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Volumn 91, Issue 1, 2003, Pages 9-32

Molecular basis of pathogenesis of FMDV

Author keywords

Attenuation; Foot and mouth disease; Interferon; Pathogenesis; Picornavirus; Receptors; Virulence

Indexed keywords

PROTEINASE; VIRUS PROTEIN;

EID: 0037232731     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1702(02)00257-5     Document Type: Review
Times cited : (269)

References (324)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F. The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution. Nature. 337:1989;709-716.
    • (1989) Nature , vol.337 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 2
    • 0017201565 scopus 로고
    • Assay of bovine interferons in cultures of the porcine cell line IB-RS-2
    • Ahl R., Rump A. Assay of bovine interferons in cultures of the porcine cell line IB-RS-2. Infect. Immun. 14:1976;603-606.
    • (1976) Infect. Immun. , vol.14 , pp. 603-606
    • Ahl, R.1    Rump, A.2
  • 3
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire M., Chernaia M.M., Malcolm B.A., James M.N. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature. 369:1994;72-76.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.4
  • 4
    • 0031835331 scopus 로고    scopus 로고
    • Construction and evaluation of an attenuated vaccine for foot-and-mouth disease: Difficulty adapting the leader proteinase-deleted strategy to the serotype O1 virus
    • Almeida M.R., Rieder E., Chinsangaram J., Ward G., Beard C., Grubman M.J., Mason P.W. Construction and evaluation of an attenuated vaccine for foot-and-mouth disease: difficulty adapting the leader proteinase-deleted strategy to the serotype O1 virus. Virus Res. 55:1998;49-60.
    • (1998) Virus Res. , vol.55 , pp. 49-60
    • Almeida, M.R.1    Rieder, E.2    Chinsangaram, J.3    Ward, G.4    Beard, C.5    Grubman, M.J.6    Mason, P.W.7
  • 5
    • 0025049209 scopus 로고
    • A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA
    • Andino R., Rieckhof G.E., Baltimore D. A functional ribonucleoprotein complex forms around the 5′ end of poliovirus RNA. Cell. 63:1990;369-380.
    • (1990) Cell , vol.63 , pp. 369-380
    • Andino, R.1    Rieckhof, G.E.2    Baltimore, D.3
  • 6
    • 0027170180 scopus 로고
    • Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA
    • Andino R., Rieckhof G.E., Achacoso P.L., Baltimore D. Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12:1993;3587-3598.
    • (1993) EMBO J. , vol.12 , pp. 3587-3598
    • Andino, R.1    Rieckhof, G.E.2    Achacoso, P.L.3    Baltimore, D.4
  • 7
    • 0026633957 scopus 로고
    • Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles
    • Ansardi D.C., Porter D.C., Morrow C.D. Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles. J. Virol. 66:1992;4556-4563.
    • (1992) J. Virol. , vol.66 , pp. 4556-4563
    • Ansardi, D.C.1    Porter, D.C.2    Morrow, C.D.3
  • 9
    • 0021770918 scopus 로고
    • Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families
    • Argos P., Kamer G., Nicklin M.J., Wimmer E. Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families. Nucleic Acids Res. 12:1984;7251-7267.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7251-7267
    • Argos, P.1    Kamer, G.2    Nicklin, M.J.3    Wimmer, E.4
  • 11
    • 0027362461 scopus 로고
    • Characterization of the foot-and-mouth disease virus 3C protease expressed in Escherichia coli
    • Bablanian G.M., Grubman M.J. Characterization of the foot-and-mouth disease virus 3C protease expressed in Escherichia coli. Virology. 197:1993;320-327.
    • (1993) Virology , vol.197 , pp. 320-327
    • Bablanian, G.M.1    Grubman, M.J.2
  • 12
    • 0001907644 scopus 로고
    • Foot-and-mouth disease virus: Properties, molecular biology and immunogenicity
    • Bachrach H.L. Foot-and-mouth disease virus: properties, molecular biology and immunogenicity. Beltsville Symp. Agric. Res. 1:1977;3-32.
    • (1977) Beltsville Symp. Agric. Res. , vol.1 , pp. 3-32
    • Bachrach, H.L.1
  • 13
    • 0016817235 scopus 로고
    • Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus
    • Bachrach H.L., Moore D.M., McKercher P.D., Polatnick J. Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus. J. Immunol. 115:1975;1636-1641.
    • (1975) J. Immunol. , vol.115 , pp. 1636-1641
    • Bachrach, H.L.1    Moore, D.M.2    McKercher, P.D.3    Polatnick, J.4
  • 14
    • 0018664140 scopus 로고
    • Foot-and-mouth disease virus immunogenic capsid protein VPT: N-terminal sequences and immunogenic peptides obtained by CNBr and tryptic cleavages
    • Bachrach H.L., Morgan D.O., Moore D.M. Foot-and-mouth disease virus immunogenic capsid protein VPT: N-terminal sequences and immunogenic peptides obtained by CNBr and tryptic cleavages. Intervirology. 12:1979;65-72.
    • (1979) Intervirology , vol.12 , pp. 65-72
    • Bachrach, H.L.1    Morgan, D.O.2    Moore, D.M.3
  • 15
    • 0020265966 scopus 로고
    • Foot-and-mouth disease virus: Immunogenicity and structure of fragments derived from capsid protein VP and of virus containing cleaved VP
    • Bachrach H.L., Morgan D.O., McKercher P.D., Moore D.M., Robertson B.H. Foot-and-mouth disease virus: immunogenicity and structure of fragments derived from capsid protein VP and of virus containing cleaved VP. Vet. Microbiol. 7:1982;85-96.
    • (1982) Vet. Microbiol. , vol.7 , pp. 85-96
    • Bachrach, H.L.1    Morgan, D.O.2    McKercher, P.D.3    Moore, D.M.4    Robertson, B.H.5
  • 16
    • 0024453841 scopus 로고
    • Guanidine-resistant mutants of poliovirus have distinct mutations in peptide 2C
    • Baltera R.F. Jr, Tershak D.R. Guanidine-resistant mutants of poliovirus have distinct mutations in peptide 2C. J. Virol. 63:1989;4441-4444.
    • (1989) J. Virol. , vol.63 , pp. 4441-4444
    • Baltera R.F., Jr.1    Tershak, D.R.2
  • 17
    • 0030831556 scopus 로고    scopus 로고
    • Poliovirus-encoded 2C polypeptide specifically binds to the 3′-terminal sequences of viral negative-strand RNA
    • Banerjee R., Echeverri A., Dasgupta A. Poliovirus-encoded 2C polypeptide specifically binds to the 3′-terminal sequences of viral negative-strand RNA. J. Virol. 71:1997;9570-9578.
    • (1997) J. Virol. , vol.71 , pp. 9570-9578
    • Banerjee, R.1    Echeverri, A.2    Dasgupta, A.3
  • 18
    • 0035261889 scopus 로고    scopus 로고
    • Interaction of poliovirus-encoded 2C/2BC polypeptides with the 3′ terminus negative-strand cloverleaf requires an intact stem-loop b
    • Banerjee R., Tsai W., Kim W., Dasgupta A. Interaction of poliovirus-encoded 2C/2BC polypeptides with the 3′ terminus negative-strand cloverleaf requires an intact stem-loop b. Virology. 280:2001;41-51.
    • (2001) Virology , vol.280 , pp. 41-51
    • Banerjee, R.1    Tsai, W.2    Kim, W.3    Dasgupta, A.4
  • 19
    • 0033931398 scopus 로고    scopus 로고
    • Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: Flexibility in aphthovirus receptor usage
    • Baranowski E., Ruiz-Jarabo C.M., Sevilla N., Andreu D., Beck E., Domingo E. Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: flexibility in aphthovirus receptor usage. J. Virol. 74:2000;1641-1647.
    • (2000) J. Virol. , vol.74 , pp. 1641-1647
    • Baranowski, E.1    Ruiz-Jarabo, C.M.2    Sevilla, N.3    Andreu, D.4    Beck, E.5    Domingo, E.6
  • 20
    • 0035975646 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus lacking the VP1 G-H Loop: The mutant spectrum uncovers interactions among antigenic sites for fitness gain
    • Baranowski E., Ruiz-Jarabo C.M., Lim F., Domingo E. Foot-and-mouth disease virus lacking the VP1 G-H Loop: the mutant spectrum uncovers interactions among antigenic sites for fitness gain. Virology. 288:2001;192-202.
    • (2001) Virology , vol.288 , pp. 192-202
    • Baranowski, E.1    Ruiz-Jarabo, C.M.2    Lim, F.3    Domingo, E.4
  • 21
    • 0018356083 scopus 로고
    • Isolation and characterization of trypsin-resistant O1 variants of foot-and-mouth disease virus
    • Barteling S.J., Meloen R.H., Wagenaar F., Gielkens A.L. Isolation and characterization of trypsin-resistant O1 variants of foot-and-mouth disease virus. J. Gen. Virol. 43:1979;383-393.
    • (1979) J. Gen. Virol. , vol.43 , pp. 383-393
    • Barteling, S.J.1    Meloen, R.H.2    Wagenaar, F.3    Gielkens, A.L.4
  • 22
    • 0030820126 scopus 로고    scopus 로고
    • Synchronous replication of poliovirus RNA: Initiation of negative-strand RNA synthesis requires the guanidine-inhibited activity of protein 2C
    • Barton D.J., Flanegan J.B. Synchronous replication of poliovirus RNA: initiation of negative-strand RNA synthesis requires the guanidine-inhibited activity of protein 2C. J. Virol. 71:1997;8482-8489.
    • (1997) J. Virol. , vol.71 , pp. 8482-8489
    • Barton, D.J.1    Flanegan, J.B.2
  • 23
    • 0035868852 scopus 로고    scopus 로고
    • 5′ Cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis
    • Barton D.J., O'Donnell B.J., Flanegan J.B. 5′ Cloverleaf in poliovirus RNA is a cis-acting replication element required for negative-strand synthesis. EMBO J. 20:2001;1439-1448.
    • (2001) EMBO J. , vol.20 , pp. 1439-1448
    • Barton, D.J.1    O'Donnell, B.J.2    Flanegan, J.B.3
  • 24
    • 0028152426 scopus 로고
    • Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 Å resolution
    • Basavappa R., Syed R., Flore O., Icenogle J.P., Filman D.J., Hogle J.M. Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 Å resolution. Protein Sci. 3:1994;1651-1669.
    • (1994) Protein Sci. , vol.3 , pp. 1651-1669
    • Basavappa, R.1    Syed, R.2    Flore, O.3    Icenogle, J.P.4    Filman, D.J.5    Hogle, J.M.6
  • 25
    • 0023240103 scopus 로고
    • Effect of lysosomotropic compounds on early events in foot-and-mouth disease virus replication
    • Baxt B. Effect of lysosomotropic compounds on early events in foot-and-mouth disease virus replication. Virus Res. 7:1987;257-271.
    • (1987) Virus Res. , vol.7 , pp. 257-271
    • Baxt, B.1
  • 26
    • 0018826982 scopus 로고
    • Early interactions of foot-and-mouth disease virus with cultured cells
    • Baxt B., Bachrach H.L. Early interactions of foot-and-mouth disease virus with cultured cells. Virology. 104:1980;42-55.
    • (1980) Virology , vol.104 , pp. 42-55
    • Baxt, B.1    Bachrach, H.L.2
  • 27
    • 0020074378 scopus 로고
    • The adsorption and degradation of foot-and-mouth disease virus by isolated BHK-21 cell plasma membranes
    • Baxt B., Bachrach H.L. The adsorption and degradation of foot-and-mouth disease virus by isolated BHK-21 cell plasma membranes. Virology. 116:1982;391-405.
    • (1982) Virology , vol.116 , pp. 391-405
    • Baxt, B.1    Bachrach, H.L.2
  • 28
    • 0025186332 scopus 로고
    • The effect of peptides containing the arginine-glycine-aspartic acid sequence on the adsorption of foot-and-mouth disease virus to tissue culture cells
    • Baxt B., Becker Y. The effect of peptides containing the arginine-glycine-aspartic acid sequence on the adsorption of foot-and-mouth disease virus to tissue culture cells. Virus Genes. 4:1990;73-83.
    • (1990) Virus Genes , vol.4 , pp. 73-83
    • Baxt, B.1    Becker, Y.2
  • 29
    • 0028913126 scopus 로고
    • Foot-and-mouth disease virus undergoes restricted replication in macrophage cell cultures following Fc receptor-mediated adsorption
    • Baxt B., Mason P.W. Foot-and-mouth disease virus undergoes restricted replication in macrophage cell cultures following Fc receptor-mediated adsorption. Virology. 207:1995;503-509.
    • (1995) Virology , vol.207 , pp. 503-509
    • Baxt, B.1    Mason, P.W.2
  • 30
    • 0024582680 scopus 로고
    • Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus
    • Baxt B., Vakharia V., Moore D.M., Franke A.J., Morgan D.O. Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus. J. Virol. 63:1989;2143-2151.
    • (1989) J. Virol. , vol.63 , pp. 2143-2151
    • Baxt, B.1    Vakharia, V.2    Moore, D.M.3    Franke, A.J.4    Morgan, D.O.5
  • 31
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications
    • Bazan J.F., Fletterick R.J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc. Natl. Acad. Sci. USA. 85:1988;7872-7876.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 32
    • 0033986361 scopus 로고    scopus 로고
    • Genetic determinants of altered virulence of Taiwanese foot-and-mouth disease virus
    • Beard C.W., Mason P.W. Genetic determinants of altered virulence of Taiwanese foot-and-mouth disease virus. J. Virol. 74:2000;987-991.
    • (2000) J. Virol. , vol.74 , pp. 987-991
    • Beard, C.W.1    Mason, P.W.2
  • 33
    • 0032549512 scopus 로고    scopus 로고
    • Site size of cooperative single-stranded RNA binding by poliovirus RNA-dependent RNA polymerase
    • Beckman M.T., Kirkegaard K. Site size of cooperative single-stranded RNA binding by poliovirus RNA-dependent RNA polymerase. J. Biol. Chem. 273:1998;6724-6730.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6724-6730
    • Beckman, M.T.1    Kirkegaard, K.2
  • 34
    • 0032846191 scopus 로고    scopus 로고
    • Requirements for RNA replication of a poliovirus replicon by coxsackievirus B3 RNA polymerase
    • Bell Y.C., Semler B.L., Ehrenfeld E. Requirements for RNA replication of a poliovirus replicon by coxsackievirus B3 RNA polymerase. J. Virol. 73:1999;9413-9421.
