메뉴 건너뛰기




Volumn 72, Issue 8, 1998, Pages 6689-6698

ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex

Author keywords

[No Author keywords available]

Indexed keywords

BICARBONATE; RNA POLYMERASE;

EID: 0031879009     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.8.6689-6698.1998     Document Type: Article
Times cited : (141)

References (55)
  • 1
    • 0027170410 scopus 로고
    • Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus
    • Baker, S. C., K. Yokomori, S. Dong, R. Carlisle, A. E. Gorbalenya, E. V. Koonin, and M. M. C. Lai. 1993. Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus. J. Virol. 67:6056-6063.
    • (1993) J. Virol. , vol.67 , pp. 6056-6063
    • Baker, S.C.1    Yokomori, K.2    Dong, S.3    Carlisle, R.4    Gorbalenya, A.E.5    Koonin, E.V.6    Lai, M.M.C.7
  • 2
    • 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
  • 3
    • 0029007414 scopus 로고
    • Characterization of the leader papain-like proteinase of MHV A-59: Identification of a new in vitro cleavage site
    • Bonilla, P. J., S. A. Hughes, J. D. Pinon, and S. R. Weiss. 1995. Characterization of the leader papain-like proteinase of MHV A-59: identification of a new in vitro cleavage site. Virology 209:489-497.
    • (1995) Virology , vol.209 , pp. 489-497
    • Bonilla, P.J.1    Hughes, S.A.2    Pinon, J.D.3    Weiss, S.R.4
  • 4
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 5
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0029074522 scopus 로고
    • Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: Identification of two papainlike cysteine proteases
    • den Boon, J. A., K. S. Faaberg, J. J. M. Meulenberg, A. L. M. Wassenaar, P. G. W. Plagemann, A. E. Gorbalenya, and E. J. Snijder. 1995. Processing and evolution of the N-terminal region of the arterivirus replicase ORF1a protein: identification of two papainlike cysteine proteases. J. Virol. 69:4500-4505.
    • (1995) J. Virol. , vol.69 , pp. 4500-4505
    • Den Boon, J.A.1    Faaberg, K.S.2    Meulenberg, J.J.M.3    Wassenaar, A.L.M.4    Plagemann, P.G.W.5    Gorbalenya, A.E.6    Snijder, E.J.7
  • 10
    • 0028840838 scopus 로고
    • Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies
    • den Boon, J. A., W. J. M. Spaan, and E. J. Snijder. 1995. Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies. Virology 213:364-372.
    • (1995) Virology , vol.213 , pp. 364-372
    • Den Boon, J.A.1    Spaan, W.J.M.2    Snijder, E.J.3
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0029910194 scopus 로고    scopus 로고
    • Reversible dissociation of the poliovirus replication complex: Functions and interactions of its components in viral RNA synthesis
    • Egger, D., L. Pasamontes, R. Bolten, V. Boyko, and K. Bienz. 1996. Reversible dissociation of the poliovirus replication complex: functions and interactions of its components in viral RNA synthesis. J. Virol. 70:8675-8683.
    • (1996) J. Virol. , vol.70 , pp. 8675-8683
    • Egger, D.1    Pasamontes, L.2    Bolten, R.3    Boyko, V.4    Bienz, K.5
  • 15
    • 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
  • 16
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A. L. Hubbard, S. Fowler, and P. B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 17
    • 0030560627 scopus 로고    scopus 로고
    • Identification of the polymerase polyprotein products p72 and p65 of the murine coronavirus MHV JHM
    • Gao, H. Q., J. J. Schiller, and S. C. Baker. 1996. Identification of the polymerase polyprotein products p72 and p65 of the murine coronavirus MHV JHM. Virus Res. 45:101-109.
    • (1996) Virus Res. , vol.45 , pp. 101-109
    • Gao, H.Q.1    Schiller, J.J.2    Baker, S.C.3
  • 19
    • 0024398958 scopus 로고
    • Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis
    • Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis. Nucleic Acids Res. 17:4847-4861.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4847-4861
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 20
    • 0031045526 scopus 로고    scopus 로고
    • Labeling of RNA transcripts of eukaryotic cells in culture with BrUTP using a liposome transfection reagent (DOTAP)
    • Haukenes, G., A. M. Szilvay, K. A. Brokstad, A. Kanestrom, and K. H. Kalland. 1997. Labeling of RNA transcripts of eukaryotic cells in culture with BrUTP using a liposome transfection reagent (DOTAP). BioTechniques 22:308-312.
    • (1997) BioTechniques , vol.22 , pp. 308-312
    • Haukenes, G.1    Szilvay, A.M.2    Brokstad, K.A.3    Kanestrom, A.4    Kalland, K.H.5
  • 21
    • 1842370236 scopus 로고    scopus 로고
    • Identification and subcellular localization of a 41 kda, polyprotein lab processing product in human coronavirus 229E-infected cells
    • Heusipp, G., C. Grotzinger, J. Herold, S. G. Siddell, and J. Ziebuhr. 1997. Identification and subcellular localization of a 41 kda, polyprotein lab processing product in human coronavirus 229E-infected cells. J. Gen. Virol. 78:2789-2794.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2789-2794
    • Heusipp, G.1    Grotzinger, C.2    Herold, J.3    Siddell, S.G.4    Ziebuhr, J.5
  • 22
    • 0027499230 scopus 로고
