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Volumn 246, Issue 2, 1998, Pages 199-210

Characterization of the thermosensitive ts453 reovirus mutant: Increased dsRNA binding of σ3 protein correlates with interferon resistance

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON;

EID: 0032486592     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9188     Document Type: Article
Times cited : (28)

References (71)
  • 1
    • 0028061661 scopus 로고
    • Proteolytic processing of reovirus is required for adherence to intestinal M cells
    • Amerongen H. M., Wilson G. R., Fields B. N., Neutra M. R. Proteolytic processing of reovirus is required for adherence to intestinal M cells. J. Virol. 68:1994;8428-8432.
    • (1994) J. Virol. , vol.68 , pp. 8428-8432
    • Amerongen, H.M.1    Wilson, G.R.2    Fields, B.N.3    Neutra, M.R.4
  • 2
    • 0025249289 scopus 로고
    • Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice
    • Bass D. M., Bodkin D., Dambrauskas R., Trier J. S., Fields B. N., Wolf J. L. Intraluminal proteolytic activation plays an important role in replication of type 1 reovirus in the intestines of neonatal mice. J. Virol. 64:1990;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
  • 3
    • 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 K. L., Tartaglia J., Perkus M. E., Paoletti E., Jacobs B. L. Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J. Virol. 69:1995;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
  • 4
    • 0024418092 scopus 로고
    • Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice
    • Bodkin D. K., Nibert M. L., Fields B. N. Proteolytic digestion of reovirus in the intestinal lumens of neonatal mice. J. Virol. 63:1989;4676-4681.
    • (1989) J. Virol. , vol.63 , pp. 4676-4681
    • Bodkin, D.K.1    Nibert, M.L.2    Fields, B.N.3
  • 5
    • 0015794052 scopus 로고
    • Specific monovalent cation effects on modification of reovirus infectivity by chymotrypsin digestionin vitro.
    • Borsa J., Sargent M. D., Copps T. P., Long D. G., Chapman J. D. Specific monovalent cation effects on modification of reovirus infectivity by chymotrypsin digestionin vitro. J. Virol. 11:1973;1017-1019.
    • (1973) J. Virol. , vol.11 , pp. 1017-1019
    • Borsa, J.1    Sargent, M.D.2    Copps, T.P.3    Long, D.G.4    Chapman, J.D.5
  • 7
    • 0018577837 scopus 로고
    • Alterations in nuclear structure and function in reovirus-infected cells
    • Chaly N., Johnstone M., Hand R. Alterations in nuclear structure and function in reovirus-infected cells. Clin. Invest. Med. 2:1980;141-152.
    • (1980) Clin. Invest. Med. , vol.2 , pp. 141-152
    • Chaly, N.1    Johnstone, M.2    Hand, R.3
  • 8
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced double-stranded RNA-dependent protein kinase
    • Chang H.-W., Jacobs B. L. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced double-stranded RNA-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 89:1992;4825-4829.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4825-4829
    • Chang, H.-W.1    Jacobs, B.L.2
  • 9
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 13:1974;222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 10
    • 0015440085 scopus 로고
    • Temperature-sensitive mutants of reovirus type 3: Studies on the synthesis of viral RNA
    • Cross R. K., Fields B. N. Temperature-sensitive mutants of reovirus type 3: Studies on the synthesis of viral RNA. J. Virol. 50:1972;799-809.
    • (1972) J. Virol. , vol.50 , pp. 799-809
    • Cross, R.K.1    Fields, B.N.2
  • 11
    • 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. Further characterization of the ts453 mutant of mammalian orthoreovirus serotype 3 and nucleotide sequence of the mutated S4 gene. Virology. 190:1992;494-498.
    • (1992) Virology , vol.190 , pp. 494-498
    • Danis, C.1    Garzon, S.2    Lemay, G.3
  • 12
    • 0027347338 scopus 로고
    • Protein synthesis in different cell lines infected with orthoreovirus serotype 3: Inhibition of host-cell protein synthesis correlates with accelerated viral multiplication and cell killing
    • Danis C., Lemay G. Protein synthesis in different cell lines infected with orthoreovirus serotype 3: Inhibition of host-cell protein synthesis correlates with accelerated viral multiplication and cell killing. Biochem. Cell Biol. 71:1993;81-85.
