메뉴 건너뛰기




Volumn 129, Issue 1, 2007, Pages 43-53

Characterization of interaction of classical swine fever virus NS3 helicase with 3′ untranslated region

Author keywords

3 UTR; Classical swine fever virus; Helicase; NS3

Indexed keywords

HELICASE; LIVE VACCINE; NONSTRUCTURAL PROTEIN 3;

EID: 34548226912     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2007.05.004     Document Type: Article
Times cited : (21)

References (55)
  • 1
    • 0035138086 scopus 로고    scopus 로고
    • Specific interaction of hepatitis C virus protease/helicase NS3 with the 3′-terminal sequences of viral positive- and negative-strand RNA
    • Banerjee R., and Dasgupta A. Specific interaction of hepatitis C virus protease/helicase NS3 with the 3′-terminal sequences of viral positive- and negative-strand RNA. J. Virol. 75 (2001) 1708-1721
    • (2001) J. Virol. , vol.75 , pp. 1708-1721
    • Banerjee, R.1    Dasgupta, A.2
  • 2
    • 0030831556 scopus 로고    scopus 로고
    • Polio virus-encoded 2C polypeptide specifically binds to the 39-terminal sequences of viral negativestrand RNA
    • Banerjee R., Echeverri A., and Dasgupta A. Polio virus-encoded 2C polypeptide specifically binds to the 39-terminal sequences of viral negativestrand RNA. J. Virol. 71 (1997) 9570-9578
    • (1997) J. Virol. , vol.71 , pp. 9570-9578
    • Banerjee, R.1    Echeverri, A.2    Dasgupta, A.3
  • 3
    • 0027287798 scopus 로고
    • Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
    • Bartenschlager R., Ahlborn-Laake L., Mous J., and Jacobsen H. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 67 (1993) 3835-3844
    • (1993) J. Virol. , vol.67 , pp. 3835-3844
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Mous, J.3    Jacobsen, H.4
  • 4
    • 0011744632 scopus 로고    scopus 로고
    • Genus Pestivirus (Flaviviridae)
    • Tidona C.A., and Darai G. (Eds), Springer-Verlag, Heidelberg, Germany
    • Becher P., and Thiel H.-J. Genus Pestivirus (Flaviviridae). In: Tidona C.A., and Darai G. (Eds). The Springer Index of Viruses (2002), Springer-Verlag, Heidelberg, Germany 327-331
    • (2002) The Springer Index of Viruses , pp. 327-331
    • Becher, P.1    Thiel, H.-J.2
  • 5
    • 0031871278 scopus 로고    scopus 로고
    • Molecular characterization of the 3′ noncoding region of classical swine fever virus vaccine strain
    • Björklund H.V., Stadejek T., Vilček S., and Belák S. Molecular characterization of the 3′ noncoding region of classical swine fever virus vaccine strain. Virus Genes 16 (1998) 307-312
    • (1998) Virus Genes , vol.16 , pp. 307-312
    • Björklund, H.V.1    Stadejek, T.2    Vilček, S.3    Belák, S.4
  • 6
    • 0032486596 scopus 로고    scopus 로고
    • Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein
    • Cui T., Sugrue R.J., Xu Q., Lee A.K., Chan Y.C., and Fu J. Recombinant dengue virus type 1 NS3 protein exhibits specific viral RNA binding and NTPase activity regulated by the NS5 protein. Virology 246 (1998) 409-417
    • (1998) Virology , vol.246 , pp. 409-417
    • Cui, T.1    Sugrue, R.J.2    Xu, Q.3    Lee, A.K.4    Chan, Y.C.5    Fu, J.6
  • 7
    • 0027942956 scopus 로고
    • Hepatitis C: progress and problems
    • Cuthbert J.A. Hepatitis C: progress and problems. Clin. Microbiol. Rev. 7 (1994) 505-532
    • (1994) Clin. Microbiol. Rev. , vol.7 , pp. 505-532
    • Cuthbert, J.A.1
  • 8
    • 0036241453 scopus 로고    scopus 로고
    • Pestivirus internal ribosome entry site (IRES) structure and function: elements in the 5′ untranslated region important for IRES function
    • Fletcher S.P., and Jackson R.J. Pestivirus internal ribosome entry site (IRES) structure and function: elements in the 5′ untranslated region important for IRES function. J. Virol. 76 (2002) 5024-5033
    • (2002) J. Virol. , vol.76 , pp. 5024-5033
    • Fletcher, S.P.1    Jackson, R.J.2
  • 10
    • 0033609061 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A
    • Gallinari P., Paolini C., Brennan D., Nardi C., Steinkuhler C., and Francesco R.D. Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A. Biochemistry 38 (1999) 5620-5632
