메뉴 건너뛰기




Volumn 244, Issue 1, 1998, Pages 1-12

Cellular factors in the transcription and replication of viral RNA genomes: A parallel to dna-dependent RNA transcription

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; VIRUS RNA;

EID: 0032565393     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9098     Document Type: Article
Times cited : (243)

References (96)
  • 1
    • 0031003235 scopus 로고    scopus 로고
    • The La antigen binds 5′ noncoding region of the hepatitis C virus RNA in the context of the initiator AUG codon and stimulates internal ribosome entry site-mediated translation
    • Ali N., Siddiqui A. The La antigen binds 5′ noncoding region of the hepatitis C virus RNA in the context of the initiator AUG codon and stimulates internal ribosome entry site-mediated translation. Proc. Natl. Acad. Sci. USA. 94:1997;2249-2254.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2249-2254
    • Ali, N.1    Siddiqui, A.2
  • 2
    • 0027170180 scopus 로고
    • Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA
    • Andino R., Rieckhof G. E., Achacoso P. L., Baltimore D. Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12:1993;3587-3598.
    • (1993) EMBO J. , vol.12 , pp. 3587-3598
    • Andino, R.1    Rieckhof, G.E.2    Achacoso, P.L.3    Baltimore, D.4
  • 3
    • 0027282394 scopus 로고
    • Different mechanisms of recognition of bacteriophage Qβ plus and minus strand RNAs by Qβ replicase
    • Barrera I., Schuppli D., Sogo J. M., Weber H. Different mechanisms of recognition of bacteriophage Qβ plus and minus strand RNAs by Qβ replicase. J. Mol. Biol. 232:1993;512-521.
    • (1993) J. Mol. Biol. , vol.232 , pp. 512-521
    • Barrera, I.1    Schuppli, D.2    Sogo, J.M.3    Weber, H.4
  • 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., 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
  • 5
    • 0026028278 scopus 로고
    • Solubilization and immunoprecipitation of alphavirus replication complexes
    • Barton D. J., Sawicki S. G., Sawicki D. L. Solubilization and immunoprecipitation of alphavirus replication complexes. J. Virol. 65:1991;1496-1506.
    • (1991) J. Virol. , vol.65 , pp. 1496-1506
    • Barton, D.J.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 6
    • 0029021092 scopus 로고
    • Isolation and characterization of an RNA-dependent RNA polymerase fromNicotiana clevelandiiplants infected with red clover necrotic mosaic dianthovirus
    • Bates H. J., Farjah M., Osman T. A. M., Buck K. W. Isolation and characterization of an RNA-dependent RNA polymerase fromNicotiana clevelandiiplants infected with red clover necrotic mosaic dianthovirus. J. Gen. Virol. 76:1995;1483-1491.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1483-1491
    • Bates, H.J.1    Farjah, M.2    Osman, T.A.M.3    Buck, K.W.4
  • 7
    • 0030051777 scopus 로고    scopus 로고
    • Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus
    • Behrens S. E., Tomei L., De Francesco R. Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus. EMBO J. 15:1996;12-22.
    • (1996) EMBO J. , vol.15 , pp. 12-22
    • Behrens, S.E.1    Tomei, L.2    De Francesco, R.3
  • 8
    • 0029792145 scopus 로고    scopus 로고
    • Specific binding of polypyrimidine tract binding protein and hnRNP A1 to HIV-1 CRS elements
    • Black A. C., Luo J., Chun S., Bakker A., Faser J. K., Rosenblatt J. D. Specific binding of polypyrimidine tract binding protein and hnRNP A1 to HIV-1 CRS elements. Virus Genes. 12:1996;275-285.
    • (1996) Virus Genes , vol.12 , pp. 275-285
    • Black, A.C.1    Luo, J.2    Chun, S.3    Bakker, A.4    Faser, J.K.5    Rosenblatt, J.D.6
  • 9
    • 0028883786 scopus 로고
    • Polypyrimidine tract-binding protein and heterogeneous nuclear ribonucleoprotein A1 bind to human T-cell leukemia virus type 2 RNA regulatory elements
    • Black A. C., Luo J., Watanabe C., Chun S., Bakker A., Faser J. K., Morgan J. P., Rosenblatt J. D. Polypyrimidine tract-binding protein and heterogeneous nuclear ribonucleoprotein A1 bind to human T-cell leukemia virus type 2 RNA regulatory elements. J. Virol. 69:1995;6852-6858.
    • (1995) J. Virol. , vol.69 , pp. 6852-6858
    • Black, A.C.1    Luo, J.2    Watanabe, C.3    Chun, S.4    Bakker, A.5    Faser, J.K.6    Morgan, J.P.7    Rosenblatt, J.D.8
  • 10
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1 alpha interacts with the 3′ stem-loop region of West Nile virus genomic RNA
    • Blackwell J. L., Brinton M. A. Translation elongation factor-1 alpha interacts with the 3′ stem-loop region of West Nile virus genomic RNA. J. Virol. 71:1997;6433-6444.
