메뉴 건너뛰기




Volumn 197, Issue , 2015, Pages 35-47

Studying classical swine fever virus: Making the best of a bad virus

Author keywords

Classical swine fever virus; CSFV life cycle; Epidemiology; Protein functions; Reverse genetics; Virulence

Indexed keywords

PROTEOME; VACCINE; ANTIVIRUS AGENT; VIRUS VACCINE;

EID: 84922811408     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2014.12.006     Document Type: Review
Times cited : (75)

References (194)
  • 1
    • 1242319434 scopus 로고    scopus 로고
    • Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus
    • Agapov E.V., Murray C.L., Frolov I., Qu L., Myers T.M., Rice C.M. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J. Virol. 2004, 78(5):2414-2425.
    • (2004) J. Virol. , vol.78 , Issue.5 , pp. 2414-2425
    • Agapov, E.V.1    Murray, C.L.2    Frolov, I.3    Qu, L.4    Myers, T.M.5    Rice, C.M.6
  • 3
    • 51449119611 scopus 로고    scopus 로고
    • Disruption of neuronal autophagy by infected microglia results in neurodegeneration
    • Alirezaei M., Kiosses W.B., Flynn C.T., Brady N.R., Fox H.S. Disruption of neuronal autophagy by infected microglia results in neurodegeneration. PLoS One 2008, 3(8):e2906.
    • (2008) PLoS One , vol.3 , Issue.8 , pp. e2906
    • Alirezaei, M.1    Kiosses, W.B.2    Flynn, C.T.3    Brady, N.R.4    Fox, H.S.5
  • 4
    • 2342648022 scopus 로고    scopus 로고
    • Cytopathogenicity of classical swine fever viruses that do not show the exaltation of Newcastle disease virus is associated with accumulation of NS3 in serum-free cultured cell lines
    • (the Japanese Society of Veterinary Science)
    • Aoki H., Sakoda Y., Nakamura S., Suzuki S., Fukusho A. Cytopathogenicity of classical swine fever viruses that do not show the exaltation of Newcastle disease virus is associated with accumulation of NS3 in serum-free cultured cell lines. J. Vet. Med. Sci. 2004, 66(2):161-167. (the Japanese Society of Veterinary Science).
    • (2004) J. Vet. Med. Sci. , vol.66 , Issue.2 , pp. 161-167
    • Aoki, H.1    Sakoda, Y.2    Nakamura, S.3    Suzuki, S.4    Fukusho, A.5
  • 5
    • 11144227045 scopus 로고    scopus 로고
    • Efficient rescue of hepatitis C virus RNA replication by trans-complementation with nonstructural protein 5A
    • Appel N., Herian U., Bartenschlager R. Efficient rescue of hepatitis C virus RNA replication by trans-complementation with nonstructural protein 5A. J. Virol. 2005, 79(2):896-909.
    • (2005) J. Virol. , vol.79 , Issue.2 , pp. 896-909
    • Appel, N.1    Herian, U.2    Bartenschlager, R.3
  • 6
    • 84899786607 scopus 로고
    • Serial passage of hog cholera virus in rabbits
    • (Society for Experimental Biology and Medicine (New York, NY))
    • Baker J.A. Serial passage of hog cholera virus in rabbits. Proc. Soc. Exp. Biol. Med. 1946, 63:183-187. (Society for Experimental Biology and Medicine (New York, NY)).
    • (1946) Proc. Soc. Exp. Biol. Med. , vol.63 , pp. 183-187
    • Baker, J.A.1
  • 8
    • 33947382185 scopus 로고    scopus 로고
    • Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation
    • Bauhofer O., Summerfield A., Sakoda Y., Tratschin J.-D., Hofmann M.A., Ruggli N. Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J. Virol. 2007, 81(7):3087-3096.
    • (2007) J. Virol. , vol.81 , Issue.7 , pp. 3087-3096
    • Bauhofer, O.1    Summerfield, A.2    Sakoda, Y.3    Tratschin, J.-D.4    Hofmann, M.A.5    Ruggli, N.6
  • 9
    • 0036849469 scopus 로고    scopus 로고
    • Development and comparison of procedures for the selection of delta ribozyme cleavage sites within the hepatitis B virus
    • Bergeron L.J., Perreault J.P. Development and comparison of procedures for the selection of delta ribozyme cleavage sites within the hepatitis B virus. Nucleic Acids Res. 2002, 30(21):4682-4691.
    • (2002) Nucleic Acids Res. , vol.30 , Issue.21 , pp. 4682-4691
    • Bergeron, L.J.1    Perreault, J.P.2
  • 10
    • 77950560631 scopus 로고    scopus 로고
    • A new type of signal peptidase cleavage site identified in an RNA virus polyprotein
    • Bintintan I., Meyers G. A new type of signal peptidase cleavage site identified in an RNA virus polyprotein. J. Biol. Chem. 2010, 285(12):8572-8584.
    • (2010) J. Biol. Chem. , vol.285 , Issue.12 , pp. 8572-8584
    • Bintintan, I.1    Meyers, G.2
  • 11
    • 0031871278 scopus 로고    scopus 로고
    • Molecular characterization of the 3' noncoding region of classical swine fever virus vaccine strains
    • Björklund H., Stadejek T., Belák S. Molecular characterization of the 3' noncoding region of classical swine fever virus vaccine strains. Virus Genes 1998, 16(3):307-312.
    • (1998) Virus Genes , vol.16 , Issue.3 , pp. 307-312
    • Björklund, H.1    Stadejek, T.2    Belák, S.3
  • 12
    • 0013907572 scopus 로고
    • Sur la stabilité de quelques caractères biologiques de la souche C de virus lapinisé de la peste porcine
    • Bran L., Mihaita S., Popa M., Totorcea N., Albu T. Sur la stabilité de quelques caractères biologiques de la souche C de virus lapinisé de la peste porcine. Bull. Off. Int. Epiz. 1966, 66:681-693.
    • (1966) Bull. Off. Int. Epiz. , vol.66 , pp. 681-693
    • Bran, L.1    Mihaita, S.2    Popa, M.3    Totorcea, N.4    Albu, T.5
  • 13
    • 2642580713 scopus 로고    scopus 로고
    • Role of N-glycan trimming in the folding and secretion of the pestivirus protein Erns
    • Branza-Nichita N., Lazar C., Dwek R.A., Zitzmann N. Role of N-glycan trimming in the folding and secretion of the pestivirus protein Erns. Biochem. Biophys. Res. Commun. 2004, 319(2):655-662.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , Issue.2 , pp. 655-662
    • Branza-Nichita, N.1    Lazar, C.2    Dwek, R.A.3    Zitzmann, N.4
  • 14
    • 0037040923 scopus 로고    scopus 로고
    • An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A
    • Brass V., Bieck E., Montserret R., Wolk B., Hellings J.A., Blum H.E., Penin F., Moradpour D. An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A. J. Biol. Chem. 2002, 277(10):8130-8139.
    • (2002) J. Biol. Chem. , vol.277 , Issue.10 , pp. 8130-8139
    • Brass, V.1    Bieck, E.2    Montserret, R.3    Wolk, B.4    Hellings, J.A.5    Blum, H.E.6    Penin, F.7    Moradpour, D.8
  • 16
    • 0043093686 scopus 로고    scopus 로고
    • IQGAP proteins are integral components of cytoskeletal regulation
    • Briggs M.W., Sacks D.B. IQGAP proteins are integral components of cytoskeletal regulation. EMBO Rep. 2003, 4(6):571-574.
    • (2003) EMBO Rep. , vol.4 , Issue.6 , pp. 571-574
    • Briggs, M.W.1    Sacks, D.B.2
  • 17
    • 0030611390 scopus 로고    scopus 로고
    • Glycoprotein Erns of pestiviruses induces apoptosis in lymphocytes of several species
    • Bruschke C., Hulst M.M., Moormann R., Van Rijn P., Van Oirschot J. Glycoprotein Erns of pestiviruses induces apoptosis in lymphocytes of several species. J. Virol. 1997, 71(9):6692-6696.
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 6692-6696
    • Bruschke, C.1    Hulst, M.M.2    Moormann, R.3    Van Rijn, P.4    Van Oirschot, J.5
  • 18
    • 2942691403 scopus 로고    scopus 로고
    • RNA interference targeting VP1 inhibits foot-and-mouth disease virus replication in BHK-21 cells and suckling mice
    • Chen W., Yan W., Du Q., Fei L., Liu M., Ni Z., Sheng Z., Zheng Z. RNA interference targeting VP1 inhibits foot-and-mouth disease virus replication in BHK-21 cells and suckling mice. J. Virol. 2004, 78(13):6900-6907.
    • (2004) J. Virol. , vol.78 , Issue.13 , pp. 6900-6907
    • Chen, W.1    Yan, W.2    Du, Q.3    Fei, L.4    Liu, M.5    Ni, Z.6    Sheng, Z.7    Zheng, Z.8
  • 19
    • 84865292048 scopus 로고    scopus 로고
    • Classical swine fever virus NS5A regulates viral RNA replication through binding to NS5B and 3' UTR
    • Chen Y., Xiao J., Xiao J., Sheng C., Wang J., Jia L., Zhi Y., Li G., Chen J., Xiao M. Classical swine fever virus NS5A regulates viral RNA replication through binding to NS5B and 3' UTR. Virology 2012, 432(2):376-388.
    • (2012) Virology , vol.432 , Issue.2 , pp. 376-388
    • Chen, Y.1    Xiao, J.2    Xiao, J.3    Sheng, C.4    Wang, J.5    Jia, L.6    Zhi, Y.7    Li, G.8    Chen, J.9    Xiao, M.10
  • 20
    • 34548566398 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus
    • Chen Z., Rijnbrand R., Jangra R.K., Devaraj S.G., Qu L., Ma Y., Lemon S.M., Li K. Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus. Virology 2007, 366(2):277-292.
    • (2007) Virology , vol.366 , Issue.2 , pp. 277-292
    • Chen, Z.1    Rijnbrand, R.2    Jangra, R.K.3    Devaraj, S.G.4    Qu, L.5    Ma, Y.6    Lemon, S.M.7    Li, K.8
  • 21
    • 34648828978 scopus 로고    scopus 로고
    • The type 2 dengue virus envelope protein interacts with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9)
    • Chiu M.-W., Shih H.-M., Yang T.-H., Yang Y.-L. The type 2 dengue virus envelope protein interacts with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). J. Biomed. Sci. 2007, 14(3):429-444.