    • (1999) Biochemistry , vol.38 , pp. 5620-5632
    • Gallinari, P.1    Paolini, C.2    Brennan, D.3    Nardi, C.4    Steinkuhler, C.5    Francesco, R.D.6
  • 11
    • 0029825147 scopus 로고    scopus 로고
    • Characterization of RNA synthesis during a one-step growth curve and of the replication mechanism of bovine viral diarrhea virus
    • Gong Y., Trowbridge R., Macnaughton T.B., Westaway E.G., Shannon A.D., and Gowans E.J. Characterization of RNA synthesis during a one-step growth curve and of the replication mechanism of bovine viral diarrhea virus. J. Gen. Virol. 77 (1996) 2729-2736
    • (1996) J. Gen. Virol. , vol.77 , pp. 2729-2736
    • Gong, Y.1    Trowbridge, R.2    Macnaughton, T.B.3    Westaway, E.G.4    Shannon, A.D.5    Gowans, E.J.6
  • 12
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya A.E., and Koonin E.V. Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res. 17 (1989) 8413-8440
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 16
    • 0033947171 scopus 로고    scopus 로고
    • The RNA helicase and nucleotide triphosphatase activities of the bovine viral diarrhea virus NS3 protein are essential for viral replication
    • Gu B., Liu C., Lin-Goerke J., Maley D.R., Gutshall L.L., Feltenberger C.A., and Del Vecchio A.M. The RNA helicase and nucleotide triphosphatase activities of the bovine viral diarrhea virus NS3 protein are essential for viral replication. J. Virol. 74 (2000) 1794-1800
    • (2000) J. Virol. , vol.74 , pp. 1794-1800
    • Gu, B.1    Liu, C.2    Lin-Goerke, J.3    Maley, D.R.4    Gutshall, L.L.5    Feltenberger, C.A.6    Del Vecchio, A.M.7
  • 18
    • 0024278568 scopus 로고
    • A new superfamily of replicative proteins
    • Hodgman T.C. A new superfamily of replicative proteins. Nature 333 (1988) 22-23
    • (1988) Nature , vol.333 , pp. 22-23
    • Hodgman, T.C.1
  • 19
    • 0032489233 scopus 로고    scopus 로고
    • Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus
    • Ishido S., Fujita T., and Hotta H. Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus. Biochem. Biophys. Res. Commun. 244 (1998) 35-40
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 35-40
    • Ishido, S.1    Fujita, T.2    Hotta, H.3
  • 20
    • 0242473186 scopus 로고    scopus 로고
    • Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus
    • Isken O., Grassmann C.W., Sarisky R.T., Kann M., Zhang S., Grosse F., Kao P.N., and Behrens S.E. Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus. EMBO J. 22 (2003) 5655-5665
    • (2003) EMBO J. , vol.22 , pp. 5655-5665
    • Isken, O.1    Grassmann, C.W.2    Sarisky, R.T.3    Kann, M.4    Zhang, S.5    Grosse, F.6    Kao, P.N.7    Behrens, S.E.8
  • 21
    • 4644233409 scopus 로고    scopus 로고
    • Complex signals in the genomic 3′ nontranslated region of bovine viral diarrhea virus coordinate translation and replication of the viral RNA
    • Isken O., Grassmann C.W., Yu H., and Behrens S.E. Complex signals in the genomic 3′ nontranslated region of bovine viral diarrhea virus coordinate translation and replication of the viral RNA. RNA 10 (2004) 1637-1652
    • (2004) RNA , vol.10 , pp. 1637-1652
    • Isken, O.1    Grassmann, C.W.2    Yu, H.3    Behrens, S.E.4
  • 22
    • 0026096150 scopus 로고
    • Enzymatic activity of poliovirus RNA polymerase mutants with single amino acid changes in the conserved YGDD amino acid motif
    • Jablonski S.A., Luo M., and Morrow C.D. Enzymatic activity of poliovirus RNA polymerase mutants with single amino acid changes in the conserved YGDD amino acid motif. J. Virol. 65 (1991) 4565-4572
    • (1991) J. Virol. , vol.65 , pp. 4565-4572
    • Jablonski, S.A.1    Luo, M.2    Morrow, C.D.3
  • 23
    • 0028884176 scopus 로고
    • Expression, isolation, and characterization of the hepatitis C virus ATPase/RNA helicase
    • Jin L., and Peterson D.L. Expression, isolation, and characterization of the hepatitis C virus ATPase/RNA helicase. Arch. Biochem. Biophys. 323 (1995) 47-53