    • (1997) J. Virol. , vol.71 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 11
    • 0018370008 scopus 로고
    • RNA replication: Function and structure of Qβ-replicase
    • Blumenthal T., Carmichael G. G. RNA replication: Function and structure of Qβ-replicase. Annu. Rev. Biochem. 48:1979;525-548.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 525-548
    • Blumenthal, T.1    Carmichael, G.G.2
  • 12
    • 0029763192 scopus 로고    scopus 로고
    • Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5′ noncoding region: Identification by automated liquid chromatography-tandem mass spectrometry
    • Blyn L. B., Swiderek K. M., Richards O., Stahl D. C., Semler B. L., Ehrenfeld E. Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5′ noncoding region: Identification by automated liquid chromatography-tandem mass spectrometry. Proc. Natl. Acad. Sci. USA. 93:1996;11115-11120.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11115-11120
    • Blyn, L.B.1    Swiderek, K.M.2    Richards, O.3    Stahl, D.C.4    Semler, B.L.5    Ehrenfeld, E.6
  • 14
    • 0019811706 scopus 로고
    • Host cell nuclear function and murine hepatitis virus replication
    • Brayton P. R., Ganges R. G., Stohlman S. A. Host cell nuclear function and murine hepatitis virus replication. J. Gen. Virol. 56:1981;457-460.
    • (1981) J. Gen. Virol. , vol.56 , pp. 457-460
    • Brayton, P.R.1    Ganges, R.G.2    Stohlman, S.A.3
  • 15
    • 0030332528 scopus 로고    scopus 로고
    • Comparison of the replication of positive-stranded RNA viruses of plants and animals
    • Buck K. W. Comparison of the replication of positive-stranded RNA viruses of plants and animals. Adv. Virus Res. 47:1996;159-251.
    • (1996) Adv. Virus Res. , vol.47 , pp. 159-251
    • Buck, K.W.1
  • 16
    • 0028130256 scopus 로고
    • Direct interactions between autoantigen La and human immunodeficiency virus leader RNA
    • Chang Y.-N., Kenan D. J., Keene J. D., Gatignol A., Jeang K.-T. Direct interactions between autoantigen La and human immunodeficiency virus leader RNA. J. Virol. 68:1994;7008-7020.
    • (1994) J. Virol. , vol.68 , pp. 7008-7020
    • Chang, Y.-N.1    Kenan, D.J.2    Keene, J.D.3    Gatignol, A.4    Jeang, K.-T.5
  • 17
    • 0024110350 scopus 로고
    • NH2-terminal acidic region of the phosphoprotein of vesicular stomatitis virus can be functionally replaced by tubulin
    • Chattopadhyay D., Banerjee A. K. NH2-terminal acidic region of the phosphoprotein of vesicular stomatitis virus can be functionally replaced by tubulin. Proc. Natl. Acad. Sci. USA. 85:1988;7977-7981.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7977-7981
    • Chattopadhyay, D.1    Banerjee, A.K.2
  • 18
    • 0031001919 scopus 로고    scopus 로고
    • RNA-protein interactions: Involvement of NS3, NS5, and 3′ noncoding regions of Japanese encephalitis virus genomic RNA
    • Chen C.-J., Kuo M.-D., Chien L.-J., Hsu S.-L., Wang Y.-M., Lin J.-H. RNA-protein interactions: Involvement of NS3, NS5, and 3′ noncoding regions of Japanese encephalitis virus genomic RNA. J. Virol. 71:1997;3466-3473.
    • (1997) J. Virol. , vol.71 , pp. 3466-3473
    • Chen, C.-J.1    Kuo, M.-D.2    Chien, L.-J.3    Hsu, S.-L.4    Wang, Y.-M.5    Lin, J.-H.6
  • 19
    • 0027501562 scopus 로고
    • Binding of the encephalomyocarditis virus RNA polymerase to the 3′-noncoding region of the viral RNA is specific and requires the 3′-poly(A) tail
    • Cui T., Sankar S., Porter A. G. Binding of the encephalomyocarditis virus RNA polymerase to the 3′-noncoding region of the viral RNA is specific and requires the 3′-poly(A) tail. J. Biol. Chem. 268:1993;26093-26098.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26093-26098
    • Cui, T.1    Sankar, S.2    Porter, A.G.3
  • 20
    • 0032539680 scopus 로고    scopus 로고
    • RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ or its activity
    • Das T., Mathur M., Gupta A. K., Janssen G. M. C., Banerjee A. K. RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ or its activity. Proc. Natl. Acad. Sci. USA. 95:1998;1460-1465.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 1460-1465
    • Das, T.1    Mathur, M.2    Gupta, A.K.3    Janssen, G.M.C.4    Banerjee, A.K.5
  • 21
    • 0018872675 scopus 로고
    • Dependence of the poliovirus replicase on a host cell protein
    • Dasgupta A., Zabel P., Baltimore D. Dependence of the poliovirus replicase on a host cell protein. Cell. 19:1980;423-429.
    • (1980) Cell , vol.19 , pp. 423-429
    • Dasgupta, A.1    Zabel, P.2    Baltimore, D.3
  • 22
    • 0030634388 scopus 로고    scopus 로고
    • Role of host proteins in gene expression of nonsegmented negative strand RNA viruses
    • De B. P., Banerjee A. K. Role of host proteins in gene expression of nonsegmented negative strand RNA viruses. Adv. Virus Res. 48:1997;169-204.
    • (1997) Adv. Virus Res. , vol.48 , pp. 169-204
    • De, B.P.1    Banerjee, A.K.2
  • 23
    • 0029760743 scopus 로고    scopus 로고
    • Specific interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and La protein with cis-acting RNAs of human parainfluenza virus type 3
    • De B. P., Gupta S., Zhao H., Drazba J. A., Banerjee A. K. Specific interaction in vitro and in vivo of glyceraldehyde-3-phosphate dehydrogenase and La protein with cis-acting RNAs of human parainfluenza virus type 3. J. Biol. Chem. 271:1996;24728-24735.
