메뉴 건너뛰기




Volumn 405, Issue 2, 2010, Pages 448-456

Frog virus 3 ORF 53R, a putative myristoylated membrane protein, is essential for virus replication in vitro

Author keywords

Antisense morpholino oligonucleotides; Frog virus 3; Immunofluorescence assay; Iridovirus; Myristoylated viral protein; Ranavirus; Transmission electron microscopy; Viral membrane protein; Virion assembly

Indexed keywords

53R PROTEIN; ANTISENSE OLIGONUCLEOTIDE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 77955653739     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.06.034     Document Type: Article
Times cited : (42)

References (59)
  • 2
    • 1842292789 scopus 로고    scopus 로고
    • Assembly of African swine fever virus: role of polyprotein pp 220
    • Andrés G., Simón-Mateo C., Viñuela E. Assembly of African swine fever virus: role of polyprotein pp 220. J. Virol. 1997, 71(3):2331-2334.
    • (1997) J. Virol. , vol.71 , Issue.3 , pp. 2331-2334
    • Andrés, G.1    Simón-Mateo, C.2    Viñuela, E.3
  • 3
    • 0036187961 scopus 로고    scopus 로고
    • Repression of African swine fever virus polyprotein pp 220-encoding gene leads to the assembly of icosahedral core-less particles
    • Andrés G., García-Escudero R., Salas M.L., Rodríguez J.M. Repression of African swine fever virus polyprotein pp 220-encoding gene leads to the assembly of icosahedral core-less particles. J. Virol. 2002, 76(6):2654-2666.
    • (2002) J. Virol. , vol.76 , Issue.6 , pp. 2654-2666
    • Andrés, G.1    García-Escudero, R.2    Salas, M.L.3    Rodríguez, J.M.4
  • 4
    • 0036891835 scopus 로고    scopus 로고
    • African swine fever virus polyproteins pp 220 and pp62 assemble into the core shell
    • Andrés G., Alejo A., Salas J., Salas M.L. African swine fever virus polyproteins pp 220 and pp62 assemble into the core shell. J. Virol. 2002, 76(24):12473-12482.
    • (2002) J. Virol. , vol.76 , Issue.24 , pp. 12473-12482
    • Andrés, G.1    Alejo, A.2    Salas, J.3    Salas, M.L.4
  • 7
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M., Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. PNAS 1990, 87:523-527.
    • (1990) PNAS , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 8
    • 34548170431 scopus 로고    scopus 로고
    • Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains
    • Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J., de la Torre J.C. Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains. J. Virol. 2007, 81:9451-9460.
    • (2007) J. Virol. , vol.81 , pp. 9451-9460
    • Capul, A.A.1    Perez, M.2    Burke, E.3    Kunz, S.4    Buchmeier, M.J.5    de la Torre, J.C.6
  • 9
    • 0036776328 scopus 로고    scopus 로고
    • Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption
    • Chandran K., Farsetta D.L., Nibert M.L. Strategy for nonenveloped virus entry: a hydrophobic conformer of the reovirus membrane penetration protein μ1 mediates membrane disruption. J. Virol. 2002, 76(19):9920-9933.
    • (2002) J. Virol. , vol.76 , Issue.19 , pp. 9920-9933
    • Chandran, K.1    Farsetta, D.L.2    Nibert, M.L.3
  • 10
    • 0036008606 scopus 로고    scopus 로고
    • Ranaviruses (family Iridoviridae): emerging cold-blooded killers
    • Chinchar V.G. Ranaviruses (family Iridoviridae): emerging cold-blooded killers. Arch. Virol. 2002, 147:447-470.
    • (2002) Arch. Virol. , vol.147 , pp. 447-470
    • Chinchar, V.G.1
  • 11
    • 0022512001 scopus 로고
    • Temperature-sensitive mutants of frog virus 3: biochemical and genetic characterization
    • Chinchar V.G., Granoff A. Temperature-sensitive mutants of frog virus 3: biochemical and genetic characterization. J. Virol. 1986, 58:192-202.