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 81-85
    • Danis, C.1    Lemay, G.2
  • 13
    • 0021877047 scopus 로고
    • Inhibition of binding to initiation complexes of nascent reovirus mRNA by double-stranded RNA-dependent protein kinase
    • DeBenedetti A., Williams G. J., Baglioni C. Inhibition of binding to initiation complexes of nascent reovirus mRNA by double-stranded RNA-dependent protein kinase. J. Virol. 54:1985;408-413.
    • (1985) J. Virol. , vol.54 , pp. 408-413
    • Debenedetti, A.1    Williams, G.J.2    Baglioni, C.3
  • 14
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng W. P., Nickoloff J. A. Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200:1992;81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 15
    • 0028106465 scopus 로고
    • Site-directed mutagenic analysis of the reovirus sigma3 protein binding to double-stranded RNA
    • Denzler K. L., Jacobs B. L. Site-directed mutagenic analysis of the reovirus sigma3 protein binding to double-stranded RNA. Virology. 204:1994;190-199.
    • (1994) Virology , vol.204 , pp. 190-199
    • Denzler, K.L.1    Jacobs, B.L.2
  • 16
    • 0016426580 scopus 로고
    • Virus development in enucleated cells: Echovirus, poliovirus, pseudorabies virus, reovirus, respiratory syncytial virus and Semliki forest virus
    • Follet E. A., Pringle C. R., Pennington T. H. Virus development in enucleated cells: echovirus, poliovirus, pseudorabies virus, reovirus, respiratory syncytial virus and Semliki forest virus. J. Gen. Virol. 26:1975;183-196.
    • (1975) J. Gen. Virol. , vol.26 , pp. 183-196
    • Follet, E.A.1    Pringle, C.R.2    Pennington, T.H.3
  • 17
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 18
    • 0024318804 scopus 로고
    • Stimulation of chloramphenicol acetyltransferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected COS cells
    • Giantini M., Shatkin A. J. Stimulation of chloramphenicol acetyltransferase mRNA translation by reovirus capsid polypeptide sigma 3 in cotransfected COS cells. J. Virol. 63:1989;2415-2421.
    • (1989) J. Virol. , vol.63 , pp. 2415-2421
    • Giantini, M.1    Shatkin, A.J.2
  • 19
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman C. M., Moffat L. F., Howard B. H. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell. Biol. 2:1982;1044-1051.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 20
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham F. L., van der Eb A. J. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52:1973;151-157.
    • (1973) Virology , vol.52 , pp. 151-157
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 21
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • Green S. R., Mathews M. B. Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev. 6:1992;2478-2490.
    • (1992) Genes Dev. , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.B.2
  • 22
    • 0019973383 scopus 로고
    • Interferon action against reovirus: Activation of interferon-induced protein kinase in mouse L929 cells upon reovirus infection
    • Gupta S. L., Holmes S. L., Mehra L. L. Interferon action against reovirus: Activation of interferon-induced protein kinase in mouse L929 cells upon reovirus infection. Virology. 120:1982;495-499.
    • (1982) Virology , vol.120 , pp. 495-499
    • Gupta, S.L.1    Holmes, S.L.2    Mehra, L.L.3
  • 23
    • 0000108932 scopus 로고
    • Interferon-induced dsRNA-activated protein kinase: Antiproliferative, antiviral and antitumoral functions
    • Hovanessian A. G. Interferon-induced dsRNA-activated protein kinase: Antiproliferative, antiviral and antitumoral functions. Semin. Virol. 4:1993;237-246.
    • (1993) Semin. Virol. , vol.4 , pp. 237-246
    • Hovanessian, A.G.1
  • 24
    • 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 W. K. Reovirus coded polypeptides in infected cells: Isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively. Virology. 70:1976;411-424.
    • (1976) Virology , vol.70 , pp. 411-424
    • Huismans, H.1    Joklik, W.K.2
  • 25
    • 0000588762 scopus 로고
    • Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein
    • Imani F., Jacobs B. L. Inhibitory activity for the interferon-induced protein kinase is associated with the reovirus serotype 1 sigma 3 protein. Proc. Natl. Acad. Sci. USA. 85:1988;7887-7891.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7887-7891
    • Imani, F.1    Jacobs, B.L.2
  • 26
    • 0026002147 scopus 로고
    • The Lang strain of reovirus serotype 1 and the Dearing strain of reovirus serotype 3 differ in their sensitivities to beta interferon
    • Jacobs B. L., Ferguson R. E. The Lang strain of reovirus serotype 1 and the Dearing strain of reovirus serotype 3 differ in their sensitivities to beta interferon. J. Virol. 65:1991;5102-5104.