    • (1996) J. Biol. Chem , vol.271 , pp. 24728-24735
    • De, B.P.1    Gupta, S.2    Zhao, H.3    Drazba, J.A.4    Banerjee, A.K.5
  • 24
    • 0026048424 scopus 로고
    • Human parainfluenza virus type 3 transcription in vitro: Role of cellular actin in mRNA synthesis
    • De B. P., Lesson A., Banerjee A. K. Human parainfluenza virus type 3 transcription in vitro: Role of cellular actin in mRNA synthesis. J. Virol. 65:1991;3268-3275.
    • (1991) J. Virol. , vol.65 , pp. 3268-3275
    • De, B.P.1    Lesson, A.2    Banerjee, A.K.3
  • 25
    • 0000605218 scopus 로고
    • Purification of cowpea mosaic virus RNA replication complex: Identification of a virus-encoded 110,000-dalton polypeptide responsible for RNA chain elongation
    • Dorssers L., van der Krol S., van der Meer J., van Kammen A., Zabel P. Purification of cowpea mosaic virus RNA replication complex: Identification of a virus-encoded 110,000-dalton polypeptide responsible for RNA chain elongation. Proc. Natl. Acad. Sci. USA. 81:1984;1951-1955.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1951-1955
    • Dorssers, L.1    Van Der Krol, S.2    Van Der Meer, J.3    Van Kammen, A.4    Zabel, P.5
  • 26
    • 0029910194 scopus 로고    scopus 로고
    • Reversible dissociation of the poliovirus replication complex: Functions and interactions of its components in viral RNA synthesis
    • Egger D., Pasamontes L., Bolten R., Boyko V., Bienz K. Reversible dissociation of the poliovirus replication complex: Functions and interactions of its components in viral RNA synthesis. J. Virol. 70:1996;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
  • 27
    • 0024430108 scopus 로고
    • Internal and terminal cis-acting sites are necessary for in vitro replication of L-A double-stranded RNA virus of yeast
    • Esteban R., Fujinami T., Wickner R. B. Internal and terminal cis-acting sites are necessary for in vitro replication of L-A double-stranded RNA virus of yeast. EMBO J. 8:1989;947-954.
    • (1989) EMBO J. , vol.8 , pp. 947-954
    • Esteban, R.1    Fujinami, T.2    Wickner, R.B.3
  • 28
    • 0030861261 scopus 로고    scopus 로고
    • Two functional complexes formed by KH domain containing proteins with the 5′ noncoding region of poliovirus RNA
    • Gamarnik A. V., Andino R. Two functional complexes formed by KH domain containing proteins with the 5′ noncoding region of poliovirus RNA. RNA. 3:1997;882-892.
    • (1997) RNA , vol.3 , pp. 882-892
    • Gamarnik, A.V.1    Andino, R.2
  • 30
    • 0022365286 scopus 로고
    • Transcription complex of Newcastle disease virus. II. Structural and functional assembly associated with the cytoskeletal framework
    • Hamaguchi M., Nishikawa K., Toyoda T., Yoshida T., Hanaichi T., Nagai Y. Transcription complex of Newcastle disease virus. II. Structural and functional assembly associated with the cytoskeletal framework. Virology. 47:1985;295-308.
    • (1985) Virology , vol.47 , pp. 295-308
    • Hamaguchi, M.1    Nishikawa, K.2    Toyoda, T.3    Yoshida, T.4    Hanaichi, T.5    Nagai, Y.6
  • 31
    • 0027959741 scopus 로고
    • Interaction of poliovirus polypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome: Identification of viral and cellular cofactors needed for efficient binding
    • Harris K. S., Xiang W., Alexander L., Lane W. S., Paul A. V., Wimmer E. Interaction of poliovirus polypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome: Identification of viral and cellular cofactors needed for efficient binding. J. Biol. Chem. 269:1994;27004-27014.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27004-27014
    • Harris, K.S.1    Xiang, W.2    Alexander, L.3    Lane, W.S.4    Paul, A.V.5    Wimmer, E.6
  • 32
    • 0025036709 scopus 로고
    • Complete replication of a eukaryotic virus RNA in vitro by a purified RNA-dependent RNA polymerase
    • Hayes R. J., Buck K. W. Complete replication of a eukaryotic virus RNA in vitro by a purified RNA-dependent RNA polymerase. Cell. 63:1990;363-368.
    • (1990) Cell , vol.63 , pp. 363-368
    • Hayes, R.J.1    Buck, K.W.2
  • 33
    • 0027172207 scopus 로고
    • A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein
    • Hellen C. U. T., Witherell G. W., Schmid M., Shin S. H., Pestova T. V., Gil A., Wimmer E. A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein. Proc. Natl. Acad. Sci. USA. 90:1993;7642-7646.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7642-7646
    • Hellen, C.U.T.1    Witherell, G.W.2    Schmid, M.3    Shin, S.H.4    Pestova, T.V.5    Gil, A.6    Wimmer, E.7
  • 34
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann J. D., Chamberlin M. J. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 57:1988;839-872.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.J.2
  • 35
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J., Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. USA. 93:1996;1060-1064.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 36
    • 0027273916 scopus 로고
    • Characterization of the in vitro system for the synthesis of mRNA from human respiratory syncytial virus
    • Huang Y. T., Romito R. R., De B. P., Banerjee A. K. Characterization of the in vitro system for the synthesis of mRNA from human respiratory syncytial virus. Virology. 193:1993;862-867.
