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Volumn 429, Issue , 2007, Pages 53-82

A Highly Efficient and Robust In Vitro Translation System for Expression of Picornavirus and Hepatitis C Virus RNA Genomes

Author keywords

[No Author keywords available]

Indexed keywords

CELL EXTRACT; NONSTRUCTURAL PROTEIN 3; NUCLEASE; PROTEINASE INHIBITOR; VIRUS RNA; VIRUS ENVELOPE PROTEIN;

EID: 36248948743     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)29004-4     Document Type: Chapter
Times cited : (14)

References (64)
  • 1
    • 0038337684 scopus 로고    scopus 로고
    • Picornavirus genome: An overview
    • Semler B.L., and Wimmer E. (Eds), ASM Press, Washington, DC
    • Agol V.I. Picornavirus genome: An overview. In: Semler B.L., and Wimmer E. (Eds). "Molecular Biology of Picornaviruses" (2002), ASM Press, Washington, DC 127-148
    • (2002) "Molecular Biology of Picornaviruses" , pp. 127-148
    • Agol, V.I.1
  • 2
    • 0015118883 scopus 로고
    • Protein synthesis directed by encephalomyocarditis virus RNA: Properties of a transfer RNA-dependent system
    • Aviv H., Boime I., and Leder P. Protein synthesis directed by encephalomyocarditis virus RNA: Properties of a transfer RNA-dependent system. Proc. Natl. Acad. Sci. USA 68 (1971) 2303-2307
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2303-2307
    • Aviv, H.1    Boime, I.2    Leder, P.3
  • 3
    • 11144246127 scopus 로고    scopus 로고
    • Novel insights into hepatitis C virus replication and persistence
    • Bartenschlager R., Frese M., and Pietschmann T. Novel insights into hepatitis C virus replication and persistence. Adv. Virus Res. 63 (2004) 71-180
    • (2004) Adv. Virus Res. , vol.63 , pp. 71-180
    • Bartenschlager, R.1    Frese, M.2    Pietschmann, T.3
  • 4
    • 0029155434 scopus 로고
    • Complete replication of poliovirus in vitro: Preinitiation RNA replication complexes require soluble cellular factors for the synthesis of VPg-linked RNA
    • Barton D.J., Black E.P., and Flanegan J.B. Complete replication of poliovirus in vitro: Preinitiation RNA replication complexes require soluble cellular factors for the synthesis of VPg-linked RNA. J. Virol. 69 (1995) 5516-5527
    • (1995) J. Virol. , vol.69 , pp. 5516-5527
    • Barton, D.J.1    Black, E.P.2    Flanegan, J.B.3
  • 6
    • 0002805260 scopus 로고    scopus 로고
    • Poliovirus RNA replication and genetic complementation in cell-free reactions
    • Semler B.L., and Wimmer E. (Eds), ASM Press, Washington, DC
    • Barton D.J., Morasco B.J., Smerage L.E., and Flanegan J.B. Poliovirus RNA replication and genetic complementation in cell-free reactions. In: Semler B.L., and Wimmer E. (Eds). "Molecular Biology of Picornaviruses" (2002), ASM Press, Washington, DC 461-469
    • (2002) "Molecular Biology of Picornaviruses" , pp. 461-469
    • Barton, D.J.1    Morasco, B.J.2    Smerage, L.E.3    Flanegan, J.B.4
  • 7
    • 0020980473 scopus 로고
    • Use of fluorography for sensitive isotope detection in polyacrylamide gel electrophoresis and related techniques
    • Bonner W.M. Use of fluorography for sensitive isotope detection in polyacrylamide gel electrophoresis and related techniques. Methods Enzymol. 96 (1983) 215-222
    • (1983) Methods Enzymol. , vol.96 , pp. 215-222
    • Bonner, W.M.1
  • 9
    • 0014572549 scopus 로고
    • Purification of encephalomyocarditis virus
    • Burness A.T. Purification of encephalomyocarditis virus. J. Gen. Virol. 5 (1969) 291-303
    • (1969) J. Gen. Virol. , vol.5 , pp. 291-303
    • Burness, A.T.1
  • 10
    • 0021256925 scopus 로고
    • In vitro translation of poliovirus RNA: Utilization of internal initiation sites in reticulocyte lysate