    • (1991) J. Virol. , vol.65 , pp. 5102-5104
    • Jacobs, B.L.1    Ferguson, R.E.2
  • 28
    • 0015398520 scopus 로고
    • Studies on the effect of chymotrypsin on reovirions
    • Joklik W. K. Studies on the effect of chymotrypsin on reovirions. Virology. 49:1972;700-715.
    • (1972) Virology , vol.49 , pp. 700-715
    • Joklik, W.K.1
  • 29
    • 0026909526 scopus 로고
    • The war against the interferon-induced dsRNA-activated protein kinase: Can viruses win
    • Katze M. G. The war against the interferon-induced dsRNA-activated protein kinase: Can viruses win. J. Interf. Res. 12:1992;241-248.
    • (1992) J. Interf. Res. , vol.12 , pp. 241-248
    • Katze, M.G.1
  • 30
    • 0000335423 scopus 로고
    • Games viruses play: A strategic initiative against the interferon-induced dsRNA-activated 68,000 Mr protein kinase
    • Katze M. G. Games viruses play: A strategic initiative against the interferon-induced dsRNA-activated 68,000 Mr protein kinase. Semin. Virol. 4:1993;259-268.
    • (1993) Semin. Virol. , vol.4 , pp. 259-268
    • Katze, M.G.1
  • 31
    • 0027408437 scopus 로고
    • The virion of mengovirus contains anti-interferon activity
    • King R. W., Simon E. H. The virion of mengovirus contains anti-interferon activity. J. Interferon Res. 13:1993;1-7.
    • (1993) J. Interferon Res. , vol.13 , pp. 1-7
    • King, R.W.1    Simon, E.H.2
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0028885797 scopus 로고
    • Effects of ethanol concentration and incubation period at 65°C on Cat activity in mammalian cell extracts
    • Leahy P., Carmichael G. G., Rossomando E. F. Effects of ethanol concentration and incubation period at 65°C on Cat activity in mammalian cell extracts. BioTechniques. 19:1995;894.
    • (1995) BioTechniques , vol.19 , pp. 894
    • Leahy, P.1    Carmichael, G.G.2    Rossomando, E.F.3
  • 34
    • 0023020029 scopus 로고
    • Expression of the cloned S4 gene of reovirus serotype 3 in transformed eucaryotic cells: Enrichment of the viral protein in the crude initiation factor fraction
    • Lemay G., Millward S. Expression of the cloned S4 gene of reovirus serotype 3 in transformed eucaryotic cells: Enrichment of the viral protein in the crude initiation factor fraction. Virus Res. 6:1986;133-140.
    • (1986) Virus Res. , vol.6 , pp. 133-140
    • Lemay, G.1    Millward, S.2
  • 35
    • 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. The viral protein sigma 3 participates in translation of late viral mRNA in reovirus-infected L cells. J. Virol. 61:1987;2472-2479.
    • (1987) J. Virol. , vol.61 , pp. 2472-2479
    • Lemieux, R.1    Lemay, G.2    Millward, S.3
  • 36
    • 0026465267 scopus 로고
    • Translational regulation by reovirus polypeptide ς3: Substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2
    • Lloyd R. M., Shatkin A. J. Translational regulation by reovirus polypeptide ς3: Substitution for VAI RNA and inhibition of phosphorylation of the α subunit of eukaryotic initiation factor 2. J. Virol. 66:1992;6878-6884.
    • (1992) J. Virol. , vol.66 , pp. 6878-6884
    • Lloyd, R.M.1    Shatkin, A.J.2
  • 37
    • 0028339916 scopus 로고
    • Mutations in a CCHC zinc-binding motif of the reovirus ς3 protein decrease its intracellular stability
    • Mabrouk T., Lemay G. Mutations in a CCHC zinc-binding motif of the reovirus ς3 protein decrease its intracellular stability. J. Virol. 68:1994a;5287-5290.
    • (1994) J. Virol. , vol.68 , pp. 5287-5290
    • Mabrouk, T.1    Lemay, G.2
  • 38
    • 0027932430 scopus 로고
    • The sequence similarity of reovirus ς3 protein to picornaviral proteases is unrelated to its role in μ1 viral protein cleavage
    • Mabrouk T., Lemay G. The sequence similarity of reovirus ς3 protein to picornaviral proteases is unrelated to its role in μ1 viral protein cleavage. Virology. 202:1994b;615-620.
