메뉴 건너뛰기




Volumn 141, Issue 1, 2009, Pages 63-70

Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase

Author keywords

Classical swine fever virus (CSFV); Helicase; NS3; NS5B; NTPase

Indexed keywords

ADENOSINE TRIPHOSPHATE; DIVALENT CATION; MALTOSE BINDING PROTEIN; MANGANESE; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 5B; NUCLEOTIDASE; RNA HELICASE; RNA POLYMERASE;

EID: 61449241639     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2008.12.014     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 0027349993 scopus 로고
    • Synthesis of dengue virus RNA in vitro: initiation and the involvement of proteins NS3 and NS5
    • Bartholomeusz A.I., and Wright P.J. Synthesis of dengue virus RNA in vitro: initiation and the involvement of proteins NS3 and NS5. Arch. Virol. 128 1-2 (1993) 111-121
    • (1993) Arch. Virol. , vol.128 , Issue.1-2 , pp. 111-121
    • Bartholomeusz, A.I.1    Wright, P.J.2
  • 3
    • 57649217269 scopus 로고    scopus 로고
    • Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase
    • Beran R.K., and Pyle A.M. Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase. J. Biol. Chem. 283 44 (2008) 29929-29937
    • (2008) J. Biol. Chem. , vol.283 , Issue.44 , pp. 29929-29937
    • Beran, R.K.1    Pyle, A.M.2
  • 4
    • 36849075152 scopus 로고    scopus 로고
    • The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate
    • Beran R.K., Serebrov V., and Pyle A.M. The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate. J. Biol. Chem. 282 48 (2007) 34913-34920
    • (2007) J. Biol. Chem. , vol.282 , Issue.48 , pp. 34913-34920
    • Beran, R.K.1    Serebrov, V.2    Pyle, A.M.3
  • 5
    • 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., and Lin J.H. RNA-protein interactions: involvement of NS3, NS5, and 3′ noncoding regions of Japanese encephalitis virus genomic RNA. J. Virol. 71 5 (1997) 3466-3473
    • (1997) J. Virol. , vol.71 , Issue.5 , 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
  • 7
    • 0029825580 scopus 로고    scopus 로고
    • An ATPase component of the transcription elongation complex is required for factor-dependent transcription termination by vaccinia RNA polymerase
    • Deng L., and Shuman S. An ATPase component of the transcription elongation complex is required for factor-dependent transcription termination by vaccinia RNA polymerase. J. Biol. Chem. 271 46 (1996) 29386-29392
    • (1996) J. Biol. Chem. , vol.271 , Issue.46 , pp. 29386-29392
    • Deng, L.1    Shuman, S.2
  • 8
    • 0027245895 scopus 로고
    • 5′ and 3′ untranslated regions of pestivirus genome: primary and secondary structure analyses
    • Deng R., and Brock K.V. 5′ and 3′ untranslated regions of pestivirus genome: primary and secondary structure analyses. Nucleic Acids Res. 21 8 (1993) 1949-1957
    • (1993) Nucleic Acids Res. , vol.21 , Issue.8 , pp. 1949-1957
    • Deng, R.1    Brock, K.V.2
  • 9
    • 33846456636 scopus 로고    scopus 로고
    • The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target
    • Frick D.N. The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target. Curr. Issues Mol. Biol. 9 1 (2007) 1-20
    • (2007) Curr. Issues Mol. Biol. , vol.9 , Issue.1 , pp. 1-20
    • Frick, D.N.1
  • 10
    • 0346463036 scopus 로고    scopus 로고
    • The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently
    • Frick D.N., Rypma R.S., Lam A.M., and Gu B. The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently. J. Biol. Chem. 279 2 (2004) 1269-1280
    • (2004) J. Biol. Chem. , vol.279 , Issue.2 , pp. 1269-1280
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.3    Gu, B.4
  • 12
    • 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 De Francesco R. Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A. Biochemistry 38 17 (1999) 5620-5632
    • (1999) Biochemistry , vol.38 , Issue.17 , pp. 5620-5632
    • Gallinari, P.1    Paolini, C.2    Brennan, D.3    Nardi, C.4    Steinkuhler, C.5    De Francesco, R.6
  • 13
    • 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 4 (2000) 1794-1800
    • (2000) J. Virol. , vol.74 , Issue.4 , 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
  • 14
    • 19544394438 scopus 로고    scopus 로고
    • The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain
    • Gu B., Pruss C.M., Gates A.T., and Khandekar S.S. The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain. Protein Pept. Lett. 12 4 (2005) 315-321
    • (2005) Protein Pept. Lett. , vol.12 , Issue.4 , pp. 315-321