    • Visualization of focal sites of transcription within human nuclei
    • Jackson, D. A., A. B. Hassan, R. J. Errington, and P. R. Cook. 1993. Visualization of focal sites of transcription within human nuclei. EMBO J. 12: 1059-1065.
    • (1993) EMBO J. , vol.12 , pp. 1059-1065
    • Jackson, D.A.1    Hassan, A.B.2    Errington, R.J.3    Cook, P.R.4
  • 23
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from RER to the Golgi complex requires only one vesicular transport step
    • Krijnse Locker, J., M. Ericsson, P. J. M. Rottier, and G. Griffiths. 1994. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol. 124:55-70.
    • (1994) J. Cell Biol. , vol.124 , pp. 55-70
    • Krijnse Locker, J.1    Ericsson, M.2    Rottier, P.J.M.3    Griffiths, G.4
  • 24
    • 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
  • 25
    • 0029036797 scopus 로고
    • Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein
    • Liu, D. X., and T. D. K. Brown. 1995. Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein. Virology 209:420-427.
    • (1995) Virology , vol.209 , pp. 420-427
    • Liu, D.X.1    Brown, T.D.K.2
  • 26
    • 0029063624 scopus 로고
    • Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59
    • Lu, Y., X. Lu, and M. R. Denison. 1995. Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59. J. Virol. 69:3554-3559.
    • (1995) J. Virol. , vol.69 , pp. 3554-3559
    • Lu, Y.1    Lu, X.2    Denison, M.R.3
  • 27
    • 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, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 1105-1120
    • Plagemann, P.G.W.1
  • 28
    • 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
  • 29
    • 0028092203 scopus 로고
    • Adenovirus replication and transcription sites are spatially separated in the nucleus of infected cells
    • Pombo, A., J. Ferreira, E. Bridge, and M. Carmo-Fonseca. 1994. Adenovirus replication and transcription sites are spatially separated in the nucleus of infected cells. EMBO J. 13:5075-5085.
    • (1994) EMBO J. , vol.13 , pp. 5075-5085
    • Pombo, A.1    Ferreira, J.2    Bridge, E.3    Carmo-Fonseca, M.4
  • 30
    • 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
  • 31
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., R. Casadio, P. Fariselli, and C. Sander. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci. 4:521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 38
    • 0026475757 scopus 로고
    • The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteine 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 cysteine 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
  • 39
    • 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
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0026167662 scopus 로고
    • Confocal fluorescence microscopy in modern cell biology
    • Stelzer, E. H., I. Wacker, and J. R. DeMey. 1991. Confocal fluorescence microscopy in modern cell biology. Semin. Cell Biol. 2:145-152.
    • (1991) Semin. Cell Biol. , vol.2 , pp. 145-152
    • Stelzer, E.H.1    Wacker, I.2    DeMey, J.R.3
  • 44
    • 0029998594 scopus 로고    scopus 로고
    • Determinants of membrane association for poliovirus protein 3AB
    • Towner, J. S., T. V. Ho, and B. L. Semler. 1996. Determinants of membrane association for poliovirus protein 3AB. J. Biol. Chem. 271:26810-26818.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26810-26818
    • Towner, J.S.1    Ho, T.V.2    Semler, B.L.3
  • 45
    • 0022182982 scopus 로고
    • Characterization of monoclonal antibodies to bromodeoxyuridine
    • Vanderlaan, M., and C. B. Thomas. 1985. Characterization of monoclonal antibodies to bromodeoxyuridine. Cytometry 66:501-505.
    • (1985) Cytometry , vol.66 , pp. 501-505
    • Vanderlaan, M.1    Thomas, C.B.2
  • 47
    • 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
  • 49
    • 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
  • 50
    • 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
  • 51
    • 0027305616 scopus 로고
    • Fluorescent labeling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus
    • Wansink, D. G., W. Schul, I. van der Kraan, B. van Steensel, R. van Driel, and L. de Jong. 1993. Fluorescent labeling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus. J. Cell Biol. 122:283-293.
    • (1993) J. Cell Biol. , vol.122 , pp. 283-293
    • Wansink, D.G.1    Schul, W.2    Van Der Kraan, I.3    Van Steensel, B.4    Van Driel, R.5    De Jong, L.6
  • 52
    • 0030856299 scopus 로고    scopus 로고
    • Alternative proteolytic processing of the arterivirus 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 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
  • 53
    • 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
  • 54
    • 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
  • 55
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr, J., J. Herold, and S. G. Siddell. 1995. Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J. Virol. 69:4331-4338.
    • (1995) J. Virol. , vol.69 , pp. 4331-4338
    • Ziebuhr, J.1    Herold, J.2    Siddell, S.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.