    • (2007) J. Biomed. Sci. , vol.14 , Issue.3 , pp. 429-444
    • Chiu, M.-W.1    Shih, H.-M.2    Yang, T.-H.3    Yang, Y.-L.4
  • 22
    • 1842481188 scopus 로고    scopus 로고
    • The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation
    • Choi K.H., Groarke J.M., Young D.C., Kuhn R.J., Smith J.L., Pevear D.C., Rossmann M.G. The structure of the RNA-dependent RNA polymerase from bovine viral diarrhea virus establishes the role of GTP in de novo initiation. Proc. Natl. Acad. Sci. U.S.A. 2004, 101(13):4425-4430.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.13 , pp. 4425-4430
    • Choi, K.H.1    Groarke, J.M.2    Young, D.C.3    Kuhn, R.J.4    Smith, J.L.5    Pevear, D.C.6    Rossmann, M.G.7
  • 23
    • 84922775815 scopus 로고    scopus 로고
    • Flaviviridae: Hepatitis C viruses: features of the nonstructural proteins
    • Lippincott Williams and Wilkins
    • David M., Knipe P.H. Flaviviridae: Hepatitis C viruses: features of the nonstructural proteins. Fields Virology 2013, 733. Lippincott Williams and Wilkins. sixth ed.
    • (2013) Fields Virology , pp. 733
    • David, M.1    Knipe, P.H.2
  • 24
    • 84922814902 scopus 로고    scopus 로고
    • Flaviviridae: pestiviruses: assembly and release of virus particles
    • Lippincott Williams and Wilkins
    • David M., Knipe P.H. Flaviviridae: pestiviruses: assembly and release of virus particles. Fields Virology 2013, 738-739. Lippincott Williams and Wilkins. sixth ed.
    • (2013) Fields Virology , pp. 738-739
    • David, M.1    Knipe, P.H.2
  • 25
    • 33845288971 scopus 로고    scopus 로고
    • Marker vaccine strategies and candidate CSFV marker vaccines
    • Dong X.N., Chen Y.H. Marker vaccine strategies and candidate CSFV marker vaccines. Vaccine 2007, 25(2):205-230.
    • (2007) Vaccine , vol.25 , Issue.2 , pp. 205-230
    • Dong, X.N.1    Chen, Y.H.2
  • 26
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • Dreux M., Gastaminza P., Wieland S.F., Chisari F.V. The autophagy machinery is required to initiate hepatitis C virus replication. Proc. Natl. Acad. Sci. 2009, 106(33):14046-14051.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , Issue.33 , pp. 14046-14051
    • Dreux, M.1    Gastaminza, P.2    Wieland, S.F.3    Chisari, F.V.4
  • 28
    • 84873133718 scopus 로고    scopus 로고
    • Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry
    • El Omari K., Iourin O., Harlos K., Grimes J.M., Stuart D.I. Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry. Cell Rep. 2013, 3(1):30-35.
    • (2013) Cell Rep. , vol.3 , Issue.1 , pp. 30-35
    • El Omari, K.1    Iourin, O.2    Harlos, K.3    Grimes, J.M.4    Stuart, D.I.5
  • 29
    • 0029893139 scopus 로고    scopus 로고
    • Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7
    • Elbers K., Tautz N., Becher P., Stoll D., Rümenapf T., Thiel H.-J. Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7. J. Virol. 1996, 70(6):4131-4135.
    • (1996) J. Virol. , vol.70 , Issue.6 , pp. 4131-4135
    • Elbers, K.1    Tautz, N.2    Becher, P.3    Stoll, D.4    Rümenapf, T.5    Thiel, H.-J.6
  • 31
    • 46749145281 scopus 로고    scopus 로고
    • Generation and characterization of an Npro-disrupted marker bovine viral diarrhea virus derived from a BAC cDNA
    • Fan Z.-C., Bird R.C. Generation and characterization of an Npro-disrupted marker bovine viral diarrhea virus derived from a BAC cDNA. J. Virol. Methods 2008, 151(2):257-263.
    • (2008) J. Virol. Methods , vol.151 , Issue.2 , pp. 257-263
    • Fan, Z.-C.1    Bird, R.C.2
  • 32
    • 84897515685 scopus 로고    scopus 로고
    • Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on classical swine fever virus replication
    • Fernández-Sainz I., Largo E., Gladue D., Fletcher P., O'Donnell V., Holinka L., Carey L., Lu X., Nieva J., Borca M. Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on classical swine fever virus replication. Virology 2014, 456:121-130.
    • (2014) Virology , vol.456 , pp. 121-130
    • Fernández-Sainz, I.1    Largo, E.2    Gladue, D.3    Fletcher, P.4    O'Donnell, V.5    Holinka, L.6    Carey, L.7    Lu, X.8    Nieva, J.9    Borca, M.10
  • 34
    • 61649097923 scopus 로고    scopus 로고
    • Alteration of the N-linked glycosylation condition in E1 glycoprotein of classical swine fever virus strain Brescia alters virulence in swine
    • Fernandez-Sainz I., Holinka L.G., Gavrilov B.K., Prarat M.V., Gladue D., Lu Z., Jia W., Risatti G.R., Borca M.V. Alteration of the N-linked glycosylation condition in E1 glycoprotein of classical swine fever virus strain Brescia alters virulence in swine. Virology 2009, 386(1):210-216.
    • (2009) Virology , vol.386 , Issue.1 , pp. 210-216
    • Fernandez-Sainz, I.1    Holinka, L.G.2    Gavrilov, B.K.3    Prarat, M.V.4    Gladue, D.5    Lu, Z.6    Jia, W.7    Risatti, G.R.8    Borca, M.V.9
  • 35
    • 79961180446 scopus 로고    scopus 로고
    • Classical swine fever virus Npro limits type I interferon induction in plasmacytoid dendritic cells by interacting with interferon regulatory factor 7
    • Fiebach A.R., Guzylack-Piriou L., Python S., Summerfield A., Ruggli N. Classical swine fever virus Npro limits type I interferon induction in plasmacytoid dendritic cells by interacting with interferon regulatory factor 7. J. Virol. 2011, 85(16):8002-8011.
    • (2011) J. Virol. , vol.85 , Issue.16 , pp. 8002-8011
    • Fiebach, A.R.1    Guzylack-Piriou, L.2    Python, S.3    Summerfield, A.4    Ruggli, N.5
  • 36
    • 0036909118 scopus 로고    scopus 로고
    • The influence of viral coding sequences on pestivirus IRES activity reveals further parallels with translation initiation in prokaryotes
    • Fletcher S.P., Ali I.K., Kaminski A., Digard P., Jackson R.J. The influence of viral coding sequences on pestivirus IRES activity reveals further parallels with translation initiation in prokaryotes. RNA 2002, 8(12):1558-1571.
    • (2002) RNA , vol.8 , Issue.12 , pp. 1558-1571
    • Fletcher, S.P.1    Ali, I.K.2    Kaminski, A.3    Digard, P.4    Jackson, R.J.5
  • 37
    • 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., Jackson R.J. Pestivirus internal ribosome entry site (IRES) structure and function: elements in the 5' untranslated region important for IRES function. J. Virol. 2002, 76(10):5024-5033.
    • (2002) J. Virol. , vol.76 , Issue.10 , pp. 5024-5033
    • Fletcher, S.P.1    Jackson, R.J.2
  • 38
    • 0034747214 scopus 로고    scopus 로고
    • Sequences in the 5' nontranslated region of hepatitis C virus required for RNA replication
    • Friebe P., Lohmann V., Krieger N., Bartenschlager R. Sequences in the 5' nontranslated region of hepatitis C virus required for RNA replication. J. Virol. 2001, 75(24):12047-12057.
    • (2001) J. Virol. , vol.75 , Issue.24 , pp. 12047-12057
    • Friebe, P.1    Lohmann, V.2    Krieger, N.3    Bartenschlager, R.4
  • 39
    • 80054070893 scopus 로고    scopus 로고
    • Effects of glycosylation on antigenicity and immunogenicity of classical swine fever virus envelope proteins
    • Gavrilov B.K., Rogers K., Fernandez-Sainz I.J., Holinka L.G., Borca M.V., Risatti G.R. Effects of glycosylation on antigenicity and immunogenicity of classical swine fever virus envelope proteins. Virology 2011, 420(2):135-145.
    • (2011) Virology , vol.420 , Issue.2 , pp. 135-145
    • Gavrilov, B.K.1    Rogers, K.2    Fernandez-Sainz, I.J.3    Holinka, L.G.4    Borca, M.V.5    Risatti, G.R.6
  • 40
    • 0037418322 scopus 로고    scopus 로고
    • RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription
    • Ge Q., McManus M.T., Nguyen T., Shen C.-H., Sharp P.A., Eisen H.N., Chen J. RNA interference of influenza virus production by directly targeting mRNA for degradation and indirectly inhibiting all viral RNA transcription. Proc. Natl. Acad. Sci. 2003, 100(5):2718-2723.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.5 , pp. 2718-2723
    • Ge, Q.1    McManus, M.T.2    Nguyen, T.3    Shen, C.-H.4    Sharp, P.A.5    Eisen, H.N.6    Chen, J.7
  • 41
    • 30344487269 scopus 로고    scopus 로고
    • The amino-terminal domain of bovine viral diarrhea virus Npro protein is necessary for alpha/beta interferon antagonism
    • Gil L.H., Ansari I.H., Vassilev V., Liang D., Lai V.C., Zhong W., Hong Z., Dubovi E.J., Donis R.O. The amino-terminal domain of bovine viral diarrhea virus Npro protein is necessary for alpha/beta interferon antagonism. J. Virol. 2006, 80(2):900-911.
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 900-911
    • Gil, L.H.1    Ansari, I.H.2    Vassilev, V.3    Liang, D.4    Lai, V.C.5    Zhong, W.6    Hong, Z.7    Dubovi, E.J.8    Donis, R.O.9
  • 42
    • 77956936911 scopus 로고    scopus 로고
    • Effects of the interactions of classical swine fever virus Core protein with proteins of the SUMOylation pathway on virulence in swine
    • Gladue D., Holinka L., Fernandez-Sainz I., Prarat M., O'donell V., Vepkhvadze N., Lu Z., Rogers K., Risatti G., Borca M. Effects of the interactions of classical swine fever virus Core protein with proteins of the SUMOylation pathway on virulence in swine. Virology 2010, 407(1):129-136.
    • (2010) Virology , vol.407 , Issue.1 , pp. 129-136
    • Gladue, D.1    Holinka, L.2    Fernandez-Sainz, I.3    Prarat, M.4    O'donell, V.5    Vepkhvadze, N.6    Lu, Z.7    Rogers, K.8    Risatti, G.9    Borca, M.10
  • 43
    • 79952533056 scopus 로고    scopus 로고
    • Interaction between core protein of classical swine fever virus with cellular IQGAP1 protein appears essential for virulence in swine
    • Gladue D., Holinka L., Fernandez-Sainz I., Prarat M., O'Donnell V., Vepkhvadze N., Lu Z., Risatti G., Borca M. Interaction between core protein of classical swine fever virus with cellular IQGAP1 protein appears essential for virulence in swine. Virology 2011, 412(1):68-74.
    • (2011) Virology , vol.412 , Issue.1 , pp. 68-74
    • Gladue, D.1    Holinka, L.2    Fernandez-Sainz, I.3    Prarat, M.4    O'Donnell, V.5    Vepkhvadze, N.6    Lu, Z.7    Risatti, G.8    Borca, M.9
  • 48
    • 0029825147 scopus 로고    scopus 로고
    • Characterization of RNA synthesis during a one-step growth curve and of the replication mechanism of bovine viral diarrhoea virus
    • Gong Y., Trowbridge R., Macnaughton T.B., Westaway E.G., Shannon A.D., Gowans E.J. Characterization of RNA synthesis during a one-step growth curve and of the replication mechanism of bovine viral diarrhoea virus. J. Gen. Virol. 1996, 77(11):2729-2736.
