.1    Ramig, R.F.2    Sharpe, A.H.3    Fields, B.N.4
  • 137
    • 0033919812 scopus 로고    scopus 로고
    • Trypsin-induced structural transformation in aquareovirus
    • Nason EL, Samal SK, Prasad BVV (2000) Trypsin-induced structural transformation in aquareovirus. J Virol 74:6546-6555
    • (2000) J Virol , vol.74 , pp. 6546-6555
    • Nason, E.L.1    Samal, S.K.2    Prasad, B.V.V.3
  • 138
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Nibert ML, Schiff LA (2001) Reoviruses and their replication. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1679-1728
    • (2001) Fields virology , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 139
    • 0026088718 scopus 로고
    • Mammalian reoviruses contain amyristoylated structural protein
    • Nibert ML, Schiff LA, Fields BN (1991) Mammalian reoviruses contain amyristoylated structural protein. J Virol 65:1960-1967
    • (1991) J Virol , vol.65 , pp. 1960-1967
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 140
    • 9644268149 scopus 로고    scopus 로고
    • Putative autocleavage of reovirus mu1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization
    • Nibert ML, Odegard AL, Agosto MA, Chandran K, Schiff LA (2005) Putative autocleavage of reovirus mu1 protein in concert with outer-capsid disassembly and activation for membrane permeabilization. J Mol Biol 345:461-474
    • (2005) J Mol Biol , vol.345 , pp. 461-474
    • Nibert, M.L.1    Odegard, A.L.2    Agosto, M.A.3    Chandran, K.4    Schiff, L.A.5
  • 141
    • 34548656690 scopus 로고    scopus 로고
    • Sequences of avian reovirus M1, M2, and M3 genes and predicted structure/function of the encoded μ proteins
    • Nov 14 [epub ahead of print
    • Noad L, Shou J, Coombs KM, Duncan R (2005) Sequences of avian reovirus M1, M2, and M3 genes and predicted structure/function of the encoded μ proteins. Virus Res Nov 14 [epub ahead of print]
    • (2005) Virus Res
    • Noad, L.1    Shou, J.2    Coombs, K.M.3    Duncan, R.4
  • 142
    • 0031055059 scopus 로고    scopus 로고
    • Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1
    • Noble S, Nibert ML (1997a) Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1. J Virol 71:2182-2191
    • (1997) J Virol , vol.71 , pp. 2182-2191
    • Noble, S.1    Nibert, M.L.2
  • 143
    • 0030610264 scopus 로고    scopus 로고
    • Core protein mu2 is a second determinant of nucleoside triphosphatase activities by reovirus cores
    • Noble S, Nibert ML (1997b) Core protein mu2 is a second determinant of nucleoside triphosphatase activities by reovirus cores. J Virol 71:7728-7735
    • (1997) J Virol , vol.71 , pp. 7728-7735
    • Noble, S.1    Nibert, M.L.2
  • 144
    • 0037404548 scopus 로고    scopus 로고
    • Disulfide bonding among mu1 trimers in mammalian reovirus outer capsid: A late and reversible step in virion morphogenesis
    • Odegard AL, Chandran K, Liemann S, Harrison SC, Nibert ML (2003) Disulfide bonding among mu1 trimers in mammalian reovirus outer capsid: a late and reversible step in virion morphogenesis. J Virol 77:5389-5400
    • (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
  • 145
    • 3543115472 scopus 로고    scopus 로고
    • Putative autocleavage of outer capsid protein mu 1, allowing release of myristoylated peptide mu 1N during particle uncoating, is critical for cell entry by reovirus
    • Odegard AL, Chandran K, Zhang X, Parker JSL, Baker TS, Nibert ML (2004) Putative autocleavage of outer capsid protein mu 1, allowing release of myristoylated peptide mu 1N during particle uncoating, is critical for cell entry by reovirus. J Virol 78:8732-8745
    • (2004) J Virol , vol.78 , pp. 8732-8745
    • Odegard, A.L.1    Chandran, K.2    Zhang, X.3    Parker, J.S.L.4    Baker, T.S.5    Nibert, M.L.6
  • 146
    • 0028156236 scopus 로고
    • Rotaviruses: Immunological determinants of protection against infection and disease
    • Offit PA (1994) Rotaviruses: immunological determinants of protection against infection and disease. Adv Virus Res 44:161-202
    • (1994) Adv Virus Res , vol.44 , pp. 161-202
    • Offit, P.A.1
  • 147
    • 0035282959 scopus 로고    scopus 로고
    • Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution
