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Volumn 73, Issue 3, 1999, Pages 2016-2026

Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS ENZYME;

EID: 0033017866     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.3.2016-2026.1999     Document Type: Article
Times cited : (248)

References (66)
  • 1
    • 0029417111 scopus 로고
    • Expression of poliovirus 2Apro in mammalian cells: Effects on translation
    • Aldabe, R., E. Feduchi, I. Novoa, and L. Carrasco. 1995. Expression of poliovirus 2Apro in mammalian cells: effects on translation. FEBS Lett. 377:1-5.
    • (1995) FEBS Lett. , vol.377 , pp. 1-5
    • Aldabe, R.1    Feduchi, E.2    Novoa, I.3    Carrasco, L.4
  • 2
    • 0029036230 scopus 로고
    • A human virus protein, poliovirus protein 2BC, induces membrane proliferation and blocks the exocytic pathway in the yeast Saccharomyces cerevisiae
    • Barco, A., and L. Carrasco. 1995. A human virus protein, poliovirus protein 2BC, induces membrane proliferation and blocks the exocytic pathway in the yeast Saccharomyces cerevisiae. EMBO J. 14:3349-3364.
    • (1995) EMBO J. , vol.14 , pp. 3349-3364
    • Barco, A.1    Carrasco, L.2
  • 3
    • 0027500350 scopus 로고
    • Coupled translation and replication of poliovirus RNA in vitro: Synthesis of functional 3D polymerase and infectious virus
    • Barton, D. J., and J. B. Flanegan. 1993. Coupled translation and replication of poliovirus RNA in vitro: synthesis of functional 3D polymerase and infectious virus. J. Virol. 67:822-831.
    • (1993) J. Virol. , vol.67 , pp. 822-831
    • Barton, D.J.1    Flanegan, J.B.2
  • 4
    • 0026028278 scopus 로고
    • Soluhilization and immunoprecipitation of alphavirus replication complexes
    • Barton, D. J., S. G. Sawicki, and D. L. Sawicki. 1991. Soluhilization and immunoprecipitation of alphavirus replication complexes. J. Virol. 65:1496-1506.
    • (1991) J. Virol. , vol.65 , pp. 1496-1506
    • Barton, D.J.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 5
    • 0026519212 scopus 로고
    • Structural and functional characterization of the poliovirus replication complex
    • Bienz, K., D. Egger, T. Pfister, and M. Troxler. 1992. Structural and functional characterization of the poliovirus replication complex. J. Virol. 66: 2740-2747.
    • (1992) J. Virol. , vol.66 , pp. 2740-2747
    • Bienz, K.1    Egger, D.2    Pfister, T.3    Troxler, M.4
  • 6
    • 0021069227 scopus 로고
    • Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures
    • Bienz, K., D. Egger, Y. Rasser, and W. Bossart. 1983. Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures. Virology 131:39-48.
    • (1983) Virology , vol.131 , pp. 39-48
    • Bienz, K.1    Egger, D.2    Rasser, Y.3    Bossart, W.4
  • 7
    • 0027421842 scopus 로고
    • Sinbis virus expression vectors: Packaging of RNA replicons by using defective helper RNAs
    • Bredenbeek, P. J., I. Frolov, C. M. Rice, and S. Schlesinger. 1993. Sinbis virus expression vectors: packaging of RNA replicons by using defective helper RNAs. J. Virol. 67:6439-6446.
    • (1993) J. Virol. , vol.67 , pp. 6439-6446
    • Bredenbeek, P.J.1    Frolov, I.2    Rice, C.M.3    Schlesinger, S.4
  • 8
  • 9
    • 0014675182 scopus 로고
    • Membranous structures associated with translation and transcription of poliovirus RNA
    • Caliguiri, L. A., and I. Tamm. 1969. Membranous structures associated with translation and transcription of poliovirus RNA. Science 166:885-886.