    • (1999) J. Virol. , vol.73 , pp. 9413-9421
    • Bell, Y.C.1    Semler, B.L.2    Ehrenfeld, E.3
  • 37
    • 0025103829 scopus 로고
    • A region of the 5′ noncoding region of foot-and-mouth disease virus RNA directs efficient internal initiation of protein synthesis within cells: Involvement with the role of L-protease in translational control
    • Belsham G.J., Brangwyn J.K. A region of the 5′ noncoding region of foot-and-mouth disease virus RNA directs efficient internal initiation of protein synthesis within cells: involvement with the role of L-protease in translational control. J. Virol. 64:1990;5389-5395.
    • (1990) J. Virol. , vol.64 , pp. 5389-5395
    • Belsham, G.J.1    Brangwyn, J.K.2
  • 38
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham G.J., McInerney G.M., Ross-Smith N. Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74:2000;272-280.
    • (2000) J. Virol. , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 40
    • 0021069227 scopus 로고
    • Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures
    • Bienz K., Egger D., Rasser Y., Bossart W. Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures. Virology. 131:1983;39-48.
    • (1983) Virology , vol.131 , pp. 39-48
    • Bienz, K.1    Egger, D.2    Rasser, Y.3    Bossart, W.4
  • 41
    • 0023415083 scopus 로고
    • Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography
    • Bienz K., Egger D., Pasamontes L. Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography. Virology. 160:1987;220-226.
    • (1987) Virology , vol.160 , pp. 220-226
    • Bienz, K.1    Egger, D.2    Pasamontes, L.3
  • 42
    • 0025236535 scopus 로고
    • Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region
    • Bienz K., Egger D., Troxler M., Pasamontes L. Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region. J. Virol. 64:1990;1156-1163.
    • (1990) J. Virol. , vol.64 , pp. 1156-1163
    • Bienz, K.1    Egger, D.2    Troxler, M.3    Pasamontes, L.4
  • 43
    • 0026519212 scopus 로고
    • Structural and functional characterization of the poliovirus replication complex
    • Bienz K., Egger D., Pfister T., Troxler M. Structural and functional characterization of the poliovirus replication complex. J. Virol. 66:1992;2740-2747.
    • (1992) J. Virol. , vol.66 , pp. 2740-2747
    • Bienz, K.1    Egger, D.2    Pfister, T.3    Troxler, M.4
  • 44
    • 0000361390 scopus 로고    scopus 로고
    • Interferons and other cytokines
    • D.M. Knipe, & P.H. Howley. Philadelphia: Lippincott Williams & Wilkins
    • Biron C.A., Sen G.C. Interferons and other cytokines. Knipe D.M., Howley P.H. Fields' Virology. 2001;321-351 Lippincott Williams & Wilkins, Philadelphia.
    • (2001) Fields' Virology , pp. 321-351
    • Biron, C.A.1    Sen, G.C.2
  • 45
    • 0030660570 scopus 로고    scopus 로고
    • Hepatitis A virus subviral particles: Purification, accumulation, and relative infectivity of virions, provirions and procapsids
    • Bishop N.E., Anderson D.A. Hepatitis A virus subviral particles: purification, accumulation, and relative infectivity of virions, provirions and procapsids. Arch. Virol. 142:1997;2147-2160.
    • (1997) Arch. Virol. , vol.142 , pp. 2147-2160
    • Bishop, N.E.1    Anderson, D.A.2
  • 46
    • 0019959784 scopus 로고
    • Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence
    • Bittle J.L., Houghten R.A., Alexander H., Shinnick T.M., Sutcliffe J.G., Lerner R.A., Rowlands D.J., Brown F. Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature. 298:1982;30-33.
    • (1982) Nature , vol.298 , pp. 30-33
    • Bittle, J.L.1    Houghten, R.A.2    Alexander, H.3    Shinnick, T.M.4    Sutcliffe, J.G.5    Lerner, R.A.6    Rowlands, D.J.7    Brown, F.8
  • 47
    • 0031687438 scopus 로고    scopus 로고
    • Intracellular localization of poliovirus plus- and minus-strand RNA visualized by strand-specific fluorescent In situ hybridization
    • Bolten R., Egger D., Gosert R., Schaub G., Landmann L., Bienz K. Intracellular localization of poliovirus plus- and minus-strand RNA visualized by strand-specific fluorescent In situ hybridization. J. Virol. 72:1998;8578-8585.
    • (1998) J. Virol. , vol.72 , pp. 8578-8585
    • Bolten, R.1    Egger, D.2    Gosert, R.3    Schaub, G.4    Landmann, L.5    Bienz, K.6
  • 48
    • 0037232763 scopus 로고    scopus 로고
    • The history of research in foot-and-mouth disease
    • Brown, F., 2003. The history of research in foot-and-mouth disease. Virus 91, 3-7.
    • (2003) Virus , vol.91 , pp. 3-7
    • Brown, F.1
  • 50
    • 0029897109 scopus 로고    scopus 로고
    • Pathogenesis of wild-type and leaderless foot-and-mouth disease virus in cattle
    • Brown C.C., Piccone M.E., Mason P.W., McKenna T.S., Grubman M.J. Pathogenesis of wild-type and leaderless foot-and-mouth disease virus in cattle. J. Virol. 70:1996;5638-5641.
    • (1996) J. Virol. , vol.70 , pp. 5638-5641
    • Brown, C.C.1    Piccone, M.E.2    Mason, P.W.3    McKenna, T.S.4    Grubman, M.J.5
  • 51
    • 0034167164 scopus 로고    scopus 로고
    • Type I interferon production in cattle infected with 2 strains of foot-and-mouth disease virus, as determined by in situ hybridization
    • Brown C.C., Chinsangaram J., Grubman M.J. Type I interferon production in cattle infected with 2 strains of foot-and-mouth disease virus, as determined by in situ hybridization. Can. J. Vet. Res. 64:2000;130-133.
    • (2000) Can. J. Vet. Res. , vol.64 , pp. 130-133
    • Brown, C.C.1    Chinsangaram, J.2    Grubman, M.J.3
  • 52
    • 0014310453 scopus 로고
    • Action of guanidine on the replication of poliovirus RNA
    • Caliguiri L.A., Tamm I. Action of guanidine on the replication of poliovirus RNA. Virology. 35:1968;408-417.
    • (1968) Virology , vol.35 , pp. 408-417
    • Caliguiri, L.A.1    Tamm, I.2
  • 53
    • 0025933448 scopus 로고
    • Comparison of the 5′ and 3′ untranslated genomic regions of virulent and attenuated foot-and-mouth disease viruses (strains O1 Campos and C3 Resende)
    • Cao X.M., Bergmann I.E., Beck E. Comparison of the 5′ and 3′ untranslated genomic regions of virulent and attenuated foot-and-mouth disease viruses (strains O1 Campos and C3 Resende). J. Gen. Virol. 72:1991;2821-2825.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2821-2825
    • Cao, X.M.1    Bergmann, I.E.2    Beck, E.3
  • 54
    • 0028908788 scopus 로고
    • Functional analysis of the two alternative translation initiation sites of foot-and-mouth disease virus
    • Cao X., Bergmann I.E., Fullkrug R., Beck E. Functional analysis of the two alternative translation initiation sites of foot-and-mouth disease virus. J. Virol. 69:1995;560-563.
    • (1995) J. Virol. , vol.69 , pp. 560-563
    • Cao, X.1    Bergmann, I.E.2    Fullkrug, R.3    Beck, E.4
  • 55
    • 0021140938 scopus 로고
    • Effect of lysosomotropic agents on the foot-and-mouth disease virus replication
    • Carrillo E.C., Giachetti C., Campos R.H. Effect of lysosomotropic agents on the foot-and-mouth disease virus replication. Virology. 135:1984;542-545.
    • (1984) Virology , vol.135 , pp. 542-545
    • Carrillo, E.C.1    Giachetti, C.2    Campos, R.H.3
  • 56
    • 0022342819 scopus 로고
    • Early steps in FMDV replication: Further analysis on the effects of chloroquine
    • Carrillo E.C., Giachetti C., Campos R. Early steps in FMDV replication: further analysis on the effects of chloroquine. Virology. 147:1985;118-125.
    • (1985) Virology , vol.147 , pp. 118-125
    • Carrillo, E.C.1    Giachetti, C.2    Campos, R.3
  • 57
    • 0017344172 scopus 로고
    • Immunogenic and cell attachment sites of FMDV: Further evidence for their location in a single capsid polypeptide
    • Cavanagh D., Sangar D.V., Rowlands D.J., Brown F. Immunogenic and cell attachment sites of FMDV: further evidence for their location in a single capsid polypeptide. J. Gen. Virol. 35:1977;149-158.
    • (1977) J. Gen. Virol. , vol.35 , pp. 149-158
    • Cavanagh, D.1    Sangar, D.V.2    Rowlands, D.J.3    Brown, F.4
  • 58
    • 0018120909 scopus 로고
    • Early events in the interaction between foot-and-mouth disease virus and primary pig kidney cells
    • Cavanagh D., Rowlands D.J., Brown F. Early events in the interaction between foot-and-mouth disease virus and primary pig kidney cells. J. Gen. Virol. 41:1978;255-264.
    • (1978) J. Gen. Virol. , vol.41 , pp. 255-264
    • Cavanagh, D.1    Rowlands, D.J.2    Brown, F.3
  • 59
    • 0032192682 scopus 로고    scopus 로고
    • Protection of swine by live and inactivated vaccines prepared from a leader proteinase-deficient serotype A12 foot-and-mouth disease virus
    • Chinsangaram J., Mason P.W., Grubman M.J. Protection of swine by live and inactivated vaccines prepared from a leader proteinase-deficient serotype A12 foot-and-mouth disease virus. Vaccine. 16:1998;1516-1522.
    • (1998) Vaccine , vol.16 , pp. 1516-1522
    • Chinsangaram, J.1    Mason, P.W.2    Grubman, M.J.3
  • 60
    • 0032731093 scopus 로고    scopus 로고
    • Ability of foot-and-mouth disease virus to form plaques in cell culture is associated with suppression of α/β-interferon
    • Chinsangaram J., Piccone M.E., Grubman M.J. Ability of foot-and-mouth disease virus to form plaques in cell culture is associated with suppression of α/β-interferon. J. Virol. 73:1999;9891-9898.
    • (1999) J. Virol. , vol.73 , pp. 9891-9898
    • Chinsangaram, J.1    Piccone, M.E.2    Grubman, M.J.3
  • 61
    • 0035010933 scopus 로고    scopus 로고
    • Inhibition of L-deleted foot-and-mouth disease virus replication by α/β-interferon involves double-stranded RNA-dependent protein kinase
    • Chinsangaram J., Koster M., Grubman M.J. Inhibition of L-deleted foot-and-mouth disease virus replication by α/β-interferon involves double-stranded RNA-dependent protein kinase. J. Virol. 75:2001;5498-5503.
    • (2001) J. Virol. , vol.75 , pp. 5498-5503
    • Chinsangaram, J.1    Koster, M.2    Grubman, M.J.3
  • 62
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho M.W., Teterina N., Egger D., Bienz K., Ehrenfeld E. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology. 202:1994;129-145.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 63
    • 0023198719 scopus 로고
    • Myristylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M., Newman J.F., Filman D., Hogle J.M., Rowlands D.J., Brown F. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature. 327:1987;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
  • 64
    • 0025885346 scopus 로고
    • Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: A mechanism for inhibition of host cell polymerase III transcription by poliovirus
    • Clark M.E., Hammerle T., Wimmer E., Dasgupta A. Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J. 10:1991;2941-2947.
    • (1991) EMBO J. , vol.10 , pp. 2941-2947
    • Clark, M.E.1    Hammerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 65
    • 0027535652 scopus 로고
    • Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
    • Clark M.E., Lieberman P.M., Berk A.J., Dasgupta A. Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro. Mol. Cell. Biol. 13:1993;1232-1237.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1232-1237
    • Clark, M.E.1    Lieberman, P.M.2    Berk, A.J.3    Dasgupta, A.4
  • 66
    • 0024077613 scopus 로고
    • Processing and assembly of foot-and-mouth disease virus proteins using subgenomic RNA
    • Clarke B.E., Sangar D.V. Processing and assembly of foot-and-mouth disease virus proteins using subgenomic RNA. J. Gen. Virol. 69:1988;2313-2325.
    • (1988) J. Gen. Virol. , vol.69 , pp. 2313-2325
    • Clarke, B.E.1    Sangar, D.V.2
  • 69
    • 0021139213 scopus 로고
    • Heterogeneity of the polyribocytidylic acid tract in aphthovirus: Biochemical and biological studies of viruses carrying polyribocytidylic acid tracts of different lengths
    • Costa Giomi M.P., Bergmann I.E., Scodeller E.A., Auge de Mello P., Gomez I., La Torre J.L. Heterogeneity of the polyribocytidylic acid tract in aphthovirus: biochemical and biological studies of viruses carrying polyribocytidylic acid tracts of different lengths. J. Virol. 51:1984;799-805.
    • (1984) J. Virol. , vol.51 , pp. 799-805
    • Costa Giomi, M.P.1    Bergmann, I.E.2    Scodeller, E.A.3    Auge de Mello, P.4    Gomez, I.5    La Torre, J.L.6
  • 70
    • 0013970637 scopus 로고
    • A third antigenic component associated with foot-and-mouth disease infection
    • Cowan K.M., Graves J.H. A third antigenic component associated with foot-and-mouth disease infection. Virology. 30:1966;528-540.
    • (1966) Virology , vol.30 , pp. 528-540
    • Cowan, K.M.1    Graves, J.H.2
  • 71
    • 0028904286 scopus 로고
    • Localization of binding site for encephalomyocarditis virus RNA polymerase in the 3′-noncoding region of the viral RNA
    • Cui T., Porter A.G. Localization of binding site for encephalomyocarditis virus RNA polymerase in the 3′-noncoding region of the viral RNA. Nucleic Acids Res. 23:1995;377-382.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 377-382
    • Cui, T.1    Porter, A.G.2
  • 72
    • 0027501562 scopus 로고
    • Binding of encephalomyocarditis virus RNA polymerase to the 3′-noncoding region of the viral RNA is specific and requires the 3′-poly(A) tail
    • Cui T., Sankar S., Porter A.G. Binding of encephalomyocarditis virus RNA polymerase to the 3′-noncoding region of the viral RNA is specific and requires the 3′-poly(A) tail. J. Biol. Chem. 268:1993;26093-26098.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26093-26098
    • Cui, T.1    Sankar, S.2    Porter, A.G.3
  • 74
    • 0029844847 scopus 로고    scopus 로고
    • The poliovirus 135S particle is infectious
    • Curry S., Chow M., Hogle J.M. The poliovirus 135S particle is infectious. J. Virol. 70:1996;7125-7131.
    • (1996) J. Virol. , vol.70 , pp. 7125-7131
    • Curry, S.1    Chow, M.2    Hogle, J.M.3
  • 75
    • 0030780581 scopus 로고    scopus 로고
    • Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: The structure of empty capsids of foot-and-mouth disease virus
    • Curry S., Fry E., Blakemore W., Abu-Ghazaleh R., Jackson T., King A., Lea S., Newman J., Stuart D. Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus. J. Virol. 71:1997;9743-9752.