    • Olland AM, Jane-Valbuena J, Schiff LA, Nibert ML, Harrison SC (2001) Structure of the reovirus outer capsid and dsRNA-binding protein σ3 at 1.8 Å resolution. EMBO J 20:979-989
    • (2001) EMBO J , vol.20 , pp. 979-989
    • Olland, A.M.1    Jane-Valbuena, J.2    Schiff, L.A.3    Nibert, M.L.4    Harrison, S.C.5
  • 148
    • 0036223620 scopus 로고    scopus 로고
    • Reovirus core protein mu 2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules
    • Parker JSL, Broering TJ, Kim J, Higgins DE, Nibert ML (2002) Reovirus core protein mu 2 determines the filamentous morphology of viral inclusion bodies by interacting with and stabilizing microtubules. J Virol 76:4483-4496
    • (2002) J Virol , vol.76 , pp. 4483-4496
    • Parker, J.S.L.1    Broering, T.J.2    Kim, J.3    Higgins, D.E.4    Nibert, M.L.5
  • 149
    • 0035947373 scopus 로고    scopus 로고
    • Generation and genetic characterization of avian reovirus temperature-sensitive mutants
    • Patrick M, Duncan R, Coombs KM (2001) Generation and genetic characterization of avian reovirus temperature-sensitive mutants. Virology 284:113-122
    • (2001) Virology , vol.284 , pp. 113-122
    • Patrick, M.1    Duncan, R.2    Coombs, K.M.3
  • 150
    • 0022610668 scopus 로고
    • Electrophoretic separation of the plus and minus strands of rotavirus SA11 double-stranded RNAs
    • Patton JT, Stacy-Phipps S (1986) Electrophoretic separation of the plus and minus strands of rotavirus SA11 double-stranded RNAs. J Virol Methods 13:185-190
    • (1986) J Virol Methods , vol.13 , pp. 185-190
    • Patton, J.T.1    Stacy-Phipps, S.2
  • 151
    • 6944226714 scopus 로고    scopus 로고
    • Replication and transcription of the rotavirus genome
    • Patton JT, Carpi RVD, Spencer E (2004) Replication and transcription of the rotavirus genome. Curr Pharma Design 10:3769-3777
    • (2004) Curr Pharma Design , vol.10 , pp. 3769-3777
    • Patton, J.T.1    Carpi, R.V.D.2    Spencer, E.3
  • 152
    • 1542328800 scopus 로고    scopus 로고
    • Self-assembly of double-stranded RNA bacteriophages
    • Poranen MM, Tuma R (2004) Self-assembly of double-stranded RNA bacteriophages. Virus Res 101:93-100
    • (2004) Virus Res , vol.101 , pp. 93-100
    • Poranen, M.M.1    Tuma, R.2
  • 153
    • 0035002345 scopus 로고    scopus 로고
    • Self-assembly of a viral molecular machine from purified protein and RNA constituents
    • Poranen MM, Paatero AO, Tuma R, Bamford DH (2001) Self-assembly of a viral molecular machine from purified protein and RNA constituents. Mol Cell 7:845-854
    • (2001) Mol Cell , vol.7 , pp. 845-854
    • Poranen, M.M.1    Paatero, A.O.2    Tuma, R.3    Bamford, D.H.4
  • 154
    • 0344982823 scopus 로고    scopus 로고
    • Identification of two histidines necessary for reovirus mRNA guanylyltransferase activity
    • Qiu T, Luongo CL (2003) Identification of two histidines necessary for reovirus mRNA guanylyltransferase activity. Virology 316:313-324
    • (2003) Virology , vol.316 , pp. 313-324
    • Qiu, T.1    Luongo, C.L.2
  • 155
    • 0014159970 scopus 로고
    • Electron microscopic studies of animal viruses with emphasis on in vivo infections
    • Rabin ER, Jenson AB (1967) Electron microscopic studies of animal viruses with emphasis on in vivo infections. Prog Med Virol 9:392-450
    • (1967) Prog Med Virol , vol.9 , pp. 392-450
    • Rabin, E.R.1    Jenson, A.B.2
  • 156
    • 0031901691 scopus 로고    scopus 로고
    • Suppression and reversion of mutant phenotype in reovirus
    • Ramig RF (1998) Suppression and reversion of mutant phenotype in reovirus. Curr Top Microbiol Immunol 233:109-135
    • (1998) Curr Top Microbiol Immunol , vol.233 , pp. 109-135
    • Ramig, R.F.1
  • 157
    • 0018424520 scopus 로고
    • Revertants of temperature-sensitive mutants of reovirus: Evidence for frequent extragenic suppression
    • Ramig RF, Fields BN (1979) Revertants of temperature-sensitive mutants of reovirus: evidence for frequent extragenic suppression. Virology 92:155-167
    • (1979) Virology , vol.92 , pp. 155-167
    • Ramig, R.F.1    Fields, B.N.2
  • 158
    • 0002116121 scopus 로고
    • Genetics of reovirus
    • ed The Reoviridae. Plenum, New York, pp
    • Ramig RF, Fields BN (1983) Genetics of reovirus. In: Jolik WK (ed) The Reoviridae. Plenum, New York, pp 197-228