    • (1996) J. Gen. Virol. , vol.77 , Issue.11 , 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
  • 49
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya A.E., Koonin E.V. Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res. 1989, 17(21):8413-8438.
    • (1989) Nucleic Acids Res. , vol.17 , Issue.21 , pp. 8413-8438
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 50
    • 84887304158 scopus 로고    scopus 로고
    • The structure of classical swine fever virus Npro: a novel cysteine autoprotease and zinc-binding protein involved in subversion of Type I interferon induction
    • Gottipati K., Ruggli N., Gerber M., Tratschin J.-D., Benning M., Bellamy H., Choi K.H. The structure of classical swine fever virus Npro: a novel cysteine autoprotease and zinc-binding protein involved in subversion of Type I interferon induction. PLoS Pathog. 2013, 9(10):e1003704.
    • (2013) PLoS Pathog. , vol.9 , Issue.10 , pp. e1003704
    • Gottipati, K.1    Ruggli, N.2    Gerber, M.3    Tratschin, J.-D.4    Benning, M.5    Bellamy, H.6    Choi, K.H.7
  • 51
    • 0034872308 scopus 로고    scopus 로고
    • Genetic analysis of the pestivirus nonstructural coding region: defects in the NS5A unit can be complemented intrans
    • Grassmann C.W., Isken O., Tautz N., Behrens S.-E. Genetic analysis of the pestivirus nonstructural coding region: defects in the NS5A unit can be complemented intrans. J. Virol. 2001, 75(17):7791-7802.
    • (2001) J. Virol. , vol.75 , Issue.17 , pp. 7791-7802
    • Grassmann, C.W.1    Isken, O.2    Tautz, N.3    Behrens, S.-E.4
  • 54
    • 84880561773 scopus 로고    scopus 로고
    • Intra-host variation structure of classical swine fever virus NS5B in relation to antiviral therapy
    • Haegeman A., Vrancken R., Neyts J., Koenen F. Intra-host variation structure of classical swine fever virus NS5B in relation to antiviral therapy. Antivir. Res. 2013, 98(2):266-272.
    • (2013) Antivir. Res. , vol.98 , Issue.2 , pp. 266-272
    • Haegeman, A.1    Vrancken, R.2    Neyts, J.3    Koenen, F.4
  • 55
    • 33747396191 scopus 로고    scopus 로고
    • Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition
    • Han Y., Chen Y.-S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., Kang P.M. Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition. Circ. Res. 2006, 99(4):415-423.
    • (2006) Circ. Res. , vol.99 , Issue.4 , pp. 415-423
    • Han, Y.1    Chen, Y.-S.2    Liu, Z.3    Bodyak, N.4    Rigor, D.5    Bisping, E.6    Pu, W.T.7    Kang, P.M.8
  • 56
    • 0033819541 scopus 로고    scopus 로고
    • E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies
    • Harada T., Tautz N., Thiel H.-J. E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies. J. Virol. 2000, 74(20):9498-9506.
    • (2000) J. Virol. , vol.74 , Issue.20 , pp. 9498-9506
    • Harada, T.1    Tautz, N.2    Thiel, H.-J.3
  • 57
    • 0024291288 scopus 로고
    • Simple RNA enzymes with new and highly specific endoribonuclease activities
    • Haseloff J., Gerlach W.L. Simple RNA enzymes with new and highly specific endoribonuclease activities. Nature 1988, 334(6183):585-591.
    • (1988) Nature , vol.334 , Issue.6183 , pp. 585-591
    • Haseloff, J.1    Gerlach, W.L.2
  • 58
    • 2342480559 scopus 로고    scopus 로고
    • Classical swine fever virus glycoprotein Erns is an endoribonuclease with an unusual base specificity
    • Hausmann Y., Roman-Sosa G., Thiel H.-J., Rümenapf T. Classical swine fever virus glycoprotein Erns is an endoribonuclease with an unusual base specificity. J. Virol. 2004, 78(10):5507-5512.
    • (2004) J. Virol. , vol.78 , Issue.10 , pp. 5507-5512
    • Hausmann, Y.1    Roman-Sosa, G.2    Thiel, H.-J.3    Rümenapf, T.4
  • 59
    • 84896720852 scopus 로고    scopus 로고
    • In vitro inhibition of the replication of classical swine fever virus by porcine Mx1 protein
    • He D.N., Zhang X.M., Liu K., Pang R., Zhao J., Zhou B., Chen P.Y. In vitro inhibition of the replication of classical swine fever virus by porcine Mx1 protein. Antivir. Res. 2014, 104:128-135.
    • (2014) Antivir. Res. , vol.104 , pp. 128-135
    • He, D.N.1    Zhang, X.M.2    Liu, K.3    Pang, R.4    Zhao, J.5    Zhou, B.6    Chen, P.Y.7
  • 60
    • 84922784698 scopus 로고    scopus 로고
    • Beta-actin interacts with the E2 protein and is involved in the early replication of classical swine fever virus
    • He F., Ling L., Liao Y., Li S., Han W., Zhao B., Sun Y., Qiu H.-J. Beta-actin interacts with the E2 protein and is involved in the early replication of classical swine fever virus. Virus Res. 2013.
    • (2013) Virus Res.
    • He, F.1    Ling, L.2    Liao, Y.3    Li, S.4    Han, W.5    Zhao, B.6    Sun, Y.7    Qiu, H.-J.8
  • 61
    • 33947285401 scopus 로고    scopus 로고
    • Interference of porcine reproductive and respiratory syndrome virus replication on MARC-145 cells using DNA-based short interfering RNAs
    • He Y.-x., Hua R.-h., Zhou Y.-j., Qiu H.-j., Tong G.-z. Interference of porcine reproductive and respiratory syndrome virus replication on MARC-145 cells using DNA-based short interfering RNAs. Antivir. Res. 2007, 74(2):83-91.
    • (2007) Antivir. Res. , vol.74 , Issue.2 , pp. 83-91
    • He, Y.-X.1    Hua, R.-H.2    Zhou, Y.-J.3    Qiu, H.-J.4    Tong, G.-Z.5
  • 62
    • 32444447231 scopus 로고    scopus 로고
    • Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase
    • Heimann M., Sosa G.R., Martoglio B., Thiel H.-J., Rümenapf T. Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase. J. Virol. 2006, 80(4):1915-1921.
    • (2006) J. Virol. , vol.80 , Issue.4 , pp. 1915-1921
    • Heimann, M.1    Sosa, G.R.2    Martoglio, B.3    Thiel, H.-J.4    Rümenapf, T.5
  • 63
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen C.U., Sarnow P. Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev. 2001, 15(13):1593-1612.
    • (2001) Genes Dev. , vol.15 , Issue.13 , pp. 1593-1612
    • Hellen, C.U.1    Sarnow, P.2
  • 65
    • 84877360123 scopus 로고    scopus 로고
    • Rapid recovery of classical swine fever virus directly from cloned cDNA
    • Huang J.-h., Li Y.-f., He F., Li D D., Sun Y., Han W., Qiu H.-j. Rapid recovery of classical swine fever virus directly from cloned cDNA. J. Integr. Agric. 2013, 12(5):877-883.
    • (2013) J. Integr. Agric. , vol.12 , Issue.5 , pp. 877-883
    • Huang, J.-H.1    Li, Y.-F.2    He, F.3    Li, D.D.4    Sun, Y.5    Han, W.6    Qiu, H.-J.7
  • 66
    • 84892827826 scopus 로고    scopus 로고
    • The challenges of classical swine fever control: modified live and E2 subunit vaccines
    • Huang Y.-L., Deng M.-C., Wang F.-I., Huang C.-C., Chang C.-Y. The challenges of classical swine fever control: modified live and E2 subunit vaccines. Virus Res. 2014, 179:1-11.
    • (2014) Virus Res. , vol.179 , pp. 1-11
    • Huang, Y.-L.1    Deng, M.-C.2    Wang, F.-I.3    Huang, C.-C.4    Chang, C.-Y.5
  • 67
    • 55249109587 scopus 로고    scopus 로고
    • Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO
    • Huh Y.H., Kim Y.E., Kim E.T., Park J.J., Song M.J., Zhu H., Hayward G.S., Ahn J.-H. Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO. J. Virol. 2008, 82(21):10444-10454.
    • (2008) J. Virol. , vol.82 , Issue.21 , pp. 10444-10454
    • Huh, Y.H.1    Kim, Y.E.2    Kim, E.T.3    Park, J.J.4    Song, M.J.5    Zhu, H.6    Hayward, G.S.7    Ahn, J.-H.8
  • 68
    • 0030704752 scopus 로고    scopus 로고
    • Inhibition of pestivirus infection in cell culture by envelope proteins Erns and E2 of classical swine fever virus: Erns and E2 interact with different receptors
    • Hulst M., Moormann R. Inhibition of pestivirus infection in cell culture by envelope proteins Erns and E2 of classical swine fever virus: Erns and E2 interact with different receptors. J. Gen. Virol. 1997, 78(11):2779-2787.
    • (1997) J. Gen. Virol. , vol.78 , Issue.11 , pp. 2779-2787
    • Hulst, M.1    Moormann, R.2
  • 69
    • 0031984987 scopus 로고    scopus 로고
    • Inactivation of the RNase activity of glycoprotein Erns of classical swine fever virus results in a cytopathogenic virus
    • Hulst M., Panoto F., Hoekman A., Van Gennip H., Moormann R. Inactivation of the RNase activity of glycoprotein Erns of classical swine fever virus results in a cytopathogenic virus. J. Virol. 1998, 72(1):151-157.
    • (1998) J. Virol. , vol.72 , Issue.1 , pp. 151-157
    • Hulst, M.1    Panoto, F.2    Hoekman, A.3    Van Gennip, H.4    Moormann, R.5
  • 71
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • Iwasaki A., Medzhitov R. Regulation of adaptive immunity by the innate immune system. Science 2010, 327(5963):291-295.
    • (2010) Science , vol.327 , Issue.5963 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 72
    • 84899871810 scopus 로고    scopus 로고
    • Vaccination influences the evolution of classical swine fever virus
    • Ji W., Niu D.D., Si H.L., Ding N.Z., He C.Q. Vaccination influences the evolution of classical swine fever virus. Infect. Genet. Evol. 2014, 25:69-77.
    • (2014) Infect. Genet. Evol. , vol.25 , pp. 69-77
    • Ji, W.1    Niu, D.D.2    Si, H.L.3    Ding, N.Z.4    He, C.Q.5
  • 74
    • 78049359266 scopus 로고    scopus 로고
    • The classical swine fever virus N-terminal protease Npro binds to cellular HAX-1
    • Johns H.L., Doceul V., Everett H., Crooke H., Charleston B., Seago J. The classical swine fever virus N-terminal protease Npro binds to cellular HAX-1. J. Gen. Virol. 2010, 91(11):2677-2686.