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 47-53
    • Jin, L.1    Peterson, D.L.2
  • 24
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadare G., and Haenni A.-L. Virus-encoded RNA helicases. J. Virol. 71 (1997) 2583-2590
    • (1997) J. Virol. , vol.71 , pp. 2583-2590
    • Kadare, G.1    Haenni, A.-L.2
  • 25
    • 34548222947 scopus 로고
    • Primary structural comparison of RNA dependent polymerases from plant, animal and bacterial viruses. Nucleic hepatitis C virus NS3 protein polynucleotide-stimulated NTPase and comparison with the related pestivirus and flavivirus enzymes
    • Kamer G., and Argos P. Primary structural comparison of RNA dependent polymerases from plant, animal and bacterial viruses. Nucleic hepatitis C virus NS3 protein polynucleotide-stimulated NTPase and comparison with the related pestivirus and flavivirus enzymes. J. Virol. 67 (1984) 6152-6158
    • (1984) J. Virol. , vol.67 , pp. 6152-6158
    • Kamer, G.1    Argos, P.2
  • 26
    • 0028817781 scopus 로고
    • C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity
    • Kim D.W., Gwack Y., Han J.H., and Choe J. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem. Biophys. Res. Commun. 215 (1995) 160-166
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 160-166
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 28
    • 0033920304 scopus 로고    scopus 로고
    • Hepatitis C virus-encoded enzymatic activities and conversed RNA elements in the 3′ nontranslated region are essential for virus replication in vivo
    • Kolykhalov A.A., Mihalik K., Feinstone S.M., and Rice C.M. Hepatitis C virus-encoded enzymatic activities and conversed RNA elements in the 3′ nontranslated region are essential for virus replication in vivo. J. Virol. 74 (2000) 2046-2051
    • (2000) J. Virol. , vol.74 , pp. 2046-2051
    • Kolykhalov, A.A.1    Mihalik, K.2    Feinstone, S.M.3    Rice, C.M.4
  • 30
    • 0024425153 scopus 로고
    • Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase like proteins
    • Laýń S., Riechmann J.L., Martýń M.T., and Garcýá J.A. Homologous potyvirus and flavivirus proteins belonging to a superfamily of helicase like proteins. Gene 82 (1989) 357-362
    • (1989) Gene , vol.82 , pp. 357-362
    • Laýń, S.1    Riechmann, J.L.2    Martýń, M.T.3    Garcýá, J.A.4
  • 31
    • 0032976077 scopus 로고    scopus 로고
    • The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids
    • Li H., Clum S., You S., Ebner K.E., and Padmanabhan R. The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids. J. Virol. 73 (1999) 3108-3116
    • (1999) J. Virol. , vol.73 , pp. 3108-3116
    • Li, H.1    Clum, S.2    You, S.3    Ebner, K.E.4    Padmanabhan, R.5
  • 32
    • 1842289764 scopus 로고    scopus 로고
    • Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity
    • Lohmann V., Körner F., Herian U., and Bartenschlager R. Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activity. J. Virol. 71 (1997) 8416-8428
    • (1997) J. Virol. , vol.71 , pp. 8416-8428
    • Lohmann, V.1    Körner, F.2    Herian, U.3    Bartenschlager, R.4
  • 34
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., and Hostomska Z. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87 (1996) 331-342
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3    Hostomsky, Z.4    Habuka, N.5    Moomaw, E.W.6    Adachi, T.7    Hostomska, Z.8
  • 36
    • 0030030337 scopus 로고    scopus 로고
    • Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus
    • Moormann R.J.M., van Gennip H.G.P., Miedema G.K.W., Hulst M.M., and van Rijn P.A. Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus. J. Virol. 70 (1996) 763-770
    • (1996) J. Virol. , vol.70 , pp. 763-770
    • Moormann, R.J.M.1    van Gennip, H.G.P.2    Miedema, G.K.W.3    Hulst, M.M.4    van Rijn, P.A.5
  • 37
    • 21644480603 scopus 로고    scopus 로고
    • Essential and nonessential elements in the 3′ nontranslated region of bovine viral diarrhea virus
    • Pankraz A., Thiel H.J., and Becher P. Essential and nonessential elements in the 3′ nontranslated region of bovine viral diarrhea virus. J. Virol. 79 (2005) 9119-9127