    • (1986) J. Virol. , vol.58 , pp. 192-202
    • Chinchar, V.G.1    Granoff, A.2
  • 12
    • 0021276175 scopus 로고
    • Early proteins are required for the formation of frog virus 3 assembly sites
    • Chinchar V.G., Goorha R., Granoff A. Early proteins are required for the formation of frog virus 3 assembly sites. Virology 1984, 135:148-156.
    • (1984) Virology , vol.135 , pp. 148-156
    • Chinchar, V.G.1    Goorha, R.2    Granoff, A.3
  • 13
    • 0021125705 scopus 로고
    • Localization of frog virus 3 proteins using monoclonal antibodies
    • Chinchar V.G., Granoff A., Goorha R. Localization of frog virus 3 proteins using monoclonal antibodies. Virology 1984, 137:211-216.
    • (1984) Virology , vol.137 , pp. 211-216
    • Chinchar, V.G.1    Granoff, A.2    Goorha, R.3
  • 16
    • 0023198719 scopus 로고
    • Myristoylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M., Newman J.F., Filman D., Hogle J.M., Rowlands D.J., Brown F. Myristoylation of picornavirus capsid protein VP4 and its structural significance. Nature 1987, 327:482-486.
    • (1987) Nature , vol.327 , pp. 482-486
    • Chow, M.1    Newman, J.F.2    Filman, D.3    Hogle, J.M.4    Rowlands, D.J.5    Brown, F.6
  • 17
    • 0029861189 scopus 로고    scopus 로고
    • Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus
    • Cobbold C., Whittle J.T., Wileman T. Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus. J. Virol. 1996, 70(12):8382-8390.
    • (1996) J. Virol. , vol.70 , Issue.12 , pp. 8382-8390
    • Cobbold, C.1    Whittle, J.T.2    Wileman, T.3
  • 18
    • 38149045135 scopus 로고    scopus 로고
    • Inhibition of red seabream iridovirus (RSIV) replication by small interfering RNA (siRNA) in a cell culture system
    • Dang L.T., Kondo H., Hirono I., Aoki T. Inhibition of red seabream iridovirus (RSIV) replication by small interfering RNA (siRNA) in a cell culture system. Antivir. Res. 2008, 77(2):142-149.
    • (2008) Antivir. Res. , vol.77 , Issue.2 , pp. 142-149
    • Dang, L.T.1    Kondo, H.2    Hirono, I.3    Aoki, T.4
  • 19
    • 33846848887 scopus 로고    scopus 로고
    • Comparative genomic analysis of the family Iridoviridae: re-annotating and defining the core set of iridovirus genes
    • Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R. Comparative genomic analysis of the family Iridoviridae: re-annotating and defining the core set of iridovirus genes. J. Virol. 2007, 4:11.
    • (2007) J. Virol. , vol.4 , pp. 11
    • Eaton, H.E.1    Metcalf, J.2    Penny, E.3    Tcherepanov, V.4    Upton, C.5    Brunetti, C.R.6
  • 20
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi T.A., Waksman G., Gordon J.I. The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 2001, 276(43):39501-39504.
    • (2001) J. Biol. Chem. , vol.276 , Issue.43 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 21
    • 33947382159 scopus 로고    scopus 로고
    • The consensus N-myristoylation motif of a geminivirus AC4 protein is required for membrane binding and pathogenicity
    • Fondong V.N., Reddy R.V., Lu C., Hankoua B., Felton C., Czymmek K., Achenjang F. The consensus N-myristoylation motif of a geminivirus AC4 protein is required for membrane binding and pathogenicity. Mol. Plant-Microbe Interact. 2007, 20(4):380-391.