    • Dorner A.J., Semler B.L., Jackson R.J., Hanecak R., Duprey E., and Wimmer E. In vitro translation of poliovirus RNA: Utilization of internal initiation sites in reticulocyte lysate. J. Virol. 50 (1984) 507-514
    • (1984) J. Virol. , vol.50 , pp. 507-514
    • Dorner, A.J.1    Semler, B.L.2    Jackson, R.J.3    Hanecak, R.4    Duprey, E.5    Wimmer, E.6
  • 11
    • 0028021952 scopus 로고
    • Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses
    • Dubuisson J., Hsu H.H., Cheung R.C., Greenberg H.B., Russell D.G., and Rice C.M. Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses. J. Virol. 68 (1994) 6147-6160
    • (1994) J. Virol. , vol.68 , pp. 6147-6160
    • Dubuisson, J.1    Hsu, H.H.2    Cheung, R.C.3    Greenberg, H.B.4    Russell, D.G.5    Rice, C.M.6
  • 12
    • 23844520885 scopus 로고    scopus 로고
    • Dipyridamole reversibly inhibits mengovirus RNA replication
    • Fata-Hartley C.L., and Palmenberg A.C. Dipyridamole reversibly inhibits mengovirus RNA replication. J. Virol. 79 (2005) 11062-11070
    • (2005) J. Virol. , vol.79 , pp. 11062-11070
    • Fata-Hartley, C.L.1    Palmenberg, A.C.2
  • 13
    • 0025773028 scopus 로고
    • Role of a viral membrane polypeptide in strand-specific initiation of poliovirus RNA synthesis
    • Giachetti C., and Semler B.L. Role of a viral membrane polypeptide in strand-specific initiation of poliovirus RNA synthesis. J. Virol. 65 (1991) 2647-2654
    • (1991) J. Virol. , vol.65 , pp. 2647-2654
    • Giachetti, C.1    Semler, B.L.2
  • 14
    • 0018567916 scopus 로고
    • Encephalomyocarditis virus-specific polypeptide p22 is involved in the processing of the viral precursor polypeptides
    • Gorbalenya A.E., Svitkin Y.V., Kazachkov Y.A., and Agol V.I. Encephalomyocarditis virus-specific polypeptide p22 is involved in the processing of the viral precursor polypeptides. FEBS Lett. 108 (1979) 1-5
    • (1979) FEBS Lett. , vol.108 , pp. 1-5
    • Gorbalenya, A.E.1    Svitkin, Y.V.2    Kazachkov, Y.A.3    Agol, V.I.4
  • 15
    • 0033919960 scopus 로고    scopus 로고
    • Poliovirus requires a precise 5′ end for efficient positive-strand RNA synthesis
    • Herold J., and Andino R. Poliovirus requires a precise 5′ end for efficient positive-strand RNA synthesis. J. Virol. 74 (2000) 6394-6400
    • (2000) J. Virol. , vol.74 , pp. 6394-6400
    • Herold, J.1    Andino, R.2
  • 16
    • 0022631940 scopus 로고
    • A detailed kinetic analysis of the in vitro synthesis and processing of encephalomyocarditis virus products
    • Jackson R.J. A detailed kinetic analysis of the in vitro synthesis and processing of encephalomyocarditis virus products. Virology 149 (1986) 114-127
    • (1986) Virology , vol.149 , pp. 114-127
    • Jackson, R.J.1
  • 17
    • 0026035295 scopus 로고
    • Potassium salts influence the fidelity of mRNA translation initiation in rabbit reticulocyte lysates: Unique features of encephalomyocarditis virus RNA translation
    • Jackson R.J. Potassium salts influence the fidelity of mRNA translation initiation in rabbit reticulocyte lysates: Unique features of encephalomyocarditis virus RNA translation. Biochim. Biophys. Acta 1088 (1991) 345-358
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 345-358
    • Jackson, R.J.1
  • 18
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA
    • Jackson R.J., and Hunt T. Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96 (1983) 50-74
    • (1983) Methods Enzymol. , vol.96 , pp. 50-74
    • Jackson, R.J.1    Hunt, T.2
  • 19
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang S.K., Kräusslich H.G., Nicklin M.J., Duke G.M., Palmenberg A.C., and Wimmer E. A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62 (1988) 2636-2643