    • (2010) J. Gen. Virol. , vol.91 , Issue.11 , pp. 2677-2686
    • Johns, H.L.1    Doceul, V.2    Everett, H.3    Crooke, H.4    Charleston, B.5    Seago, J.6
  • 75
    • 0242353590 scopus 로고
    • Propagation of hog cholera virus in rabbits
    • (Society for Experimental Biology and Medicine (New York, NY))
    • Koprowski H., James T.R., Cox H.R. Propagation of hog cholera virus in rabbits. Proc. Soc. Exp. Biol. Med. 1946, 63:178-183. (Society for Experimental Biology and Medicine (New York, NY)).
    • (1946) Proc. Soc. Exp. Biol. Med. , vol.63 , pp. 178-183
    • Koprowski, H.1    James, T.R.2    Cox, H.R.3
  • 76
    • 84861041347 scopus 로고    scopus 로고
    • Crystal structure of the pestivirus envelope glycoprotein Erns and mechanistic analysis of its ribonuclease activity
    • Krey T., Bontems F., Vonrhein C., Vaney M.-C., Bricogne G., Rümenapf T., Rey Félix A. Crystal structure of the pestivirus envelope glycoprotein Erns and mechanistic analysis of its ribonuclease activity. Structure 2012, 20(5):862-873.
    • (2012) Structure , vol.20 , Issue.5 , pp. 862-873
    • Krey, T.1    Bontems, F.2    Vonrhein, C.3    Vaney, M.-C.4    Bricogne, G.5    Rümenapf, T.6    Rey Félix, A.7
  • 77
    • 0037219580 scopus 로고    scopus 로고
    • Reactivation of lytic replication from B cells latently infected with Epstein-Barr virus occurs with high S-phase cyclin-dependent kinase activity while inhibiting cellular DNA replication
    • Kudoh A., Fujita M., Kiyono T., Kuzushima K., Sugaya Y., Izuta S., Nishiyama Y., Tsurumi T. Reactivation of lytic replication from B cells latently infected with Epstein-Barr virus occurs with high S-phase cyclin-dependent kinase activity while inhibiting cellular DNA replication. J. Virol. 2003, 77(2):851-861.
    • (2003) J. Virol. , vol.77 , Issue.2 , pp. 851-861
    • Kudoh, A.1    Fujita, M.2    Kiyono, T.3    Kuzushima, K.4    Sugaya, Y.5    Izuta, S.6    Nishiyama, Y.7    Tsurumi, T.8
  • 79
    • 31944434363 scopus 로고    scopus 로고
    • Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis
    • Lackner T., Thiel H.-J., Tautz N. Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103(5):1510-1515.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.5 , pp. 1510-1515
    • Lackner, T.1    Thiel, H.-J.2    Tautz, N.3
  • 80
    • 50149114689 scopus 로고    scopus 로고
    • Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A
    • Lai C.-K., Jeng K.-S., Machida K., Lai M.M. Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. J. Virol. 2008, 82(17):8838-8848.
    • (2008) J. Virol. , vol.82 , Issue.17 , pp. 8838-8848
    • Lai, C.-K.1    Jeng, K.-S.2    Machida, K.3    Lai, M.M.4
  • 82
    • 84886928302 scopus 로고    scopus 로고
    • Autocatalytic cleavage within classical swine fever virus NS3 leads to a functional separation of protease and helicase
    • Lamp B., Riedel C., Wentz E., Tortorici M.-A., Rümenapf T. Autocatalytic cleavage within classical swine fever virus NS3 leads to a functional separation of protease and helicase. J. Virol. 2013, 87(21):11872-11883.
    • (2013) J. Virol. , vol.87 , Issue.21 , pp. 11872-11883
    • Lamp, B.1    Riedel, C.2    Wentz, E.3    Tortorici, M.-A.4    Rümenapf, T.5
  • 83
    • 0036785507 scopus 로고    scopus 로고
    • A structural model of pestivirus Erns based on disulfide bond connectivity and homology modeling reveals an extremely rare vicinal disulfide
    • Langedijk J., Van Veelen P., Schaaper W., De Ru A., Meloen R., Hulst M. A structural model of pestivirus Erns based on disulfide bond connectivity and homology modeling reveals an extremely rare vicinal disulfide. J. Virol. 2002, 76(20):10383-10392.
    • (2002) J. Virol. , vol.76 , Issue.20 , pp. 10383-10392
    • Langedijk, J.1    Van Veelen, P.2    Schaaper, W.3    De Ru, A.4    Meloen, R.5    Hulst, M.6
  • 84
    • 0037085304 scopus 로고    scopus 로고
    • Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop
    • Langedijk J.P. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J. Biol. Chem. 2002, 277(7):5308-5314.
    • (2002) J. Biol. Chem. , vol.277 , Issue.7 , pp. 5308-5314
    • Langedijk, J.P.1
  • 85
    • 23244435310 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis
    • Lecot S., Belouzard S., Dubuisson J., Rouillé Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J. Virol. 2005, 79(16):10826-10829.
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10826-10829
    • Lecot, S.1    Belouzard, S.2    Dubuisson, J.3    Rouillé, Y.4
  • 87
    • 82255160640 scopus 로고    scopus 로고
    • Clustering of classical swine fever virus isolates by codon pair bias
    • Leifer I., Hoeper D., Blome S., Beer M., Ruggli N. Clustering of classical swine fever virus isolates by codon pair bias. BMC Res. Notes 2011, 4(1):521.
    • (2011) BMC Res. Notes , vol.4 , Issue.1 , pp. 521
    • Leifer, I.1    Hoeper, D.2    Blome, S.3    Beer, M.4    Ruggli, N.5
  • 88
    • 84875255515 scopus 로고    scopus 로고
    • Approaches to define the viral genetic basis of classical swine fever virus virulence
    • Leifer I., Ruggli N., Blome S. Approaches to define the viral genetic basis of classical swine fever virus virulence. Virology 2013, 438(2):51-55.
    • (2013) Virology , vol.438 , Issue.2 , pp. 51-55
    • Leifer, I.1    Ruggli, N.2    Blome, S.3
  • 89
    • 84876017437 scopus 로고    scopus 로고
    • Efficient and stable rescue of classical swine fever virus from cloned cDNA using an RNA polymerase II system
    • Li C., Huang J., Li Y., He F., Li D., Sun Y., Han W., Li S., Qiu H.-J. Efficient and stable rescue of classical swine fever virus from cloned cDNA using an RNA polymerase II system. Arch. Virol. 2013, 158(4):901-907.
    • (2013) Arch. Virol. , vol.158 , Issue.4 , pp. 901-907
    • Li, C.1    Huang, J.2    Li, Y.3    He, F.4    Li, D.5    Sun, Y.6    Han, W.7    Li, S.8    Qiu, H.-J.9
  • 90
    • 84896308614 scopus 로고    scopus 로고
    • The role of noncoding regions of classical swine fever virus C-strain in its adaptation to the rabbit
    • Li C., Li Y., Shen L., Huang J., Sun Y., Luo Y., Zhao B., Wang C., Yuan J., Qiu H.-J. The role of noncoding regions of classical swine fever virus C-strain in its adaptation to the rabbit. Virus Res. 2014, 183:117-122.
    • (2014) Virus Res. , vol.183 , pp. 117-122
    • Li, C.1    Li, Y.2    Shen, L.3    Huang, J.4    Sun, Y.5    Luo, Y.6    Zhao, B.7    Wang, C.8    Yuan, J.9    Qiu, H.-J.10
  • 91
    • 84904975200 scopus 로고    scopus 로고
    • The classic swine fever virus (CSFV) core protein can enhance de novo-initiated RNA synthesis by the CSFV polymerase NS5B
    • Li W., Zhang Y., Kao C.C. The classic swine fever virus (CSFV) core protein can enhance de novo-initiated RNA synthesis by the CSFV polymerase NS5B. Virus Genes 2014, 49(1):106-115.
    • (2014) Virus Genes , vol.49 , Issue.1 , pp. 106-115
    • Li, W.1    Zhang, Y.2    Kao, C.C.3
  • 92
    • 84905971496 scopus 로고    scopus 로고
    • Visualization of the Npro protein in living cells using biarsenically labeling tetracysteine-tagged classical swine fever virus
    • Li Y., Shen L., Li C., Huang J., Zhao B., Sun Y., Li S., Luo Y., Qiu H.-J. Visualization of the Npro protein in living cells using biarsenically labeling tetracysteine-tagged classical swine fever virus. Virus Res. 2014.
    • (2014) Virus Res.
    • Li, Y.1    Shen, L.2    Li, C.3    Huang, J.4    Zhao, B.5    Sun, Y.6    Li, S.7    Luo, Y.8    Qiu, H.-J.9
  • 93
    • 84880625971 scopus 로고    scopus 로고
    • Simplified serum neutralization test based on enhanced green fluorescent protein-tagged classical swine fever virus
    • Li Y., Shen L., Sun Y., Yuan J., Huang J., Li C., Li S., Luo Y., Qiu H.-J. Simplified serum neutralization test based on enhanced green fluorescent protein-tagged classical swine fever virus. J. Clin. Microbiol. 2013, 51(8):2710-2712.
    • (2013) J. Clin. Microbiol. , vol.51 , Issue.8 , pp. 2710-2712
    • Li, Y.1    Shen, L.2    Sun, Y.3    Yuan, J.4    Huang, J.5    Li, C.6    Li, S.7    Luo, Y.8    Qiu, H.-J.9
  • 94
    • 84876865608 scopus 로고    scopus 로고
    • Crystal structure of glycoprotein E2 from bovine viral diarrhea virus
    • Li Y., Wang J., Kanai R., Modis Y. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proc. Natl. Acad. Sci. 2013, 110(17):6805-6810.
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , Issue.17 , pp. 6805-6810
    • Li, Y.1    Wang, J.2    Kanai, R.3    Modis, Y.4
  • 95
    • 0036199633 scopus 로고    scopus 로고
    • Human T-lymphotropic virus type 1 oncoprotein tax promotes S-phase entry but blocks mitosis
    • Liang M.-H., Geisbert T., Yao Y., Hinrichs S.H., Giam C.-Z. Human T-lymphotropic virus type 1 oncoprotein tax promotes S-phase entry but blocks mitosis. J. Virol. 2002, 76(8):4022-4033.
    • (2002) J. Virol. , vol.76 , Issue.8 , pp. 4022-4033
    • Liang, M.-H.1    Geisbert, T.2    Yao, Y.3    Hinrichs, S.H.4    Giam, C.-Z.5
  • 98
    • 0016039326 scopus 로고
    • Virus multiplication in pigs inoculated with lapinized hog cholera live vaccine
    • Lin T.C., Shieh C.M., Su J.F. Virus multiplication in pigs inoculated with lapinized hog cholera live vaccine. Zhonghua Minguo wei sheng wu xue za zhi 1974, 7(1):13-19.