    • (1983) Jolik WK , pp. 197-228
    • Ramig, R.F.1    Fields, B.N.2
  • 159
    • 0017804481 scopus 로고
    • A genetic map of reovirus. II. Assignment of the double-stranded RNA-negative mutant groups C, D, and E to genome segments
    • Ramig RF, Mustoe TA, Sharpe AH, Fields BN (1978) A genetic map of reovirus. II. Assignment of the double-stranded RNA-negative mutant groups C, D, and E to genome segments. Virology 85:531-534
    • (1978) Virology , vol.85 , pp. 531-534
    • Ramig, R.F.1    Mustoe, T.A.2    Sharpe, A.H.3    Fields, B.N.4
  • 160
    • 0020637199 scopus 로고    scopus 로고
    • Ramig RF, Ahmed R, Fields BN (1983) A genetic map of reovirus: assignment of the newly defined mutant groups H, I, and J to genome segments. Virology 125:299-313
    • Ramig RF, Ahmed R, Fields BN (1983) A genetic map of reovirus: assignment of the newly defined mutant groups H, I, and J to genome segments. Virology 125:299-313
  • 161
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • Reinisch KM, Nibert ML, Harrison SC (2000) Structure of the reovirus core at 3.6 Å resolution. Nature 404:960-967
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 162
    • 0001530748 scopus 로고
    • Cytochemical, fluorescent-antibody and electron microscopic studies on the growth of reovirus (Echo 10) in tissue culture
    • Rhim JS, Jordan LE, Mayor HD (1962) Cytochemical, fluorescent-antibody and electron microscopic studies on the growth of reovirus (Echo 10) in tissue culture. Virology 17:342-355
    • (1962) Virology , vol.17 , pp. 342-355
    • Rhim, J.S.1    Jordan, L.E.2    Mayor, H.D.3
  • 163
    • 0031707093 scopus 로고    scopus 로고
    • Reovirus growth in cell culture does not require the full complement of viral proteins: Identification of a σ1s-null mutant
    • Rodgers SE, Connolly JL, Chappell JD, Dermody TS (1998) Reovirus growth in cell culture does not require the full complement of viral proteins: identification of a σ1s-null mutant. J Virol 72:8597-8604
    • (1998) J Virol , vol.72 , pp. 8597-8604
    • Rodgers, S.E.1    Connolly, J.L.2    Chappell, J.D.3    Dermody, T.S.4
  • 164
    • 0033257949 scopus 로고    scopus 로고
    • Rescue systems for dsRNA viruses of higher organisms
    • Roner MR (1999) Rescue systems for dsRNA viruses of higher organisms. Adv Virus Res 53:355-367
    • (1999) Adv Virus Res , vol.53 , pp. 355-367
    • Roner, M.R.1
  • 165
    • 0034937715 scopus 로고    scopus 로고
    • Reovirus reverse genetics: Incorporation of the CAT gene into the reovirus genome
    • Roner MR, Joklik WK (2001) Reovirus reverse genetics: Incorporation of the CAT gene into the reovirus genome. Proc Natl Acad Sci U S A 98:8036-8041
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8036-8041
    • Roner, M.R.1    Joklik, W.K.2
  • 167
    • 0029558023 scopus 로고
    • Identification of signals required for the insertion of heterologous genome segments into the reovirus genome
    • Roner MR, Lin PN, Nepluev I, Kong LJ, Joklik WK (1995) Identification of signals required for the insertion of heterologous genome segments into the reovirus genome. Proc Natl Acad Sci U S A 92:12362-12366
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12362-12366
    • Roner, M.R.1    Lin, P.N.2    Nepluev, I.3    Kong, L.J.4    Joklik, W.K.5
  • 168
    • 0030930495 scopus 로고    scopus 로고
    • Construction and characterization of a reovirus double temperature-sensitive mutant
    • Roner MR, Nepliouev I, Sherry B, Joklik WK (1997) Construction and characterization of a reovirus double temperature-sensitive mutant. Proc Natl Acad Sci U S A 94:6826-6830
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6826-6830
    • Roner, M.R.1    Nepliouev, I.2    Sherry, B.3    Joklik, W.K.4
  • 169
    • 7044226236 scopus 로고    scopus 로고
    • Identification of the 5′ sequences required for incorporation of an engineered ssRNA into the reovirus genome
    • Roner MR, Bassett K, Roehr, J (2004) Identification of the 5′ sequences required for incorporation of an engineered ssRNA into the reovirus genome. Virology 329:348-360
    • (2004) Virology , vol.329 , pp. 348-360
    • Roner, M.R.1    Bassett, K.2    Roehr, J.3
  • 170