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Kräusslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 21
    • 0001815885 scopus 로고    scopus 로고
    • The double-stranded RNA-activated protein kinase PKR
    • Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Kaufman R.J. The double-stranded RNA-activated protein kinase PKR. In: Sonenberg N., Hershey J.W.B., and Mathews M.B. (Eds). "Translational Control of Gene Expression" (2000), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 503-527
    • (2000) "Translational Control of Gene Expression" , pp. 503-527
    • Kaufman, R.J.1
  • 22
    • 0015304196 scopus 로고
    • Simple method for the isolation of encephalomyocarditis virus ribonucleic acid
    • Kerr I.M., and Martin E.M. Simple method for the isolation of encephalomyocarditis virus ribonucleic acid. J. Virol. 9 (1972) 559-561
    • (1972) J. Virol. , vol.9 , pp. 559-561
    • Kerr, I.M.1    Martin, E.M.2
  • 23
    • 0013892859 scopus 로고
    • Factors controlling amino acid incorporation by ribosomes from Krebs II mouse ascites-tumour cells
    • Kerr I.M., Cohen N., and Work T.S. Factors controlling amino acid incorporation by ribosomes from Krebs II mouse ascites-tumour cells. Biochem. J. 98 (1966) 826-835
    • (1966) Biochem. J. , vol.98 , pp. 826-835
    • Kerr, I.M.1    Cohen, N.2    Work, T.S.3
  • 24
    • 0028290389 scopus 로고
    • Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini
    • Lin C., Lindenbach B.D., Pragai B.M., McCourt D.W., and Rice C.M. Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini. J. Virol. 68 (1994) 5063-5073
    • (1994) J. Virol. , vol.68 , pp. 5063-5073
    • Lin, C.1    Lindenbach, B.D.2    Pragai, B.M.3    McCourt, D.W.4    Rice, C.M.5
  • 25
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams & Wilkins, Philadelphia, PA
    • Lindenbach B.D., and Rice C.M. Flaviviridae: the viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). "Fields Virology" Vol. 1 (2001), Lippincott Williams & Wilkins, Philadelphia, PA 991-1042
    • (2001) "Fields Virology" , vol.1 , pp. 991-1042
    • Lindenbach, B.D.1    Rice, C.M.2
  • 27
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley F., Trimble R.B., Tarentino A.L., and Plummer Jr. T.H. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 180 (1989) 195-204
    • (1989) Anal. Biochem. , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 28
    • 52049101910 scopus 로고
    • Studies on protein and nucleic acid metabolism in virus-infected mammalian cells. 1. Encephalomyocarditis virus in Krebs II mouse-ascites-tumour cells
    • Martin E.M., Malec J., Sved S., and Work T.S. Studies on protein and nucleic acid metabolism in virus-infected mammalian cells. 1. Encephalomyocarditis virus in Krebs II mouse-ascites-tumour cells. Biochem. J. 80 (1961) 585-597
    • (1961) Biochem. J. , vol.80 , pp. 585-597
    • Martin, E.M.1    Malec, J.2    Sved, S.3    Work, T.S.4
  • 29
    • 0014914434 scopus 로고
    • Mammalian cell-free protein synthesis directed by viral ribonucleic acid
    • Mathews M., and Korner A. Mammalian cell-free protein synthesis directed by viral ribonucleic acid. Eur. J. Biochem. 17 (1970) 328-338
    • (1970) Eur. J. Biochem. , vol.17 , pp. 328-338
    • Mathews, M.1    Korner, A.2
  • 30
    • 33846204799 scopus 로고    scopus 로고
    • A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins
    • Mikami S., Kobayashi T., Yokoyama S., and Imataka H. A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins. J. Biotechnol. 127 (2006) 65-78
    • (2006) J. Biotechnol. , vol.127 , pp. 65-78
    • Mikami, S.1    Kobayashi, T.2    Yokoyama, S.3    Imataka, H.4
  • 31
    • 33645395535 scopus 로고    scopus 로고
    • An efficient mammalian cell-free translation system supplemented with translation factors