    • (1993) Virology , vol.193 , pp. 862-867
    • Huang, Y.T.1    Romito, R.R.2    De, B.P.3    Banerjee, A.K.4
  • 37
    • 0031459463 scopus 로고    scopus 로고
    • Yeast mutations in multiple complementation groups inhibit brome mosaic virus RNA replication and transcription and perturb regulated expression of the viral polymerase-like gene
    • Ishikawa M., Diez J., Restrepo-Hartwig M., Ahlquist P. Yeast mutations in multiple complementation groups inhibit brome mosaic virus RNA replication and transcription and perturb regulated expression of the viral polymerase-like gene. Proc. Natl. Acad. Sci. USA. 94:1997;13810-13815.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13810-13815
    • Ishikawa, M.1    Diez, J.2    Restrepo-Hartwig, M.3    Ahlquist, P.4
  • 38
    • 0030812847 scopus 로고    scopus 로고
    • Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of hepatitis C virus RNA genome
    • Ito T., Lai M. M. C. Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of hepatitis C virus RNA genome. J. Virol. 71:1997;8698-8706.
    • (1997) J. Virol. , vol.71 , pp. 8698-8706
    • Ito, T.1    Lai, M.M.C.2
  • 39
    • 0027469808 scopus 로고
    • RNA-dependent replication, transcription, and persistence of brome mosaic virus RNA replicons in S. cerevisiae
    • Janda M., Ahlquist P. RNA-dependent replication, transcription, and persistence of brome mosaic virus RNA replicons in S. cerevisiae. Cell. 72:1993;961-970.
    • (1993) Cell , vol.72 , pp. 961-970
    • Janda, M.1    Ahlquist, P.2
  • 40
    • 0022740202 scopus 로고
    • Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1α. Search for a function
    • Joshi R. L., Ravel J. M., Haenni A. L. Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1α. Search for a function. EMBO J. 5:1986;1143-1148.
    • (1986) EMBO J. , vol.5 , pp. 1143-1148
    • Joshi, R.L.1    Ravel, J.M.2    Haenni, A.L.3
  • 41
    • 0019409081 scopus 로고
    • Temperature-sensitive host-dependent mutants of Sindbis virus
    • Kowal K. J., Stollar V. Temperature-sensitive host-dependent mutants of Sindbis virus. Virology. 114:1981;140-148.
    • (1981) Virology , vol.114 , pp. 140-148
    • Kowal, K.J.1    Stollar, V.2
  • 42
    • 0026443665 scopus 로고
    • Attenuation of Sindbis virus neurovirulence by using defined mutations in nontranslated regions of the genome RNA
    • Kuhn R. J., Griffin D. E., Zhang H., Niesters H. G. M., Strauss J. H. Attenuation of Sindbis virus neurovirulence by using defined mutations in nontranslated regions of the genome RNA. J. Virol. 66:1981;7121-7127.
    • (1981) J. Virol. , vol.66 , pp. 7121-7127
    • Kuhn, R.J.1    Griffin, D.E.2    Zhang, H.3    Niesters, H.G.M.4    Strauss, J.H.5
  • 43
    • 0021253722 scopus 로고
    • Nucleotide sequence and host La protein interactions of rabies virus leader RNA
    • Kurilla M. G., Cabradilla C. D., Holloway B. P., Keene J. D. Nucleotide sequence and host La protein interactions of rabies virus leader RNA. J. Virol. 50:1984;773-778.
    • (1984) J. Virol. , vol.50 , pp. 773-778
    • Kurilla, M.G.1    Cabradilla, C.D.2    Holloway, B.P.3    Keene, J.D.4
  • 44
    • 0020559403 scopus 로고
    • The leader RNA of vesicular stomatitis virus is bound by a cellular protein reactive with anti-La lupus antibodies
    • Kurilla M. G., Keene J. D. The leader RNA of vesicular stomatitis virus is bound by a cellular protein reactive with anti-La lupus antibodies. Cell. 34:1983;837-845.
    • (1983) Cell , vol.34 , pp. 837-845
    • Kurilla, M.G.1    Keene, J.D.2
  • 45
    • 0030030793 scopus 로고    scopus 로고
    • RNA-protein interactions at the 3′ end of the hepatitis A virus RNA
    • Kusov Y., Weitz M., Dollenmeier G., Gauss-Muller V., Siegl G. RNA-protein interactions at the 3′ end of the hepatitis A virus RNA. J. Virol. 70:1996;1890-1897.
    • (1996) J. Virol. , vol.70 , pp. 1890-1897
    • Kusov, Y.1    Weitz, M.2    Dollenmeier, G.3    Gauss-Muller, V.4    Siegl, G.5
  • 46
    • 0027294694 scopus 로고
    • Contributions of the brome mosaic virus RNA-3 3′-nontranslated region to replication and translation
    • Lahser F. C., Marsh L. E., Hall T. C. Contributions of the brome mosaic virus RNA-3 3′-nontranslated region to replication and translation. J. Virol. 67:1993;3295-3303.