    • 0242721455 scopus 로고    scopus 로고
    • Incorporation of epitope-tagged viral sigma 3 proteins to reovirus virions
    • Rouault E, Lemay G (2003) Incorporation of epitope-tagged viral sigma 3 proteins to reovirus virions. Can J Microbiol 49:407-417
    • (2003) Can J Microbiol , vol.49 , pp. 407-417
    • Rouault, E.1    Lemay, G.2
  • 171
    • 0008512898 scopus 로고    scopus 로고
    • Orbiviruses
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Roy P (2001) Orbiviruses. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1835-1869
    • (2001) Fields virology , pp. 1835-1869
    • Roy, P.1
  • 172
    • 0031949549 scopus 로고    scopus 로고
    • Reovirus capsid proteins sigma3 and mu 1: Interactions that influence viral entry, assembly, and translational control
    • Schiff LA (1998)Reovirus capsid proteins sigma3 and mu 1: interactions that influence viral entry, assembly, and translational control. Curr Top Microbiol Immunol 233:167-183
    • (1998) Curr Top Microbiol Immunol , vol.233 , pp. 167-183
    • Schiff, L.A.1
  • 173
    • 0023673325 scopus 로고
    • Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3
    • Schiff LA, Nibert ML, Co MS, Brown EG, Fields BN (1988) Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3. Mol Cell Biol 8:273-283
    • (1988) Mol Cell Biol , vol.8 , pp. 273-283
    • Schiff, L.A.1    Nibert, M.L.2    Co, M.S.3    Brown, E.G.4    Fields, B.N.5
  • 174
    • 18744380673 scopus 로고    scopus 로고
    • Genome replication and progeny virion production of herpes simplex virus type 1 mutants with temperature-sensitive lesions in the origin-binding protein
    • Schildgen O, Graper S, Blumel J, Matz B (2005) Genome replication and progeny virion production of herpes simplex virus type 1 mutants with temperature-sensitive lesions in the origin-binding protein. J Virol 79:7273-7278
    • (2005) J Virol , vol.79 , pp. 7273-7278
    • Schildgen, O.1    Graper, S.2    Blumel, J.3    Matz, B.4
  • 175
    • 0030921401 scopus 로고    scopus 로고
    • Preferential translation of reovirus mRNA by a sigma3-dependent mechanism
    • Schmechel S, Chute M, Skinner P, Anderson R, Schiff L (1997) Preferential translation of reovirus mRNA by a sigma3-dependent mechanism. Virology 232:62-73
    • (1997) Virology , vol.232 , pp. 62-73
    • Schmechel, S.1    Chute, M.2    Skinner, P.3    Anderson, R.4    Schiff, L.5
  • 176
    • 0027242115 scopus 로고
    • Analysis of a temperature-sensitive mutation affecting the integration protein of Moloney murine leukemia virus
    • Schwartzberg PL, Roth MJ, Tanese N, Goff SP (1993) Analysis of a temperature-sensitive mutation affecting the integration protein of Moloney murine leukemia virus. Virology 192:673-678
    • (1993) Virology , vol.192 , pp. 673-678
    • Schwartzberg, P.L.1    Roth, M.J.2    Tanese, N.3    Goff, S.P.4
  • 177
    • 0033653368 scopus 로고    scopus 로고
    • Transient resistance of influenza virus to interferon action attributed to random multiple packaging and activity of NS genes
    • Sekellick MJ, Carra SA, Bowman A, Hopkins DA, Marcus PI (2000) Transient resistance of influenza virus to interferon action attributed to random multiple packaging and activity of NS genes. J Interferon Cytokine Res 20:963-970
    • (2000) J Interferon Cytokine Res , vol.20 , pp. 963-970
    • Sekellick, M.J.1    Carra, S.A.2    Bowman, A.3    Hopkins, D.A.4    Marcus, P.I.5
  • 178
    • 0019516611 scopus 로고
    • Reovirus inhibition of cellular DNA synthesis: Role of the S1 gene
    • Sharpe AH, Fields BN (1981) Reovirus inhibition of cellular DNA synthesis: role of the S1 gene. J Virol 38:389-392
    • (1981) J Virol , vol.38 , pp. 389-392
    • Sharpe, A.H.1    Fields, B.N.2
  • 179
    • 0020378988 scopus 로고
    • Reovirus inhibition of cellular RNA and protein synthesis: Role of the S4 gene
    • Sharpe AH, Fields BN (1982) Reovirus inhibition of cellular RNA and protein synthesis: role of the S4 gene. Virology 122:381-391
    • (1982) Virology , vol.122 , pp. 381-391
    • Sharpe, A.H.1    Fields, B.N.2
  • 180
    • 0016272591 scopus 로고
    • Methylated messenger RNA synthesis in vitro by purified reovirus
    • Shatkin AJ (1974) Methylated messenger RNA synthesis in vitro by purified reovirus. Proc Natl Acad Sci U S A 71:3204-3207