    • (1969) Science , vol.166 , pp. 885-886
    • Caliguiri, L.A.1    Tamm, I.2
  • 10
    • 0030634897 scopus 로고    scopus 로고
    • Nidovirales: A new order comprising Coronaviridae and Arteriviridae
    • Cavanagh, D. 1997. Nidovirales: a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 142:629-633.
    • (1997) Arch. Virol. , vol.142 , pp. 629-633
    • Cavanagh, D.1
  • 11
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho, M. W., N. Teterina, D. Egger, K. Bienz, and E. Ehrenfeld. 1994. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202:129-145.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 12
    • 0000115806 scopus 로고
    • Electron microscopic study of the formation of poliovirus
    • Dales, S., H. J. Eggers, I. Tamm, and G. E. Palade. 1965. Electron microscopic study of the formation of poliovirus. Virology 26:379-389.
    • (1965) Virology , vol.26 , pp. 379-389
    • Dales, S.1    Eggers, H.J.2    Tamm, I.3    Palade, G.E.4
  • 13
    • 0027265170 scopus 로고
    • Localization and biochemical characterization of alfalfa mosaic virus replication complexes
    • de Graaff, M., L. Coscoy, and E. M. Jaspars. 1993. Localization and biochemical characterization of alfalfa mosaic virus replication complexes. Virology 194:878-881.
    • (1993) Virology , vol.194 , pp. 878-881
    • De Graaff, M.1    Coscoy, L.2    Jaspars, E.M.3
  • 14
    • 0029974217 scopus 로고    scopus 로고
    • Equine arteritis virus subgenomic mRNA synthesis: Analysis of leader-body junctions and replicative-form RNAs
    • den Boon, J. A., M. F. Kleijnen, W. J. M. Spaan, and E. J. Snijder. 1996. Equine arteritis virus subgenomic mRNA synthesis: analysis of leader-body junctions and replicative-form RNAs. J. Virol. 70:4291-4298.
    • (1996) J. Virol. , vol.70 , pp. 4291-4298
    • Den Boon, J.A.1    Kleijnen, M.F.2    Spaan, W.J.M.3    Snijder, E.J.4
  • 17
    • 0030861788 scopus 로고    scopus 로고
    • The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses
    • de Vries, A. A. F., M. C. Horzinek, P. J. M. Rottier, and R. J. de Groot. 1997. The genome organization of the Nidovirales: similarities and differences between arteri-, toro-, and coronaviruses. Semin. Virol. 8:33-47.
    • (1997) Semin. Virol. , vol.8 , pp. 33-47
    • De Vries, A.A.F.1    Horzinek, M.C.2    Rottier, P.J.M.3    De Groot, R.J.4
  • 18
    • 0030728931 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis
    • Doedens, J. R., T. H. Giddings, and K. Kirkegaard. 1997. Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J. Virol. 71:9054-9064.
    • (1997) J. Virol. , vol.71 , pp. 9054-9064
    • Doedens, J.R.1    Giddings, T.H.2    Kirkegaard, K.3
  • 19
    • 0028918959 scopus 로고
    • Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A
    • Doedens, J. R., and K. Kirkegaard. 1995. Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J. 14:894-907.
    • (1995) EMBO J. , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 20
    • 0002425455 scopus 로고
    • Isolation of a filterable agent causing arteritis of horses and abortion of mares. Its differentiation from the equine (abortion) influenza virus
    • Doll, E. R., J. T. Bryans, W. H. M. McCollum, and M. E. Wallace. 1957. Isolation of a filterable agent causing arteritis of horses and abortion of mares. Its differentiation from the equine (abortion) influenza virus. Cornell Vet. 47:3-41.
    • (1957) Cornell Vet. , vol.47 , pp. 3-41
    • Doll, E.R.1    Bryans, J.T.2    McCollum, W.H.M.3    Wallace, M.E.4
  • 21
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn, W. A. J. 1994. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol. 4:139-143.