    • Gu, B.1    Pruss, C.M.2    Gates, A.T.3    Khandekar, S.S.4
  • 15
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow E., and Lane D. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 16
    • 0029950090 scopus 로고    scopus 로고
    • Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system
    • Hong Z., Ferrari E., Wright-Minogue J., Chase R., Risano C., Seelig G., Lee C.G., and Kwong A.D. Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system. J. Virol. 70 7 (1996) 4261-4268
    • (1996) J. Virol. , vol.70 , Issue.7 , pp. 4261-4268
    • Hong, Z.1    Ferrari, E.2    Wright-Minogue, J.3    Chase, R.4    Risano, C.5    Seelig, G.6    Lee, C.G.7    Kwong, A.D.8
  • 17
    • 0033059980 scopus 로고    scopus 로고
    • A novel recombinant single-chain hepatitis C virus NS3-NS4A protein with improved helicase activity
    • Howe A.Y., Chase R., Taremi S.S., Risano C., Beyer B., Malcolm B., and Lau J.Y. A novel recombinant single-chain hepatitis C virus NS3-NS4A protein with improved helicase activity. Protein Sci. 8 6 (1999) 1332-1341
    • (1999) Protein Sci. , vol.8 , Issue.6 , pp. 1332-1341
    • Howe, A.Y.1    Chase, R.2    Taremi, S.S.3    Risano, C.4    Beyer, B.5    Malcolm, B.6    Lau, J.Y.7
  • 18
    • 0029027850 scopus 로고
    • Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5
    • Kapoor M., Zhang L., Ramachandra M., Kusukawa J., Ebner K.E., and Padmanabhan R. Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5. J. Biol. Chem. 270 32 (1995) 19100-19106
    • (1995) J. Biol. Chem. , vol.270 , Issue.32 , pp. 19100-19106
    • Kapoor, M.1    Zhang, L.2    Ramachandra, M.3    Kusukawa, J.4    Ebner, K.E.5    Padmanabhan, R.6
  • 19
    • 0342872087 scopus 로고    scopus 로고
    • Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein
    • Kim D.W., Gwack Y., Han J.H., and Choe J. Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein. Virus Res. 49 1 (1997) 17-25
    • (1997) Virus Res. , vol.49 , Issue.1 , pp. 17-25
    • Kim, D.W.1    Gwack, Y.2    Han, J.H.3    Choe, J.4
  • 21
    • 0029816423 scopus 로고    scopus 로고
    • Characterization of the NTPase activity of Japanese encephalitis virus NS3 protein
    • Kuo M.D., Chin C., Hsu S.L., Shiao J.Y., Wang T.M., and Lin J.H. Characterization of the NTPase activity of Japanese encephalitis virus NS3 protein. J. Gen. Virol. 77 Pt 9 (1996) 2077-2084
    • (1996) J. Gen. Virol. , vol.77 , Issue.PART 9 , pp. 2077-2084
    • Kuo, M.D.1    Chin, C.2    Hsu, S.L.3    Shiao, J.Y.4    Wang, T.M.5    Lin, J.H.6
  • 22
    • 0037377763 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 ATPases/helicases from different genotypes exhibit variations in enzymatic properties
    • Lam A.M., Keeney D., Eckert P.Q., and Frick D.N. Hepatitis C virus NS3 ATPases/helicases from different genotypes exhibit variations in enzymatic properties. J. Virol. 77 7 (2003) 3950-3961
    • (2003) J. Virol. , vol.77 , Issue.7 , pp. 3950-3961
    • Lam, A.M.1    Keeney, D.2    Eckert, P.Q.3    Frick, D.N.4
  • 23
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta P.A., Alvarez L.J., Reinach P.S., and Candia O.A. An improved assay for nanomole amounts of inorganic phosphate. Anal. Chem. 100 (1979) 95-97
    • (1979) Anal. Chem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 24
    • 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 4 (1999) 3108-3116
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 3108-3116
    • Li, H.1    Clum, S.2    You, S.3    Ebner, K.E.4    Padmanabhan, R.5
  • 25
    • 0032824138 scopus 로고    scopus 로고
    • Structure-based mutagenesis study of hepatitis C virus NS3 helicase
    • Lin C., and Kim J.L. Structure-based mutagenesis study of hepatitis C virus NS3 helicase. J. Virol. 73 10 (1999) 8798-8807
    • (1999) J. Virol. , vol.73 , Issue.10 , pp. 8798-8807
    • Lin, C.1    Kim, J.L.2
  • 26
    • 0030333528 scopus 로고    scopus 로고
    • Molecular characterization of pestiviruses
    • Meyers G., and Thiel H.J. Molecular characterization of pestiviruses. Adv. Virus Res. 47 (1996) 53-118
    • (1996) Adv. Virus Res. , vol.47 , pp. 53-118
    • Meyers, G.1    Thiel, H.J.2
  • 27
    • 0031000887 scopus 로고    scopus 로고
    • Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells
    • Morgenstern K.A., Landro J.A., Hsiao K., Lin C., Gu Y., Su M.S., and Thomson J.A. Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells. J. Virol. 71 5 (1997) 3767-3775