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 3204-3207
    • Shatkin, A.J.1
  • 181
    • 0002388168 scopus 로고
    • Biochemical aspects of reovirus transcription and translation
    • ed The Reoviridae. Plenum, New York, pp
    • Shatkin AJ, Kozak M (1983) Biochemical aspects of reovirus transcription and translation. In: Jolik WK (ed) The Reoviridae. Plenum, New York, pp 79-106
    • (1983) Jolik WK , pp. 79-106
    • Shatkin, A.J.1    Kozak, M.2
  • 182
    • 0015416711 scopus 로고
    • Transcription by infectious subviral particles of reovirus
    • Shatkin AJ, LaFiandra AJ (1972) Transcription by infectious subviral particles of reovirus. J Virol 10:698-706
    • (1972) J Virol , vol.10 , pp. 698-706
    • Shatkin, A.J.1    LaFiandra, A.J.2
  • 183
    • 0028889733 scopus 로고
    • Association of reovirus outer capsid proteins sigma 3 andmu 1 causes a conformational change that renders sigma 3 protease sensitive
    • Shepard DA, Ehnstrom JG, Schiff LA (1995) Association of reovirus outer capsid proteins sigma 3 andmu 1 causes a conformational change that renders sigma 3 protease sensitive. J Virol 69:8180-8184
    • (1995) J Virol , vol.69 , pp. 8180-8184
    • Shepard, D.A.1    Ehnstrom, J.G.2    Schiff, L.A.3
  • 184
    • 0030047557 scopus 로고    scopus 로고
    • Mutations in the zinc-binding motif of the reovirus capsid protein delta 3 eliminate its ability to associate with capsid protein mu 1
    • Shepard DA, Ehnstrom JG, Skinner PJ, Schiff LA (1996) Mutations in the zinc-binding motif of the reovirus capsid protein delta 3 eliminate its ability to associate with capsid protein mu 1. J Virol 70:2065-2068
    • (1996) J Virol , vol.70 , pp. 2065-2068
    • Shepard, D.A.1    Ehnstrom, J.G.2    Skinner, P.J.3    Schiff, L.A.4
  • 185
    • 0024465775 scopus 로고
    • The reovirus M1 gene, encoding a viral core protein, is associated with themyocarditic phenotype of a reovirus variant
    • Sherry B, Fields BN (1989) The reovirus M1 gene, encoding a viral core protein, is associated with themyocarditic phenotype of a reovirus variant. J Virol 63:4850-4856
    • (1989) J Virol , vol.63 , pp. 4850-4856
    • Sherry, B.1    Fields, B.N.2
  • 186
    • 0030580588 scopus 로고    scopus 로고
    • Assembly of the reovirus outer capsid requires mu 1/sigma 3 interactions which are prevented by misfolded sigma 3 protein in temperature-sensitive mutant tsG453
    • Shing M, Coombs KM (1996) Assembly of the reovirus outer capsid requires mu 1/sigma 3 interactions which are prevented by misfolded sigma 3 protein in temperature-sensitive mutant tsG453. Virus Res 46:19-29
    • (1996) Virus Res , vol.46 , pp. 19-29
    • Shing, M.1    Coombs, K.M.2
  • 189
    • 0018864693 scopus 로고
    • Reovirus-induced modification of cap-dependent translation in infected L cells
    • Skup D, Millward S (1980) Reovirus-induced modification of cap-dependent translation in infected L cells. Proc Natl Acad Sci U S A 77:152-156
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 152-156
    • Skup, D.1    Millward, S.2
  • 190
    • 13444259767 scopus 로고    scopus 로고
    • Involvement of the interferon-regulated antiviral proteins PKR and RNase L in reovirus-induced shutoff of cellular translation
    • Smith JA, Schmechel SC, Williams BR, Silverman RH, Schiff LA (2005) Involvement of the interferon-regulated antiviral proteins PKR and RNase L in reovirus-induced shutoff of cellular translation. J Virol 79:2240-2250
    • (2005) J Virol , vol.79 , pp. 2240-2250
    • Smith, J.A.1    Schmechel, S.C.2    Williams, B.R.3    Silverman, R.H.4    Schiff, L.A.5
  • 191
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus type 3
    • Smith RE, Zweerink HJ, Joklik WK (1969) Polypeptide components of virions, top component and cores of reovirus type 3. Virology 39:791-810
    • (1969) Virology , vol.39 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 192
    • 0017253776 scopus 로고
    • Regulated transcription of the genomes of defective virions and temperature-sensitive mutants of reovirus
    • Spandidos DA, Krystal G, Graham AF (1976) Regulated transcription of the genomes of defective virions and temperature-sensitive mutants of reovirus. J Virol 18:7-19