    • (1993) J. Virol. , vol.67 , pp. 3295-3303
    • Lahser, F.C.1    Marsh, L.E.2    Hall, T.C.3
  • 47
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • New York: Academic Press. p. 1-100
    • Lai M. M. C., Cavanagh D. The molecular biology of coronaviruses. Advances in Virus Research. 1997;Academic Press, New York. p. 1-100.
    • (1997) Advances in Virus Research
    • Lai, M.M.C.1    Cavanagh, D.2
  • 48
    • 0028047922 scopus 로고
    • Coronavirus: How a large RNA viral genome is replicated and transcribed
    • Lai M. M. C., Liao C.-L., Lin Y.-J., Zhang X. Coronavirus: How a large RNA viral genome is replicated and transcribed. Infect. Agents Dis. 3:1994;98-105.
    • (1994) Infect. Agents Dis. , vol.3 , pp. 98-105
    • Lai, M.M.C.1    Liao, C.-L.2    Lin, Y.-J.3    Zhang, X.4
  • 49
    • 0027296795 scopus 로고
    • A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation
    • Leathers V., Tanguay R., Kobayashi M., Gallie D. R. A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation. Mol. Cell. Biol. 13:1993;5331-5347.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5331-5347
    • Leathers, V.1    Tanguay, R.2    Kobayashi, M.3    Gallie, D.R.4
  • 50
    • 0030885826 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA
    • Li H.-P., Zhang X., Duncan R., Comai L., Lai M. M. C. Heterogeneous nuclear ribonucleoprotein A1 binds to the transcription-regulatory region of mouse hepatitis virus RNA. Proc. Natl. Acad. Sci. USA. 94:1997;9544-9549.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9544-9549
    • Li, H.-P.1    Zhang, X.2    Duncan, R.3    Comai, L.4    Lai, M.M.C.5
  • 51
    • 0028234463 scopus 로고
    • Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription
    • Liao C.-L., Lai M. M. C. Requirement of the 5′-end genomic sequence as an upstream cis-acting element for coronavirus subgenomic mRNA transcription. J. Virol. 68:1994;4727-4737.
    • (1994) J. Virol. , vol.68 , pp. 4727-4737
    • Liao, C.-L.1    Lai, M.M.C.2
  • 52
    • 0029036798 scopus 로고
    • A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA
    • Liao C. L., Lai M. M. C. A cis-acting viral protein is not required for the replication of a coronavirus defective-interfering RNA. Virology. 209:1995;428-436.
    • (1995) Virology , vol.209 , pp. 428-436
    • Liao, C.L.1    Lai, M.M.C.2
  • 53
    • 0029836505 scopus 로고    scopus 로고
    • The 3′ untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA
    • Lin Y. J., Zhang X. M., Wu R. C., Lai M. M. C. The 3′ untranslated region of coronavirus RNA is required for subgenomic mRNA transcription from a defective interfering RNA. J. Virol. 70:1996;7236-7240.
    • (1996) J. Virol. , vol.70 , pp. 7236-7240
    • Lin, Y.J.1    Zhang, X.M.2    Wu, R.C.3    Lai, M.M.C.4
  • 54
    • 0026093588 scopus 로고
    • The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure
    • Luo G., Luytjes W., Enami M., Palese P. The polyadenylation signal of influenza virus RNA involves a stretch of uridines followed by the RNA duplex of the panhandle structure. J. Virol. 65:1991;2861-2867.
    • (1991) J. Virol. , vol.65 , pp. 2861-2867
    • Luo, G.1    Luytjes, W.2    Enami, M.3    Palese, P.4
  • 55
    • 0026525537 scopus 로고
    • Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells
    • Macejak D. G., Sarnow P. Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells. J. Virol. 66:1992;1520-1527.
    • (1992) J. Virol. , vol.66 , pp. 1520-1527
    • MacEjak, D.G.1    Sarnow, P.2
  • 56
    • 0029911783 scopus 로고    scopus 로고
    • Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells
    • McBride A. E., Schlegel A., Kirkegaard K. Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells. Proc. Natl. Acad. Sci. USA. 93:1996;2296-2301.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2296-2301
    • McBride, A.E.1    Schlegel, A.2    Kirkegaard, K.3
  • 58
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A., Paul A. V., 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
  • 59
    • 0025356092 scopus 로고
    • Host cell proteins required for measles virus reproduction
    • Moyer S. A., Baker S. C., Horikami S. M. Host cell proteins required for measles virus reproduction. J. Gen. Virol. 71:1990;775-783.
    • (1990) J. Gen. Virol. , vol.71 , pp. 775-783
    • Moyer, S.A.1    Baker, S.C.2    Horikami, S.M.3
  • 60
    • 0007784673 scopus 로고
    • Tubulin: A factor necessary for the synthesis of both Sendai virus and vesicular stomatitis virus RNAs
    • Moyer S. A., Baker S. C., Lessard J. L. Tubulin: A factor necessary for the synthesis of both Sendai virus and vesicular stomatitis virus RNAs. Proc. Natl. Acad. Sci. USA. 83:1986;5405-5409.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5405-5409
    • Moyer, S.A.1    Baker, S.C.2    Lessard, J.L.3
  • 61
  • 62
    • 0028136217 scopus 로고
    • Coupling between genome translation and replication in an RNA virus
    • Novak J. E., Kirkegaard K. Coupling between genome translation and replication in an RNA virus. Genes Dev. 8:1994;1726-1737.