    • (1997) J. Virol. , vol.71 , pp. 9743-9752
    • Curry, S.1    Fry, E.2    Blakemore, W.3    Abu-Ghazaleh, R.4    Jackson, T.5    King, A.6    Lea, S.7    Newman, J.8    Stuart, D.9
  • 76
    • 0028300959 scopus 로고
    • Expression and subcellular localization of poliovirus VPg-precursor protein 3AB in eukaryotic cells: Evidence for glycosylation in vitro
    • Datta U., Dasgupta A. Expression and subcellular localization of poliovirus VPg-precursor protein 3AB in eukaryotic cells: evidence for glycosylation in vitro. J. Virol. 68:1994;4468-4477.
    • (1994) J. Virol. , vol.68 , pp. 4468-4477
    • Datta, U.1    Dasgupta, A.2
  • 78
    • 0024110509 scopus 로고
    • Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex
    • Devaney M.A., Vakharia V.N., Lloyd R.E., Ehrenfeld E., Grubman M.J. Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex. J. Virol. 62:1988;4407-4409.
    • (1988) J. Virol. , vol.62 , pp. 4407-4409
    • Devaney, M.A.1    Vakharia, V.N.2    Lloyd, R.E.3    Ehrenfeld, E.4    Grubman, M.J.5
  • 79
    • 0345482977 scopus 로고
    • GTP-binding domain: Three consensus sequence elements with distinct spacing
    • Dever T.E., Glynias M.J., Merrick W.C. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl. Acad. Sci. USA. 84:1987;1814-1818.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1814-1818
    • Dever, T.E.1    Glynias, M.J.2    Merrick, W.C.3
  • 80
    • 0025739318 scopus 로고
    • Encephalomyocarditis virus RNA polymerase preparations, with and without RNA helicase activity
    • Dmitrieva T.M., Norkina K.B., Agol V.I. Encephalomyocarditis virus RNA polymerase preparations, with and without RNA helicase activity. J. Virol. 65:1991;2714-2717.
    • (1991) J. Virol. , vol.65 , pp. 2714-2717
    • Dmitrieva, T.M.1    Norkina, K.B.2    Agol, V.I.3
  • 81
    • 0028918959 scopus 로고
    • Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A
    • Doedens J.R., Kirkegaard K. Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J. 14:1995;894-907.
    • (1995) EMBO J. , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 82
    • 0030728931 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis
    • Doedens J.R., Giddings T.H. Jr, Kirkegaard K. Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J. Virol. 71:1997;9054-9064.
    • (1997) J. Virol. , vol.71 , pp. 9054-9064
    • Doedens, J.R.1    Giddings T.H., Jr.2    Kirkegaard, K.3
  • 85
    • 0035005706 scopus 로고    scopus 로고
    • The 'cleavage' activities of foot-and-mouth disease virus 2A site- directed mutants and naturally occurring '2A-like' sequences
    • Donnelly M.L., Hughes L.E., Luke G., Mendoza H., ten Dam E., Gani D., Ryan M.D. The 'cleavage' activities of foot-and-mouth disease virus 2A site- directed mutants and naturally occurring '2A-like' sequences. J. Gen. Virol. 82:2001;1027-1041.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1027-1041
    • Donnelly, M.L.1    Hughes, L.E.2    Luke, G.3    Mendoza, H.4    Ten Dam, E.5    Gani, D.6    Ryan, M.D.7
  • 86
    • 0035015174 scopus 로고    scopus 로고
    • Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: A putative ribosomal 'skip'
    • Donnelly M.L., Luke G., Mehrotra A., Li X., Hughes L.E., Gani D., Ryan M.D. Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'. J. Gen. Virol. 82:2001;1013-1025.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1013-1025
    • Donnelly, M.L.1    Luke, G.2    Mehrotra, A.3    Li, X.4    Hughes, L.E.5    Gani, D.6    Ryan, M.D.7
  • 87
    • 0016765926 scopus 로고
    • Replication of picornaviruses. I. Evidence from in vitro RNA synthesis that poly(A) of the poliovirus genome is genetically coded
    • Dorsch-Hasler K., Yogo Y., Wimmer E. Replication of picornaviruses. I. Evidence from in vitro RNA synthesis that poly(A) of the poliovirus genome is genetically coded. J. Virol. 16:1975;1512-1517.
    • (1975) J. Virol. , vol.16 , pp. 1512-1517
    • Dorsch-Hasler, K.1    Yogo, Y.2    Wimmer, E.3
  • 88
    • 0031008581 scopus 로고    scopus 로고
    • Cold-adapted poliovirus mutants bypass a postentry replication block
    • Dove A.W., Racaniello V.R. Cold-adapted poliovirus mutants bypass a postentry replication block. J. Virol. 71:1997;4728-4735.
    • (1997) J. Virol. , vol.71 , pp. 4728-4735
    • Dove, A.W.1    Racaniello, V.R.2
  • 89
    • 0024507859 scopus 로고
    • Cloning and synthesis of infectious cardiovirus RNAs containing short, discrete poly(C) tracts
    • Duke G.M., Palmenberg A.C. Cloning and synthesis of infectious cardiovirus RNAs containing short, discrete poly(C) tracts. J. Virol. 63:1989;1822-1826.
    • (1989) J. Virol. , vol.63 , pp. 1822-1826
    • Duke, G.M.1    Palmenberg, A.C.2
  • 90
    • 0025089824 scopus 로고
    • Attenuation of Mengo virus through genetic engineering of the 5′-noncoding poly(C) tract
    • Duke G.M., Osorio J.E., Palmenberg A.C. Attenuation of Mengo virus through genetic engineering of the 5′-noncoding poly(C) tract. Nature. 343:1990;474-476.
    • (1990) Nature , vol.343 , pp. 474-476
    • Duke, G.M.1    Osorio, J.E.2    Palmenberg, A.C.3
  • 91
    • 0026558056 scopus 로고
    • Sequence and structural elements that contribute to efficient encephalomyocarditis virus RNA translation
    • Duke G.M., Hoffman M.A., Palmenberg A.C. Sequence and structural elements that contribute to efficient encephalomyocarditis virus RNA translation. J. Virol. 66:1992;1602-1609.
    • (1992) J. Virol. , vol.66 , pp. 1602-1609
    • Duke, G.M.1    Hoffman, M.A.2    Palmenberg, A.C.3
  • 92
    • 0031575152 scopus 로고    scopus 로고
    • Natural adaption to pigs of a Taiwanese isolate of foot-and-mouth disease virus
    • Dunn C.S., Donaldson A.I. Natural adaption to pigs of a Taiwanese isolate of foot-and-mouth disease virus. Vet. Rec. 141:1997;174-175.
    • (1997) Vet. Rec. , vol.141 , pp. 174-175
    • Dunn, C.S.1    Donaldson, A.I.2
  • 93
    • 0035101289 scopus 로고    scopus 로고
    • Phenotypic characterization of three phylogenetically conserved stem- loop motifs in the mengovirus 3′ untranslated region
    • Duque H., Palmenberg A.C. Phenotypic characterization of three phylogenetically conserved stem- loop motifs in the mengovirus 3′ untranslated region. J. Virol. 75:2001;3111-3120.
    • (2001) J. Virol. , vol.75 , pp. 3111-3120
    • Duque, H.1    Palmenberg, A.C.2
  • 94
    • 0026474872 scopus 로고
    • Modifications of the 5′ untranslated region of foot-and-mouth disease virus after prolonged persistence in cell culture
    • Escarmis C., Toja M., Medina M., Domingo E. Modifications of the 5′ untranslated region of foot-and-mouth disease virus after prolonged persistence in cell culture. Virus Res. 26:1992;113-125.
    • (1992) Virus Res. , vol.26 , pp. 113-125
    • Escarmis, C.1    Toja, M.2    Medina, M.3    Domingo, E.4
  • 95
    • 0028871163 scopus 로고
    • Large deletions in the 5′-untranslated region of foot-and-mouth disease virus of serotype C
    • Escarmis C., Dopazo J., Davila M., Palma E.L., Domingo E. Large deletions in the 5′-untranslated region of foot-and-mouth disease virus of serotype C. Virus Res. 35:1995;155-167.
    • (1995) Virus Res. , vol.35 , pp. 155-167
    • Escarmis, C.1    Dopazo, J.2    Davila, M.3    Palma, E.L.4    Domingo, E.5
  • 96
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220 000-Da polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison D., Milburn S.C., Edery I., Sonenberg N., Hershey J.W. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220 000-Da polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J. Biol. Chem. 257:1982;14806-14810.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 97
    • 0021915123 scopus 로고
    • Increased neurovirulence associated with a single nucleotide change in a noncoding region of the Sabin type 3 poliovaccine genome
    • Evans D.M., Dunn G., Minor P.D., Schild G.C., Cann A.J., Stanway G., Almond J.W., Currey K., Maizel J.V. Jr. Increased neurovirulence associated with a single nucleotide change in a noncoding region of the Sabin type 3 poliovaccine genome. Nature. 314:1985;548-550.
    • (1985) Nature , vol.314 , pp. 548-550
    • Evans, D.M.1    Dunn, G.2    Minor, P.D.3    Schild, G.C.4    Cann, A.J.5    Stanway, G.6    Almond, J.W.7    Currey, K.8    Maizel J.V., Jr.9
  • 98
    • 0024382865 scopus 로고
    • Eclipse products of poliovirus after cold-synchronized infection of HeLa cells
    • Everaert L., Vrijsen R., Boeye A. Eclipse products of poliovirus after cold-synchronized infection of HeLa cells. Virology. 171:1989;76-82.
    • (1989) Virology , vol.171 , pp. 76-82
    • Everaert, L.1    Vrijsen, R.2    Boeye, A.3
  • 99
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk M.M., Grigera P.R., Bergmann I.E., Zibert A., Multhaup G., Beck E. Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. J. Virol. 64:1990;748-756.
    • (1990) J. Virol. , vol.64 , pp. 748-756
    • Falk, M.M.1    Grigera, P.R.2    Bergmann, I.E.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 100
    • 0026591750 scopus 로고
    • VPg gene amplification correlates with infective particle formation in foot-and-mouth disease virus
    • Falk M.M., Sobrino F., Beck E. VPg gene amplification correlates with infective particle formation in foot-and-mouth disease virus. J. Virol. 66:1992;2251-2260.
    • (1992) J. Virol. , vol.66 , pp. 2251-2260
    • Falk, M.M.1    Sobrino, F.2    Beck, E.3
  • 101
    • 0142073982 scopus 로고
    • Poliovirus-specific primer-dependent RNA polymerase able to copy poly(A)
    • Flanegan J.B., Baltimore D. Poliovirus-specific primer-dependent RNA polymerase able to copy poly(A). Proc. Natl. Acad. Sci. USA. 74:1977;3677-3680.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3677-3680
    • Flanegan, J.B.1    Baltimore, D.2
  • 102
    • 0017325958 scopus 로고
    • Covalent linkage of a protein to a defined nucleotide sequence at the 5′-terminus of virion and replicative intermediate RNAs of poliovirus
    • Flanegan J.B., Petterson R.F., Ambros V., Hewlett N.J., Baltimore D. Covalent linkage of a protein to a defined nucleotide sequence at the 5′-terminus of virion and replicative intermediate RNAs of poliovirus. Proc. Natl. Acad. Sci. USA. 74:1977;961-965.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 961-965
    • Flanegan, J.B.1    Petterson, R.F.2    Ambros, V.3    Hewlett, N.J.4    Baltimore, D.5
  • 103
    • 0020491230 scopus 로고
    • A tandem repeat gene in a picornavirus
    • Forss S., Schaller H. A tandem repeat gene in a picornavirus. Nucleic Acids Res. 10:1982;6441-6450.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 6441-6450
    • Forss, S.1    Schaller, H.2
  • 104
    • 0021769942 scopus 로고
    • Nucleotide sequence and genome organization of foot-and-mouth disease virus
    • Forss S., Strebel K., Beck E., Schaller H. Nucleotide sequence and genome organization of foot-and-mouth disease virus. Nucleic Acids Res. 12:1984;6587-6601.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 6587-6601
    • Forss, S.1    Strebel, K.2    Beck, E.3    Schaller, H.4
  • 105
    • 0024639043 scopus 로고
    • The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid)
    • Fox G., Parry N.R., Barnett P.V., McGinn B., Rowlands D.J., Brown F. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J. Gen. Virol. 70:1989;625-637.
    • (1989) J. Gen. Virol. , vol.70 , pp. 625-637
    • Fox, G.1    Parry, N.R.2    Barnett, P.V.3    McGinn, B.4    Rowlands, D.J.5    Brown, F.6
  • 106
    • 0035109517 scopus 로고    scopus 로고
    • Adaptation of primate cell-adapted hepatitis A virus strain HM175 to growth in guinea pig cells is independent of mutations in the 5′-nontranslated region
    • Frings W., Dotzauer A. Adaptation of primate cell-adapted hepatitis A virus strain HM175 to growth in guinea pig cells is independent of mutations in the 5′-nontranslated region. J. Gen. Virol. 82:2001;597-602.
    • (2001) J. Gen. Virol. , vol.82 , pp. 597-602
    • Frings, W.1    Dotzauer, A.2
  • 108
    • 0030861261 scopus 로고    scopus 로고
    • Two functional complexes formed by KH domain containing proteins with the 5′-noncoding region of poliovirus RNA
    • Gamarnik A.V., Andino R. Two functional complexes formed by KH domain containing proteins with the 5′-noncoding region of poliovirus RNA. RNA. 3:1997;882-892.
    • (1997) RNA , vol.3 , pp. 882-892
    • Gamarnik, A.V.1    Andino, R.2
  • 110
    • 0034766987 scopus 로고    scopus 로고
    • Biochemical and genetic studies of the initiation of human rhinovirus 2 RNA replication: Identification of a cis-replicating element in the coding sequence of 2A(pro)
    • Gerber K., Wimmer E., Paul A.V. Biochemical and genetic studies of the initiation of human rhinovirus 2 RNA replication: identification of a cis-replicating element in the coding sequence of 2A(pro). J. Virol. 75:2001;10979-10990.
    • (2001) J. Virol. , vol.75 , pp. 10979-10990
    • Gerber, K.1    Wimmer, E.2    Paul, A.V.3
  • 111
    • 0023115693 scopus 로고
    • Isolation and characterization of recombinants between attenuated and virulent aphthovirus strains
    • Giraudo A.T., Sagedahl A., Bergmann I.E., La Torre J.L., Scodeller E.A. Isolation and characterization of recombinants between attenuated and virulent aphthovirus strains. J. Virol. 61:1987;419-425.