    • (1976) J Virol , vol.18 , pp. 7-19
    • Spandidos, D.A.1    Krystal, G.2    Graham, A.F.3
  • 193
    • 0031257722 scopus 로고    scopus 로고
    • IRIS explorer software for radial-depth cueing reovirus particles and other macromolecular structures determined by cryoelectron microscopy and image reconstruction
    • Spencer SM, Sgro JY, Dryden KA, Baker TS, Nibert ML (1997) IRIS explorer software for radial-depth cueing reovirus particles and other macromolecular structures determined by cryoelectron microscopy and image reconstruction. J Struct Biol 120:11-21
    • (1997) J Struct Biol , vol.120 , pp. 11-21
    • Spencer, S.M.1    Sgro, J.Y.2    Dryden, K.A.3    Baker, T.S.4    Nibert, M.L.5
  • 194
    • 1842649747 scopus 로고
    • Binding to selected regions of reovirus mRNAs by a nonstructural reovirus protein
    • Stamatos NM, Gomatos PJ (1982) Binding to selected regions of reovirus mRNAs by a nonstructural reovirus protein. Proc Natl Acad Sci U S A 79:3457-3461
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 3457-3461
    • Stamatos, N.M.1    Gomatos, P.J.2
  • 195
    • 0027177215 scopus 로고
    • Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase
    • Starnes MC, Joklik WK (1993) Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase. Virology 193:356-366
    • (1993) Virology , vol.193 , pp. 356-366
    • Starnes, M.C.1    Joklik, W.K.2
  • 196
    • 0025866624 scopus 로고
    • Biochemical and biophysical characterization of the reovirus cell attachment protein sigma 1: Evidence that it is a homotrimer
    • Strong JE, Leone G, Duncan R, Sharma RK, Lee PW (1991) Biochemical and biophysical characterization of the reovirus cell attachment protein sigma 1: evidence that it is a homotrimer. Virology 184:23-32
    • (1991) Virology , vol.184 , pp. 23-32
    • Strong, J.E.1    Leone, G.2    Duncan, R.3    Sharma, R.K.4    Lee, P.W.5
  • 197
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker LJ, Nibert M, Furlong D, Fields BN (1987) Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J Virol 61:2351-2361
    • (1987) J Virol , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 198
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-structural studies of reovirus polymerase lambda3
    • Tao Y, Farsetta DL, Nibert ML, Harrison SC (2002) RNA synthesis in a cage-structural studies of reovirus polymerase lambda3. Cell 111:733-745
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 199
    • 1542268891 scopus 로고    scopus 로고
    • Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae
    • 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
    • (2004) Virus Res , vol.101 , pp. 57-66
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 200
    • 0026608639 scopus 로고
    • Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells
    • Tillotson L, Shatkin AJ (1992) Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells. J Virol 66:2180-2186
    • (1992) J Virol , vol.66 , pp. 2180-2186
    • Tillotson, L.1    Shatkin, A.J.2
  • 201
    • 0027429139 scopus 로고
    • Ion channels induced in lipid bilayers by subvirion particles of the nonenveloped mammalian reoviruses
    • Tosteson MT, Nibert ML, Fields BN (1993) Ion channels induced in lipid bilayers by subvirion particles of the nonenveloped mammalian reoviruses. Proc Natl Acad Sci U S A 90:10549-10552
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10549-10552
    • Tosteson, M.T.1    Nibert, M.L.2    Fields, B.N.3
  • 202
    • 0001578626 scopus 로고    scopus 로고
    • Mammalian reoviruses
    • Knipe DM, Howley M, Griffen DE et al eds, Lippincott Williams & Wilkins, Philadelphia, pp
    • Tyler KL (2001) Mammalian reoviruses. In: Knipe DM, Howley M, Griffen DE et al (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 1729-1745
    • (2001) Fields virology , pp. 1729-1745
    • Tyler, K.L.1
  • 203
    • 0022449010 scopus 로고
    • Distinct pathways of viral spread in the host determined by reovirus S1 gene segment
    • Tyler KL, McPhee DA, Fields BN (1986) Distinct pathways of viral spread in the host determined by reovirus S1 gene segment. Science 233:770-774
    • (1986) Science , vol.233 , pp. 770-774