    • (1994) Virology , vol.202 , pp. 615-620
    • Mabrouk, T.1    Lemay, G.2
  • 39
    • 0029264544 scopus 로고
    • Two basic motifs of reovirus ς3 protein are involved in double-stranded RNA binding
    • Mabrouk T., Danis C., Lemay G. Two basic motifs of reovirus ς3 protein are involved in double-stranded RNA binding. Biochem. Cell Biol. 73:1995;137-145.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 137-145
    • Mabrouk, T.1    Danis, C.2    Lemay, G.3
  • 40
    • 0027292944 scopus 로고
    • Analysis of the stimulation of reporter gene expression by the sigma3 protein of reovirus in co-transfected cells
    • Martin P. E. M., McCrae M. A. Analysis of the stimulation of reporter gene expression by the sigma3 protein of reovirus in co-transfected cells. J. Gen. Virol. 74:1993;1055-1062.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1055-1062
    • Martin, P.E.M.1    McCrae, M.A.2
  • 41
    • 0026716255 scopus 로고
    • Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/elF-2 alpha protein kinase
    • McCormack S. J., Thomis D. C., Samuel C. E. Mechanism of interferon action: Identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/elF-2 alpha protein kinase. Virology. 188:1992;47-56.
    • (1992) Virology , vol.188 , pp. 47-56
    • McCorMacK, S.J.1    Thomis, D.C.2    Samuel, C.E.3
  • 42
    • 0027210449 scopus 로고
    • Human papillomavirus type 18 E7 protein requires intact Cys-X-X-Cys motif for zinc binding, dimerization, and transformation but not for Rb binding
    • McIntyre M. C., Frattini M. G., Grossman S. R., Laimins L. A. Human papillomavirus type 18 E7 protein requires intact Cys-X-X-Cys motif for zinc binding, dimerization, and transformation but not for Rb binding. J. Virol. 67:1993;3142-3150.
    • (1993) J. Virol. , vol.67 , pp. 3142-3150
    • McIntyre, M.C.1    Frattini, M.G.2    Grossman, S.R.3    Laimins, L.A.4
  • 43
    • 0026072563 scopus 로고
    • The three-dimensional structure of reovirus obtained by cryo-electron microscopy
    • Metcalf P., Cyrklaff M., Adrian M. The three-dimensional structure of reovirus obtained by cryo-electron microscopy. EMBO J. 10:1991;3129-3136.
    • (1991) EMBO J. , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 44
    • 0026785224 scopus 로고
    • Proteolytic cleavage of the reovirus sigma 3 protein results in enhanced double-stranded RNA-binding activity: Identification of a repeated basic amino acid motif within the C-terminal binding region
    • Miller F. E., Samuel C. E. Proteolytic cleavage of the reovirus sigma 3 protein results in enhanced double-stranded RNA-binding activity: Identification of a repeated basic amino acid motif within the C-terminal binding region. J. Virol. 66:1992;5347-5356.
    • (1992) J. Virol. , vol.66 , pp. 5347-5356
    • Miller, F.E.1    Samuel, C.E.2
  • 45
    • 0019169556 scopus 로고
    • Mechanism of interferon action: Interferon-mediated inhibition of reovirus mRNA translation in the absence of detectable mRNA degradation but in the presence of protein phosphorylation
    • Miyamoto N. G., Samuel C. E. Mechanism of interferon action: Interferon-mediated inhibition of reovirus mRNA translation in the absence of detectable mRNA degradation but in the presence of protein phosphorylation. Virology. 107:1980;461-475.
    • (1980) Virology , vol.107 , pp. 461-475
    • Miyamoto, N.G.1    Samuel, C.E.2
  • 46
    • 0016146228 scopus 로고
    • Reovirus morphogenesis: Core-like particles in cells infected at 39 degrees with wild-type reovirus and temperature sensitive mutants of groups B and G
    • Morgan E. M., Zweerink H. J. Reovirus morphogenesis: Core-like particles in cells infected at 39 degrees with wild-type reovirus and temperature sensitive mutants of groups B and G. Virology. 59:1974;556-565.