    • (1987) J. Virol. , vol.61 , pp. 419-425
    • Giraudo, A.T.1    Sagedahl, A.2    Bergmann, I.E.3    La Torre, J.L.4    Scodeller, E.A.5
  • 112
    • 0025280282 scopus 로고
    • Identification of a nucleotide deletion in parts of polypeptide 3A in two independent attenuated aphthovirus strains
    • Giraudo A.T., Beck E., Strebel K., de Mello P.A., La Torre J.L., Scodeller E.A., Bergmann I.E. Identification of a nucleotide deletion in parts of polypeptide 3A in two independent attenuated aphthovirus strains. Virology. 177:1990;780-783.
    • (1990) Virology , vol.177 , pp. 780-783
    • Giraudo, A.T.1    Beck, E.2    Strebel, K.3    De Mello, P.A.4    La Torre, J.L.5    Scodeller, E.A.6    Bergmann, I.E.7
  • 114
    • 0034652706 scopus 로고    scopus 로고
    • Engineering cowpea mosaic virus RNA-2 into a vector to express heterologous proteins in plants
    • Gopinath K., Wellink J., Porta C., Taylor K.M., Lomonossoff G.P., van Kammen A. Engineering cowpea mosaic virus RNA-2 into a vector to express heterologous proteins in plants. Virology. 267:2000;159-173.
    • (2000) Virology , vol.267 , pp. 159-173
    • Gopinath, K.1    Wellink, J.2    Porta, C.3    Taylor, K.M.4    Lomonossoff, G.P.5    Van Kammen, A.6
  • 115
    • 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. 17:1989;8413-8440.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 116
    • 0024595639 scopus 로고
    • An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication
    • Gorbalenya A.E., Blinov V.M., Donchenko A.P., Koonin E.V. An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication. J. Mol. Evol. 28:1989;256-268.
    • (1989) J. Mol. Evol. , vol.28 , pp. 256-268
    • Gorbalenya, A.E.1    Blinov, V.M.2    Donchenko, A.P.3    Koonin, E.V.4
  • 117
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold
    • Gorbalenya A.E., Donchenko A.P., Blinov V.M., Koonin E.V. Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold. FEBS Lett. 243:1989;103-114.
    • (1989) FEBS Lett. , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koonin, E.V.4
  • 118
    • 0025739985 scopus 로고
    • Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses
    • Gorbalenya A.E., Koonin E.V., Lai M.M. Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi- and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha- and coronaviruses. FEBS Lett. 288:1991;201-205.
    • (1991) FEBS Lett. , vol.288 , pp. 201-205
    • Gorbalenya, A.E.1    Koonin, E.V.2    Lai, M.M.3
  • 119
    • 0034606694 scopus 로고    scopus 로고
    • A cytopathic and a cell culture adapted hepatitis A virus strain differ in cell killing but not in intracellular membrane rearrangements
    • Gosert R., Egger D., Bienz K. A cytopathic and a cell culture adapted hepatitis A virus strain differ in cell killing but not in intracellular membrane rearrangements. Virology. 266:2000;157-169.
    • (2000) Virology , vol.266 , pp. 157-169
    • Gosert, R.1    Egger, D.2    Bienz, K.3
  • 120
    • 0027968278 scopus 로고
    • Mutational events in consecutive passages of hepatitis A virus strain GBM during cell culture adaptation
    • Graff J., Kasang C., Normann A., Pfisterer-Hunt M., Feinstone S.M., Flehmig B. Mutational events in consecutive passages of hepatitis A virus strain GBM during cell culture adaptation. Virology. 204:1994;60-68.
    • (1994) Virology , vol.204 , pp. 60-68
    • Graff, J.1    Kasang, C.2    Normann, A.3    Pfisterer-Hunt, M.4    Feinstone, S.M.5    Flehmig, B.6
  • 121
    • 0028127766 scopus 로고
    • Nucleotide sequence of wild-type hepatitis A virus GBM in comparison with two cell culture-adapted variants
    • Graff J., Normann A., Feinstone S.M., Flehmig B. Nucleotide sequence of wild-type hepatitis A virus GBM in comparison with two cell culture-adapted variants. J. Virol. 68:1994;548-554.
    • (1994) J. Virol. , vol.68 , pp. 548-554
    • Graff, J.1    Normann, A.2    Feinstone, S.M.3    Flehmig, B.4
  • 122
    • 0021152933 scopus 로고
    • Histone H3 modification in BHK cells infected with foot-and-mouth disease virus
    • Grigera P.R., Tisminetzky S.G. Histone H3 modification in BHK cells infected with foot-and-mouth disease virus. Virology. 136:1984;10-19.
    • (1984) Virology , vol.136 , pp. 10-19
    • Grigera, P.R.1    Tisminetzky, S.G.2
  • 123
    • 0034531981 scopus 로고    scopus 로고
    • Expression of a foreign epitope by porcine reproductive and respiratory syndrome virus
    • Groot Bramel-Verheije M.H., Rottier P.J., Meulenberg J.J. Expression of a foreign epitope by porcine reproductive and respiratory syndrome virus. Virology. 278:2000;380-389.
    • (2000) Virology , vol.278 , pp. 380-389
    • Groot Bramel-Verheije, M.H.1    Rottier, P.J.2    Meulenberg, J.J.3
  • 124
    • 0018820346 scopus 로고
    • The 5′-end of foot-and-mouth disease virion RNA contains a protein covalently linked to the nucleotide pUp
    • Grubman M.J. The 5′-end of foot-and-mouth disease virion RNA contains a protein covalently linked to the nucleotide pUp. Arch. Virol. 63:1980;311-315.
    • (1980) Arch. Virol. , vol.63 , pp. 311-315
    • Grubman, M.J.1
  • 125
    • 0018566287 scopus 로고
    • Isolation of foot-and-mouth disease virus messenger RNA from membrane- bound polyribosomes and characterization of its 5′- and 3′-termini
    • Grubman M.J., Bachrach H.L. Isolation of foot-and-mouth disease virus messenger RNA from membrane- bound polyribosomes and characterization of its 5′- and 3′-termini. Virology. 98:1979;466-470.
    • (1979) Virology , vol.98 , pp. 466-470
    • Grubman, M.J.1    Bachrach, H.L.2
  • 126
    • 0012536309 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus: The role of the leader proteinase in viral pathogenesis
    • Grubman M.J., Chinsangaram J. Foot-and-mouth disease virus: The role of the leader proteinase in viral pathogenesis. Recent Res. Dev. Virol. 2:2000;123-134.
    • (2000) Recent Res. Dev. Virol. , vol.2 , pp. 123-134
    • Grubman, M.J.1    Chinsangaram, J.2
  • 127
  • 128
    • 0022182915 scopus 로고
    • Capsid intermediates assembled in a foot-and-mouth disease virus genome RNA-programmed cell-free translation system and in infected cells
    • Grubman M.J., Morgan D.O., Kendall J., Baxt B. Capsid intermediates assembled in a foot-and-mouth disease virus genome RNA-programmed cell-free translation system and in infected cells. J. Virol. 56:1985;120-126.
    • (1985) J. Virol. , vol.56 , pp. 120-126
    • Grubman, M.J.1    Morgan, D.O.2    Kendall, J.3    Baxt, B.4
  • 129
    • 0023256016 scopus 로고
    • Antigenic comparison of the polypeptides of foot-and-mouth disease virus serotypes and other picornaviruses
    • Grubman M.J., Zellner M., Wagner J. Antigenic comparison of the polypeptides of foot-and-mouth disease virus serotypes and other picornaviruses. Virology. 158:1987;133-140.
    • (1987) Virology , vol.158 , pp. 133-140
    • Grubman, M.J.1    Zellner, M.2    Wagner, J.3
  • 130
    • 0028802290 scopus 로고
    • Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus
    • Grubman M.J., Zellner M., Bablanian G., Mason P.W., Piccone M.E. Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus. Virology. 213:1995;581-589.
    • (1995) Virology , vol.213 , pp. 581-589
    • Grubman, M.J.1    Zellner, M.2    Bablanian, G.3    Mason, P.W.4    Piccone, M.E.5
  • 131
    • 0032534805 scopus 로고    scopus 로고
    • Structure of the foot-and-mouth disease virus leader protease: A papain- like fold adapted for self-processing and eIF4G recognition
    • Guarne A., Tormo J., Kirchweger R., Pfistermueller D., Fita I., Skern T. Structure of the foot-and-mouth disease virus leader protease: a papain- like fold adapted for self-processing and eIF4G recognition. EMBO J. 17:1998;7469-7479.
    • (1998) EMBO J. , vol.17 , pp. 7469-7479
    • Guarne, A.1    Tormo, J.2    Kirchweger, R.3    Pfistermueller, D.4    Fita, I.5    Skern, T.6
  • 132
    • 0028143559 scopus 로고
    • Specific inhibition of aphthovirus infection by RNAs transcribed from both the 5′- and the 3′-noncoding regions
    • Gutierrez A., Martinez-Salas E., Pintado B., Sobrino F. Specific inhibition of aphthovirus infection by RNAs transcribed from both the 5′- and the 3′-noncoding regions. J. Virol. 68:1994;7426-7432.
    • (1994) J. Virol. , vol.68 , pp. 7426-7432
    • Gutierrez, A.1    Martinez-Salas, E.2    Pintado, B.3    Sobrino, F.4
  • 133
    • 0017736745 scopus 로고
    • Morphogenesis of poliovirus. IV. existence of particles sedimenting at 150S and having the properties of provirion
    • Guttman N., Baltimore D. Morphogenesis of poliovirus. IV. existence of particles sedimenting at 150S and having the properties of provirion. J. Virol. 23:1977;363-367.
    • (1977) J. Virol. , vol.23 , pp. 363-367
    • Guttman, N.1    Baltimore, D.2
  • 134
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen J.L., Long A.M., Schultz S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure. 5:1997;1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 135
    • 0026017496 scopus 로고
    • Catalysis of poliovirus VP0 maturation cleavage is not mediated by serine 10 of VP2
    • Harber J.J., Bradley J., Anderson C.W., Wimmer E. Catalysis of poliovirus VP0 maturation cleavage is not mediated by serine 10 of VP2. J. Virol. 65:1991;326-334.
    • (1991) J. Virol. , vol.65 , pp. 326-334
    • Harber, J.J.1    Bradley, J.2    Anderson, C.W.3    Wimmer, E.4
  • 136
    • 0017325653 scopus 로고
    • Biochemical analysis of a virulent and an avirulent strain of foot-and-mouth disease virus
    • Harris T.J., Brown F. Biochemical analysis of a virulent and an avirulent strain of foot-and-mouth disease virus. J. Gen. Virol. 34:1977;87-105.
    • (1977) J. Gen. Virol. , vol.34 , pp. 87-105
    • Harris, T.J.1    Brown, F.2
  • 137
    • 0027959741 scopus 로고
    • Interaction of poliovirus polypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding
    • Harris K.S., Xiang W., Alexander L., Lane W.S., Paul A.V., Wimmer E. Interaction of poliovirus polypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding. J. Biol. Chem. 269:1994;27004-27014.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27004-27014
    • Harris, K.S.1    Xiang, W.2    Alexander, L.3    Lane, W.S.4    Paul, A.V.5    Wimmer, E.6
  • 139
    • 0031024024 scopus 로고    scopus 로고
    • EIF4G: A multipurpose ribosome adapter
    • Hentze M.W. eIF4G: a multipurpose ribosome adapter. Science. 275:1997;500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 140
    • 0035265836 scopus 로고    scopus 로고
    • Poliovirus RNA replication requires genome circularization through a protein-protein bridge
    • Herold J., Andino R. Poliovirus RNA replication requires genome circularization through a protein-protein bridge. Mol. Cell. 7:2001;581-591.
    • (2001) Mol. Cell. , vol.7 , pp. 581-591
    • Herold, J.1    Andino, R.2
  • 141
    • 0032881997 scopus 로고    scopus 로고
    • Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4
    • Hindiyeh M., Li Q.H., Basavappa R., Hogle J.M., Chow M. Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4. J. Virol. 73:1999;9072-9079.
    • (1999) J. Virol. , vol.73 , pp. 9072-9079
    • Hindiyeh, M.1    Li, Q.H.2    Basavappa, R.3    Hogle, J.M.4    Chow, M.5
  • 143
    • 0016263269 scopus 로고
    • A possible precursor containing RNA of a bovine enterovirus: The provirion 11
    • Hoey E.M., Martin S.J. A possible precursor containing RNA of a bovine enterovirus: the provirion 11. J. Gen. Virol. 24:1974;515-524.
    • (1974) J. Gen. Virol. , vol.24 , pp. 515-524
    • Hoey, E.M.1    Martin, S.J.2
  • 144
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 A resolution
    • Hogle J.M., Chow M., Filman D.J. Three-dimensional structure of poliovirus at 2.9 A resolution. Science. 229:1985;1358-1365.
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 145
    • 0034307483 scopus 로고    scopus 로고
    • Internal ribosome initiation of translation and the control of cell death
    • Holcik M., Sonenberg N., Korneluk R.G. Internal ribosome initiation of translation and the control of cell death. Trends Genet. 16:2000;469-473.
    • (2000) Trends Genet. , vol.16 , pp. 469-473
    • Holcik, M.1    Sonenberg, N.2    Korneluk, R.G.3
  • 146
    • 0030732120 scopus 로고    scopus 로고
    • Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB
    • Hope D.A., Diamond S.E., Kirkegaard K. Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB. J. Virol. 71:1997;9490-9498.
    • (1997) J. Virol. , vol.71 , pp. 9490-9498
    • Hope, D.A.1    Diamond, S.E.2    Kirkegaard, K.3
  • 147
    • 0033856715 scopus 로고    scopus 로고
    • Is the 135S poliovirus particle an intermediate during cell entry
    • Huang Y., Hogle J.M., Chow M. Is the 135S poliovirus particle an intermediate during cell entry. J. Virol. 74:2000;8757-8761.
    • (2000) J. Virol. , vol.74 , pp. 8757-8761
    • Huang, Y.1    Hogle, J.M.2    Chow, M.3
  • 149
    • 0033625053 scopus 로고    scopus 로고
    • The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus
    • Jackson T., Sheppard D., Denyer M., Blakemore W., King A.M. The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus. J. Virol. 74:2000;4949-4956.
    • (2000) J. Virol. , vol.74 , pp. 4949-4956
    • Jackson, T.1    Sheppard, D.2    Denyer, M.3    Blakemore, W.4    King, A.M.5
  • 150
    • 0037232963 scopus 로고    scopus 로고
    • Structure and receptor binding
    • Jackson, T., Stuart, D.I., Fry, E., 2003. Structure and receptor binding. Virus 91, 33-46.