    • (1974) Zhonghua Minguo wei sheng wu xue za zhi , vol.7 , Issue.1 , pp. 13-19
    • Lin, T.C.1    Shieh, C.M.2    Su, J.F.3
  • 100
    • 84910628426 scopus 로고    scopus 로고
    • Classical swine fever virus (CSFV) and p7 protein induce secretion of IL-1β in Macrophages
    • Lin Z., Liang W., Kang K., Li H., Cao Z., Zhang Y. Classical swine fever virus (CSFV) and p7 protein induce secretion of IL-1β in Macrophages. J. Gen. Virol. 2014, 95(Pt 12):2693-2699.
    • (2014) J. Gen. Virol. , vol.95 , pp. 2693-2699
    • Lin, Z.1    Liang, W.2    Kang, K.3    Li, H.4    Cao, Z.5    Zhang, Y.6
  • 101
    • 0031931830 scopus 로고    scopus 로고
    • The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator
    • Liu J.-J., Wong M.-L., Chang T.-J. The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator. Virus Res. 1998, 53(1):75-80.
    • (1998) Virus Res. , vol.53 , Issue.1 , pp. 75-80
    • Liu, J.-J.1    Wong, M.-L.2    Chang, T.-J.3
  • 102
    • 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., 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. 1997, 71(11):8416-8428.
    • (1997) J. Virol. , vol.71 , Issue.11 , pp. 8416-8428
    • Lohmann, V.1    Körner, F.2    Herian, U.3    Bartenschlager, R.4
  • 103
    • 0007691481 scopus 로고
    • Classical swine fever: properties of a clone (strain"Thiverval") isolated from a cellular culture at a low temperature: application in vaccination
    • LunaisM A. Classical swine fever: properties of a clone (strain"Thiverval") isolated from a cellular culture at a low temperature: application in vaccination. Rev. Med. Vet. (Toulouse) 1972, 123(12):1537-1554.
    • (1972) Rev. Med. Vet. (Toulouse) , vol.123 , Issue.12 , pp. 1537-1554
    • Lunais, M.A.1
  • 104
    • 84903446871 scopus 로고    scopus 로고
    • Classical swine fever in China: a minireview
    • Luo Y., Li S., Sun Y., Qiu H.-J. Classical swine fever in China: a minireview. Vet. Microbiol. 2014, 172(1-2):1-6.
    • (2014) Vet. Microbiol. , vol.172 , Issue.1-2 , pp. 1-6
    • Luo, Y.1    Li, S.2    Sun, Y.3    Qiu, H.-J.4
  • 105
    • 60749120273 scopus 로고    scopus 로고
    • The viral RNase Erns prevents IFN type-I triggering by pestiviral single- and double-stranded RNAs
    • Mätzener P., Magkouras I., Rümenapf T., Peterhans E., Schweizer M. The viral RNase Erns prevents IFN type-I triggering by pestiviral single- and double-stranded RNAs. Virus Res. 2009, 140(1-2):15-23.
    • (2009) Virus Res. , vol.140 , Issue.1-2 , pp. 15-23
    • Mätzener, P.1    Magkouras, I.2    Rümenapf, T.3    Peterhans, E.4    Schweizer, M.5
  • 106
    • 54449090843 scopus 로고    scopus 로고
    • RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses
    • Magkouras I., Mätzener P., Rümenapf T., Peterhans E., Schweizer M. RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses. J. Gen. Virol. 2008, 89(10):2501-2506.
    • (2008) J. Gen. Virol. , vol.89 , Issue.10 , pp. 2501-2506
    • Magkouras, I.1    Mätzener, P.2    Rümenapf, T.3    Peterhans, E.4    Schweizer, M.5
  • 107
    • 0344665684 scopus 로고    scopus 로고
    • Attenuation of classical swine fever virus by deletion of the viral Npro gene
    • Mayer D., Hofmann M.A., Tratschin J.-D. Attenuation of classical swine fever virus by deletion of the viral Npro gene. Vaccine 2004, 22(3):317-328.
    • (2004) Vaccine , vol.22 , Issue.3 , pp. 317-328
    • Mayer, D.1    Hofmann, M.A.2    Tratschin, J.-D.3
  • 108
    • 0345148344 scopus 로고    scopus 로고
    • Mutations abrogating the RNase activity in glycoprotein Erns of the pestivirus classical swine fever virus lead to virus attenuation
    • Meyers G., Saalmüller A., Büttner M. Mutations abrogating the RNase activity in glycoprotein Erns of the pestivirus classical swine fever virus lead to virus attenuation. J. Virol. 1999, 73(12):10224-10235.
    • (1999) J. Virol. , vol.73 , Issue.12 , pp. 10224-10235
    • Meyers, G.1    Saalmüller, A.2    Büttner, M.3
  • 109
    • 0030030478 scopus 로고    scopus 로고
    • Classical swine fever virus: recovery of infectious viruses from cDNA constructs and generation of recombinant cytopathogenic defective interfering particles
    • Meyers G., Thiel H.-J., Rümenapf T. Classical swine fever virus: recovery of infectious viruses from cDNA constructs and generation of recombinant cytopathogenic defective interfering particles. J. Virol. 1996, 70(3):1588-1595.
    • (1996) J. Virol. , vol.70 , Issue.3 , pp. 1588-1595
    • Meyers, G.1    Thiel, H.-J.2    Rümenapf, T.3
  • 110
    • 0030030337 scopus 로고    scopus 로고
    • Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus
    • Moormann R., Van Gennip H., Miedema G., Hulst M., Van Rijn P. Infectious RNA transcribed from an engineered full-length cDNA template of the genome of a pestivirus. J. Virol. 1996, 70(2):763-770.
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 763-770
    • Moormann, R.1    Van Gennip, H.2    Miedema, G.3    Hulst, M.4    Van Rijn, P.5
  • 111
    • 0032864837 scopus 로고    scopus 로고
    • Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus
    • Moser C., Stettler P., Tratschin J.-D., Hofmann M.A. Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus. J. Virol. 1999, 73(9):7787-7794.
    • (1999) J. Virol. , vol.73 , Issue.9 , pp. 7787-7794
    • Moser, C.1    Stettler, P.2    Tratschin, J.-D.3    Hofmann, M.A.4
  • 112
    • 34547686361 scopus 로고    scopus 로고
    • Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation
    • Moulin H.R., Seuberlich T., Bauhofer O., Bennett L.C., Tratschin J.-D., Hofmann M.A., Ruggli N. Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation. Virology 2007, 365(2):376-389.
    • (2007) Virology , vol.365 , Issue.2 , pp. 376-389
    • Moulin, H.R.1    Seuberlich, T.2    Bauhofer, O.3    Bennett, L.C.4    Tratschin, J.-D.5    Hofmann, M.A.6    Ruggli, N.7
  • 113
    • 0013770135 scopus 로고
    • Studies on the tissue culture of hog cholera virus. II. Neutralization test by means of the influence of hog cholera virus infection on Newcastle disease virus infection (HEIC method)
    • Nishimura Y., Sato U., Hanaki T., Nobuto K. Studies on the tissue culture of hog cholera virus. II. Neutralization test by means of the influence of hog cholera virus infection on Newcastle disease virus infection (HEIC method). Nihon juigaku zasshi 1964, 26(3):133-140.
    • (1964) Nihon juigaku zasshi , vol.26 , Issue.3 , pp. 133-140
    • Nishimura, Y.1    Sato, U.2    Hanaki, T.3    Nobuto, K.4
  • 117
    • 19644396270 scopus 로고    scopus 로고
    • Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its self-association
    • Palacios S., Perez L.H., Welsch S., Schleich S., Chmielarska K., Melchior F., Locker J.K. Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its self-association. Mol. Biol. Cell 2005, 16(6):2822-2835.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.6 , pp. 2822-2835
    • Palacios, S.1    Perez, L.H.2    Welsch, S.3    Schleich, S.4    Chmielarska, K.5    Melchior, F.6    Locker, J.K.7
  • 118
    • 84860753740 scopus 로고    scopus 로고
    • Establishment and characterization of an infectious cDNA clone of a classical swine fever virus LOM strain
    • Park G.-S., Lim S.-I., Hong S.-H., Song J.-Y. Establishment and characterization of an infectious cDNA clone of a classical swine fever virus LOM strain. J. Vet. Sci. 2012, 13(1):81-91.
    • (2012) J. Vet. Sci. , vol.13 , Issue.1 , pp. 81-91
    • Park, G.-S.1    Lim, S.-I.2    Hong, S.-H.3    Song, J.-Y.4
  • 119
  • 120
    • 0039730838 scopus 로고
    • Immunogenicity and safety of the new attenuated Cellpest vaccine against swine fever
    • Pejsak Z.L.A., Markowska I., Dzierzawski A., Mokrzycka A. Immunogenicity and safety of the new attenuated Cellpest vaccine against swine fever. Med. Weter. 1991, 47(10):461-463.
    • (1991) Med. Weter. , vol.47 , Issue.10 , pp. 461-463
    • Pejsak, Z.L.A.1    Markowska, I.2    Dzierzawski, A.3    Mokrzycka, A.4
  • 121
    • 77949652934 scopus 로고    scopus 로고
    • RNA interference targeting nucleocapsid protein (C) inhibits classical swine fever virus replication in SK-6 cells
    • Porntrakulpipat S., Supankong S., Chatchawanchonteera A., Pakdee P. RNA interference targeting nucleocapsid protein (C) inhibits classical swine fever virus replication in SK-6 cells. Vet. Microbiol. 2010, 142(1):41-44.
    • (2010) Vet. Microbiol. , vol.142 , Issue.1 , pp. 41-44
    • Porntrakulpipat, S.1    Supankong, S.2    Chatchawanchonteera, A.3    Pakdee, P.4
  • 123
    • 0031935816 scopus 로고    scopus 로고
    • N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis
    • Rümenapf T., Stark R., Heimann M., Thiel H.-J. N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis. J. Virol. 1998, 72(3):2544-2547.
    • (1998) J. Virol. , vol.72 , Issue.3 , pp. 2544-2547
    • Rümenapf, T.1    Stark, R.2    Heimann, M.3    Thiel, H.-J.4
  • 124
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rümenapf T., Unger G., Strauss J.H., Thiel H.-J. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 1993, 67(6):3288-3294.
    • (1993) J. Virol. , vol.67 , Issue.6 , pp. 3288-3294
    • Rümenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.-J.4
  • 125
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings N.D., Waller M., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 2014, 42(D1):D503-D509.
    • (2014) Nucleic Acids Res. , vol.42 , Issue.D1 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 126
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Lippincott Williams and Wilkins
    • Rice L. Flaviviridae: the viruses and their replication. Fields Virology 2001, 991-1041. Lippincott Williams and Wilkins.
    • (2001) Fields Virology , pp. 991-1041
    • Rice, L.1
  • 127
    • 77957953361 scopus 로고    scopus 로고
    • Characterization of essential domains and plasticity of the classical swine fever virus core protein
    • Riedel C., Lamp B., Heimann M., Rümenapf T. Characterization of essential domains and plasticity of the classical swine fever virus core protein. J. Virol. 2010, 84(21):11523-11531.