    • (1994) Trends Cell Biol. , vol.4 , pp. 139-143
    • Dunn, W.A.J.1
  • 22
    • 0029832449 scopus 로고    scopus 로고
    • Membrane association of the C-terminal half of the open reading frame 1a protein of lactate dehydrogenase-elevating virus
    • Faaberg, K. S., and P. G. W. Plagemann. 1996. Membrane association of the C-terminal half of the open reading frame 1a protein of lactate dehydrogenase-elevating virus. Arch. Virol. 141:1337-1348.
    • (1996) Arch. Virol. , vol.141 , pp. 1337-1348
    • Faaberg, K.S.1    Plagemann, P.G.W.2
  • 23
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer, S., J. Kartenbeck, and A. Helenius. 1988. Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes. J. Cell Biol. 107:2075-2086.
    • (1988) J. Cell Biol. , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 25
    • 0003936148 scopus 로고
    • Non-immunological high-affinity interactions used for labelling
    • G. Griffiths (ed.), Springer Verlag, Heidelberg, Germany
    • Griffiths, G. 1993. Non-immunological high-affinity interactions used for labelling, p. 307-344. In G. Griffiths (ed.), Fine structure immuno-cytochemistry. Springer Verlag, Heidelberg, Germany.
    • (1993) Fine Structure Immuno-cytochemistry , pp. 307-344
    • Griffiths, G.1
  • 26
    • 0020995629 scopus 로고
    • Immunoelectron microscopy using thin, frozen sections: Application to studies of the intracellular transport of Semliki Forest virus spike glycoproteins
    • Griffiths, G., K. Simons, G. Warren, and K. T. Tokuyasu. 1983. Immunoelectron microscopy using thin, frozen sections: application to studies of the intracellular transport of Semliki Forest virus spike glycoproteins. Methods Enzymol. 96:466-485.
    • (1983) Methods Enzymol. , vol.96 , pp. 466-485
    • Griffiths, G.1    Simons, K.2    Warren, G.3    Tokuyasu, K.T.4
  • 27
    • 0015402498 scopus 로고
    • Specific membranous structures associated with the replication of group A arboviruses
    • Grimley, P. M., J. G. Levin, I. K. Berezesky, and R. M. Friedman. 1972. Specific membranous structures associated with the replication of group A arboviruses. J. Virol. 10:492-503.
    • (1972) J. Virol. , vol.10 , pp. 492-503
    • Grimley, P.M.1    Levin, J.G.2    Berezesky, I.K.3    Friedman, R.M.4
  • 28
    • 0026794415 scopus 로고
    • Involvement of membrane traffic in the replication of poliovirus genomes: Effects of brefeldin A
    • Irurzun, A., L. Perez, and L. Carrasco. 1992. Involvement of membrane traffic in the replication of poliovirus genomes: effects of brefeldin A. Virology 191:166-175.
    • (1992) Virology , vol.191 , pp. 166-175
    • Irurzun, A.1    Perez, L.2    Carrasco, L.3
  • 29
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 30
    • 0032565393 scopus 로고    scopus 로고
    • Cellular factors in the transcription and replication of viral RNA genomes: A parallel to DNA-dependent RNA transcription
    • Lai, M. M. C. 1998. Cellular factors in the transcription and replication of viral RNA genomes: a parallel to DNA-dependent RNA transcription. Virology 244:1-12.
    • (1998) Virology , vol.244 , pp. 1-12
    • Lai, M.M.C.1
  • 31
    • 0028331985 scopus 로고
    • Characterization of rubella virus replication complexes using antibodies to double-stranded RNA
    • Lee, J. Y., J. A. Marshall, and D. S. Bowden. 1994. Characterization of rubella virus replication complexes using antibodies to double-stranded RNA. Virology 200:307-312.
    • (1994) Virology , vol.200 , pp. 307-312
    • Lee, J.Y.1    Marshall, J.A.2    Bowden, D.S.3
  • 33
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka, K., L. Orci, M. Amherdt, S. Y. Bednarek, S. Hamamoto, R. Schekman, and T. Yeung. 1998. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93:263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 34
    • 0026533754 scopus 로고
    • Inhibition of poliovirus RNA synthesis by brefeldin A
    • Maynell, L. A., K. Kirkegaard, and M. W. Klymkowsky. 1992. Inhibition of poliovirus RNA synthesis by brefeldin A. J. Virol. 66:1985-1994.