    • (2003) Virus , vol.91 , pp. 33-46
    • Jackson, T.1    Stuart, D.I.2    Fry, E.3
  • 151
    • 0014331325 scopus 로고
    • Polypeptide cleavages in the formation of poliovirus proteins
    • Jacobson M.F., Baltimore D. Polypeptide cleavages in the formation of poliovirus proteins. Proc. Natl. Acad. Sci. USA. 61:1968;77-84.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 77-84
    • Jacobson, M.F.1    Baltimore, D.2
  • 152
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang S.K., Krausslich H.G., Nicklin M.J., Duke G.M., Palmenberg A.C., Wimmer E. A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62:1988;2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 153
    • 0032488261 scopus 로고    scopus 로고
    • Membrane permeability induced by hepatitis A virus proteins 2B and 2BC and proteolytic processing of HAV 2BC
    • Jecht M., Probst C., Gauss-Muller V. Membrane permeability induced by hepatitis A virus proteins 2B and 2BC and proteolytic processing of HAV 2BC. Virology. 252:1998;218-227.
    • (1998) Virology , vol.252 , pp. 218-227
    • Jecht, M.1    Probst, C.2    Gauss-Muller, V.3
  • 154
    • 0017335458 scopus 로고
    • Induction of neutralizing antibodies and immunity in vaccinated guinea pigs by cyanogen bromide-peptides of VP3 of foot-and-mouth disease virus
    • Kaaden O.R., Adam K.H., Strohmeier K. Induction of neutralizing antibodies and immunity in vaccinated guinea pigs by cyanogen bromide-peptides of VP3 of foot-and-mouth disease virus. J. Gen. Virol. 34:1977;397-400.
    • (1977) J. Gen. Virol. , vol.34 , pp. 397-400
    • Kaaden, O.R.1    Adam, K.H.2    Strohmeier, K.3
  • 155
    • 0024596811 scopus 로고
    • Determinants in the 5′ noncoding region of poliovirus Sabin 1 RNA that influence the attenuation phenotype
    • Kawamura N., Kohara M., Abe S., Komatsu T., Tago K., Arita M., Nomoto A. Determinants in the 5′ noncoding region of poliovirus Sabin 1 RNA that influence the attenuation phenotype. J. Virol. 63:1989;1302-1309.
    • (1989) J. Virol. , vol.63 , pp. 1302-1309
    • Kawamura, N.1    Kohara, M.2    Abe, S.3    Komatsu, T.4    Tago, K.5    Arita, M.6    Nomoto, A.7
  • 156
    • 0018827691 scopus 로고
    • Heterogeneity of the genome-linked protein of foot-and-mouth disease virus
    • King A.M., Sangar D.V., Harris T.J., Brown F. Heterogeneity of the genome-linked protein of foot-and-mouth disease virus. J. Virol. 34:1980;627-634.
    • (1980) J. Virol. , vol.34 , pp. 627-634
    • King, A.M.1    Sangar, D.V.2    Harris, T.J.3    Brown, F.4
  • 159
    • 0025076813 scopus 로고
    • Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: Evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites
    • Kitson J.D., McCahon D., Belsham G.J. Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites. Virology. 179:1990;26-34.
    • (1990) Virology , vol.179 , pp. 26-34
    • Kitson, J.D.1    McCahon, D.2    Belsham, G.J.3
  • 161
    • 0032699505 scopus 로고    scopus 로고
    • Echovirus 9 strain barty non-structural protein 2C has NTPase activity
    • Klein M., Eggers H.J., Nelsen-Salz B. Echovirus 9 strain barty non-structural protein 2C has NTPase activity. Virus Res. 65:1999;155-160.
    • (1999) Virus Res. , vol.65 , pp. 155-160
    • Klein, M.1    Eggers, H.J.2    Nelsen-Salz, B.3
  • 162
    • 0034028109 scopus 로고    scopus 로고
    • The picornavirus replication inhibitors HBB and guanidine in the echovirus-9 system: The significance of viral protein 2C
    • Klein M., Hadaschik D., Zimmermann H., Eggers H.J., Nelsen-Salz B. The picornavirus replication inhibitors HBB and guanidine in the echovirus-9 system: the significance of viral protein 2C. J. Gen. Virol. 81:(Pt. 4):2000;895-901.
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 4 , pp. 895-901
    • Klein, M.1    Hadaschik, D.2    Zimmermann, H.3    Eggers, H.J.4    Nelsen-Salz, B.5
  • 163
    • 0026492939 scopus 로고
    • Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus
    • Kleina L.G., Grubman M.J. Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus. J. Virol. 66:1992;7168-7175.
    • (1992) J. Virol. , vol.66 , pp. 7168-7175
    • Kleina, L.G.1    Grubman, M.J.2
  • 164
    • 0021236936 scopus 로고
    • Biologically active protease of foot and mouth disease virus is expressed from cloned viral cDNA in Escherichia coli
    • Klump W., Marquardt O., Hofschneider P.H. Biologically active protease of foot and mouth disease virus is expressed from cloned viral cDNA in Escherichia coli. Proc. Natl. Acad. Sci. USA. 81:1984;3351-3355.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3351-3355
    • Klump, W.1    Marquardt, O.2    Hofschneider, P.H.3
  • 165
    • 0030947008 scopus 로고    scopus 로고
    • Characterization of synthetic foot-and-mouth disease virus provirions separates acid-mediated disassembly from infectivity
    • Knipe T., Rieder E., Baxt B., Ward G., Mason P.W. Characterization of synthetic foot-and-mouth disease virus provirions separates acid-mediated disassembly from infectivity. J. Virol. 71:1997;2851-2856.
    • (1997) J. Virol. , vol.71 , pp. 2851-2856
    • Knipe, T.1    Rieder, E.2    Baxt, B.3    Ward, G.4    Mason, P.W.5
  • 166
    • 0037235302 scopus 로고    scopus 로고
    • Molecular epidemiology of foot-and-mouth disease virus
    • Knowles, N.J., Samuel, A.R., 2003. Molecular epidemiology of foot-and-mouth disease virus. Virus 91, 65-80.
    • (2003) Virus , vol.91 , pp. 65-80
    • Knowles, N.J.1    Samuel, A.R.2
  • 167
    • 0035152346 scopus 로고    scopus 로고
    • Emergence in Asia of foot-and-mouth disease viruses with altered host range: Characterization of alterations in the 3A protein
    • Knowles N.J., Davies P.R., Henry T., O'Donnell V., Pacheco J.M., Mason P.W. Emergence in Asia of foot-and-mouth disease viruses with altered host range: characterization of alterations in the 3A protein. J. Virol. 75:2001;1551-1556.
    • (2001) J. Virol. , vol.75 , pp. 1551-1556
    • Knowles, N.J.1    Davies, P.R.2    Henry, T.3    O'Donnell, V.4    Pacheco, J.M.5    Mason, P.W.6
  • 168
    • 0032763630 scopus 로고    scopus 로고
    • Production of biologically active, heterodimeric porcine interleukin-12 using a monocistronic baculoviral expression system
    • Kokuho T., Watanabe S., Yokomizo Y., Inumaru S. Production of biologically active, heterodimeric porcine interleukin-12 using a monocistronic baculoviral expression system. Vet. Immunol. Immunopathol. 72:1999;289-302.
    • (1999) Vet. Immunol. Immunopathol. , vol.72 , pp. 289-302
    • Kokuho, T.1    Watanabe, S.2    Yokomizo, Y.3    Inumaru, S.4
  • 169
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G. Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO J. 18:1999;6249-6259.
    • (1999) EMBO J. , vol.18 , pp. 6249-6259
    • Kolatkar, P.R.1    Bella, J.2    Olson, N.H.3    Bator, C.M.4    Baker, T.S.5    Rossmann, M.G.6
  • 170
    • 0025013589 scopus 로고
    • Functional analysis of the internal translation initiation site of foot-and-mouth disease virus
    • Kuhn R., Luz N., Beck E. Functional analysis of the internal translation initiation site of foot-and-mouth disease virus. J. Virol. 64:1990;4625-4631.
    • (1990) J. Virol. , vol.64 , pp. 4625-4631
    • Kuhn, R.1    Luz, N.2    Beck, E.3
  • 171
    • 0029057801 scopus 로고
    • A role for 3AB protein in poliovirus genome replication
    • Lama J., Sanz M.A., Rodriguez P.L. A role for 3AB protein in poliovirus genome replication. J. Biol. Chem. 270:1995;14430-14438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14430-14438
    • Lama, J.1    Sanz, M.A.2    Rodriguez, P.L.3
  • 172
    • 0031817128 scopus 로고    scopus 로고
    • Genetic analysis of poliovirus protein 3A: Characterization of a non-cytopathic mutant virus defective in killing Vero cells
    • Lama J., Sanz M.A., Carrasco L. Genetic analysis of poliovirus protein 3A: characterization of a non-cytopathic mutant virus defective in killing Vero cells. J. Gen. Virol. 79:1998;1911-1921.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1911-1921
    • Lama, J.1    Sanz, M.A.2    Carrasco, L.3
  • 173
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation
    • Lamphear B.J., Kirchweger R., Skern T., Rhoads R.E. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation. J. Biol. Chem. 270:1995;21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 176
    • 0027532370 scopus 로고
    • Role of maturation cleavage in infectivity of picornaviruses: Activation of an infectosome
    • Lee W.M., Monroe S.S., Rueckert R.R. Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome. J. Virol. 67:1993;2110-2122.
    • (1993) J. Virol. , vol.67 , pp. 2110-2122
    • Lee, W.M.1    Monroe, S.S.2    Rueckert, R.R.3
  • 177
    • 0030614463 scopus 로고    scopus 로고
    • Point mutations within the βG-βH loop of foot-and-mouth disease virus O1K affect virus attachment to target cells
    • Leippert M., Beck E., Weiland F., Pfaff E. Point mutations within the βG-βH loop of foot-and-mouth disease virus O1K affect virus attachment to target cells. J. Virol. 71:1997;1046-1051.
    • (1997) J. Virol. , vol.71 , pp. 1046-1051
    • Leippert, M.1    Beck, E.2    Weiland, F.3    Pfaff, E.4
  • 178
    • 0026069630 scopus 로고
    • Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: Evidence for genetic recombination
    • Lemon S.M., Murphy P.C., Shields P.A., Ping L.H., Feinstone S.M., Cromeans T., Jansen R.W. Antigenic and genetic variation in cytopathic hepatitis A virus variants arising during persistent infection: evidence for genetic recombination. J. Virol. 65:1991;2056-2065.
    • (1991) J. Virol. , vol.65 , pp. 2056-2065
    • Lemon, S.M.1    Murphy, P.C.2    Shields, P.A.3    Ping, L.H.4    Feinstone, S.M.5    Cromeans, T.6    Jansen, R.W.7
  • 179
    • 0030053396 scopus 로고    scopus 로고
    • Equine rhinovirus 1 is more closely related to foot-and-mouth disease virus than to other picornaviruses
    • Li F., Browning G.F., Studdert M.J., Crabb B.S. Equine rhinovirus 1 is more closely related to foot-and-mouth disease virus than to other picornaviruses. Proc. Natl. Acad. Sci. USA. 93:1996;990-995.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 990-995
    • Li, F.1    Browning, G.F.2    Studdert, M.J.3    Crabb, B.S.4
  • 180
    • 0023774517 scopus 로고
    • Relationship of p220 cleavage during picornavirus infection to 2A proteinase sequencing
    • Lloyd R.E., Grubman M.J., Ehrenfeld E. Relationship of p220 cleavage during picornavirus infection to 2A proteinase sequencing. J. Virol. 62:1988;4216-4223.
    • (1988) J. Virol. , vol.62 , pp. 4216-4223
    • Lloyd, R.E.1    Grubman, M.J.2    Ehrenfeld, E.3
  • 181
  • 183
    • 0017142638 scopus 로고
    • Physical and metabolic requirements for early interaction of poliovirus and human rhinovirus with HeLa cells
    • Lonberg-Holm K., Whiteley N.M. Physical and metabolic requirements for early interaction of poliovirus and human rhinovirus with HeLa cells. J. Virol. 19:1976;857-870.
    • (1976) J. Virol. , vol.19 , pp. 857-870
    • Lonberg-Holm, K.1    Whiteley, N.M.2
  • 184
    • 0030999946 scopus 로고    scopus 로고
    • Conserved structural motifs located in distal loops of aphthovirus internal ribosome entry site domain 3 are required for internal initiation of translation
    • Lopez de Quinto S., Martinez-Salas E. Conserved structural motifs located in distal loops of aphthovirus internal ribosome entry site domain 3 are required for internal initiation of translation. J. Virol. 71:1997;4171-4175.
    • (1997) J. Virol. , vol.71 , pp. 4171-4175
    • Lopez de Quinto, S.1    Martinez-Salas, E.2
  • 185
    • 2542509984 scopus 로고    scopus 로고
    • Involvement of the aphthovirus RNA region located between the two functional AUGs in start codon selection
    • Lopez de Quinto S., Martinez-Salas E. Involvement of the aphthovirus RNA region located between the two functional AUGs in start codon selection. Virology. 255:1999;324-336.
    • (1999) Virology , vol.255 , pp. 324-336
    • Lopez de Quinto, S.1    Martinez-Salas, E.2
  • 186
    • 0033623486 scopus 로고    scopus 로고
    • Interaction of the eIF4G initiation factor with the aphthovirus IRES is essential for internal translation initiation in vivo
    • Lopez de Quinto S., Martinez-Salas E. Interaction of the eIF4G initiation factor with the aphthovirus IRES is essential for internal translation initiation in vivo. RNA. 6:2000;1380-1392.
    • (2000) RNA , vol.6 , pp. 1380-1392
    • Lopez de Quinto, S.1    Martinez-Salas, E.2
  • 187
    • 0034852292 scopus 로고    scopus 로고
    • IRES interaction with translation initiation factors: Functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII
    • Lopez de Quinto S., Lafuente E., Martinez-Salas E. IRES interaction with translation initiation factors: functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII. RNA. 7:2001;1213-1226.
    • (2001) RNA , vol.7 , pp. 1213-1226
    • Lopez de Quinto, S.1    Lafuente, E.2    Martinez-Salas, E.3
  • 188
    • 0019406258 scopus 로고
    • Isolation of a soluble and template-dependent foot-and-mouth disease virus RNA polymerase
    • Lowe P.A., Brown F. Isolation of a soluble and template-dependent foot-and-mouth disease virus RNA polymerase. Virology. 111:1981;23-32.
    • (1981) Virology , vol.111 , pp. 23-32
    • Lowe, P.A.1    Brown, F.2
  • 189
    • 0029330515 scopus 로고
    • Identification of native foot-and-mouth disease virus non-structural protein 2C as a serological indicator to differentiate infected from vaccinated livestock
    • Lubroth J., Brown F. Identification of native foot-and-mouth disease virus non-structural protein 2C as a serological indicator to differentiate infected from vaccinated livestock. Res. Vet. Sci. 59:1995;70-78.