    • (2010) J. Virol. , vol.84 , Issue.21 , pp. 11523-11531
    • Riedel, C.1    Lamp, B.2    Heimann, M.3    Rümenapf, T.4
  • 128
    • 14744267515 scopus 로고    scopus 로고
    • The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine
    • Risatti G., Borca M., Kutish G., Lu Z., Holinka L., French R., Tulman E., Rock D. The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine. J. Virol. 2005, 79(6):3787-3796.
    • (2005) J. Virol. , vol.79 , Issue.6 , pp. 3787-3796
    • Risatti, G.1    Borca, M.2    Kutish, G.3    Lu, Z.4    Holinka, L.5    French, R.6    Tulman, E.7    Rock, D.8
  • 129
    • 33750071094 scopus 로고    scopus 로고
    • Identification of a novel virulence determinant within the E2 structural glycoprotein of classical swine fever virus
    • Risatti G., Holinka L., Carrillo C., Kutish G., Lu Z., Tulman E., Sainz I.F., Borca M. Identification of a novel virulence determinant within the E2 structural glycoprotein of classical swine fever virus. Virology 2006, 355(1):94-101.
    • (2006) Virology , vol.355 , Issue.1 , pp. 94-101
    • Risatti, G.1    Holinka, L.2    Carrillo, C.3    Kutish, G.4    Lu, Z.5    Tulman, E.6    Sainz, I.F.7    Borca, M.8
  • 130
    • 34249886051 scopus 로고    scopus 로고
    • Mutations in the carboxyl terminal region of E2 glycoprotein of classical swine fever virus are responsible for viral attenuation in swine
    • Risatti G., Holinka L., Fernandez Sainz I., Carrillo C., Kutish G., Lu Z., Zhu J., Rock D., Borca M. Mutations in the carboxyl terminal region of E2 glycoprotein of classical swine fever virus are responsible for viral attenuation in swine. Virology 2007, 364(2):371-382.
    • (2007) Virology , vol.364 , Issue.2 , pp. 371-382
    • Risatti, G.1    Holinka, L.2    Fernandez Sainz, I.3    Carrillo, C.4    Kutish, G.5    Lu, Z.6    Zhu, J.7    Rock, D.8    Borca, M.9
  • 131
    • 27644442081 scopus 로고    scopus 로고
    • Mutation of E1 glycoprotein of classical swine fever virus affects viral virulence in swine
    • Risatti G., Holinka L., Lu Z., Kutish G., Tulman E., French R., Sur J., Rock D., Borca M. Mutation of E1 glycoprotein of classical swine fever virus affects viral virulence in swine. Virology 2005, 343(1):116-127.
    • (2005) Virology , vol.343 , Issue.1 , pp. 116-127
    • Risatti, G.1    Holinka, L.2    Lu, Z.3    Kutish, G.4    Tulman, E.5    French, R.6    Sur, J.7    Rock, D.8    Borca, M.9
  • 132
    • 33846110885 scopus 로고    scopus 로고
    • N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine
    • Risatti G., Holinka L., Sainz I.F., Carrillo C., Lu Z., Borca M. N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine. J. Virol. 2007, 81(2):924-933.
    • (2007) J. Virol. , vol.81 , Issue.2 , pp. 924-933
    • Risatti, G.1    Holinka, L.2    Sainz, I.F.3    Carrillo, C.4    Lu, Z.5    Borca, M.6
  • 133
    • 24944492937 scopus 로고    scopus 로고
    • Npro of classical swine fever virus is an antagonist of double-stranded RNA-mediated apoptosis and IFN-α/β induction
    • Ruggli N., Bird B.H., Liu L., Bauhofer O., Tratschin J.-D., Hofmann M.A. Npro of classical swine fever virus is an antagonist of double-stranded RNA-mediated apoptosis and IFN-α/β induction. Virology 2005, 340(2):265-276.
    • (2005) Virology , vol.340 , Issue.2 , pp. 265-276
    • Ruggli, N.1    Bird, B.H.2    Liu, L.3    Bauhofer, O.4    Tratschin, J.-D.5    Hofmann, M.A.6
  • 134
    • 0038805518 scopus 로고    scopus 로고
    • Classical swine fever virus interferes with cellular antiviral defense: evidence for a novel function of Npro
    • Ruggli N., Tratschin J.-D., Schweizer M., McCullough K.C., Hofmann M.A., Summerfield A. Classical swine fever virus interferes with cellular antiviral defense: evidence for a novel function of Npro. J. Virol. 2003, 77(13):7645-7654.
    • (2003) J. Virol. , vol.77 , Issue.13 , pp. 7645-7654
    • Ruggli, N.1    Tratschin, J.-D.2    Schweizer, M.3    McCullough, K.C.4    Hofmann, M.A.5    Summerfield, A.6
  • 135
    • 36549074575 scopus 로고    scopus 로고
    • Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine
    • Sainz I.F., Holinka L.G., Lu Z., Risatti G.R., Borca M.V. Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine. Virology 2008, 370(1):122-129.
    • (2008) Virology , vol.370 , Issue.1 , pp. 122-129
    • Sainz, I.F.1    Holinka, L.G.2    Lu, Z.3    Risatti, G.R.4    Borca, M.V.5
  • 136
    • 0014521311 scopus 로고
    • Field experiments of hog cholera live vaccine prepared in guinea-pig kidney cell culture
    • Sasahara J., Kumagai T., Shimizu Y., Furuuchi S. Field experiments of hog cholera live vaccine prepared in guinea-pig kidney cell culture. Natl. Inst. Anim. Health Q. 1969, 9(2):83.
    • (1969) Natl. Inst. Anim. Health Q. , vol.9 , Issue.2 , pp. 83
    • Sasahara, J.1    Kumagai, T.2    Shimizu, Y.3    Furuuchi, S.4
  • 137
    • 36248953962 scopus 로고    scopus 로고
    • The Npro product of classical swine fever virus and bovine viral diarrhea virus uses a conserved mechanism to target interferon regulatory factor-3
    • Seago J., Hilton L., Reid E., Doceul V., Jeyatheesan J., Moganeradj K., McCauley J., Charleston B., Goodbourn S. The Npro product of classical swine fever virus and bovine viral diarrhea virus uses a conserved mechanism to target interferon regulatory factor-3. J. Gen. Virol. 2007, 88(11):3002-3006.
    • (2007) J. Gen. Virol. , vol.88 , Issue.11 , pp. 3002-3006
    • Seago, J.1    Hilton, L.2    Reid, E.3    Doceul, V.4    Jeyatheesan, J.5    Moganeradj, K.6    McCauley, J.7    Charleston, B.8    Goodbourn, S.9
  • 138
    • 0036140439 scopus 로고    scopus 로고
    • K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function
    • Sharp T.V., Wang H.-W., Koumi A., Hollyman D., Endo Y., Ye H., Du M.-Q., Boshoff C. K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function. J. Virol. 2002, 76(2):802-816.
    • (2002) J. Virol. , vol.76 , Issue.2 , pp. 802-816
    • Sharp, T.V.1    Wang, H.-W.2    Koumi, A.3    Hollyman, D.4    Endo, Y.5    Ye, H.6    Du, M.-Q.7    Boshoff, C.8
  • 139
    • 84904790808 scopus 로고    scopus 로고
    • Generation of a recombinant classical swine fever virus stably expressing the firefly luciferase gene for quantitative antiviral assay
    • Shen L., Li Y., Chen J., Li C., Huang J., Luo Y., Sun Y., Li S., Qiu H.-J. Generation of a recombinant classical swine fever virus stably expressing the firefly luciferase gene for quantitative antiviral assay. Antivir. Res. 2014, 109:15-21.
    • (2014) Antivir. Res. , vol.109 , pp. 15-21
    • Shen, L.1    Li, Y.2    Chen, J.3    Li, C.4    Huang, J.5    Luo, Y.6    Sun, Y.7    Li, S.8    Qiu, H.-J.9
  • 140
    • 84862796348 scopus 로고    scopus 로고
    • Classical swine fever virus NS5A protein interacts with 3'-untranslated region and regulates viral RNA synthesis
    • Sheng C., Chen Y., Xiao J., Xiao J., Wang J., Li G., Chen J., Xiao M. Classical swine fever virus NS5A protein interacts with 3'-untranslated region and regulates viral RNA synthesis. Virus Res. 2012, 163(2):636-643.
    • (2012) Virus Res. , vol.163 , Issue.2 , pp. 636-643
    • Sheng, C.1    Chen, Y.2    Xiao, J.3    Xiao, J.4    Wang, J.5    Li, G.6    Chen, J.7    Xiao, M.8
  • 141
    • 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., Gu F. Characterization of interaction of classical swine fever virus NS3 helicase with 3' untranslated region. Virus Res. 2007, 129(1):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
  • 142
    • 71549130396 scopus 로고    scopus 로고
    • Characterization of NS3, NS5A and NS5B of classical swine fever virus through mutation and complementation analysis
    • Sheng C., Zhu Z., Yu J., Wan L., Wang Y., Chen J., Gu F., Xiao M. Characterization of NS3, NS5A and NS5B of classical swine fever virus through mutation and complementation analysis. Vet. Microbiol. 2010, 140(1):72-80.
    • (2010) Vet. Microbiol. , vol.140 , Issue.1 , pp. 72-80
    • Sheng, C.1    Zhu, Z.2    Yu, J.3    Wan, L.4    Wang, Y.5    Chen, J.6    Gu, F.7    Xiao, M.8
  • 143
    • 0014864028 scopus 로고
    • A mutant of hog cholera virus inducing interference in swine testicle cell cultures
    • Shimizu Y., Furuuchi S., Kumagai T., Sasahara J. A mutant of hog cholera virus inducing interference in swine testicle cell cultures. Am. J. Vet. Res. 1970, 31:1787-1794.
    • (1970) Am. J. Vet. Res. , vol.31 , pp. 1787-1794
    • Shimizu, Y.1    Furuuchi, S.2    Kumagai, T.3    Sasahara, J.4
  • 144
    • 47949112577 scopus 로고    scopus 로고
    • SUMO mediates interaction of Ebp2p, the yeast homolog of Epstein-Barr virus nuclear antigen 1-binding protein 2, with a RING finger protein Ris1p
    • 0806060934
    • Shirai C., Mizuta K. SUMO mediates interaction of Ebp2p, the yeast homolog of Epstein-Barr virus nuclear antigen 1-binding protein 2, with a RING finger protein Ris1p. Biosci. Biotechnol. Biochem. 2008, 0806060934.
    • (2008) Biosci. Biotechnol. Biochem.
    • Shirai, C.1    Mizuta, K.2
  • 145
    • 0036298810 scopus 로고    scopus 로고
    • Dissecting virus entry via endocytosis
    • Sieczkarski S.B., Whittaker G.R. Dissecting virus entry via endocytosis. J. Gen. Virol. 2002, 83(7):1535-1545.