    • (1992) J. Virol. , vol.66 , pp. 1985-1994
    • Maynell, L.A.1    Kirkegaard, K.2    Klymkowsky, M.W.3
  • 35
    • 0000100028 scopus 로고    scopus 로고
    • Lactate dehydrogenase-elevating virus and related viruses
    • B. N. Fields, P. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers. Philadelphia, Pa.
    • Plagemann, P. G. W. 1996. Lactate dehydrogenase-elevating virus and related viruses, p. 1105-1120. In B. N. Fields, P. M. Knipe, and P. M. Howley (ed.). Fields virology. Lippincott-Raven Publishers. Philadelphia, Pa.
    • (1996) Fields Virology , pp. 1105-1120
    • Plagemann, P.G.W.1
  • 36
    • 0030876795 scopus 로고    scopus 로고
    • Comparative morphogenesis of three PRRS virus strains
    • Pol, J. M., F., Wagenaar, and J. E. G. Reus. 1997. Comparative morphogenesis of three PRRS virus strains. Vet. Microbiol. 55:203-208.
    • (1997) Vet. Microbiol. , vol.55 , pp. 203-208
    • Pol, J.M.1    Wagenaar, F.2    Reus, J.E.G.3
  • 37
    • 0020583314 scopus 로고
    • Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin
    • Quinn, P., G. Griffiths, and G. Warren. 1983. Dissection of the Golgi complex. II. Density separation of specific Golgi functions in virally infected cells treated with monensin. J. Cell Biol. 96:851-856.
    • (1983) J. Cell Biol. , vol.96 , pp. 851-856
    • Quinn, P.1    Griffiths, G.2    Warren, G.3
  • 38
    • 0029910198 scopus 로고    scopus 로고
    • Brome mosaic virus helicase-and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis
    • Restrepo-Hartwig, M. A., and P. Ahlquist. 1996. Brome mosaic virus helicase-and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis. J. Virol. 70:8908-8916.
    • (1996) J. Virol. , vol.70 , pp. 8908-8916
    • Restrepo-Hartwig, M.A.1    Ahlquist, P.2
  • 39
    • 0030010469 scopus 로고    scopus 로고
    • A novel immunogold cryoelectron microscopic approach to investigate the structure of the intracellular and extracellular forms of vaccinia virus
    • Roos, N., M. Cyrklaff, S. Cudmore, R. Blasco, J. Krijnse Locker, and G. Griffiths. 1996. A novel immunogold cryoelectron microscopic approach to investigate the structure of the intracellular and extracellular forms of vaccinia virus. EMBO J. 15:2343-2355.
    • (1996) EMBO J. , vol.15 , pp. 2343-2355
    • Roos, N.1    Cyrklaff, M.2    Cudmore, S.3    Blasco, R.4    Krijnse Locker, J.5    Griffiths, G.6
  • 40
    • 0025236253 scopus 로고
    • Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis
    • Sawicki, S. G., and D. L. Sawicki. 1990. Coronavirus transcription: subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis. J. Virol. 64:1050-1056.
    • (1990) J. Virol. , vol.64 , pp. 1050-1056
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 41
    • 0030915143 scopus 로고    scopus 로고
    • Formation of plant RNA virus replication complexes on membranes: Role of an endoplasmic reticulum-targeted viral protein
    • Schaad, M. C., P. E. Jensen, and J. C. Carrington. 1997. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J. 16:4049-4059.
    • (1997) EMBO J. , vol.16 , pp. 4049-4059
    • Schaad, M.C.1    Jensen, P.E.2    Carrington, J.C.3
  • 42
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel, A., T. H. Giddings, M. S. Ladinsky, and K. Kirkegaard. 1996. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:6576-6588.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings, T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 43
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S. L. 1997. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66:511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 44
    • 0030866422 scopus 로고    scopus 로고
    • Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes
    • Sethna, P. B., and D. A. Brian. 1997. Coronavirus genomic and subgenomic minus-strand RNAs copartition in membrane-protected replication complexes. J. Virol. 71:7744-7749.