    • (1995) Res. Vet. Sci. , vol.59 , pp. 70-78
    • Lubroth, J.1    Brown, F.2
  • 191
    • 0025075251 scopus 로고
    • A cellular 57 kDa protein binds to two regions of the internal translation initiation site of foot-and-mouth disease virus
    • Luz N., Beck E. A cellular 57 kDa protein binds to two regions of the internal translation initiation site of foot-and-mouth disease virus. FEBS Lett. 269:1990;311-314.
    • (1990) FEBS Lett. , vol.269 , pp. 311-314
    • Luz, N.1    Beck, E.2
  • 192
    • 0025789625 scopus 로고
    • Interaction of a cellular 57-kDa protein with the internal translation initiation site of foot-and-mouth disease virus
    • Luz N., Beck E. Interaction of a cellular 57-kDa protein with the internal translation initiation site of foot-and-mouth disease virus. J. Virol. 65:1991;6486-6494.
    • (1991) J. Virol. , vol.65 , pp. 6486-6494
    • Luz, N.1    Beck, E.2
  • 193
    • 0025883162 scopus 로고
    • Internal initiation of translation mediated by the 5′ leader of a cellular mRNA
    • Macejak D.G., Sarnow P. Internal initiation of translation mediated by the 5′ leader of a cellular mRNA. Nature. 353:1991;90-94.
    • (1991) Nature , vol.353 , pp. 90-94
    • Macejak, D.G.1    Sarnow, P.2
  • 194
    • 0025806070 scopus 로고
    • A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly
    • Marc D., Girard M., van der Werf S. A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly. J. Gen. Virol. 72:1991;1151-1157.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1151-1157
    • Marc, D.1    Girard, M.2    Van der Werf, S.3
  • 195
    • 0019512309 scopus 로고
    • Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids
    • Marongiu M.E., Pani A., Corrias M.V., Sau M., La Colla P. Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids. J. Virol. 39:1981;341-347.
    • (1981) J. Virol. , vol.39 , pp. 341-347
    • Marongiu, M.E.1    Pani, A.2    Corrias, M.V.3    Sau, M.4    La Colla, P.5
  • 196
    • 0030950412 scopus 로고    scopus 로고
    • Evolution subverting essentiality: Dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus
    • Martinez M.A., Verdaguer N., Mateu M.G., Domingo E. Evolution subverting essentiality: dispensability of the cell attachment Arg-Gly-Asp motif in multiply passaged foot-and-mouth disease virus. Proc. Natl. Acad. Sci. USA. 94:1997;6798-6802.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6798-6802
    • Martinez, M.A.1    Verdaguer, N.2    Mateu, M.G.3    Domingo, E.4
  • 197
    • 0021807074 scopus 로고
    • Sequence of the viral replicase gene from foot-and-mouth disease virus C1-Santa Pau (C-S8)
    • Martinez-Salas E., Ortin J., Domingo E. Sequence of the viral replicase gene from foot-and-mouth disease virus C1-Santa Pau (C-S8). Gene. 35:1985;55-61.
    • (1985) Gene , vol.35 , pp. 55-61
    • Martinez-Salas, E.1    Ortin, J.2    Domingo, E.3
  • 198
    • 0027289282 scopus 로고
    • A single nucleotide substitution in the internal ribosome entry site of foot-and-mouth disease virus leads to enhanced cap-independent translation in vivo
    • Martinez-Salas E., Saiz J.C., Davila M., Belsham G.J., Domingo E. A single nucleotide substitution in the internal ribosome entry site of foot-and-mouth disease virus leads to enhanced cap-independent translation in vivo. J. Virol. 67:1993;3748-3755.
    • (1993) J. Virol. , vol.67 , pp. 3748-3755
    • Martinez-Salas, E.1    Saiz, J.C.2    Davila, M.3    Belsham, G.J.4    Domingo, E.5
  • 199
    • 0343431434 scopus 로고    scopus 로고
    • Functional interactions in internal translation initiation directed by viral and cellular IRES elements
    • Martinez-Salas E., Ramos R., Lafuente E., Lopez de Quinto S. Functional interactions in internal translation initiation directed by viral and cellular IRES elements. J. Gen. Virol. 82:2001;973-984.
    • (2001) J. Gen. Virol. , vol.82 , pp. 973-984
    • Martinez-Salas, E.1    Ramos, R.2    Lafuente, E.3    Lopez de Quinto, S.4
  • 200
    • 0027257937 scopus 로고
    • Antibody-complexed foot-and-mouth disease virus, but not poliovirus, can infect normally insusceptible cells via the Fc receptor
    • Mason P.W., Baxt B., Brown F., Harber J., Murdin A., Wimmer E. Antibody-complexed foot-and-mouth disease virus, but not poliovirus, can infect normally insusceptible cells via the Fc receptor. Virology. 192:1993;568-577.
    • (1993) Virology , vol.192 , pp. 568-577
    • Mason, P.W.1    Baxt, B.2    Brown, F.3    Harber, J.4    Murdin, A.5    Wimmer, E.6
  • 201
    • 0028201747 scopus 로고
    • RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway
    • Mason P.W., Rieder E., Baxt B. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc. Natl. Acad. Sci. USA. 91:1994;1932-1936.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1932-1936
    • Mason, P.W.1    Rieder, E.2    Baxt, B.3
  • 202
    • 0031555642 scopus 로고    scopus 로고
    • Evaluation of a live-attenuated foot-and-mouth disease virus as a vaccine candidate
    • Mason P.W., Piccone M.E., McKenna T.S., Chinsangaram J., Grubman M.J. Evaluation of a live-attenuated foot-and-mouth disease virus as a vaccine candidate. Virology. 227:1997;96-102.
    • (1997) Virology , vol.227 , pp. 96-102
    • Mason, P.W.1    Piccone, M.E.2    McKenna, T.S.3    Chinsangaram, J.4    Grubman, M.J.5
  • 203
    • 0036776467 scopus 로고    scopus 로고
    • Identification and characterization of a cis-acting replication element (cre) adjacent to the internal ribosome entry site of foot-and-mouth disease virus
    • Mason P.W., Bezborodova S.V., Henry T.M. Identification and characterization of a cis-acting replication element (cre) adjacent to the internal ribosome entry site of foot-and-mouth disease virus. J. Virol. 76:2002;9686-9694.
    • (2002) J. Virol. , vol.76 , pp. 9686-9694
    • Mason, P.W.1    Bezborodova, S.V.2    Henry, T.M.3
  • 204
    • 0029101761 scopus 로고
    • Antibody recognition of picornaviruses and escape from neutralization: A structural view
    • Mateu M.G. Antibody recognition of picornaviruses and escape from neutralization: a structural view. Virus Res. 38:1995;1-24.
    • (1995) Virus Res. , vol.38 , pp. 1-24
    • Mateu, M.G.1
  • 205
    • 0027957786 scopus 로고
    • Antigenic heterogeneity of a foot-and-mouth disease virus serotype in the field is mediated by very limited sequence variation at several antigenic sites
    • Mateu M.G., Hernandez J., Martinez M.A., Feigelstock D., Lea S., Perez J.J., Giralt E., Stuart D., Palma E.L., Domingo E. Antigenic heterogeneity of a foot-and-mouth disease virus serotype in the field is mediated by very limited sequence variation at several antigenic sites. J. Virol. 68:1994;1407-1417.
    • (1994) J. Virol. , vol.68 , pp. 1407-1417
    • Mateu, M.G.1    Hernandez, J.2    Martinez, M.A.3    Feigelstock, D.4    Lea, S.5    Perez, J.J.6    Giralt, E.7    Stuart, D.8    Palma, E.L.9    Domingo, E.10
  • 207
    • 0029819347 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 2A protease mediates cleavage in attenuated Sabin 3 poliovirus vectors engineered for delivery of foreign antigens
    • Mattion N.M., Harnish E.C., Crowley J.C., Reilly P.A. Foot-and-mouth disease virus 2A protease mediates cleavage in attenuated Sabin 3 poliovirus vectors engineered for delivery of foreign antigens. J. Virol. 70:1996;8124-8127.
    • (1996) J. Virol. , vol.70 , pp. 8124-8127
    • Mattion, N.M.1    Harnish, E.C.2    Crowley, J.C.3    Reilly, P.A.4
  • 209
    • 0029092344 scopus 로고
    • Receptor binding site-deleted foot-and-mouth disease (FMD) virus protects cattle from FMD
    • McKenna T.S., Lubroth J., Rieder E., Baxt B., Mason P.W. Receptor binding site-deleted foot-and-mouth disease (FMD) virus protects cattle from FMD. J. Virol. 69:1995;5787-5790.
    • (1995) J. Virol. , vol.69 , pp. 5787-5790
    • McKenna, T.S.1    Lubroth, J.2    Rieder, E.3    Baxt, B.4    Mason, P.W.5
  • 210
    • 0030025543 scopus 로고    scopus 로고
    • Capsid coding sequence is required for efficient replication of human rhinovirus 14 RNA
    • McKnight K.L., Lemon S.M. Capsid coding sequence is required for efficient replication of human rhinovirus 14 RNA. J. Virol. 70:1996;1941-1952.
    • (1996) J. Virol. , vol.70 , pp. 1941-1952
    • McKnight, K.L.1    Lemon, S.M.2
  • 211
    • 0031762554 scopus 로고    scopus 로고
    • The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication
    • McKnight K.L., Lemon S.M. The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication. RNA. 4:1998;1569-1584.
    • (1998) RNA , vol.4 , pp. 1569-1584
    • McKnight, K.L.1    Lemon, S.M.2
  • 212
    • 0027275622 scopus 로고
    • The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities
    • Medina M., Domingo E., Brangwyn J.K., Belsham G.J. The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities. Virology. 194:1993;355-359.
    • (1993) Virology , vol.194 , pp. 355-359
    • Medina, M.1    Domingo, E.2    Brangwyn, J.K.3    Belsham, G.J.4
  • 213
    • 0031060472 scopus 로고    scopus 로고
    • Kissing of the two predominant hairpin loops in the coxsackie B virus 3′ untranslated region is the essential structural feature of the origin of replication required for negative-strand RNA synthesis
    • Melchers W.J., Hoenderop J.G., Bruins Slot H.J., Pleij C.W., Pilipenko E.V., Agol V.I., Galama J.M. Kissing of the two predominant hairpin loops in the coxsackie B virus 3′ untranslated region is the essential structural feature of the origin of replication required for negative-strand RNA synthesis. J. Virol. 71:1997;686-696.
    • (1997) J. Virol. , vol.71 , pp. 686-696
    • Melchers, W.J.1    Hoenderop, J.G.2    Bruins Slot, H.J.3    Pleij, C.W.4    Pilipenko, E.V.5    Agol, V.I.6    Galama, J.M.7
  • 214
    • 0028958332 scopus 로고
    • Interaction of eukaryotic initiation factor eIF-4B with a picornavirus internal translation initiation site
    • Meyer K., Petersen A., Niepmann M., Beck E. Interaction of eukaryotic initiation factor eIF-4B with a picornavirus internal translation initiation site. J. Virol. 69:1995;2819-2824.
    • (1995) J. Virol. , vol.69 , pp. 2819-2824
    • Meyer, K.1    Petersen, A.2    Niepmann, M.3    Beck, E.4
  • 215
    • 0018163925 scopus 로고
    • Effect of trypsin and chymotrypsin on the polypeptides of large and small plaque variants of foot-and-mouth disease virus: Relationship to specific antigenicity and infectivity
    • Moore D.M., Cowan K.M. Effect of trypsin and chymotrypsin on the polypeptides of large and small plaque variants of foot-and-mouth disease virus: relationship to specific antigenicity and infectivity. J. Gen. Virol. 41:1978;549-562.
    • (1978) J. Gen. Virol. , vol.41 , pp. 549-562
    • Moore, D.M.1    Cowan, K.M.2
  • 216
    • 0027158749 scopus 로고
    • Mutations in the 3A genomic region of two cytopathic strains of hepatitis A virus isolated in Italy
    • Morace G., Pisani G., Beneduce F., Divizia M., Pana A. Mutations in the 3A genomic region of two cytopathic strains of hepatitis A virus isolated in Italy. Virus Res. 28:1993;187-194.
    • (1993) Virus Res. , vol.28 , pp. 187-194
    • Morace, G.1    Pisani, G.2    Beneduce, F.3    Divizia, M.4    Pana, A.5
  • 218
    • 0025773025 scopus 로고
    • Myristoylation is important at multiple stages in poliovirus assembly
    • Moscufo N., Simons J., Chow M. Myristoylation is important at multiple stages in poliovirus assembly. J. Virol. 65:1991;2372-2380.
    • (1991) J. Virol. , vol.65 , pp. 2372-2380
    • Moscufo, N.1    Simons, J.2    Chow, M.3
  • 219
    • 0024539215 scopus 로고
    • Mapping of attenuating sequences of an avirulent poliovirus type 2 strain
    • Moss E.G., O'Neill R.E., Racaniello V.R. Mapping of attenuating sequences of an avirulent poliovirus type 2 strain. J. Virol. 63:1989;1884-1890.
    • (1989) J. Virol. , vol.63 , pp. 1884-1890
    • Moss, E.G.1    O'Neill, R.E.2    Racaniello, V.R.3
  • 222
    • 0033862235 scopus 로고    scopus 로고
    • 3 as a receptor for foot-and-mouth disease virus is dependent on the bovine β(3) subunit
    • 3 as a receptor for foot-and-mouth disease virus is dependent on the bovine β(3) subunit. J. Virol. 74:2000;7298-7306.
    • (2000) J. Virol. , vol.74 , pp. 7298-7306
    • Neff, S.1    Mason, P.W.2    Baxt, B.3
  • 223
    • 0018712607 scopus 로고
    • Purification and identification of the RNA-dependent RNA polymerase of foot-and-mouth disease virus
    • Newman J.F., Cartwright B., Doel T.R., Brown F. Purification and identification of the RNA-dependent RNA polymerase of foot-and-mouth disease virus. J. Gen. Virol. 45:1979;497-507.
    • (1979) J. Gen. Virol. , vol.45 , pp. 497-507
    • Newman, J.F.1    Cartwright, B.2    Doel, T.R.3    Brown, F.4
  • 224
    • 0022340096 scopus 로고
    • The sequence of foot-and-mouth disease virus RNA to the 5′ side of the poly(C) tract
    • Newton S.E., Carroll A.R., Campbell R.O., Clarke B.E., Rowlands D.J. The sequence of foot-and-mouth disease virus RNA to the 5′ side of the poly(C) tract. Gene. 40:1985;331-336.