    • (2002) J. Gen. Virol. , vol.83 , Issue.7 , pp. 1535-1545
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 147
    • 84900555522 scopus 로고    scopus 로고
    • Npro of classical swine fever virus contributes to pathogenicity in pigs by preventing type I interferon induction at local replication sites
    • Tamura T., Nagashima N., Ruggli N., Summerfield A., Kida H., Sakoda Y. Npro of classical swine fever virus contributes to pathogenicity in pigs by preventing type I interferon induction at local replication sites. Vet. Res. 2014, 45:47.
    • (2014) Vet. Res. , vol.45 , pp. 47
    • Tamura, T.1    Nagashima, N.2    Ruggli, N.3    Summerfield, A.4    Kida, H.5    Sakoda, Y.6
  • 148
    • 84865076620 scopus 로고    scopus 로고
    • Selection of classical swine fever virus with enhanced pathogenicity reveals synergistic virulence determinants in E2 and NS4B
    • Tamura T., Sakoda Y., Yoshino F., Nomura T., Yamamoto N., Sato Y., Okamatsu M., Ruggli N., Kida H. Selection of classical swine fever virus with enhanced pathogenicity reveals synergistic virulence determinants in E2 and NS4B. J. Virol. 2012, 86(16):8602-8613.
    • (2012) J. Virol. , vol.86 , Issue.16 , pp. 8602-8613
    • Tamura, T.1    Sakoda, Y.2    Yoshino, F.3    Nomura, T.4    Yamamoto, N.5    Sato, Y.6    Okamatsu, M.7    Ruggli, N.8    Kida, H.9
  • 149
    • 79959733990 scopus 로고    scopus 로고
    • Classical swine fever virus NS2 protein promotes interleukin-8 expression and inhibits MG132-induced apoptosis
    • Tang Q., Guo K., Kang K., Zhang Y., He L., Wang J. Classical swine fever virus NS2 protein promotes interleukin-8 expression and inhibits MG132-induced apoptosis. Virus Genes 2011, 42(3):355-362.
    • (2011) Virus Genes , vol.42 , Issue.3 , pp. 355-362
    • Tang, Q.1    Guo, K.2    Kang, K.3    Zhang, Y.4    He, L.5    Wang, J.6
  • 150
    • 77649300652 scopus 로고    scopus 로고
    • Classic swine fever virus NS2 protein leads to the induction of cell cycle arrest at S-phase and endoplasmic reticulum stress
    • Tang Q., Zhang Y., Fan L., Tong G., He L., Dai C. Classic swine fever virus NS2 protein leads to the induction of cell cycle arrest at S-phase and endoplasmic reticulum stress. Virol. J. 2010, 7(4).
    • (2010) Virol. J. , vol.7 , Issue.4
    • Tang, Q.1    Zhang, Y.2    Fan, L.3    Tong, G.4    He, L.5    Dai, C.6
  • 152
    • 0030960350 scopus 로고    scopus 로고
    • Serine protease of pestiviruses: determination of cleavage sites
    • Tautz N., Elbers K., Stoll D., Meyers G., Thiel H. Serine protease of pestiviruses: determination of cleavage sites. J. Virol. 1997, 71(7):5415-5422.
    • (1997) J. Virol. , vol.71 , Issue.7 , pp. 5415-5422
    • Tautz, N.1    Elbers, K.2    Stoll, D.3    Meyers, G.4    Thiel, H.5
  • 153
    • 0034254958 scopus 로고    scopus 로고
    • NS3 serine protease of bovine viral diarrhea virus: characterization of active site residues, NS4A cofactor domain, and protease-cofactor interactions
    • Tautz N., Kaiser A., Thiel H.-J. NS3 serine protease of bovine viral diarrhea virus: characterization of active site residues, NS4A cofactor domain, and protease-cofactor interactions. Virology 2000, 273(2):351-363.
    • (2000) Virology , vol.273 , Issue.2 , pp. 351-363
    • Tautz, N.1    Kaiser, A.2    Thiel, H.-J.3
  • 154
    • 84899881668 scopus 로고
    • Progress of classical swine fever virus and the prevention of the disease (partII)
    • Tc Z. Progress of classical swine fever virus and the prevention of the disease (partII). Chin J Vet sci Technol 1980, 5:30-39.
    • (1980) Chin J Vet sci Technol , vol.5 , pp. 30-39
    • Tc, Z.1
  • 155
    • 84922823525 scopus 로고
    • Swine kidney cell culture, and its use in vaccine production
    • Google Patents.
    • Terpstra, C., 1992. Swine kidney cell culture, and its use in vaccine production. Google Patents.
    • (1992)
    • Terpstra, C.1
  • 156
    • 65349124093 scopus 로고    scopus 로고
    • Mutation of cysteine 171 of pestivirus Erns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus
    • Tews B.A., Schürmann E.-M., Meyers G. Mutation of cysteine 171 of pestivirus Erns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus. J. Virol. 2009, 83(10):4823-4834.
    • (2009) J. Virol. , vol.83 , Issue.10 , pp. 4823-4834
    • Tews, B.A.1    Schürmann, E.-M.2    Meyers, G.3
  • 157
    • 0025955758 scopus 로고
    • Hog cholera virus: molecular composition of virions from a pestivirus
    • Thiel H., Stark R., Weiland E., Rümenapf T., Meyers G. Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 1991, 65(9):4705-4712.
    • (1991) J. Virol. , vol.65 , Issue.9 , pp. 4705-4712
    • Thiel, H.1    Stark, R.2    Weiland, E.3    Rümenapf, T.4    Meyers, G.5
  • 158
    • 0031821664 scopus 로고    scopus 로고
    • Classical swine fever virus leader proteinase Npro is not required for viral replication in cell culture
    • Tratschin J.-D., Moser C., Ruggli N., Hofmann M.A. Classical swine fever virus leader proteinase Npro is not required for viral replication in cell culture. J. Virol. 1998, 72(9):7681-7684.
    • (1998) J. Virol. , vol.72 , Issue.9 , pp. 7681-7684
    • Tratschin, J.-D.1    Moser, C.2    Ruggli, N.3    Hofmann, M.A.4
  • 159
    • 0032979005 scopus 로고    scopus 로고
    • Recovery of infectious classical swine fever virus (CSFV) from full-length genomic cDNA clones by a swine kidney cell line expressing bacteriophage T7 RNA polymerase
    • Van Gennip H., Van Rijn P., Widjojoatmodjo M., Moormann R. Recovery of infectious classical swine fever virus (CSFV) from full-length genomic cDNA clones by a swine kidney cell line expressing bacteriophage T7 RNA polymerase. J. Virol. Methods 1999, 78(1):117-128.
    • (1999) J. Virol. Methods , vol.78 , Issue.1 , pp. 117-128
    • Van Gennip, H.1    Van Rijn, P.2    Widjojoatmodjo, M.3    Moormann, R.4
  • 160
    • 3543075655 scopus 로고    scopus 로고
    • Determinants of virulence of classical swine fever virus strain Brescia
    • Van Gennip H.G., Vlot A.C., Hulst M.M., De Smit A.J., Moormann R.J. Determinants of virulence of classical swine fever virus strain Brescia. J. Virol. 2004, 78(16):8812-8823.
    • (2004) J. Virol. , vol.78 , Issue.16 , pp. 8812-8823
    • Van Gennip, H.G.1    Vlot, A.C.2    Hulst, M.M.3    De Smit, A.J.4    Moormann, R.J.5
  • 161
    • 0034668183 scopus 로고    scopus 로고
    • Chimeric classical swine fever viruses containing envelope protein ERNS or E2 of bovine viral diarrhoea virus protect pigs against challenge with CSFV and induce a distinguishable antibody response
    • van Gennip H.G.P., van Rijn P.A., Widjojoatmodjo M.N., de Smit A.J., Moormann R.J.M. Chimeric classical swine fever viruses containing envelope protein ERNS or E2 of bovine viral diarrhoea virus protect pigs against challenge with CSFV and induce a distinguishable antibody response. Vaccine 2000, 19(4-5):447-459.
    • (2000) Vaccine , vol.19 , Issue.4-5 , pp. 447-459
    • van Gennip, H.G.P.1    van Rijn, P.A.2    Widjojoatmodjo, M.N.3    de Smit, A.J.4    Moormann, R.J.M.5
  • 162
    • 0242289456 scopus 로고    scopus 로고
    • Vaccinology of classical swine fever: from lab to field
    • Van Oirschot J. Vaccinology of classical swine fever: from lab to field. Vet. Microbiol. 2003, 96(4):367-384.
    • (2003) Vet. Microbiol. , vol.96 , Issue.4 , pp. 367-384
    • Van Oirschot, J.1
  • 163
    • 0028321652 scopus 로고
    • Antigenic structure of envelope glycoprotein E1 of hog cholera virus
    • Van Rijn P., Miedema G., Wensvoort G., Van Gennip H., Moormann R. Antigenic structure of envelope glycoprotein E1 of hog cholera virus. J. Virol. 1994, 68(6):3934-3942.
    • (1994) J. Virol. , vol.68 , Issue.6 , pp. 3934-3942
    • Van Rijn, P.1    Miedema, G.2    Wensvoort, G.3    Van Gennip, H.4    Moormann, R.5
  • 164
    • 0027486713 scopus 로고
    • Epitope mapping of envelope glycoprotein E1 of hog cholera virus strain Brescia
    • Van Rijn P., Van Gennip H., De Meijer E., Moormann R. Epitope mapping of envelope glycoprotein E1 of hog cholera virus strain Brescia. J. Gen. Virol. 1993, 74:2053-2060.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2053-2060
    • Van Rijn, P.1    Van Gennip, H.2    De Meijer, E.3    Moormann, R.4
  • 165
    • 35348839828 scopus 로고    scopus 로고
    • Immunity against NS3 protein of classical swine fever virus does not protect against lethal challenge infection
    • Voigt H., Wienhold D., Marquardt C., Muschko K., Pfaff E., Buettner M. Immunity against NS3 protein of classical swine fever virus does not protect against lethal challenge infection. Viral Immunol. 2007, 20(3):487-494.
    • (2007) Viral Immunol. , vol.20 , Issue.3 , pp. 487-494
    • Voigt, H.1    Wienhold, D.2    Marquardt, C.3    Muschko, K.4    Pfaff, E.5    Buettner, M.6
  • 168
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982, 1(8):945.
    • (1982) EMBO J. , vol.1 , Issue.8 , pp. 945
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 169
    • 75149124014 scopus 로고    scopus 로고
    • Classical swine fever virus NS3 enhances RNA-dependent RNA polymerase activity by binding to NS5B
    • Wang P., Wang Y., Zhao Y., Zhu Z., Yu J., Wan L., Chen J., Xiao M. Classical swine fever virus NS3 enhances RNA-dependent RNA polymerase activity by binding to NS5B. Virus Res. 2010, 148(1):17-23.