    • (2007) Mol. Plant-Microbe Interact. , vol.20 , Issue.4 , pp. 380-391
    • Fondong, V.N.1    Reddy, R.V.2    Lu, C.3    Hankoua, B.4    Felton, C.5    Czymmek, K.6    Achenjang, F.7
  • 22
    • 70350312842 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus assembly: processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner
    • Goodwin S., Tuthill T.J., Arias A., Killington R.A., Rowlands D.J. Foot-and-mouth disease virus assembly: processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner. J. Virol. 2009, 83(21):11275-11282.
    • (2009) J. Virol. , vol.83 , Issue.21 , pp. 11275-11282
    • Goodwin, S.1    Tuthill, T.J.2    Arias, A.3    Killington, R.A.4    Rowlands, D.J.5
  • 23
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Göttlinger H.G., Sodroski J.G., Haseltine W.A. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. PNAS 1989, 86:5781-5785.
    • (1989) PNAS , vol.86 , pp. 5781-5785
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 24
    • 0013908835 scopus 로고
    • Viruses and renal carcinoma of Rana pipiens: the isolation and properties of virus from normal and tumor tissue
    • Granoff A., Came P.E., Breeze D.C. Viruses and renal carcinoma of Rana pipiens: the isolation and properties of virus from normal and tumor tissue. Virology 1966, 29:133-148.
    • (1966) Virology , vol.29 , pp. 133-148
    • Granoff, A.1    Came, P.E.2    Breeze, D.C.3
  • 25
    • 0036411698 scopus 로고    scopus 로고
    • Epizootiology of sixty-four amphibian morbidity and mortality events in the USA 1996-2001
    • Green D., Converse K., Schrader A. Epizootiology of sixty-four amphibian morbidity and mortality events in the USA 1996-2001. Ann. NY Acad. Sci. 2002, 969:323-339.
    • (2002) Ann. NY Acad. Sci. , vol.969 , pp. 323-339
    • Green, D.1    Converse, K.2    Schrader, A.3
  • 26
    • 0027272237 scopus 로고
    • Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation
    • Harper D.R., Gilbert R.L., Blunt C., McIlhinney R.A. Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation. J. Gen. Virol. 1993, 74(Pt 6):1181-1184.
    • (1993) J. Gen. Virol. , vol.74 , Issue.PT 6 , pp. 1181-1184
    • Harper, D.R.1    Gilbert, R.L.2    Blunt, C.3    McIlhinney, R.A.4
  • 27
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath C.M., Windsor M., Wileman T. Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 2001, 153:449-455.
    • (2001) J. Cell Biol. , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 29
    • 33645076499 scopus 로고    scopus 로고
    • Evolutionary genomics of nucleo-cytoplasmic large DNA viruses
    • Iyer L.M., Balaji S., Koonin E.V., Aravind L. Evolutionary genomics of nucleo-cytoplasmic large DNA viruses. Virus Res. 2006, 117:156-184.
    • (2006) Virus Res. , vol.117 , pp. 156-184
    • Iyer, L.M.1    Balaji, S.2    Koonin, E.V.3    Aravind, L.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970, 227:251-254.
    • (1970) Nature , vol.227 , pp. 251-254
    • Laemmli, U.K.1
  • 31
    • 0025082005 scopus 로고
    • Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles
    • Marc D., Masson M., Girard M., van der Werf S. Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles. J. Virol. 1990, 64:4099-4107.
    • (1990) J. Virol. , vol.64 , pp. 4099-4107
    • Marc, D.1    Masson, M.2    Girard, M.3    van der Werf, S.4
  • 32
    • 0025806070 scopus 로고
    • A Gly to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly
    • Marc D., Girard M., van der Werf S. A Gly to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly. J. Gen. Virol. 1991, 72:1151-1157.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1151-1157
    • Marc, D.1    Girard, M.2    van der Werf, S.3
  • 33
    • 0030910253 scopus 로고    scopus 로고
    • Identification and analysis of three myristylated vaccinia virus late proteins
    • Martin K.H., Grosenbach D.W., Franke C.A., Hruby D.E. Identification and analysis of three myristylated vaccinia virus late proteins. J. Virol. 1997, 71(7):5218-5226.