    • (1974) Virology , vol.59 , pp. 556-565
    • Morgan, E.M.1    Zweerink, H.J.2
  • 47
    • 0017872929 scopus 로고
    • A genetic map of reovirus. III. Assignment of the double-stranded RNA mutant groups A, B, and G to genome segments
    • Mustoe T. A., Ramig R. F., Sharpe A. H., Fields B. N. A genetic map of reovirus. III. Assignment of the double-stranded RNA mutant groups A, B, and G to genome segments. Virology. 85:1978;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
  • 48
    • 0025936096 scopus 로고
    • Mechanisms of viral pathogenesis: Distinct forms of reoviruses and their roles during replication in cells and host
    • Nibert M. L., Furlong D. B., Fields B. N. Mechanisms of viral pathogenesis: Distinct forms of reoviruses and their roles during replication in cells and host. J. Clin. Invest. 88:1991;727-734.
    • (1991) J. Clin. Invest. , vol.88 , pp. 727-734
    • Nibert, M.L.1    Furlong, D.B.2    Fields, B.N.3
  • 49
    • 0000432516 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • Philadelphia: Lippincott-Raven. p. 691-730
    • Nibert M. L., Schiff L. A., Fields B. N. Reoviruses and their replication. Fundamental Virology. 1996;Lippincott-Raven, Philadelphia. p. 691-730.
    • (1996) Fundamental Virology
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 50
    • 0020465410 scopus 로고
    • Inhibition of protein synthesis in reovirus-infected HeLa cells with elevated levels of interferon-induced protein kinase activity
    • Nilsen T. W., Maroney P. A., Baglioni C. Inhibition of protein synthesis in reovirus-infected HeLa cells with elevated levels of interferon-induced protein kinase activity. J. Biol. Chem. 257:1982;14593-14596.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14593-14596
    • Nilsen, T.W.1    Maroney, P.A.2    Baglioni, C.3
  • 51
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J., Carlsson J., Olsson I., Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature. 258:1975;598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 52
    • 0002116121 scopus 로고
    • Genetics of reovirus
    • W.K. Joklik. New York: Plenum
    • Ramig R., Fields B. N. Genetics of reovirus. Joklik W. K. The Reoviridae. 1983;197-228 Plenum, New York.
    • (1983) The Reoviridae , pp. 197-228
    • Ramig, R.1    Fields, B.N.2
  • 53
    • 33745158157 scopus 로고
    • A simple method for estimating fifty per cent endpoints
    • Reed L. J., Muench H. A simple method for estimating fifty per cent endpoints. Am. J. Hyg. 27:1938;493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 54
    • 0025739093 scopus 로고
    • Antiviral actions of interferon: Interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel C. E. Antiviral actions of interferon: Interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology. 183:1991;1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 55
    • 0023673325 scopus 로고
    • Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3
    • Schiff L. A., Nibert M. L., Co M. S., Brown E. G., Fields B. N. Distinct binding sites for zinc and double-stranded RNA in the reovirus outer capsid protein sigma 3. Mol. Cell. Biol. 8:1988;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
  • 56
    • 0030921401 scopus 로고    scopus 로고
    • Preferential translation of reovirus mRNA by a ς3-dependent mechanism
    • Schmechel S., Chute M., Skinner P., Anderson R., Schiff L. Preferential translation of reovirus mRNA by a ς3-dependent mechanism. Virology. 232:1997;62-73.
    • (1997) Virology , vol.232 , pp. 62-73
    • Schmechel, S.1    Chute, M.2    Skinner, P.3    Anderson, R.4    Schiff, L.5
  • 57
    • 0026603671 scopus 로고
    • Translational effects and sequence comparisons of the three serotypes of the reovirus S4 gene
    • Seliger L. S., Giantini M., Shatkin A. J. Translational effects and sequence comparisons of the three serotypes of the reovirus S4 gene. Virology. 187:1992;202-210.
    • (1992) Virology , vol.187 , pp. 202-210
    • Seliger, L.S.1    Giantini, M.2    Shatkin, A.J.3
  • 58
    • 0028889733 scopus 로고
    • Association of reovirus outer capsid protein ς3 and μ1 causes a conformational change that renders ς3 protease sensitive
    • Shepard D. A., Ehnstrom J. G., Schiff L. A. Association of reovirus outer capsid protein ς3 and μ1 causes a conformational change that renders ς3 protease sensitive. J. Virol. 69:1995;8180-8184.