    • Mikami S., Masutani M., Sonenberg N., Yokoyama S., and Imataka H. An efficient mammalian cell-free translation system supplemented with translation factors. Protein Expr. Purif. 46 (2006) 348-357
    • (2006) Protein Expr. Purif. , vol.46 , pp. 348-357
    • Mikami, S.1    Masutani, M.2    Sonenberg, N.3    Yokoyama, S.4    Imataka, H.5
  • 32
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A., Paul A.V., and Wimmer E. Cell-free, de novo synthesis of poliovirus. Science 254 (1991) 1647-1651
    • (1991) Science , vol.254 , pp. 1647-1651
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 34
    • 0025310854 scopus 로고
    • mRNA poly(A) tail, a 3′ enhancer of translational initiation
    • Munroe D., and Jacobson A. mRNA poly(A) tail, a 3′ enhancer of translational initiation. Mol. Cell. Biol. 10 (1990) 3441-3455
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3441-3455
    • Munroe, D.1    Jacobson, A.2
  • 35
    • 0025939363 scopus 로고
    • Improved method for detecting poliovirus negative strands used to demonstrate specificity of positive-strand encapsidation and the ratio of positive to negative strands in infected cells
    • Novak J.E., and Kirkegaard K. Improved method for detecting poliovirus negative strands used to demonstrate specificity of positive-strand encapsidation and the ratio of positive to negative strands in infected cells. J. Virol. 65 (1991) 3384-3387
    • (1991) J. Virol. , vol.65 , pp. 3384-3387
    • Novak, J.E.1    Kirkegaard, K.2
  • 36
    • 0018634036 scopus 로고
    • Protease required for processing picornaviral coat protein resides in the viral replicase gene
    • Palmenberg A.C., Pallansch M.A., and Rueckert R.R. Protease required for processing picornaviral coat protein resides in the viral replicase gene. J. Virol. 32 (1979) 770-778
    • (1979) J. Virol. , vol.32 , pp. 770-778
    • Palmenberg, A.C.1    Pallansch, M.A.2    Rueckert, R.R.3
  • 37
    • 0001856730 scopus 로고    scopus 로고
    • Possible unifying mechanism of picornavirus genome replication
    • Semler B.L., and Wimmer E. (Eds), ASM Press, Washington, DC
    • Paul A.V. Possible unifying mechanism of picornavirus genome replication. In: Semler B.L., and Wimmer E. (Eds). "Molecular Biology of Picornaviruses" (2002), ASM Press, Washington, DC 227-246
    • (2002) "Molecular Biology of Picornaviruses" , pp. 227-246
    • Paul, A.V.1
  • 39
    • 0017808009 scopus 로고
    • Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme
    • Pelham H.R.B. Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme. Eur. J. Biochem. 85 (1978) 457-462
    • (1978) Eur. J. Biochem. , vol.85 , pp. 457-462
    • Pelham, H.R.B.1
  • 40
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • Pelham H.R., and Jackson R.J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur. J. Biochem. 67 (1976) 247-256
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.1    Jackson, R.J.2
  • 41
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J., and Sonenberg N. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 334 (1988) 320-325
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 42
    • 0031905698 scopus 로고    scopus 로고
    • A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs
    • Pestova T.V., Shatsky I.N., Fletcher S.P., Jackson R.J., and Hellen C.U. A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs. Genes Dev. 12 (1998) 67-83
    • (1998) Genes Dev. , vol.12 , pp. 67-83
    • Pestova, T.V.1    Shatsky, I.N.2    Fletcher, S.P.3    Jackson, R.J.4    Hellen, C.U.5
  • 43
    • 0033992516 scopus 로고    scopus 로고
    • Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties