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3767-3775
    • Morgenstern, K.A.1    Landro, J.A.2    Hsiao, K.3    Lin, C.4    Gu, Y.5    Su, M.S.6    Thomson, J.A.7
  • 28
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang P.S., Jankowsky E., Planet P.J., and Pyle A.M. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J. 21 5 (2002) 1168-1176
    • (2002) EMBO J. , vol.21 , Issue.5 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 29
    • 0034054773 scopus 로고    scopus 로고
    • Enzymatic properties of hepatitis C virus NS3-associated helicase
    • Paolini C., De Francesco R., and Gallinari P. Enzymatic properties of hepatitis C virus NS3-associated helicase. J. Gen. Virol. 81 Pt 5 (2000) 1335-1345
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 5 , pp. 1335-1345
    • Paolini, C.1    De Francesco, R.2    Gallinari, P.3
  • 30
    • 0028936474 scopus 로고
    • A proposed division of the pestivirus genus using monoclonal antibodies, supported by cross-neutralisation assays and genetic sequencing
    • Paton D.J., Sands J.J., Lowings J.P., Smith J.E., Ibata G., and Edwards S. A proposed division of the pestivirus genus using monoclonal antibodies, supported by cross-neutralisation assays and genetic sequencing. Vet. Res. 26 2 (1995) 92-109
    • (1995) Vet. Res. , vol.26 , Issue.2 , pp. 92-109
    • Paton, D.J.1    Sands, J.J.2    Lowings, J.P.3    Smith, J.E.4    Ibata, G.5    Edwards, S.6
  • 31
    • 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 47 (2002) 45670-45679
    • (2002) J. Biol. Chem. , vol.277 , Issue.47 , pp. 45670-45679
    • Piccininni, S.1    Varaklioti, A.2    Nardelli, M.3    Dave, B.4    Raney, K.D.5    McCarthy, J.E.6
  • 32
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Fields B.N., Knipe D.M., and Howley P.M. (Eds), Lippincott-Raven Press, Philadelphia, PA
    • Rice C.M. Flaviviridae: the viruses and their replication. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). Fields' Virology. 3rd ed. vol. 1 (1996), Lippincott-Raven Press, Philadelphia, PA 931-959
    • (1996) Fields' Virology. 3rd ed. , vol.1 , pp. 931-959
    • Rice, C.M.1
  • 33
    • 34548226912 scopus 로고    scopus 로고
    • Characterization of interaction of classical swine fever virus NS3 helicase with 3′ untranslated region
    • Sheng C., Xiao M., Geng X., Liu J., Wang Y., and Gu F. Characterization of interaction of classical swine fever virus NS3 helicase with 3′ untranslated region. Virus Res. 129 1 (2007) 43-53
    • (2007) Virus Res. , vol.129 , Issue.1 , pp. 43-53
    • Sheng, C.1    Xiao, M.2    Geng, X.3    Liu, J.4    Wang, Y.5    Gu, F.6
  • 34
    • 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 10 (1993) 6152-6158
    • (1993) J. Virol. , vol.67 , Issue.10 , 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
  • 35
    • 15444371665 scopus 로고    scopus 로고
    • Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro
    • Tackett A.J., Chen Y., Cameron C.E., and Raney K.D. Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro. J. Biol. Chem. 280 11 (2005) 10797-10806
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 10797-10806
    • Tackett, A.J.1    Chen, Y.2    Cameron, C.E.3    Raney, K.D.4
  • 36
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)
    • Tai C.L., Chi W.K., Chen D.S., and Hwang L.H. The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3). J. Virol. 70 12 (1996) 8477-8484
    • (1996) J. Virol. , vol.70 , Issue.12 , pp. 8477-8484
    • Tai, C.L.1    Chi, W.K.2    Chen, D.S.3    Hwang, L.H.4
  • 37
    • 0027254336 scopus 로고
    • RNA-stimulated NTPase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus
    • Tamura J.K., Warrener P., and Collett M.S. RNA-stimulated NTPase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus. Virology 193 1 (1993) 1-10
    • (1993) Virology , vol.193 , Issue.1 , pp. 1-10
    • Tamura, J.K.1    Warrener, P.2    Collett, M.S.3
  • 38
    • 0027176287 scopus 로고
    • NS3 is a serine protease required for processing of hepatitis C virus polyprotein
    • Tomei L., Failla C., Santolini E., De Francesco R., and La Monica N. NS3 is a serine protease required for processing of hepatitis C virus polyprotein. J. Virol. 67 7 (1993) 4017-4026
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 4017-4026
    • Tomei, L.1    Failla, C.2    Santolini, E.3    De Francesco, R.4    La Monica, N.5
  • 40
    • 34547177172 scopus 로고    scopus 로고