    • (1995) J. Virol. , vol.69 , pp. 8180-8184
    • Shepard, D.A.1    Ehnstrom, J.G.2    Schiff, L.A.3
  • 59
    • 0030047557 scopus 로고    scopus 로고
    • Mutations in the zinc-binding motif of the reovirus capsid protein ς3 eliminate its ability to associate with capsid protein μ1
    • Shepard D. A., Ehnstrom J. G., Skinner P. J., Schiff L. A. Mutations in the zinc-binding motif of the reovirus capsid protein ς3 eliminate its ability to associate with capsid protein μ1. J. Virol. 70:1996;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
  • 60
    • 0030580588 scopus 로고    scopus 로고
    • Assembly of the reovirus outer capsid requires μ1/ς3 interactions which are prevented by misfolded ς3 protein in temperature-sensitive mutant tsG453
    • Shing M., Coombs K. M. Assembly of the reovirus outer capsid requires μ1/ς3 interactions which are prevented by misfolded ς3 protein in temperature-sensitive mutant tsG453. Virus Res. 46:1996;19-29.
    • (1996) Virus Res. , vol.46 , pp. 19-29
    • Shing, M.1    Coombs, K.M.2
  • 61
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus 3
    • Smith R. E., Zweerink H. J., Joklik W. K. Polypeptide components of virions, top component and cores of reovirus 3. Virology. 89:1969;791-810.
    • (1969) Virology , vol.89 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 63
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker L. J., Nibert M., Furlong D., Fields B. N. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 61:1987;2351-2361.
    • (1987) J. Virol. , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 64
    • 0026608639 scopus 로고
    • Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu1 are required for site-specific cleavage to mu1c in transfected cells
    • Tillotson L., Shatkin A. J. Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu1 are required for site-specific cleavage to mu1c in transfected cells. J. Virol. 66:1992;2180-2186.
    • (1992) J. Virol. , vol.66 , pp. 2180-2186
    • Tillotson, L.1    Shatkin, A.J.2
  • 65
    • 0009482260 scopus 로고
    • Electrotransfer of proteins from polyacrylamide gel to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrotransfer of proteins from polyacrylamide gel to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 66
    • 0029895394 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the double-stranded RNA binding domain of bacterially expressed ς3 protein
    • Wang Q., Bergeron J., Mabrouk T., Lemay G. Site-directed mutagenesis of the double-stranded RNA binding domain of bacterially expressed ς3 protein. Virus Res. 41:1996;141-151.
    • (1996) Virus Res. , vol.41 , pp. 141-151
    • Wang, Q.1    Bergeron, J.2    Mabrouk, T.3    Lemay, G.4
  • 67
    • 0016526478 scopus 로고
    • The mechanism of inhibition of reovirus replication by interferon
    • Wiebe M. E., Joklik W. K. The mechanism of inhibition of reovirus replication by interferon. Virology. 66:1975;229-240.
    • (1975) Virology , vol.66 , pp. 229-240
    • Wiebe, M.E.1    Joklik, W.K.2
  • 68
    • 0030047418 scopus 로고    scopus 로고
    • Regulated, stable expression and nuclear presence of reovirus double-stranded RNA-binding protein ς3 in HeLa cells
    • Yue Z., Shatkin A. J. Regulated, stable expression and nuclear presence of reovirus double-stranded RNA-binding protein ς3 in HeLa cells. J. Virol. 70:1996;3497-3501.
    • (1996) J. Virol. , vol.70 , pp. 3497-3501
    • Yue, Z.1    Shatkin, A.J.2
  • 69
    • 0030836687 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins
    • Yue Z., Shatkin A. J. Double-stranded RNA-dependent protein kinase (PKR) is regulated by reovirus structural proteins. Virology. 234:1997;364-371.
    • (1997) Virology , vol.234 , pp. 364-371
    • Yue, Z.1    Shatkin, A.J.2
  • 70
    • 0027255150 scopus 로고
    • Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene
    • Yuwen H., Cox J. H., Yewdell J. W., Bennink J. R., Moss B. Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene. Virology. 195:1993;732-744.
    • (1993) Virology , vol.195 , pp. 732-744
    • Yuwen, H.1    Cox, J.H.2    Yewdell, J.W.3    Bennink, J.R.4    Moss, B.5
  • 71
    • 0002803627 scopus 로고
    • The reovirus multiplication cycle
    • W.K. Joklik. New York: Plenum
    • Zarbl H., Millward S. The reovirus multiplication cycle. Joklik W. K. The Reoviridae. 1983;197-228 Plenum, New York.
    • (1983) The Reoviridae , pp. 197-228
    • Zarbl, H.1    Millward, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.