    • Tyler, K.L.1    McPhee, D.A.2    Fields, B.N.3
  • 205
    • 0015400079 scopus 로고
    • Association of reovirus mRNA with viral proteins: A possible mechanism for linking the genome segments
    • Ward RL, Shatkin AJ (1972) Association of reovirus mRNA with viral proteins: a possible mechanism for linking the genome segments. Arch Biochem Biophys 152:378-384
    • (1972) Arch Biochem Biophys , vol.152 , pp. 378-384
    • Ward, R.L.1    Shatkin, A.J.2
  • 206
    • 0015251012 scopus 로고
    • Reovirus-specific ribonucleic acid from polysomes of infected L cells
    • Ward R, Banerjee AK, LaFiandra A, Shatkin AJ (1972) Reovirus-specific ribonucleic acid from polysomes of infected L cells. J Virol 9:61-69
    • (1972) J Virol , vol.9 , pp. 61-69
    • Ward, R.1    Banerjee, A.K.2    LaFiandra, A.3    Shatkin, A.J.4
  • 207
    • 0141856265 scopus 로고    scopus 로고
    • Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes
    • Watanabe T, Watanabe S, Noda T, Fujii Y, Kawaoka Y (2003) Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes. J Virol 77:10575-10583
    • (2003) J Virol , vol.77 , pp. 10575-10583
    • Watanabe, T.1    Watanabe, S.2    Noda, T.3    Fujii, Y.4    Kawaoka, Y.5
  • 208
    • 0014058302 scopus 로고
    • Selective inhibition of reovirus ribonucleic acid synthesis by cycloheximide
    • Watanabe Y, Kudo H, Graham AF (1967) Selective inhibition of reovirus ribonucleic acid synthesis by cycloheximide. J Virol 1:36-44
    • (1967) J Virol , vol.1 , pp. 36-44
    • Watanabe, Y.1    Kudo, H.2    Graham, A.F.3
  • 209
    • 0014433097 scopus 로고
    • Regulation of transcription of the reovirus genome
    • Watanabe Y, Millward S, Graham AF (1968) Regulation of transcription of the reovirus genome. J Mol Biol 36:107-123
    • (1968) J Mol Biol , vol.36 , pp. 107-123
    • Watanabe, Y.1    Millward, S.2    Graham, A.F.3
  • 211
    • 0018150839 scopus 로고
    • Identification of the gene coding for the hemagglutinin of reovirus
    • Weiner HL, Ramig RF, Mustoe TA, Fields BN (1978) Identification of the gene coding for the hemagglutinin of reovirus. Virology 86:581-584
    • (1978) Virology , vol.86 , pp. 581-584
    • Weiner, H.L.1    Ramig, R.F.2    Mustoe, T.A.3    Fields, B.N.4
  • 212
    • 0018818532 scopus 로고
    • Absolute linkage of virulence and central nervous system cell tropism of reoviruses to viral hemagglutinin
    • Weiner HL, Powers ML, Fields BN (1980) Absolute linkage of virulence and central nervous system cell tropism of reoviruses to viral hemagglutinin. J Infect Dis 141:609-616
    • (1980) J Infect Dis , vol.141 , pp. 609-616
    • Weiner, H.L.1    Powers, M.L.2    Fields, B.N.3
  • 213
    • 0017295002 scopus 로고
    • Studies on the structure of reovirus cores: Selective removal of polypeptide lambda 2
    • White CK, Zweerink HJ (1976) Studies on the structure of reovirus cores: selective removal of polypeptide lambda 2. Virology 70:171-180
    • (1976) Virology , vol.70 , pp. 171-180
    • White, C.K.1    Zweerink, H.J.2
  • 214
    • 0023511779 scopus 로고
    • Comparison of the reovirus serotype 1, 2, and 3 S3 genome segments encoding the nonstructural protein sigma NS
    • Wiener JR, Joklik WK (1987) Comparison of the reovirus serotype 1, 2, and 3 S3 genome segments encoding the nonstructural protein sigma NS. Virology 161:332-339
    • (1987) Virology , vol.161 , pp. 332-339
    • Wiener, J.R.1    Joklik, W.K.2
  • 215
    • 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
    • Wiener JR, Joklik WK (1989) 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 169:194-203
    • (1989) Virology , vol.169 , pp. 194-203
    • Wiener, J.R.1    Joklik, W.K.2
  • 216
    • 0024477320 scopus 로고
    • The sequences of reovirus serotype 3 genome segments M1 and M3 encoding the minor protein mu 2 and the major nonstructural protein mu NS, respectively
    • Wiener JR, Bartlett JA, Joklik WK (1989a) The sequences of reovirus serotype 3 genome segments M1 and M3 encoding the minor protein mu 2 and the major nonstructural protein mu NS, respectively. Virology 169:293-304
    • (1989) Virology , vol.169 , pp. 293-304
    • Wiener, J.R.1    Bartlett, J.A.2    Joklik, W.K.3
  • 217
    • 0024566698 scopus 로고