    • (1997) J. Virol. , vol.71 , Issue.7 , pp. 5218-5226
    • Martin, K.H.1    Grosenbach, D.W.2    Franke, C.A.3    Hruby, D.E.4
  • 34
    • 0032972234 scopus 로고    scopus 로고
    • Novel acylation of poxvirus A type inclusion proteins
    • Martin K.H., Franke C.A., Hruby D.E. Novel acylation of poxvirus A type inclusion proteins. Virus Res. 1999, 60:147-157.
    • (1999) Virus Res. , vol.60 , pp. 147-157
    • Martin, K.H.1    Franke, C.A.2    Hruby, D.E.3
  • 35
    • 0036295384 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Refinement of the sequence motif and its taxon-specific differences
    • Maurer-Stroh S., Eisenhaber B., Eisenhaber F. N-terminal N-myristoylation of proteins: Refinement of the sequence motif and its taxon-specific differences. J. Mol. Biol. 2002, 317:523-540.
    • (2002) J. Mol. Biol. , vol.317 , pp. 523-540
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 37
    • 0024386622 scopus 로고
    • Synthesis of FV3 proteins occurs on intermediate filament-bound polyribosomes
    • Murti K.G., Goorha R. Synthesis of FV3 proteins occurs on intermediate filament-bound polyribosomes. Biol. Cell 1989, 65:205-214.
    • (1989) Biol. Cell , vol.65 , pp. 205-214
    • Murti, K.G.1    Goorha, R.2
  • 38
    • 0022283062 scopus 로고
    • Interaction of frog virus 3 with the cytomatrix: III. Role of microfilaments in virus release
    • Murti K.G., Chen M., Goorha R. Interaction of frog virus 3 with the cytomatrix: III. Role of microfilaments in virus release. Virology 1985, 142(2):317-325.
    • (1985) Virology , vol.142 , Issue.2 , pp. 317-325
    • Murti, K.G.1    Chen, M.2    Goorha, R.3
  • 40
    • 0032283290 scopus 로고    scopus 로고
    • Viral diseases in cultured marine fish in Japan
    • Nakajima K., Inouye K., Sorimachi M. Viral diseases in cultured marine fish in Japan. Fish Pathol. 1998, 33:181-188.
    • (1998) Fish Pathol. , vol.33 , pp. 181-188
    • Nakajima, K.1    Inouye, K.2    Sorimachi, M.3
  • 41
    • 4644243004 scopus 로고    scopus 로고
    • Myristoylation of the RING finger Z protein is essential for arenavirus budding
    • Perez M., Greenwald D.L., de la Torre J.C. Myristoylation of the RING finger Z protein is essential for arenavirus budding. J. Virol. 2004, 78(20):11443-11448.
    • (2004) J. Virol. , vol.78 , Issue.20 , pp. 11443-11448
    • Perez, M.1    Greenwald, D.L.2    de la Torre, J.C.3
  • 42
    • 0028227884 scopus 로고
    • Characterization of the vaccinia virus L1R myristylprotein as a component of the intracellular virion envelope
    • Ravanello M.P., Hruby D.E. Characterization of the vaccinia virus L1R myristylprotein as a component of the intracellular virion envelope. J. Gen. Virol. 1994, 75(Pt 6):1479-1483.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PT 6 , pp. 1479-1483
    • Ravanello, M.P.1    Hruby, D.E.2
  • 43
    • 0027968128 scopus 로고
    • Conditional lethal expression of the vaccinia virus L1R myristylated protein reveals a role in virion assembly
    • Ravanello M.P., Hruby D.E. Conditional lethal expression of the vaccinia virus L1R myristylated protein reveals a role in virion assembly. J. Virol. 1994, 68(10):6401-6410.