    • (1994) Genes Dev. , vol.8 , pp. 1726-1737
    • Novak, J.E.1    Kirkegaard, K.2
  • 63
    • 0028068073 scopus 로고
    • Cis-acting signals and trans-acting factors involved in influenza virus RNA synthesis
    • O'Neill R. E., Palese P. Cis-acting signals and trans-acting factors involved in influenza virus RNA synthesis. Infect. Agents Dis. 3:1994;77-84.
    • (1994) Infect. Agents Dis. , vol.3 , pp. 77-84
    • O'Neill, R.E.1    Palese, P.2
  • 64
    • 0029839350 scopus 로고    scopus 로고
    • The highly inducible member of the 70 kDa family of heat shock proteins increases canine distemper virus polymerase activity
    • Oglesbee M. J., Liu Z., Kennery H., Brooks C. L. The highly inducible member of the 70 kDa family of heat shock proteins increases canine distemper virus polymerase activity. J. Gen. Virol. 77:1996;2125-2135.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2125-2135
    • Oglesbee, M.J.1    Liu, Z.2    Kennery, H.3    Brooks, C.L.4
  • 65
    • 0030738093 scopus 로고    scopus 로고
    • The tobacco mosaic virus RNA polymerase complex contains a plant protein related to the RNA-binding subunit of yeast eIF-3
    • Osman T. A. M., Buck K. W. The tobacco mosaic virus RNA polymerase complex contains a plant protein related to the RNA-binding subunit of yeast eIF-3. J. Virol. 71:1997;6075-6082.
    • (1997) J. Virol. , vol.71 , pp. 6075-6082
    • Osman, T.A.M.1    Buck, K.W.2
  • 66
    • 0030060397 scopus 로고    scopus 로고
    • Mosquito homolog of the La autoantigen binds to Sindbis virus RNA
    • Pardigon N., Strauss J. H. Mosquito homolog of the La autoantigen binds to Sindbis virus RNA. J. Virol. 70:1996;1173-1187.
    • (1996) J. Virol. , vol.70 , pp. 1173-1187
    • Pardigon, N.1    Strauss, J.H.2
  • 67
    • 0030820403 scopus 로고    scopus 로고
    • Poly (rC) binding protein 2 forms a ternary complex with the 5′-terminal sequences of poliovirus RNA and the viral 3CD proteinase
    • Parsley T. B., Towner J. S., Blyn L. B., Ehrenfeld E., Semler B. L. Poly (rC) binding protein 2 forms a ternary complex with the 5′-terminal sequences of poliovirus RNA and the viral 3CD proteinase. RNA. 3:1997;1124-1134.
    • (1997) RNA , vol.3 , pp. 1124-1134
    • Parsley, T.B.1    Towner, J.S.2    Blyn, L.B.3    Ehrenfeld, E.4    Semler, B.L.5
  • 68
    • 0026572608 scopus 로고
    • Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: A proposal for the existence of tRNA-like terminal structures
    • Pilipenko E. V., Maslova S. V., Sinyakov A. N., Agol V. I. Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: A proposal for the existence of tRNA-like terminal structures. Nucleic Acids Res. 20:1992;1739-1745.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1739-1745
    • Pilipenko, E.V.1    Maslova, S.V.2    Sinyakov, A.N.3    Agol, V.I.4
  • 69
    • 0026500564 scopus 로고
    • The requirement for a 5′ stem-loop structure in brome mosaic virus replication supports a new model for viral positive-strand RNA initiation
    • Pogue G. P., Hall T. C. The requirement for a 5′ stem-loop structure in brome mosaic virus replication supports a new model for viral positive-strand RNA initiation. J. Virol. 66:1992;674-684.
    • (1992) J. Virol. , vol.66 , pp. 674-684
    • Pogue, G.P.1    Hall, T.C.2
  • 71
    • 0029823996 scopus 로고    scopus 로고
    • Complete replication of an animal virus and maintenance of expression vectors derived from it inSacchromyces cerevisiae
    • Price B. D., Rueckert R. R., Ahlquist P. Complete replication of an animal virus and maintenance of expression vectors derived from it inSacchromyces cerevisiae. Proc. Natl. Acad. Sci. USA. 93:1996;9465-9470.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9465-9470
    • Price, B.D.1    Rueckert, R.R.2    Ahlquist, P.3
  • 72
    • 0028999960 scopus 로고
    • Formation of brome mosaic virus RNA-dependent RNA polymerase in yeast requires coexpression of viral proteins and viral RNA
    • Quadt R., Ishikawa M., Janda M., Ahlquist P. Formation of brome mosaic virus RNA-dependent RNA polymerase in yeast requires coexpression of viral proteins and viral RNA. Proc. Natl. Acad. Sci. USA. 92:1995;4892-4896.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4892-4896
    • Quadt, R.1    Ishikawa, M.2    Janda, M.3    Ahlquist, P.4
  • 73
    • 0027497972 scopus 로고
    • Characterization of a host protein associated with brome mosaic virus RNA-dependent RNA polymerase
    • Quadt R., Kao C. C., Browning K. S., Hershberger R. P., Ahlquist P. Characterization of a host protein associated with brome mosaic virus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. USA. 90:1993;1498-1502.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1498-1502
    • Quadt, R.1    Kao, C.C.2    Browning, K.S.3    Hershberger, R.P.4    Ahlquist, P.5
  • 74
    • 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., Ahlquist P. Brome mosaic virus helicase- and polymerase-like proteins colocalize on the endoplasmic reticulum at sites of viral RNA synthesis. J. Virol. 70:1996;8908-8916.