    • Reed K.E., and Rice C.M. Overview of hepatitis C virus genome structure, polyprotein processing, and protein properties. Curr. Top. Microbiol. Immunol. 242 (2000) 55-84
    • (2000) Curr. Top. Microbiol. Immunol. , vol.242 , pp. 55-84
    • Reed, K.E.1    Rice, C.M.2
  • 44
    • 0019750557 scopus 로고
    • Preparation and characterization of encephalomyocarditis (EMC) virus
    • Rueckert R.R., and Pallansch M.A. Preparation and characterization of encephalomyocarditis (EMC) virus. Methods Enzymol. 78 (1981) 315-325
    • (1981) Methods Enzymol. , vol.78 , pp. 315-325
    • Rueckert, R.R.1    Pallansch, M.A.2
  • 46
    • 0030788587 scopus 로고    scopus 로고
    • Transmembrane topology of a CLC chloride channel
    • Schmidt-Rose T., and Jentsch T.J. Transmembrane topology of a CLC chloride channel. Proc. Natl. Acad. Sci. USA 94 (1997) 7633-7638
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7633-7638
    • Schmidt-Rose, T.1    Jentsch, T.J.2
  • 47
    • 0028040540 scopus 로고
    • Complex processing and protein:protein interactions in the E2:NS2 region of HCV
    • Selby M.J., Glazer E., Masiarz F., and Houghton M. Complex processing and protein:protein interactions in the E2:NS2 region of HCV. Virology 204 (1994) 114-122
    • (1994) Virology , vol.204 , pp. 114-122
    • Selby, M.J.1    Glazer, E.2    Masiarz, F.3    Houghton, M.4
  • 48
    • 0017813407 scopus 로고
    • Complete translation of encephalomyocarditis virus RNA and faithful cleavage of virus-specific proteins in a cell-free system from Krebs-2 cells
    • Svitkin Y.V., and Agol V.I. Complete translation of encephalomyocarditis virus RNA and faithful cleavage of virus-specific proteins in a cell-free system from Krebs-2 cells. FEBS Lett. 87 (1978) 7-11
    • (1978) FEBS Lett. , vol.87 , pp. 7-11
    • Svitkin, Y.V.1    Agol, V.I.2
  • 49
    • 0038702518 scopus 로고    scopus 로고
    • Cell-free synthesis of encephalomyocarditis virus
    • Svitkin Y.V., and Sonenberg N. Cell-free synthesis of encephalomyocarditis virus. J. Virol. 77 (2003) 6551-6555
    • (2003) J. Virol. , vol.77 , pp. 6551-6555
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 50
    • 2142826526 scopus 로고    scopus 로고
    • An efficient system for cap- and poly(A)-dependent translation in vitro
    • Svitkin Y.V., and Sonenberg N. An efficient system for cap- and poly(A)-dependent translation in vitro. Methods Mol. Biol. 257 (2004) 155-170
    • (2004) Methods Mol. Biol. , vol.257 , pp. 155-170
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 51
    • 0018602213 scopus 로고
    • Encephalomyocarditis virus-specific polypeptide p22 possessing a proteolytic activity: Preliminary mapping on the viral genome
    • Svitkin Y.V., Gorbalenya A.E., Kazachkov Y.A., and Agol V.I. Encephalomyocarditis virus-specific polypeptide p22 possessing a proteolytic activity: Preliminary mapping on the viral genome. FEBS Lett. 108 (1979) 6-9
    • (1979) FEBS Lett. , vol.108 , pp. 6-9
    • Svitkin, Y.V.1    Gorbalenya, A.E.2    Kazachkov, Y.A.3    Agol, V.I.4
  • 52
    • 0019470852 scopus 로고
    • Translation of tick-borne encephalitis virus (flavivirus) genome in vitro: Synthesis of two structural polypeptides
    • Svitkin Y.V., Ugarova T.Y., Chernovskaya T.V., Lyapustin V.N., Lashkevich V.A., and Agol V.I. Translation of tick-borne encephalitis virus (flavivirus) genome in vitro: Synthesis of two structural polypeptides. Virology 110 (1981) 26-34
    • (1981) Virology , vol.110 , pp. 26-34
    • Svitkin, Y.V.1    Ugarova, T.Y.2    Chernovskaya, T.V.3    Lyapustin, V.N.4    Lashkevich, V.A.5    Agol, V.I.6
  • 53
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • Svitkin Y.V., Ovchinnikov L.P., Dreyfuss G., and Sonenberg N. General RNA binding proteins render translation cap dependent. EMBO J. 15 (1996) 7147-7155