    • (1997) J. Virol. , vol.71 , pp. 7744-7749
    • Sethna, P.B.1    Brian, D.A.2
  • 45
    • 0031925071 scopus 로고    scopus 로고
    • The molecular biology of arteriviruses
    • Snijder, E. J., and J. J. M. Meulenberg. 1998. The molecular biology of arteriviruses. J. Gen. Virol. 79:961-979.
    • (1998) J. Gen. Virol. , vol.79 , pp. 961-979
    • Snijder, E.J.1    Meulenberg, J.J.M.2
  • 46
    • 0002049970 scopus 로고
    • The coronaviruslike superfamily
    • S. G. Siddell (ed.), Plenum Press, New York, N.Y.
    • Snijder, E. J., and W. J. M. Spaan. 1995. The coronaviruslike superfamily, p. 239-255. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 239-255
    • Snijder, E.J.1    Spaan, W.J.M.2
  • 47
    • 0026475757 scopus 로고
    • The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteinc protease
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1992. The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteinc protease. J. Virol. 66:7040-7048.
    • (1992) J. Virol. , vol.66 , pp. 7040-7048
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 48
    • 0028067318 scopus 로고
    • Proteolytic processing of the replicase ORF1a protein of equine arteritis virus
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1994. Proteolytic processing of the replicase ORF1a protein of equine arteritis virus. J. Virol. 68:5755-5764.
    • (1994) J. Virol. , vol.68 , pp. 5755-5764
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 49
    • 0029044301 scopus 로고
    • The arterivirus nsp2 protease: An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases
    • Snijder, E. J., A. L. M. Wassenaar, W. J. M. Spaan, and A. E. Gorbalenya. 1995. The arterivirus nsp2 protease: an unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases. J. Biol. Chem. 270:16671-16676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16671-16676
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3    Gorbalenya, A.E.4
  • 50
    • 0029966508 scopus 로고    scopus 로고
    • The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
    • Snijder, E. J., A. L. M. Wassenaar, L. C. van Dinten, W. J. M. Spaan, and A. E. Gorbalenya. 1996. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases. J. Biol. Chem. 271:4864-4871.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4864-4871
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Van Dinten, L.C.3    Spaan, W.J.M.4    Gorbalenya, A.E.5
  • 53
    • 0030807887 scopus 로고    scopus 로고
    • Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells
    • Teterina, N. L., A. E. Gorbalenya, D. Egger, K. Bienz, and E. Ehrenfeld. 1997. Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells. J. Virol. 71:8962-8972.
    • (1997) J. Virol. , vol.71 , pp. 8962-8972
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 54
    • 0027067061 scopus 로고
    • Intracellular localization of poliovirus RNA by in situ hybridization at the ultrastructural level using single-stranded riboprobes
    • Troxler, M., D. Egger, T. Pfister, and K. Bienz. 1992. Intracellular localization of poliovirus RNA by in situ hybridization at the ultrastructural level using single-stranded riboprobes. Virology 191:687-697.
    • (1992) Virology , vol.191 , pp. 687-697
    • Troxler, M.1    Egger, D.2    Pfister, T.3    Bienz, K.4
  • 56
    • 0031879009 scopus 로고    scopus 로고
    • ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex
    • van der Meer, Y., H. van Tol, J. Krijnse Locker, and E. J. Snijder. 1998. ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex. J. Virol. 72:6689-6698.