    • (2005) J. Virol. , vol.79 , pp. 9119-9127
    • Pankraz, A.1    Thiel, H.J.2    Becher, P.3
  • 38
    • 0033548596 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication
    • Pfister T., and Wimmer E. Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. J. Biol. Chem. 274 (1999) 6992-7001
    • (1999) J. Biol. Chem. , vol.274 , pp. 6992-7001
    • Pfister, T.1    Wimmer, E.2
  • 39
    • 0347457077 scopus 로고    scopus 로고
    • Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein
    • Piccininni S., Varaklioti A., Nardelli M., Dave B., Raney K.D., and McCarthy J.E. Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein. J. Biol. Chem. 277 (2002) 45670-45679
    • (2002) J. Biol. Chem. , vol.277 , pp. 45670-45679
    • Piccininni, S.1    Varaklioti, A.2    Nardelli, M.3    Dave, B.4    Raney, K.D.5    McCarthy, J.E.6
  • 40
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • Preugschat F., Averett D.R., Clarke B.E., and Porter D.J.T. A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain. J. Biol. Chem. 271 (1996) 24449-24457
    • (1996) J. Biol. Chem. , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clarke, B.E.3    Porter, D.J.T.4
  • 41
    • 0035166768 scopus 로고    scopus 로고
    • HCV RNA-dependent RNA polymerases replicates in vitro the 3′ terminal region of the minus-strand viral RNA more efficiently than the 3′ terminal region of the plus-strand RNA
    • Reigadas S., Ventura M., Sarih-Cottin L., Castroviejo M., Litvak S., and Astier-Gin T. HCV RNA-dependent RNA polymerases replicates in vitro the 3′ terminal region of the minus-strand viral RNA more efficiently than the 3′ terminal region of the plus-strand RNA. Eur. J. Biochem. 268 (2001) 5857-5867
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5857-5867
    • Reigadas, S.1    Ventura, M.2    Sarih-Cottin, L.3    Castroviejo, M.4    Litvak, S.5    Astier-Gin, T.6
  • 42
    • 0032882393 scopus 로고    scopus 로고
    • The RNA-dependent RNA polymerase of different members of the family Flaviviridae exhibits similar properties in vitro
    • Steffen S., Thiel H.J., and Behrens S.E. The RNA-dependent RNA polymerase of different members of the family Flaviviridae exhibits similar properties in vitro. J. Gen. Virol. 80 (1999) 2583-2590
    • (1999) J. Gen. Virol. , vol.80 , pp. 2583-2590
    • Steffen, S.1    Thiel, H.J.2    Behrens, S.E.3
  • 43
    • 0027199917 scopus 로고
    • Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes
    • Suzich J.A., Tamura J.K., Palmer-Hill F., Warrener P., Grakoui A., Rice C.M., Feinstone S.M., and Collett M.S. Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes. J. Virol. 67 (1993) 6152-6158
    • (1993) J. Virol. , vol.67 , pp. 6152-6158
    • Suzich, J.A.1    Tamura, J.K.2    Palmer-Hill, F.3    Warrener, P.4    Grakoui, A.5    Rice, C.M.6    Feinstone, S.M.7    Collett, M.S.8
  • 44
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3
    • Tai C.-L., Chi W.-K., Chen D.-S., and Hwang L.H. The helicase activity associated with hepatitis C virus nonstructural protein 3. J. Virol. 70 (1996) 8477-8484
    • (1996) J. Virol. , vol.70 , pp. 8477-8484
    • Tai, C.-L.1    Chi, W.-K.2    Chen, D.-S.3    Hwang, L.H.4
  • 45
    • 0028872259 scopus 로고
    • Pestivirus NS3 (p80) protein possesses helicase activity
    • Warrener P., and Collett M.S. Pestivirus NS3 (p80) protein possesses helicase activity. J. Virol. 69 (1995) 1720-1726
    • (1995) J. Virol. , vol.69 , pp. 1720-1726
    • Warrener, P.1    Collett, M.S.2
  • 46
    • 0034865496 scopus 로고    scopus 로고
    • Attenuated lapinized Chinese strain of classical swine fever virus: complete nucleotide sequence and character of 3′-noncoding region
    • Wu H.X., Wang J.F., Zhang C.Y., Fu L.Z., Pan Z.S., Wang N., Zhang P.W., and Zhao W.G. Attenuated lapinized Chinese strain of classical swine fever virus: complete nucleotide sequence and character of 3′-noncoding region. Virus Genes 23 (2001) 69-76
    • (2001) Virus Genes , vol.23 , pp. 69-76