    • (1996) EMBO J. , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4
  • 54
    • 0031800940 scopus 로고    scopus 로고
    • Rapamycin and wortmannin enhance replication of a defective encephalomyocarditis virus
    • Svitkin Y.V., Hahn H., Gingras A.C., Palmenberg A.C., and Sonenberg N. Rapamycin and wortmannin enhance replication of a defective encephalomyocarditis virus. J. Virol. 72 (1998) 5811-5819
    • (1998) J. Virol. , vol.72 , pp. 5811-5819
    • Svitkin, Y.V.1    Hahn, H.2    Gingras, A.C.3    Palmenberg, A.C.4    Sonenberg, N.5
  • 55
    • 27944483724 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation
    • Svitkin Y.V., Herdy B., Costa-Mattioli M., Gingras A.C., Raught B., and Sonenberg N. Eukaryotic translation initiation factor 4E availability controls the switch between cap-dependent and internal ribosomal entry site-mediated translation. Mol. Cell. Biol. 25 (2005) 10556-10565
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10556-10565
    • Svitkin, Y.V.1    Herdy, B.2    Costa-Mattioli, M.3    Gingras, A.C.4    Raught, B.5    Sonenberg, N.6
  • 56
    • 18744378008 scopus 로고    scopus 로고
    • Complete translation of the hepatitis C virus genome in vitro: Membranes play a critical role in the maturation of all virus proteins except for NS3
    • Svitkin Y.V., Pause A., Lopez-Lastra M., Perreault S., and Sonenberg N. Complete translation of the hepatitis C virus genome in vitro: Membranes play a critical role in the maturation of all virus proteins except for NS3. J. Virol. 79 (2005) 6868-6881
    • (2005) J. Virol. , vol.79 , pp. 6868-6881
    • Svitkin, Y.V.1    Pause, A.2    Lopez-Lastra, M.3    Perreault, S.4    Sonenberg, N.5
  • 57
    • 0036835590 scopus 로고    scopus 로고
    • Hepatitis C therapeutics: Current status and emerging strategies
    • Tan S.L., Pause A., Shi Y., and Sonenberg N. Hepatitis C therapeutics: Current status and emerging strategies. Nat. Rev. Drug Discov. 1 (2002) 867-881
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 867-881
    • Tan, S.L.1    Pause, A.2    Shi, Y.3    Sonenberg, N.4
  • 58
    • 0026513651 scopus 로고
    • Internal ribosome entry site within hepatitis C virus RNA
    • Tsukiyama-Kohara K., Iizuka N., Kohara M., and Nomoto A. Internal ribosome entry site within hepatitis C virus RNA. J. Virol. 66 (1992) 1476-1483
    • (1992) J. Virol. , vol.66 , pp. 1476-1483
    • Tsukiyama-Kohara, K.1    Iizuka, N.2    Kohara, M.3    Nomoto, A.4
  • 60
    • 0016023099 scopus 로고
    • Translation of reovirus mRNA, poliovirus RNA and bacteriophage Qb RNA in cell-free extracts of mammalian cells
    • Villa-Komaroff L., McDowell M., Baltimore D., and Lodish H.F. Translation of reovirus mRNA, poliovirus RNA and bacteriophage Qb RNA in cell-free extracts of mammalian cells. Methods Enzymol. 30 (1974) 709-723
    • (1974) Methods Enzymol. , vol.30 , pp. 709-723
    • Villa-Komaroff, L.1    McDowell, M.2    Baltimore, D.3    Lodish, H.F.4
  • 63
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter P., and Blobel G. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96 (1983) 84-93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 64
    • 0030740520 scopus 로고    scopus 로고
    • Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee
    • Yanagi M., Purcell R.H., Emerson S.U., and Bukh J. Transcripts from a single full-length cDNA clone of hepatitis C virus are infectious when directly transfected into the liver of a chimpanzee. Proc. Natl. Acad. Sci. USA 94 (1997) 8738-8743
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8738-8743
    • Yanagi, M.1    Purcell, R.H.2    Emerson, S.U.3    Bukh, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.