    • (1994) J. Virol. , vol.68 , Issue.10 , pp. 6401-6410
    • Ravanello, M.P.1    Hruby, D.E.2
  • 44
    • 0027340008 scopus 로고
    • An NH2-terminal peptide from the vaccinia virus L1R protein directs the myristoylation and virion envelope localization of a heterologous fusion protein
    • Ravanello M.P., Franke C.A., Hruby D.E. An NH2-terminal peptide from the vaccinia virus L1R protein directs the myristoylation and virion envelope localization of a heterologous fusion protein. J. Biol. Chem. 1993, 268(10):7585-7593.
    • (1993) J. Biol. Chem. , vol.268 , Issue.10 , pp. 7585-7593
    • Ravanello, M.P.1    Franke, C.A.2    Hruby, D.E.3
  • 45
    • 12144288809 scopus 로고    scopus 로고
    • African swine fever virus structural protein p54 is essential for the recruitment of envelope precursors to assembly sites
    • Rodriguez J.M., Garcia-Escudero R., Salas M.L., Andres G. African swine fever virus structural protein p54 is essential for the recruitment of envelope precursors to assembly sites. J. Virol. 2004, 78:4299-4313.
    • (2004) J. Virol. , vol.78 , pp. 4299-4313
    • Rodriguez, J.M.1    Garcia-Escudero, R.2    Salas, M.L.3    Andres, G.4
  • 46
    • 33645239489 scopus 로고    scopus 로고
    • African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase
    • Rodríguez I., Redrejo-Rodríguez M., Rodríguez J.M., Alejo A., Salas J., Salas M.L. African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase. J. Virol. 2006, 80(7):3157-3166.
    • (2006) J. Virol. , vol.80 , Issue.7 , pp. 3157-3166
    • Rodríguez, I.1    Redrejo-Rodríguez, M.2    Rodríguez, J.M.3    Alejo, A.4    Salas, J.5    Salas, M.L.6
  • 47
    • 70450170092 scopus 로고    scopus 로고
    • The African swine fever virus virion membrane protein pE248R is required for virus infectivity and an early postentry event
    • Rodríguez I., Nogal M.L., Redrejo-Rodríguez M., Bustos M.J., Salas M.L. The African swine fever virus virion membrane protein pE248R is required for virus infectivity and an early postentry event. J. Virol. 2009, 83(23):12290-12300.
    • (2009) J. Virol. , vol.83 , Issue.23 , pp. 12290-12300
    • Rodríguez, I.1    Nogal, M.L.2    Redrejo-Rodríguez, M.3    Bustos, M.J.4    Salas, M.L.5
  • 48
    • 0031937630 scopus 로고    scopus 로고
    • African swine fever virus is wrapped by the endoplasmic reticulum
    • Rouiller I., Brookes S.M., Hyatt A.D., Windsor M., Wileman T. African swine fever virus is wrapped by the endoplasmic reticulum. J. Virol. 1998, 72(3):2373-2387.
    • (1998) J. Virol. , vol.72 , Issue.3 , pp. 2373-2387
    • Rouiller, I.1    Brookes, S.M.2    Hyatt, A.D.3    Windsor, M.4    Wileman, T.5
  • 49
    • 33846343155 scopus 로고    scopus 로고
    • Inhibition of protein synthesis and viral replication by antisense morpholino oligonucleotides targeted to the major capsid protein, 18kDa immediate-early protein, and viral homolog of RNA polymerase II
    • Sample R.C., Bryan L., Long S., Majji S., Hoskins G., Sinning A., Chinchar V.G. Inhibition of protein synthesis and viral replication by antisense morpholino oligonucleotides targeted to the major capsid protein, 18kDa immediate-early protein, and viral homolog of RNA polymerase II. Virology 2007, 358:311-320.
    • (2007) Virology , vol.358 , pp. 311-320
    • Sample, R.C.1    Bryan, L.2    Long, S.3    Majji, S.4    Hoskins, G.5    Sinning, A.6    Chinchar, V.G.7
  • 50
    • 72849132036 scopus 로고    scopus 로고
    • African swine fever virus polyprotein pp 62 is essential for viral core development
    • Suárez C., Salas M.L., Rodríguez J.M. African swine fever virus polyprotein pp 62 is essential for viral core development. J. Virol. 2010, 84(1):176-178.