    • Construction and pathogenicity of infectious cDNA clone of classical swine fever virus (CSFV)
    • Wang Y., Wu H.X., and Zhang C.Y. Construction and pathogenicity of infectious cDNA clone of classical swine fever virus (CSFV). Chin. J. Virol. 21 (2005) 43-47
    • (2005) Chin. J. Virol. , vol.21 , pp. 43-47
    • Wang, Y.1    Wu, H.X.2    Zhang, C.Y.3
  • 41
    • 0033030027 scopus 로고    scopus 로고
    • Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein
    • Wardell A.D., Errington W., Ciaramella G., Merson J., and McGarvey M.J. Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein. J. Gen. Virol. 80 Pt 3 (1999) 701-709
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 3 , pp. 701-709
    • Wardell, A.D.1    Errington, W.2    Ciaramella, G.3    Merson, J.4    McGarvey, M.J.5
  • 42
    • 0028872259 scopus 로고
    • Pestivirus NS3 (p80) protein possesses RNA helicase activity
    • Warrener P., and Collett M.S. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol. 69 3 (1995) 1720-1726
    • (1995) J. Virol. , vol.69 , Issue.3 , pp. 1720-1726
    • Warrener, P.1    Collett, M.S.2
  • 43
    • 0027446550 scopus 로고
    • RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria
    • Warrener P., Tamura J.K., and Collett M.S. RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria. J. Virol. 67 2 (1993) 989-996
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 989-996
    • Warrener, P.1    Tamura, J.K.2    Collett, M.S.3
  • 44
    • 34547233100 scopus 로고    scopus 로고
    • Identification and characterization of the NTPase activity of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) expressed in bacteria
    • Wen G., Chen C., Luo X., Wang Y., Zhang C., and Pan Z. Identification and characterization of the NTPase activity of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) expressed in bacteria. Arch. Virol. 152 8 (2007) 1565-1573
    • (2007) Arch. Virol. , vol.152 , Issue.8 , pp. 1565-1573
    • Wen, G.1    Chen, C.2    Luo, X.3    Wang, Y.4    Zhang, C.5    Pan, Z.6
  • 45
    • 0025865788 scopus 로고
    • In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids
    • Wengler G., Czaya G., Farber P.M., and Hegemann J.H. In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids. J. Gen. Virol. 72 Pt 4 (1991) 851-858
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 4 , pp. 851-858
    • Wengler, G.1    Czaya, G.2    Farber, P.M.3    Hegemann, J.H.4
  • 46
    • 45549109719 scopus 로고    scopus 로고
    • Effect of NS3 and NS5B proteins on classical swine fever virus internal ribosome entry site-mediated translation and its host cellular translation
    • Xiao M., Bai Y., Xu H., Geng X., Chen J., Wang Y., Chen J., and Li B. Effect of NS3 and NS5B proteins on classical swine fever virus internal ribosome entry site-mediated translation and its host cellular translation. J. Gen. Virol. 89 Pt 4 (2008) 994-999
    • (2008) J. Gen. Virol. , vol.89 , Issue.PART 4 , pp. 994-999
    • Xiao, M.1    Bai, Y.2    Xu, H.3    Geng, X.4    Chen, J.5    Wang, Y.6    Chen, J.7    Li, B.8
  • 47
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus NS3 serine proteinase: 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.S., and Rice C.M. Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication. J. Virol. 71 7 (1997) 5312-5322
    • (1997) J. Virol. , vol.71 , Issue.7 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.S.6    Rice, C.M.7
  • 48
    • 0346249755 scopus 로고    scopus 로고
    • De novo RNA synthesis by a recombinant classical swine fever virus RNA-dependent RNA polymerase
    • Yi G.H., Zhang C.Y., Cao S., Wu H.X., and Wang Y. De novo RNA synthesis by a recombinant classical swine fever virus RNA-dependent RNA polymerase. Eur. J. Biochem. 270 24 (2003) 4952-4961
    • (2003) Eur. J. Biochem. , vol.270 , Issue.24 , pp. 4952-4961
    • Yi, G.H.1    Zhang, C.Y.2    Cao, S.3    Wu, H.X.4    Wang, Y.5
  • 49
    • 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 5 (1999) 3638-3648
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 3638-3648
    • Yu, H.1    Grassmann, C.W.2    Behrens, S.E.3
  • 50
    • 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., Cai Z., 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 14 (2005) 8687-8697
    • (2005) J. Virol. , vol.79 , Issue.14 , pp. 8687-8697
    • Zhang, C.1    Cai, Z.2    Kim, Y.C.3    Kumar, R.4    Yuan, F.5    Shi, P.Y.6    Kao, C.7    Luo, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.