    • (2010) Virus Res. , vol.148 , Issue.1 , pp. 17-23
    • Wang, P.1    Wang, Y.2    Zhao, Y.3    Zhu, Z.4    Yu, J.5    Wan, L.6    Chen, J.7    Xiao, M.8
  • 170
    • 33846116117 scopus 로고    scopus 로고
    • Mutational analysis of the GDD sequence motif of classical swine fever virus RNA-dependent RNA polymerases
    • Wang Y., Xiao M., Chen J., Zhang W., Luo J., Bao K., Nie M., Chen J., Li B. Mutational analysis of the GDD sequence motif of classical swine fever virus RNA-dependent RNA polymerases. Virus Genes 2007, 34(1):63-65.
    • (2007) Virus Genes , vol.34 , Issue.1 , pp. 63-65
    • Wang, Y.1    Xiao, M.2    Chen, J.3    Zhang, W.4    Luo, J.5    Bao, K.6    Nie, M.7    Chen, J.8    Li, B.9
  • 171
    • 79951813025 scopus 로고    scopus 로고
    • Characterisation of interaction between NS3 and NS5B protein of classical swine fever virus by deletion of terminal sequences of NS5B
    • Wang Y., Zhu Z., Wang P., Yu J., Wan L., Chen J., Xiao M. Characterisation of interaction between NS3 and NS5B protein of classical swine fever virus by deletion of terminal sequences of NS5B. Virus Res. 2011, 156(1-2):98-106.
    • (2011) Virus Res. , vol.156 , Issue.1-2 , pp. 98-106
    • Wang, Y.1    Zhu, Z.2    Wang, P.3    Yu, J.4    Wan, L.5    Chen, J.6    Xiao, M.7
  • 172
    • 7444268500 scopus 로고    scopus 로고
    • Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry
    • Wang Z., Nie Y., Wang P., Ding M., Deng H. Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry. Virology 2004, 330(1):332-341.
    • (2004) Virology , vol.330 , Issue.1 , pp. 332-341
    • Wang, Z.1    Nie, Y.2    Wang, P.3    Ding, M.4    Deng, H.5
  • 174
    • 0026665695 scopus 로고
    • A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus
    • Weiland E., Ahl R., Stark R., Weiland F., Thiel H.-J. A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus. J. Virol. 1992, 66(6):3677-3682.
    • (1992) J. Virol. , vol.66 , Issue.6 , pp. 3677-3682
    • Weiland, E.1    Ahl, R.2    Stark, R.3    Weiland, F.4    Thiel, H.-J.5
  • 175
    • 0025307406 scopus 로고
    • Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer
    • Weiland E., Stark R., Haas B., Rümenapf T., Meyers G., Thiel H.-J. Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer. J. Virol. 1990, 64(8):3563-3569.
    • (1990) J. Virol. , vol.64 , Issue.8 , pp. 3563-3569
    • Weiland, E.1    Stark, R.2    Haas, B.3    Rümenapf, T.4    Meyers, G.5    Thiel, H.-J.6
  • 176
    • 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., Pan Z. Identification and characterization of the NTPase activity of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) expressed in bacteria. Arch. Virol. 2007, 152(8):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
  • 177
    • 61449241639 scopus 로고    scopus 로고
    • Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase
    • Wen G., Xue J., Shen Y., Zhang C., Pan Z. Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase. Virus Res. 2009, 141(1):63-70.
    • (2009) Virus Res. , vol.141 , Issue.1 , pp. 63-70
    • Wen, G.1    Xue, J.2    Shen, Y.3    Zhang, C.4    Pan, Z.5
  • 178
    • 0025306126 scopus 로고
    • Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus
    • Wensvoort G., Boonstra J., Bodzinga B. Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus. J. Gen. Virol. 1990, 71(3):531-540.
    • (1990) J. Gen. Virol. , vol.71 , Issue.3 , pp. 531-540
    • Wensvoort, G.1    Boonstra, J.2    Bodzinga, B.3
  • 179
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong J., Zhang J., Si X., Gao G., Mao I., McManus B.M., Luo H. Autophagosome supports coxsackievirus B3 replication in host cells. J. Virol. 2008, 82(18):9143-9153.
    • (2008) J. Virol. , vol.82 , Issue.18 , pp. 9143-9153
    • Wong, J.1    Zhang, J.2    Si, X.3    Gao, G.4    Mao, I.5    McManus, B.M.6    Luo, H.7
  • 180
    • 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., 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. 2008, 89(4):994-999.
    • (2008) J. Gen. Virol. , vol.89 , Issue.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
  • 181
    • 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., Li B. Specific interaction between the classical swine fever virus NS5B protein and the viral genome. Eur. J. Biochem. 2004, 271(19):3888-3896.
    • (2004) Eur. J. Biochem. , vol.271 , Issue.19 , pp. 3888-3896
    • Xiao, M.1    Gao, J.2    Wang, W.3    Wang, Y.4    Chen, J.5    Chen, J.6    Li, B.7
  • 182
    • 31644445842 scopus 로고    scopus 로고
    • Characterization of the N-terminal domain of classical swine fever virus RNA-dependent RNA polymerase
    • Xiao M., Li H., Wang Y., Wang X., Wang W., Peng J., Chen J., Li B. Characterization of the N-terminal domain of classical swine fever virus RNA-dependent RNA polymerase. J. Gen. Virol. 2006, 87(2):347-356.
    • (2006) J. Gen. Virol. , vol.87 , Issue.2 , 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
  • 183
    • 70849111059 scopus 로고    scopus 로고
    • Influence of NS5A protein of classical swine fever virus (CSFV) on CSFV internal ribosome entry site-dependent translation
    • Xiao M., Wang Y., Zhu Z., Yu J., Wan L., Chen J. Influence of NS5A protein of classical swine fever virus (CSFV) on CSFV internal ribosome entry site-dependent translation. J. Gen. Virol. 2009, 90(12):2923-2928.
    • (2009) J. Gen. Virol. , vol.90 , Issue.12 , pp. 2923-2928
    • Xiao, M.1    Wang, Y.2    Zhu, Z.3    Yu, J.4    Wan, L.5    Chen, J.6
  • 184
    • 0036375705 scopus 로고    scopus 로고
    • Classical swine fever virus NS5B-GFP fusion protein possesses an RNA-dependent RNA polymerase activity
    • Xiao M., Zhang C., Pan Z., Wu H., Guo J. Classical swine fever virus NS5B-GFP fusion protein possesses an RNA-dependent RNA polymerase activity. Arch. Virol. 2002, 147(9):1779-1787.
    • (2002) Arch. Virol. , vol.147 , Issue.9 , pp. 1779-1787
    • Xiao, M.1    Zhang, C.2    Pan, Z.3    Wu, H.4    Guo, J.5
  • 185
    • 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., 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. 1997, 71(7):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
  • 186
    • 33748944822 scopus 로고    scopus 로고
    • HCV NS2 protein inhibits cell proliferation and induces cell cycle arrest in the S-phase in mammalian cells through down-regulation of cyclin A expression
    • Yang X.-J., Liu J., Ye L., Liao Q.-J., Wu J.-G., Gao J.-R., She Y.-L., Wu Z.-H., Ye L.-B. HCV NS2 protein inhibits cell proliferation and induces cell cycle arrest in the S-phase in mammalian cells through down-regulation of cyclin A expression. Virus Res. 2006, 121(2):134-143.
    • (2006) Virus Res. , vol.121 , Issue.2 , pp. 134-143
    • Yang, X.-J.1    Liu, J.2    Ye, L.3    Liao, Q.-J.4    Wu, J.-G.5    Gao, J.-R.6    She, Y.-L.7    Wu, Z.-H.8    Ye, L.-B.9
  • 187
    • 84904286525 scopus 로고    scopus 로고
    • Specific ligands for classical swine fever virus screened from landscape phage display library
    • Yin L., Luo Y., Liang B., Wang F., Du M., Petrenko V.A., Qiu H.-J., Liu A. Specific ligands for classical swine fever virus screened from landscape phage display library. Antivir. Res. 2014, 109:68-71.
    • (2014) Antivir. Res. , vol.109 , pp. 68-71
    • Yin, L.1    Luo, Y.2    Liang, B.3    Wang, F.4    Du, M.5    Petrenko, V.A.6    Qiu, H.-J.7    Liu, A.8
  • 188
    • 33645966803 scopus 로고    scopus 로고
    • Interaction of Moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection
    • Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-y., Goff S.P. Interaction of Moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection. J. Virol. 2006, 80(1):342-352.
    • (2006) J. Virol. , vol.80 , Issue.1 , pp. 342-352
    • Yueh, A.1    Leung, J.2    Bhattacharyya, S.3    Perrone, L.A.4    de Los Santos, K.5    Pu, S.-Y.6    Goff, S.P.7
  • 189
    • 0002939223 scopus 로고
    • Progress of classical swine fever virus and the prevention of the disease (partI)
    • Zhou T. Progress of classical swine fever virus and the prevention of the disease (partI). Chin. J. Vet. Sci. Technol. 1980, 4:23-33.
    • (1980) Chin. J. Vet. Sci. Technol. , vol.4 , pp. 23-33
    • Zhou, T.1
  • 190
    • 79951812451 scopus 로고    scopus 로고
    • Human MxA protein inhibits the replication of classical swine fever virus
    • Zhao Y., Pang D., Wang T., Yang X., Wu R., Ren L., Yuan T., Huang Y., Ouyang H. Human MxA protein inhibits the replication of classical swine fever virus. Virus Res. 2011, 156(1-2):151-155.
    • (2011) Virus Res. , vol.156 , Issue.1-2 , pp. 151-155
    • Zhao, Y.1    Pang, D.2    Wang, T.3    Yang, X.4    Wu, R.5    Ren, L.6    Yuan, T.7    Huang, Y.8    Ouyang, H.9
  • 191
    • 33847613290 scopus 로고    scopus 로고
    • Effective inhibition of porcine transmissible gastroenteritis virus replication in ST cells by shRNAs targeting RNA-dependent RNA polymerase gene
    • Zhou J.-f., Hua X.-g., Cui L., Zhu J.-g., Miao D.-n., Zou Y., He X.-z., Su W.-g. Effective inhibition of porcine transmissible gastroenteritis virus replication in ST cells by shRNAs targeting RNA-dependent RNA polymerase gene. Antivir. Res. 2007, 74(1):36-42.
    • (2007) Antivir. Res. , vol.74 , Issue.1 , pp. 36-42
    • Zhou, J.-F.1    Hua, X.-G.2    Cui, L.3    Zhu, J.-G.4    Miao, D.-N.5    Zou, Y.6    He, X.-Z.7    Su, W.-G.8
  • 193
    • 77956232456 scopus 로고    scopus 로고
    • Classical swine fever virus NS3 is an IRES-binding protein and increases IRES-dependent translation
    • Zhu Z., Wang Y., Yu J., Wan L., Chen J., Xiao M. Classical swine fever virus NS3 is an IRES-binding protein and increases IRES-dependent translation. Virus Res. 2010, 153(1):106-112.
    • (2010) Virus Res. , vol.153 , Issue.1 , pp. 106-112
    • Zhu, Z.1    Wang, Y.2    Yu, J.3    Wan, L.4    Chen, J.5    Xiao, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.