    • (1996) J. Virol. , vol.70 , pp. 8908-8916
    • Restrepo-Hartwig, M.A.1    Ahlquist, P.2
  • 75
    • 0028949310 scopus 로고
    • Poliovirus infection enhances the formation of two ribonucleoprotein complexes at the 3′-end of viral negative-strand RNA
    • Roehl H. H., Semler B. L. Poliovirus infection enhances the formation of two ribonucleoprotein complexes at the 3′-end of viral negative-strand RNA. J. Virol. 69:1995;2954-2961.
    • (1995) J. Virol. , vol.69 , pp. 2954-2961
    • Roehl, H.H.1    Semler, B.L.2
  • 76
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A., Giddings T. H. J., Ladinsky M. S., Kirkegaard K. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:1996;6576-6588.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings, T.H.J.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 77
    • 0029927267 scopus 로고    scopus 로고
    • Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis A virus
    • Schultz D. E., Hardin C. C., Lemon S. M. Specific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5′-nontranslated RNA of hepatitis A virus. J. Biol. Chem. 271:1996;14134-14142.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14134-14142
    • Schultz, D.E.1    Hardin, C.C.2    Lemon, S.M.3
  • 78
    • 0028598355 scopus 로고
    • Regulation of influenza virus RNA polymerase activity by cellular and viral factors
    • Shimizu K., Handa H., Nakada S., Nagata K. Regulation of influenza virus RNA polymerase activity by cellular and viral factors. Nucleic Acids Res. 22:1994;5047-5053.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5047-5053
    • Shimizu, K.1    Handa, H.2    Nakada, S.3    Nagata, K.4
  • 79
    • 0027280985 scopus 로고
    • Temperature-sensitive mouse cell factors for strand-specific initiation of poliovirus RNA synthesis
    • Shiroki K., Kato H., Koike S., Odaka T., Nomoto A. Temperature-sensitive mouse cell factors for strand-specific initiation of poliovirus RNA synthesis. J. Virol. 67:1993;3989-3996.
    • (1993) J. Virol. , vol.67 , pp. 3989-3996
    • Shiroki, K.1    Kato, H.2    Koike, S.3    Odaka, T.4    Nomoto, A.5
  • 80
    • 0030761264 scopus 로고    scopus 로고
    • Sequence-specific recognition of a subgenomic RNA promoter by a viral RNA polymerase
    • Siegel R. W., Adkins S., Kao C. C. Sequence-specific recognition of a subgenomic RNA promoter by a viral RNA polymerase. Proc. Natl. Acad. Sci. USA. 94:1997;11238-11243.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11238-11243
    • Siegel, R.W.1    Adkins, S.2    Kao, C.C.3
  • 81
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh N. K., Atreya C. D., Nakhasi H. L. Identification of calreticulin as a rubella virus RNA binding protein. Proc. Natl. Acad. Sci. USA. 91:1994;12770-12774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12770-12774
    • Singh, N.K.1    Atreya, C.D.2    Nakhasi, H.L.3
  • 82
    • 0028584238 scopus 로고
    • RNA-dependent RNA polymerase from plants infected with turnip crinkle virus can transcribe (+)- and (-)-strands of virus-associated RNAs
    • Song C., Simon A. E. RNA-dependent RNA polymerase from plants infected with turnip crinkle virus can transcribe (+)- and (-)-strands of virus-associated RNAs. Proc. Natl. Acad. Sci. USA. 91:1994;8792-8796.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8792-8796
    • Song, C.1    Simon, A.E.2
  • 83
    • 0028034999 scopus 로고
    • La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA
    • Svitkin Y. V., Pause A., Sonenberg N. La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA. J. Virol. 68:1994;7001-7007.
    • (1994) J. Virol. , vol.68 , pp. 7001-7007
    • Svitkin, Y.V.1    Pause, A.2    Sonenberg, N.3
  • 84
    • 0029863798 scopus 로고    scopus 로고
    • Recombinant dengue type 1 virus NS5 protein expressed inEscherichia coliexhibits RNA-dependent RNA polymerase activity
    • Tan B.-H., Fu J., Sugrue R. J., Yap E.-H., Chan Y.-C., Tan Y.-H. Recombinant dengue type 1 virus NS5 protein expressed inEscherichia coliexhibits RNA-dependent RNA polymerase activity. Virology. 216:1996;317-325.
    • (1996) Virology , vol.216 , pp. 317-325
    • Tan, B.-H.1    Fu, J.2    Sugrue, R.J.3    Yap, E.-H.4    Chan, Y.-C.5    Tan, Y.-H.6
  • 85
    • 0028228459 scopus 로고
    • Sequence-specific binding of the influenza virus RNA polymerase to sequences located at the 5′-ends of the viral RNAs
    • Tiley L. S., Hagen M., Matthews J. T., Krystal M. Sequence-specific binding of the influenza virus RNA polymerase to sequences located at the 5′-ends of the viral RNAs. J. Virol. 68:1994;5108-5116.
    • (1994) J. Virol. , vol.68 , pp. 5108-5116
    • Tiley, L.S.1    Hagen, M.2    Matthews, J.T.3    Krystal, M.4
  • 86
    • 0030802760 scopus 로고    scopus 로고
    • Replication-competent picornaviruses with complete genomic RNA 3′ noncoding region deletions
    • Todd S., Towner J. S., Brown D. M., Semler B. L. Replication-competent picornaviruses with complete genomic RNA 3′ noncoding region deletions. J. Virol. 71:1997;8868-8874.