    • The sequences of the S2 genome segments of reovirus serotype 3 and of the dsRNA-negative mutant ts447
    • Wiener JR, McLaughlin T, Joklik WK (1989b) The sequences of the S2 genome segments of reovirus serotype 3 and of the dsRNA-negative mutant ts447. Virology 170:340-341
    • (1989) Virology , vol.170 , pp. 340-341
    • Wiener, J.R.1    McLaughlin, T.2    Joklik, W.K.3
  • 218
    • 0027993529 scopus 로고
    • Association of the reovirus S1 gene with serotype 3-induced biliary atresia in mice
    • Wilson GA, Morrison LA, Fields BN (1994) Association of the reovirus S1 gene with serotype 3-induced biliary atresia in mice. J Virol 68:6458-6465
    • (1994) J Virol , vol.68 , pp. 6458-6465
    • Wilson, G.A.1    Morrison, L.A.2    Fields, B.N.3
  • 219
    • 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
  • 220
    • 4644319640 scopus 로고    scopus 로고
    • Avian reovirus temperature-sensitive mutant tsA12 has a lesion in major core protein sigma A and is defective in assembly
    • Xu W, Patrick MK, Hazelton PR, Coombs KM (2004) Avian reovirus temperature-sensitive mutant tsA12 has a lesion in major core protein sigma A and is defective in assembly. J Virol 78:11142-11151
    • (2004) J Virol , vol.78 , pp. 11142-11151
    • Xu, W.1    Patrick, M.K.2    Hazelton, P.R.3    Coombs, K.M.4
  • 221
    • 22544459335 scopus 로고    scopus 로고
    • Assignment of avian reovirus temperature-sensitive mutant recombination groups B, C, and D to genome segments
    • Xu W, Tran AT, Patrick MK, Coombs KM (2005) Assignment of avian reovirus temperature-sensitive mutant recombination groups B, C, and D to genome segments. Virology 338:227-235
    • (2005) Virology , vol.338 , pp. 227-235
    • Xu, W.1    Tran, A.T.2    Patrick, M.K.3    Coombs, K.M.4
  • 222
    • 0000234954 scopus 로고    scopus 로고
    • Transcriptionally active reovirus core particles visualized by electron cryo-microscopy and image reconstruction
    • Yeager M, Weiner SG, Coombs KM (1996) Transcriptionally active reovirus core particles visualized by electron cryo-microscopy and image reconstruction. Biophys J 70:484
    • (1996) Biophys J , vol.70 , pp. 484
    • Yeager, M.1    Weiner, S.G.2    Coombs, K.M.3
  • 223
    • 0030030595 scopus 로고    scopus 로고
    • The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles
    • Yin P, Cheang M, Coombs KM (1996) The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles. J Virol 70:1223-1227
    • (1996) J Virol , vol.70 , pp. 1223-1227
    • Yin, P.1    Cheang, M.2    Coombs, K.M.3
  • 225
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 angstrom
    • Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS (2003) Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 angstrom. Nature Struct Biol 10:1011-1018
    • (2003) Nature 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
  • 226
    • 27644594455 scopus 로고    scopus 로고
    • Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction
    • Zhang X, Tang J, Walker SB, O'Hara D, Nibert ML, Duncan R, Baker TS (2005) Structure of avian orthoreovirus virion by electron cryomicroscopy and image reconstruction. Virology 343:25-35
    • (2005) Virology , vol.343 , pp. 25-35
    • Zhang, X.1    Tang, J.2    Walker, S.B.3    O'Hara, D.4    Nibert, M.L.5    Duncan, R.6    Baker, T.S.7
  • 227
    • 0026606507 scopus 로고
    • Identification of sequence elements containing signals for replication and encapsidation of the reovirus M1 genome segment
    • Zou S, Brown EG (1992) Identification of sequence elements containing signals for replication and encapsidation of the reovirus M1 genome segment. Virology 186:377-388
    • (1992) Virology , vol.186 , pp. 377-388
    • Zou, S.1    Brown, E.G.2
  • 228
    • 0029971762 scopus 로고    scopus 로고
    • Stable expression of the reovirus mu2 protein in mouse L cells complements the growth of a reovirus ts mutant with a defect in its M1 gene
    • Zou S, Brown EG (1996) Stable expression of the reovirus mu2 protein in mouse L cells complements the growth of a reovirus ts mutant with a defect in its M1 gene. Virology 217:42-48
    • (1996) Virology , vol.217 , pp. 42-48
    • Zou, S.1    Brown, E.G.2


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