    • (1985) Gene , vol.40 , pp. 331-336
    • Newton, S.E.1    Carroll, A.R.2    Campbell, R.O.3    Clarke, B.E.4    Rowlands, D.J.5
  • 225
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • Nugent C.I., Johnson K.L., Sarnow P., Kirkegaard K. Functional coupling between replication and packaging of poliovirus replicon RNA. J. Virol. 73:1999;427-435.
    • (1999) J. Virol. , vol.73 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 226
    • 0035082836 scopus 로고    scopus 로고
    • A single amino acid substitution in nonstructural protein 3A can mediate adaptation of foot-and-mouth disease virus to the guinea pig
    • Nunez J.I., Baranowski E., Molina N., Ruiz-Jarabo C.M., Sanchez C., Domingo E., Sobrino F. A single amino acid substitution in nonstructural protein 3A can mediate adaptation of foot-and-mouth disease virus to the guinea pig. J. Virol. 75:2001;3977-3983.
    • (2001) J. Virol. , vol.75 , pp. 3977-3983
    • Nunez, J.I.1    Baranowski, E.2    Molina, N.3    Ruiz-Jarabo, C.M.4    Sanchez, C.5    Domingo, E.6    Sobrino, F.7
  • 227
    • 0035881530 scopus 로고    scopus 로고
    • Subcellular distribution of the foot-and-mouth disease virus 3A protein in cells infected with viruses encoding wild-type and bovine-attenuated forms of 3A
    • O'Donnell V.K., Pacheco J.M., Henry T.M., Mason P.W. Subcellular distribution of the foot-and-mouth disease virus 3A protein in cells infected with viruses encoding wild-type and bovine-attenuated forms of 3A. Virology. 287:2001;151-162.
    • (2001) Virology , vol.287 , pp. 151-162
    • O'Donnell, V.K.1    Pacheco, J.M.2    Henry, T.M.3    Mason, P.W.4
  • 228
    • 0032865671 scopus 로고    scopus 로고
    • Translation initiation factor eIF4B interacts with a picornavirus internal ribosome entry site in both 48S and 80S initiation complexes independently of initiator AUG location
    • Ochs K., Rust R.C., Niepmann M. Translation initiation factor eIF4B interacts with a picornavirus internal ribosome entry site in both 48S and 80S initiation complexes independently of initiator AUG location. J. Virol. 73:1999;7505-7514.
    • (1999) J. Virol. , vol.73 , pp. 7505-7514
    • Ochs, K.1    Rust, R.C.2    Niepmann, M.3
  • 229
    • 0023265132 scopus 로고
    • A novel method for obtaining poliovirus 14S pentamers from procapsids and their self-assembly into virus-like shells
    • Onodera S., Phillips B.A. A novel method for obtaining poliovirus 14S pentamers from procapsids and their self-assembly into virus-like shells. Virology. 159:1987;278-287.
    • (1987) Virology , vol.159 , pp. 278-287
    • Onodera, S.1    Phillips, B.A.2
  • 230
    • 0025011840 scopus 로고
    • Proteolytic processing of picornaviral polyprotein
    • Palmenberg A.C. Proteolytic processing of picornaviral polyprotein. Annu. Rev. Microbiol. 44:1990;603-623.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 603-623
    • Palmenberg, A.C.1
  • 231
    • 0026758421 scopus 로고
    • Proteolytic processing of the cardioviral P2 region: Primary 2A/2B cleavage in clone-derived precursors
    • Palmenberg A.C., Parks G.D., Hall D.J., Ingraham R.H., Seng T.W., Pallai P.V. Proteolytic processing of the cardioviral P2 region: primary 2A/2B cleavage in clone-derived precursors. Virology. 190:1992;754-762.
    • (1992) Virology , vol.190 , pp. 754-762
    • Palmenberg, A.C.1    Parks, G.D.2    Hall, D.J.3    Ingraham, R.H.4    Seng, T.W.5    Pallai, P.V.6
  • 232
    • 0029330222 scopus 로고
    • Functional oligomerization of poliovirus RNA-dependent RNA polymerase
    • Pata J.D., Schultz S.C., Kirkegaard K. Functional oligomerization of poliovirus RNA-dependent RNA polymerase. RNA. 1:1995;466-477.
    • (1995) RNA , vol.1 , pp. 466-477
    • Pata, J.D.1    Schultz, S.C.2    Kirkegaard, K.3
  • 233
    • 0017808009 scopus 로고
    • Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme
    • Pelham H.R. Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme. Eur. J. Biochem. 85:1978;457-462.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 457-462
    • Pelham, H.R.1
  • 234
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J., Sonenberg N. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature. 334:1988;320-325.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 235
  • 236
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • Pestova T.V., Hellen C.U., Shatsky I.N. Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol. Cell. Biol. 16:1996;6859-6869.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 237
    • 0029968997 scopus 로고    scopus 로고
    • Functional dissection of eukaryotic initiation factor 4F: The 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes
    • Pestova T.V., Shatsky I.N., Hellen C.U. Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes. Mol. Cell. Biol. 16:1996;6870-6878.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6870-6878
    • Pestova, T.V.1    Shatsky, I.N.2    Hellen, C.U.3
  • 239
    • 0033548596 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication
    • Pfister T., Wimmer E. Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. J. Biol. Chem. 274:1999;6992-7001.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6992-7001
    • Pfister, T.1    Wimmer, E.2
  • 240
    • 1042283148 scopus 로고
    • Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus
    • Pfaff E., Mussgay M., Bohm H.O., Schulz G.E., Schaller H. Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus. EMBO J. 1:1982;869-874.
    • (1982) EMBO J. , vol.1 , pp. 869-874
    • Pfaff, E.1    Mussgay, M.2    Bohm, H.O.3    Schulz, G.E.4    Schaller, H.5
  • 241
    • 0024021169 scopus 로고
    • Analysis of neutralizing epitopes on foot-and-mouth disease virus
    • Pfaff E., Thiel H.J., Beck E., Strohmaier K., Schaller H. Analysis of neutralizing epitopes on foot-and-mouth disease virus. J. Virol. 62:1988;2033-2040.
    • (1988) J. Virol. , vol.62 , pp. 2033-2040
    • Pfaff, E.1    Thiel, H.J.2    Beck, E.3    Strohmaier, K.4    Schaller, H.5
  • 242
    • 0033988485 scopus 로고    scopus 로고
    • A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro
    • Pfister T., Jones K.W., Wimmer E. A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro. J. Virol. 74:2000;334-343.
    • (2000) J. Virol. , vol.74 , pp. 334-343
    • Pfister, T.1    Jones, K.W.2    Wimmer, E.3
  • 243
    • 0029122520 scopus 로고
    • The foot-and-mouth disease virus leader proteinase gene is not required for viral replication
    • Piccone M.E., Rieder E., Mason P.W., Grubman M.J. The foot-and-mouth disease virus leader proteinase gene is not required for viral replication. J. Virol. 69:1995;5376-5382.
    • (1995) J. Virol. , vol.69 , pp. 5376-5382
    • Piccone, M.E.1    Rieder, E.2    Mason, P.W.3    Grubman, M.J.4
  • 244
    • 0029034840 scopus 로고
    • Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus
    • Piccone M.E., Zellner M., Kumosinski T.F., Mason P.W., Grubman M.J. Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus. J. Virol. 69:1995;4950-4956.
    • (1995) J. Virol. , vol.69 , pp. 4950-4956
    • Piccone, M.E.1    Zellner, M.2    Kumosinski, T.F.3    Mason, P.W.4    Grubman, M.J.5
  • 245
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher M.D., Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. USA. 81:1984;5985-5988.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 246
    • 0024355303 scopus 로고
    • Conservation of the secondary structure elements of the 5′-untranslated region of cardio- and aphthovirus RNAs
    • Pilipenko E.V., Blinov V.M., Chernov B.K., Dmitrieva T.M., Agol V.I. Conservation of the secondary structure elements of the 5′-untranslated region of cardio- and aphthovirus RNAs. Nucleic Acids Res. 17:1989;5701-5711.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5701-5711
    • Pilipenko, E.V.1    Blinov, V.M.2    Chernov, B.K.3    Dmitrieva, T.M.4    Agol, V.I.5
  • 247
    • 0024544364 scopus 로고
    • Conserved structural domains in the 5′-untranslated region of picornaviral genomes: An analysis of the segment controlling translation and neurovirulence
    • Pilipenko E.V., Blinov V.M., Romanova L.I., Sinyakov A.N., Maslova S.V., Agol V.I. Conserved structural domains in the 5′-untranslated region of picornaviral genomes: an analysis of the segment controlling translation and neurovirulence. Virology. 168:1989;201-209.
    • (1989) Virology , vol.168 , pp. 201-209
    • Pilipenko, E.V.1    Blinov, V.M.2    Romanova, L.I.3    Sinyakov, A.N.4    Maslova, S.V.5    Agol, V.I.6
  • 248
    • 0026502591 scopus 로고
    • Prokaryotic-like cis-elements in the cap-independent internal initiation of translation on picornavirus RNA
    • Pilipenko E.V., Gmyl A.P., Maslova S.V., Svitkin Y.V., Sinyakov A.N., Agol V.I. Prokaryotic-like cis-elements in the cap-independent internal initiation of translation on picornavirus RNA. Cell. 68:1992;119-131.
    • (1992) Cell , vol.68 , pp. 119-131
    • Pilipenko, E.V.1    Gmyl, A.P.2    Maslova, S.V.3    Svitkin, Y.V.4    Sinyakov, A.N.5    Agol, V.I.6
  • 249
    • 0026572608 scopus 로고
    • Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: A proposal for the existence of tRNA-like terminal structures
    • Pilipenko E.V., Maslova S.V., Sinyakov A.N., Agol V.I. Towards identification of cis-acting elements involved in the replication of enterovirus and rhinovirus RNAs: a proposal for the existence of tRNA-like terminal structures. Nucleic Acids Res. 20:1992;1739-1745.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1739-1745
    • Pilipenko, E.V.1    Maslova, S.V.2    Sinyakov, A.N.3    Agol, V.I.4
  • 250
    • 0029838843 scopus 로고    scopus 로고
    • Cis-element, oriR, involved in the initiation of (-) strand poliovirus RNA: A quasi-globular multi-domain RNA structure maintained by tertiary ('kissing') interactions
    • Pilipenko E.V., Poperechny K.V., Maslova S.V., Melchers W.J., Slot H.J., Agol V.I. Cis-element, oriR, involved in the initiation of (-) strand poliovirus RNA: a quasi-globular multi-domain RNA structure maintained by tertiary ('kissing') interactions. EMBO J. 15:1996;5428-5436.
    • (1996) EMBO J. , vol.15 , pp. 5428-5436
    • Pilipenko, E.V.1    Poperechny, K.V.2    Maslova, S.V.3    Melchers, W.J.4    Slot, H.J.5    Agol, V.I.6
  • 252
    • 0023001243 scopus 로고
    • Production of guanidine-resistant and -dependent poliovirus mutants from cloned cDNA: Mutations in polypeptide 2C are directly responsible for altered guanidine sensitivity
    • Pincus S.E., Wimmer E. Production of guanidine-resistant and -dependent poliovirus mutants from cloned cDNA: mutations in polypeptide 2C are directly responsible for altered guanidine sensitivity. J. Virol. 60:1986;793-796.
    • (1986) J. Virol. , vol.60 , pp. 793-796
    • Pincus, S.E.1    Wimmer, E.2
  • 253
    • 0022623016 scopus 로고
    • Guanidine-selected mutants of poliovirus: Mapping of point mutations to polypeptide 2C
    • Pincus S.E., Diamond D.C., Emini E.A., Wimmer E. Guanidine-selected mutants of poliovirus: mapping of point mutations to polypeptide 2C. J. Virol. 57:1986;638-646.
    • (1986) J. Virol. , vol.57 , pp. 638-646
    • Pincus, S.E.1    Diamond, D.C.2    Emini, E.A.3    Wimmer, E.4
  • 254
    • 0018845022 scopus 로고
    • Isolation of a foot-and-mouth disease polyuridylic acid polymerase and its inhibition by antibody
    • Polatnick J. Isolation of a foot-and-mouth disease polyuridylic acid polymerase and its inhibition by antibody. J. Virol. 33:1980;774-779.
    • (1980) J. Virol. , vol.33 , pp. 774-779
    • Polatnick, J.1
  • 255
    • 0014075558 scopus 로고
    • Foot-and-mouth disease virus-induced ribonucleic acid polymerase in baby hamster kidney cells
    • Polatnick J., Arlinghaus R.B. Foot-and-mouth disease virus-induced ribonucleic acid polymerase in baby hamster kidney cells. Virology. 31:1967;601-608.
    • (1967) Virology , vol.31 , pp. 601-608
    • Polatnick, J.1    Arlinghaus, R.B.2
  • 256
    • 0020653333 scopus 로고
    • Association of foot-and-mouth disease virus induced RNA polymerase with host cell organelles
    • Polatnick J., Wool S.H. Association of foot-and-mouth disease virus induced RNA polymerase with host cell organelles. Comp. Immunol. Microbiol. Infect. Dis. 6:1983;265-272.
    • (1983) Comp. Immunol. Microbiol. Infect. Dis. , vol.6 , pp. 265-272
    • Polatnick, J.1    Wool, S.H.2
  • 257
    • 0021056051 scopus 로고
    • Correlation of surface and internal ultrastructural changes in cells infected with foot-and-mouth disease virus
    • Polatnick J., Wool S.H. Correlation of surface and internal ultrastructural changes in cells infected with foot-and-mouth disease virus. Can. J. Comp. Med. 47:1983;440-444.
    • (1983) Can. J. Comp. Med. , vol.47 , pp. 440-444
    • Polatnick, J.1    Wool, S.H.2
  • 258
    • 0014071427 scopus 로고
    • Inhibition of cell-free foot-and-mouth disease virus-ribonucleic acid synthesis by antibody
    • Polatnick J., Arlinghaus R.B., Graves J.H., Cowan K.M. Inhibition of cell-free foot-and-mouth disease virus-ribonucleic acid synthesis by antibody. Virology. 31:1967;609-615.
    • (1967) Virology , vol.31 , pp. 609-615
    • Polatnick, J.1    Arlinghaus, R.B.2    Graves, J.H.3    Cowan, K.M.4
  • 259
    • 0019810316 scopus 로고
    • Differences between poliovirus empty capsids formed in vivo and those formed in vitro: A role for the morphopoietic factor
    • Putnak J.R., Phillips B.A. Differences between poliovirus empty capsids formed in vivo and those formed in vitro: a role for the morphopoietic factor. J. Virol. 40:1981;173-183.