    • (1998) J. Virol. , vol.72 , pp. 6689-6698
    • Van Der Meer, Y.1    Van Tol, H.2    Krijnse Locker, J.3    Snijder, E.J.4
  • 57
    • 0031017109 scopus 로고    scopus 로고
    • An infectious arterivirus cDNA clone: Identification of a replicase point mutation which abolishes discontinuous mRNA transcription
    • van Dinten, L. C., J. A. den Boon, A. L. M. Wassenaar, W. J. M. Spaan, and E. J. Snijder. 1997. An infectious arterivirus cDNA clone: identification of a replicase point mutation which abolishes discontinuous mRNA transcription. Proc. Natl. Acad. Sci. USA 94:991-996.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 991-996
    • Van Dinten, L.C.1    Den Boon, J.A.2    Wassenaar, A.L.M.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 58
    • 0032982143 scopus 로고    scopus 로고
    • Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication
    • van Dinten, L. C., S. Rensen, A. E. Gorbalenya, and E. J. Snijder. 1999. Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication. J. Virol. 73:2027-2037.
    • (1999) J. Virol. , vol.73 , pp. 2027-2037
    • Van Dinten, L.C.1    Rensen, S.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 59
    • 0029844841 scopus 로고    scopus 로고
    • Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains
    • van Dinten, L. C., A. L. M. Wassenaar, A. E. Gorbalenya, W. J. M. Spaan, and E. J. Snijder. 1996. Processing of the equine arteritis virus replicase ORF1b protein: identification of cleavage products containing the putative viral polymerase and helicase domains. J. Virol. 70:6625-6633.
    • (1996) J. Virol. , vol.70 , pp. 6625-6633
    • Van Dinten, L.C.1    Wassenaar, A.L.M.2    Gorbalenya, A.E.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 60
    • 0025282543 scopus 로고
    • Identification by anti-idiotypic antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal
    • Vaux, D., J. Tooze, and S. Fuller. 1990. Identification by anti-idiotypic antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal. Nature 345:495-502.
    • (1990) Nature , vol.345 , pp. 495-502
    • Vaux, D.1    Tooze, J.2    Fuller, S.3
  • 61
    • 0030856299 scopus 로고    scopus 로고
    • Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease
    • Wassenaar, A. L. M., W. J. M. Spaan, A. E. Gorbalenya, and E. J. Snijder. 1997. Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease. J. Virol. 71:9313-9322.
    • (1997) J. Virol. , vol.71 , pp. 9313-9322
    • Wassenaar, A.L.M.1    Spaan, W.J.M.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 63
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA, and of NS2b with NS3, in virus-induced membrane structures
    • Westaway, E. G., J. M. Mackenzie, M. T. Kenney, M. K. Jones, and A. A. Khromykh. 1997. Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2b with NS3, in virus-induced membrane structures. J. Virol. 71:6650-6661.
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 64
    • 0014729128 scopus 로고
    • Electron microscopic study of tissue cultures infected with simian haemorrhagic fever virus
    • Wood, O., N. M. Tauraso, and H. Liebhaber. 1970. Electron microscopic study of tissue cultures infected with simian haemorrhagic fever virus. J. Gen. Virol. 7:129-136.
    • (1970) J. Gen. Virol. , vol.7 , pp. 129-136
    • Wood, O.1    Tauraso, N.M.2    Liebhaber, H.3
  • 65
    • 0026441145 scopus 로고
    • Active complete in vitro replication of nodavirus RNA requires glycerophospholipid
    • Wu, S. X., P. Ahlquist, and P. Kaesberg. 1992. Active complete in vitro replication of nodavirus RNA requires glycerophospholipid. Proc. Natl. Acad. Sci. USA 89:11136-11140.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11136-11140
    • Wu, S.X.1    Ahlquist, P.2    Kaesberg, P.3
  • 66
    • 0029122824 scopus 로고
    • Detection of histidine-tagged fusion proteins by using a high-specific mouse monoclonal anti-histidine tag antibody
    • Zentgraf, H., M. Frey, S. Schwinn, C. Tessmer, B. Willemann, Y. Samstag, and I. Velhagen. 1995. Detection of histidine-tagged fusion proteins by using a high-specific mouse monoclonal anti-histidine tag antibody. Nucleic Acids Res. 23:3347-3348.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3347-3348
    • Zentgraf, H.1    Frey, M.2    Schwinn, S.3    Tessmer, C.4    Willemann, B.5    Samstag, Y.6    Velhagen, I.7


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