    • Wu, H.X.1    Wang, J.F.2    Zhang, C.Y.3    Fu, L.Z.4    Pan, Z.S.5    Wang, N.6    Zhang, P.W.7    Zhao, W.G.8
  • 47
    • 0036108666 scopus 로고    scopus 로고
    • Prediction of recognition sites of classical swine fever virus genomic replication with information analysis
    • Xiao M., Zhi Z.Z., Liu J., and Zhang C.Y. Prediction of recognition sites of classical swine fever virus genomic replication with information analysis. Mol. Biol. 36 (2002) 34-43
    • (2002) Mol. Biol. , vol.36 , pp. 34-43
    • Xiao, M.1    Zhi, Z.Z.2    Liu, J.3    Zhang, C.Y.4
  • 48
    • 1842850942 scopus 로고    scopus 로고
    • Influence of a 12-nt insertion present in the 3′untranslated region of classical swine fever virus HCLV strain genome on RNA synthesis
    • Xiao M., Gao J., Wang Y., Wang X., Lu W., Zhen Y., Chen J., and Li B. Influence of a 12-nt insertion present in the 3′untranslated region of classical swine fever virus HCLV strain genome on RNA synthesis. Virus Res. 102 (2004) 191-198
    • (2004) Virus Res. , vol.102 , pp. 191-198
    • Xiao, M.1    Gao, J.2    Wang, Y.3    Wang, X.4    Lu, W.5    Zhen, Y.6    Chen, J.7    Li, B.8
  • 49
    • 4944265553 scopus 로고    scopus 로고
    • Specific interaction between the classical swine fever virus NS5B protein and the viral genome
    • Xiao M., Gao J., Wang W., Wang Y., Chen J., Chen J., and Li B. Specific interaction between the classical swine fever virus NS5B protein and the viral genome. Eur. J. Biochem. 271 (2004) 3888-3896
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3888-3896
    • Xiao, M.1    Gao, J.2    Wang, W.3    Wang, Y.4    Chen, J.5    Chen, J.6    Li, B.7
  • 50
    • 3242881963 scopus 로고    scopus 로고
    • The necessary site for initiation of RNA synthesis in 3′noncoding region of classical swine fever virus genome
    • Xiao M., Lu W., Chen J., Wang Y., Zhen Y., Chen J., and Li B. The necessary site for initiation of RNA synthesis in 3′noncoding region of classical swine fever virus genome. Mol. Biol. 38 (2004) 343-351
    • (2004) Mol. Biol. , vol.38 , pp. 343-351
    • Xiao, M.1    Lu, W.2    Chen, J.3    Wang, Y.4    Zhen, Y.5    Chen, J.6    Li, B.7
  • 51
    • 31644445842 scopus 로고    scopus 로고
    • Characterization of the N-terminal domain of classical swine fever virus RNA-dependent RNA polymeras
    • Xiao M., Li H., Wang Y., Wang X., Wang W., Peng J., Chen J., and Li B. Characterization of the N-terminal domain of classical swine fever virus RNA-dependent RNA polymeras. J. Gen. Virol. 87 (2006) 347-356
    • (2006) J. Gen. Virol. , vol.87 , pp. 347-356
    • Xiao, M.1    Li, H.2    Wang, Y.3    Wang, X.4    Wang, W.5    Peng, J.6    Chen, J.7    Li, B.8
  • 52
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication
    • Xu J., Mendez E., Caron P.R., Lin C., Murcko M.A., Collett M.C., and Rice C.M. Bovine viral diarrhea virus: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication. J. Virol. 71 (1997) 5312-5322
    • (1997) J. Virol. , vol.71 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.C.6    Rice, C.M.7
  • 54
    • 0032958430 scopus 로고    scopus 로고
    • Sequence and structural elements at the 3′ terminus of bovine viral diarrhea virus genomic RNA: functional role during RNA replication
    • Yu H., Grassmann C.W., and Behrens S.E. Sequence and structural elements at the 3′ terminus of bovine viral diarrhea virus genomic RNA: functional role during RNA replication. J. Virol. 73 (1999) 3638-3648
    • (1999) J. Virol. , vol.73 , pp. 3638-3648
    • Yu, H.1    Grassmann, C.W.2    Behrens, S.E.3
  • 55
    • 21644463166 scopus 로고    scopus 로고
    • Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase
    • Zhang C., Kim Y.C., Kumar R., Yuan F., Shi P.Y., Kao C., and Luo G. Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase. J. Virol. 79 (2005) 8687-8697
    • (2005) J. Virol. , vol.79 , pp. 8687-8697
    • Zhang, C.1    Kim, Y.C.2    Kumar, R.3    Yuan, F.4    Shi, P.Y.5    Kao, C.6    Luo, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.