    • (2010) J. Virol. , vol.84 , Issue.1 , pp. 176-178
    • Suárez, C.1    Salas, M.L.2    Rodríguez, J.M.3
  • 51
    • 2542454676 scopus 로고    scopus 로고
    • Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae)
    • Tan W., Barkman T.J., Chinchar V.G., Essani K. Comparative genomic analyses of frog virus 3, type species of the genus Ranavirus (family Iridoviridae). Virology 2004, 323:70-84.
    • (2004) Virology , vol.323 , pp. 70-84
    • Tan, W.1    Barkman, T.J.2    Chinchar, V.G.3    Essani, K.4
  • 52
    • 0017657487 scopus 로고
    • Frog virus 3 morphogenesis: effect of temperature and metabolic inhibitors
    • Tripier F., Braunwald J., Markovic L., Kirn A. Frog virus 3 morphogenesis: effect of temperature and metabolic inhibitors. J. Gen. Virol. 1977, 37(1):39-52.
    • (1977) J. Gen. Virol. , vol.37 , Issue.1 , pp. 39-52
    • Tripier, F.1    Braunwald, J.2    Markovic, L.3    Kirn, A.4
  • 54
    • 0030098837 scopus 로고    scopus 로고
    • Spread of epizootic haematopoietic necrosis virus (EHNV) infection in redfin perch (Perca fluviatilis) in southern Australia
    • Whittington R., Kearns C., Hyatt A., Hengstberger S., Rutzou T. Spread of epizootic haematopoietic necrosis virus (EHNV) infection in redfin perch (Perca fluviatilis) in southern Australia. Aust. Vet. J. 1996, 73:112-114.
    • (1996) Aust. Vet. J. , vol.73 , pp. 112-114
    • Whittington, R.1    Kearns, C.2    Hyatt, A.3    Hengstberger, S.4    Rutzou, T.5
  • 57
    • 20644438444 scopus 로고    scopus 로고
    • Inhibition of reporter gene and Iridovirus-tiger frog virus in fish cell by RNA interference
    • Xie J., Lü L., Deng M., Weng S., Zhu J., Wu Y., Gan L., Chan S.M., He J. Inhibition of reporter gene and Iridovirus-tiger frog virus in fish cell by RNA interference. Virology 2005, 338:43-52.
    • (2005) Virology , vol.338 , pp. 43-52
    • Xie, J.1    Lü, L.2    Deng, M.3    Weng, S.4    Zhu, J.5    Wu, Y.6    Gan, L.7    Chan, S.M.8    He, J.9
  • 58
    • 0035923976 scopus 로고    scopus 로고
    • Characterization of an iridovirus from the cultured pig frog Rana grylio with lethal syndrome
    • Zhang Q.Y., Xiao F., Li Z.Q., Gui J.F., Mao J.H., Chinchar V.G. Characterization of an iridovirus from the cultured pig frog Rana grylio with lethal syndrome. Dis. Aquat. Org. 2001, 48:27-36.
    • (2001) Dis. Aquat. Org. , vol.48 , pp. 27-36
    • Zhang, Q.Y.1    Xiao, F.2    Li, Z.Q.3    Gui, J.F.4    Mao, J.H.5    Chinchar, V.G.6
  • 59
    • 50549093958 scopus 로고    scopus 로고
    • Identification and characterization of a novel envelope protein in Rana grylio virus
    • Zhao Z., Ke F., Huang Y., Zhao J., Gui J., Zhang Q. Identification and characterization of a novel envelope protein in Rana grylio virus. J. Gen. Virol. 2008, 89:1866-1872.
    • (2008) J. Gen. Virol. , vol.89 , pp. 1866-1872
    • Zhao, Z.1    Ke, F.2    Huang, Y.3    Zhao, J.4    Gui, J.5    Zhang, Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.