    • (1997) J. Virol. , vol.71 , pp. 8868-8874
    • Todd, S.1    Towner, J.S.2    Brown, D.M.3    Semler, B.L.4
  • 87
    • 0030861248 scopus 로고    scopus 로고
    • Specific interaction of polypyrimidine tract-binding protein with the extreme 3′-terminal structure of the hepatitis C virus genome, the 3′X
    • Tsuchihara K., Tanaka T., Hijikata M., Kuge S., Toyoda H., Nomoto A., Yamamoto N., Shimotohno K. Specific interaction of polypyrimidine tract-binding protein with the extreme 3′-terminal structure of the hepatitis C virus genome, the 3′X. J. Virol. 71:1997;6720-6726.
    • (1997) J. Virol. , vol.71 , pp. 6720-6726
    • Tsuchihara, K.1    Tanaka, T.2    Hijikata, M.3    Kuge, S.4    Toyoda, H.5    Nomoto, A.6    Yamamoto, N.7    Shimotohno, K.8
  • 88
    • 0029013594 scopus 로고
    • Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus
    • van der Most R. G., Luytjes W., Rutjes S., Spaan W. J. M. Translation but not the encoded sequence is essential for the efficient propagation of the defective interfering RNAs of the coronavirus mouse hepatitis virus. J. Virol. 69:1995;3744-3751.
    • (1995) J. Virol. , vol.69 , pp. 3744-3751
    • Van Der Most, R.G.1    Luytjes, W.2    Rutjes, S.3    Spaan, W.J.M.4
  • 89
    • 0028834373 scopus 로고
    • Characterization of sequences controlling the synthesis of alfalfa mosaic virus subgenomic RNA in vivo
    • van der Vossen E. A. G., Notenboom T., Bol J. F. Characterization of sequences controlling the synthesis of alfalfa mosaic virus subgenomic RNA in vivo. Virology. 212:1995;663-672.
    • (1995) Virology , vol.212 , pp. 663-672
    • Van Der Vossen, E.A.G.1    Notenboom, T.2    Bol, J.F.3
  • 90
    • 0000694197 scopus 로고
    • Single-stranded RNA bacteriophages
    • New York: Plenum. p. 117-178
    • van Duin J. Single-stranded RNA bacteriophages. The Bacteriophages. 1988;Plenum, New York. p. 117-178.
    • (1988) The Bacteriophages
    • Van Duin, J.1
  • 91
    • 0028122443 scopus 로고
    • Extent of terminal complementarity modulates the balance between transcription and replication of vesicular stomatitis virus RNA
    • Wertz G. W., Whelan S., LeGrone A., Ball L. A. Extent of terminal complementarity modulates the balance between transcription and replication of vesicular stomatitis virus RNA. Proc. Natl. Acad. Sci. USA. 91:1994;8587-8591.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8587-8591
    • Wertz, G.W.1    Whelan, S.2    Legrone, A.3    Ball, L.A.4
  • 92
    • 0026594261 scopus 로고
    • Coding capacity determines in vivo accumulation of a defective RNA of clover yellow mosaic virus
    • White K. A., Bancroft J. B., Mackie G. A. Coding capacity determines in vivo accumulation of a defective RNA of clover yellow mosaic virus. J. Virol. 66:1992;3069-3076.
    • (1992) J. Virol. , vol.66 , pp. 3069-3076
    • White, K.A.1    Bancroft, J.B.2    MacKie, G.A.3
  • 93
    • 0019420713 scopus 로고
    • The replication of murine coronaviruses in enucleated cells
    • Wilhelmsen K. C., Leibowitz J. L., Bond C. W., Robb J. A. The replication of murine coronaviruses in enucleated cells. Virology. 110:1981;225-230.
    • (1981) Virology , vol.110 , pp. 225-230
    • Wilhelmsen, K.C.1    Leibowitz, J.L.2    Bond, C.W.3    Robb, J.A.4
  • 94
    • 0021081965 scopus 로고
    • A host protein (La) binds to a unique species of minus-sense leader RNA during replication of vesicular stomatitis virus
    • Wilusz J., Kurilla M. G., Keene J. D. A host protein (La) binds to a unique species of minus-sense leader RNA during replication of vesicular stomatitis virus. Proc. Natl. Acad. Sci. USA. 80:1983;5827-5831.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5827-5831
    • Wilusz, J.1    Kurilla, M.G.2    Keene, J.D.3
  • 95
    • 0028889896 scopus 로고
    • Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed
    • Zhang X., Lai M. M. C. Interactions between the cytoplasmic proteins and the intergenic (promoter) sequence of mouse hepatitis virus RNA: Correlation with the amounts of subgenomic mRNA transcribed. J. Virol. 69:1995;1637-1644.
    • (1995) J. Virol. , vol.69 , pp. 1637-1644
    • Zhang, X.1    Lai, M.M.C.2
  • 96
    • 0028284497 scopus 로고
    • Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis
    • Zhang X., Liao C.-L., Lai M. M. C. Coronavirus leader RNA regulates and initiates subgenomic mRNA transcription, both in trans and in cis. J. Virol. 68:1994;4738-4746.
    • (1994) J. Virol. , vol.68 , pp. 4738-4746
    • Zhang, X.1    Liao, C.-L.2    Lai, M.M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.