    • (1981) J. Virol. , vol.40 , pp. 173-183
    • Putnak, J.R.1    Phillips, B.A.2
  • 260
    • 0344980095 scopus 로고    scopus 로고
    • Long-range RNA interactions between structural domains of the aphthovirus internal ribosome entry site (IRES)
    • Ramos R., Martinez-Salas E. Long-range RNA interactions between structural domains of the aphthovirus internal ribosome entry site (IRES). RNA. 5:1999;1374-1383.
    • (1999) RNA , vol.5 , pp. 1374-1383
    • Ramos, R.1    Martinez-Salas, E.2
  • 261
    • 0031847222 scopus 로고    scopus 로고
    • Utilization of chimeras between human (HM-175) and simian (AGM-27) strains of hepatitis A virus to study the molecular basis of virulence
    • Raychaudhuri G., Govindarajan S., Shapiro M., Purcell R.H., Emerson S.U. Utilization of chimeras between human (HM-175) and simian (AGM-27) strains of hepatitis A virus to study the molecular basis of virulence. J. Virol. 72:1998;7467-7475.
    • (1998) J. Virol. , vol.72 , pp. 7467-7475
    • Raychaudhuri, G.1    Govindarajan, S.2    Shapiro, M.3    Purcell, R.H.4    Emerson, S.U.5
  • 263
    • 0032557456 scopus 로고    scopus 로고
    • Effects of poliovirus 3AB protein on 3D polymerase-catalyzed reaction
    • Richards O.C., Ehrenfeld E. Effects of poliovirus 3AB protein on 3D polymerase-catalyzed reaction. J. Biol. Chem. 273:1998;12832-12840.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12832-12840
    • Richards, O.C.1    Ehrenfeld, E.2
  • 264
    • 0027324214 scopus 로고
    • Genetically engineered foot-and-mouth disease viruses with poly(C) tracts of two nucleotides are virulent in mice
    • Rieder E., Bunch T., Brown F., Mason P.W. Genetically engineered foot-and-mouth disease viruses with poly(C) tracts of two nucleotides are virulent in mice. J. Virol. 67:1993;5139-5145.
    • (1993) J. Virol. , vol.67 , pp. 5139-5145
    • Rieder, E.1    Bunch, T.2    Brown, F.3    Mason, P.W.4
  • 265
    • 0029841919 scopus 로고    scopus 로고
    • Propagation of an attenuated virus by design: Engineering a novel receptor for a noninfectious foot-and-mouth disease virus
    • Rieder E., Berinstein A., Baxt B., Kang A., Mason P.W. Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus. Proc. Natl. Acad. Sci. USA. 93:1996;10428-10433.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10428-10433
    • Rieder, E.1    Berinstein, A.2    Baxt, B.3    Kang, A.4    Mason, P.W.5
  • 266
    • 0023751790 scopus 로고
    • Comparative sequence analysis of the 5′ noncoding region of the enteroviruses and rhinoviruses
    • Rivera V.M., Welsh J.D., Maizel J.V. Jr. Comparative sequence analysis of the 5′ noncoding region of the enteroviruses and rhinoviruses. Virology. 165:1988;42-50.
    • (1988) Virology , vol.165 , pp. 42-50
    • Rivera, V.M.1    Welsh, J.D.2    Maizel J.V., Jr.3
  • 267
    • 0028884251 scopus 로고
    • Identification of critical amino acids within the foot-and-mouth disease virus leader protein, a cysteine protease
    • Roberts P.J., Belsham G.J. Identification of critical amino acids within the foot-and-mouth disease virus leader protein, a cysteine protease. Virology. 213:1995;140-146.
    • (1995) Virology , vol.213 , pp. 140-146
    • Roberts, P.J.1    Belsham, G.J.2
  • 268
    • 0020656955 scopus 로고
    • Identification of an exposed region of the immunogenic capsid polypeptide VP1 on foot-and-mouth disease virus
    • Robertson B.H., Moore D.M., Grubman M.J., Kleid D.G. Identification of an exposed region of the immunogenic capsid polypeptide VP1 on foot-and-mouth disease virus. J. Virol. 46:1983;311-316.
    • (1983) J. Virol. , vol.46 , pp. 311-316
    • Robertson, B.H.1    Moore, D.M.2    Grubman, M.J.3    Kleid, D.G.4
  • 271
    • 0027537974 scopus 로고
    • Poliovirus protein 2C has ATPase and GTPase activities
    • Rodriguez P.L., Carrasco L. Poliovirus protein 2C has ATPase and GTPase activities. J. Biol. Chem. 268:1993;8105-8110.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8105-8110
    • Rodriguez, P.L.1    Carrasco, L.2
  • 272
    • 0028824892 scopus 로고
    • The 3′ untranslated region of picornavirus RNA: Features required for efficient genome replication
    • Rohll J.B., Moon D.H., Evans D.J., Almond J.W. The 3′ untranslated region of picornavirus RNA: features required for efficient genome replication. J. Virol. 69:1995;7835-7844.
    • (1995) J. Virol. , vol.69 , pp. 7835-7844
    • Rohll, J.B.1    Moon, D.H.2    Evans, D.J.3    Almond, J.W.4
  • 273
    • 0026032983 scopus 로고
    • In vitro assembly of poliovirus 14S subunits: Identification of the assembly promoting activity of infected cell extracts
    • Rombaut B., Foriers A., Boeye A. In vitro assembly of poliovirus 14S subunits: identification of the assembly promoting activity of infected cell extracts. Virology. 180:1991;781-787.
    • (1991) Virology , vol.180 , pp. 781-787
    • Rombaut, B.1    Foriers, A.2    Boeye, A.3
  • 275
    • 0000327130 scopus 로고    scopus 로고
    • Picornaviridae: The viruses and their replication
    • B.N. Fields, D.M. Knipe, & P.H. Howley. Philadelphia and New York: Lippincott-Raven Publishers
    • Rueckert R.R. Picornaviridae: the viruses and their replication. Fields B.N., Knipe D.M., Howley P.H. Field's Virology. 1996;609-654 Lippincott-Raven Publishers, Philadelphia and New York.
    • (1996) Field's Virology , pp. 609-654
    • Rueckert, R.R.1
  • 276
    • 0021269982 scopus 로고
    • Systematic nomenclature of picornavirus proteins
    • Rueckert R.R., Wimmer E. Systematic nomenclature of picornavirus proteins. J. Virol. 50:1984;957-959.
    • (1984) J. Virol. , vol.50 , pp. 957-959
    • Rueckert, R.R.1    Wimmer, E.2
  • 277
    • 0032990430 scopus 로고    scopus 로고
    • Interaction of eukaryotic initiation factor eIF4B with the internal ribosome entry site of foot-and-mouth disease virus is independent of the polypyrimidine tract-binding protein
    • Rust R.C., Ochs K., Meyer K., Beck E., Niepmann M. Interaction of eukaryotic initiation factor eIF4B with the internal ribosome entry site of foot-and-mouth disease virus is independent of the polypyrimidine tract-binding protein. J. Virol. 73:1999;6111-6113.
    • (1999) J. Virol. , vol.73 , pp. 6111-6113
    • Rust, R.C.1    Ochs, K.2    Meyer, K.3    Beck, E.4    Niepmann, M.5
  • 278
    • 0028058011 scopus 로고
    • Foot-and-mouth disease virus 2A oligopeptide mediated cleavage of an artificial polyprotein
    • Ryan M.D., Drew J. Foot-and-mouth disease virus 2A oligopeptide mediated cleavage of an artificial polyprotein. EMBO J. 13:1994;928-933.
    • (1994) EMBO J. , vol.13 , pp. 928-933
    • Ryan, M.D.1    Drew, J.2
  • 279
    • 0024418411 scopus 로고
    • Specificity of enzyme-substrate interactions in foot-and-mouth disease virus polyprotein processing
    • Ryan M.D., Belsham G.J., King A.M. Specificity of enzyme-substrate interactions in foot-and-mouth disease virus polyprotein processing. Virology. 173:1989;35-45.
    • (1989) Virology , vol.173 , pp. 35-45
    • Ryan, M.D.1    Belsham, G.J.2    King, A.M.3
  • 280
    • 0025934319 scopus 로고
    • Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence
    • Ryan M.D., King A.M., Thomas G.P. Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence. J. Gen. Virol. 72:1991;2727-2732.
    • (1991) J. Gen. Virol. , vol.72 , pp. 2727-2732
    • Ryan, M.D.1    King, A.M.2    Thomas, G.P.3
  • 281
    • 0034056841 scopus 로고    scopus 로고
    • Alpha/beta interferon protects adult mice from fatal Sindbis virus infection and is an important determinant of cell and tissue tropism
    • Ryman K.D., Klimstra W.B., Nguyen K.B., Biron C.A., Johnston R.E. Alpha/beta interferon protects adult mice from fatal Sindbis virus infection and is an important determinant of cell and tissue tropism. J. Virol. 74:2000;3366-3378.
    • (2000) J. Virol. , vol.74 , pp. 3366-3378
    • Ryman, K.D.1    Klimstra, W.B.2    Nguyen, K.B.3    Biron, C.A.4    Johnston, R.E.5
  • 282
    • 0030971779 scopus 로고    scopus 로고
    • Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle
    • Sa-Carvalho D., Rieder E., Baxt B., Rodarte R., Tanuri A., Mason P.W. Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle. J. Virol. 71:1997;5115-5123.
    • (1997) J. Virol. , vol.71 , pp. 5115-5123
    • Sa-Carvalho, D.1    Rieder, E.2    Baxt, B.3    Rodarte, R.4    Tanuri, A.5    Mason, P.W.6
  • 283
    • 0023139782 scopus 로고
    • Biochemical characterization of an aphthovirus type C3 strain Resende attenuated for cattle by serial passages in chicken embryos
    • Sagedahl A., Giraudo A.T., De Mello P.A., Bergmann I.E., La Torre J.L., Scodeller E.A. Biochemical characterization of an aphthovirus type C3 strain Resende attenuated for cattle by serial passages in chicken embryos. Virology. 157:1987;366-374.
    • (1987) Virology , vol.157 , pp. 366-374
    • Sagedahl, A.1    Giraudo, A.T.2    De Mello, P.A.3    Bergmann, I.E.4    La Torre, J.L.5    Scodeller, E.A.6
  • 284
    • 0035170571 scopus 로고    scopus 로고
    • Deletion or substitution of the aphthovirus 3′ NCR abrogates infectivity and virus replication
    • Saiz M., Gomez S., Martinez-Salas E., Sobrino F. Deletion or substitution of the aphthovirus 3′ NCR abrogates infectivity and virus replication. J. Gen. Virol. 82:2001;93-101.
    • (2001) J. Gen. Virol. , vol.82 , pp. 93-101
    • Saiz, M.1    Gomez, S.2    Martinez-Salas, E.3    Sobrino, F.4
  • 285
    • 0035062960 scopus 로고    scopus 로고
    • Functional interaction of translation initiation factor eIF4G with the foot-and-mouth disease virus internal ribosome entry site
    • Saleh L., Rust R.C., Fullkrug R., Beck E., Bassili G., Ochs K., Niepmann M. Functional interaction of translation initiation factor eIF4G with the foot-and-mouth disease virus internal ribosome entry site. J. Gen. Virol. 82:2001;757-763.
    • (2001) J. Gen. Virol. , vol.82 , pp. 757-763
    • Saleh, L.1    Rust, R.C.2    Fullkrug, R.3    Beck, E.4    Bassili, G.5    Ochs, K.6    Niepmann, M.7
  • 286
    • 0017672667 scopus 로고
    • Protein covalently linked to foot-and-mouth disease virus RNA
    • Sangar D.V., Rowlands D.J., Harris T.J., Brown F. Protein covalently linked to foot-and-mouth disease virus RNA. Nature. 268:1977;648-650.
    • (1977) Nature , vol.268 , pp. 648-650
    • Sangar, D.V.1    Rowlands, D.J.2    Harris, T.J.3    Brown, F.4
  • 287
    • 0023663461 scopus 로고
    • All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs
    • Sangar D.V., Newton S.E., Rowlands D.J., Clarke B.E. All foot and mouth disease virus serotypes initiate protein synthesis at two separate AUGs. Nucleic Acids Res. 15:1987;3305-3315.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3305-3315
    • Sangar, D.V.1    Newton, S.E.2    Rowlands, D.J.3    Clarke, B.E.4
  • 288
    • 0020065896 scopus 로고
    • Guanidine-resistant mutants of aphthovirus induce the synthesis of an altered nonstructural polypeptide, P34
    • Saunders K., King A.M. Guanidine-resistant mutants of aphthovirus induce the synthesis of an altered nonstructural polypeptide, P34. J. Virol. 42:1982;389-394.
    • (1982) J. Virol. , vol.42 , pp. 389-394
    • Saunders, K.1    King, A.M.2
  • 289
    • 0022337979 scopus 로고
    • Recombination and oligonucleotide analysis of guanidine-resistant foot-and-mouth disease virus mutants
    • Saunders K., King A.M., McCahon D., Newman J.W., Slade W.R., Forss S. Recombination and oligonucleotide analysis of guanidine-resistant foot-and-mouth disease virus mutants. J. Virol. 56:1985;921-929.
    • (1985) J. Virol. , vol.56 , pp. 921-929
    • Saunders, K.1    King, A.M.2    McCahon, D.3    Newman, J.W.4    Slade, W.R.5    Forss, S.6
  • 290
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A., Giddings T.H. Jr, Ladinsky M.S., Kirkegaard K. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:1996;6576-6588.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings T.H., Jr.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 291
    • 0020436427 scopus 로고
    • Competition for cellular receptor sites among selected aphthoviruses
    • Sekiguchi K., Franke A.J., Baxt B. Competition for cellular receptor sites among selected aphthoviruses. Arch. Virol. 74:1982;53-64.
    • (1982) Arch. Virol. , vol.74 , pp. 53-64
    • Sekiguchi, K.1    Franke, A.J.2    Baxt, B.3
  • 292
    • 0000099985 scopus 로고
    • Multiplication, interferon production and sensitivity of virulent and attenuated strains of the virus of foot-and-mouth disease
    • Sellers R.F. Multiplication, interferon production and sensitivity of virulent and attenuated strains of the virus of foot-and-mouth disease. Nature. 198:1963;1228-1229.
    • (1963) Nature , vol.198 , pp. 1228-1229
    • Sellers, R.F.1
  • 293
    • 0024318295 scopus 로고
    • New model for the secondary structure of the 5′ non-coding RNA of poliovirus is supported by biochemical and genetic data that also show that RNA secondary structure is important in neurovirulence
    • Skinner M.A., Racaniello V.R., Dunn G., Cooper J., Minor P.D., Almond J.W. New model for the secondary structure of the 5′ non-coding RNA of poliovirus is supported by biochemical and genetic data that also show that RNA secondary structure is important in neurovirulence. J. Mol. Biol. 207:1989;379-392.
    • (1989) J. Mol. Biol. , vol.207 , pp. 379-392
    • Skinner, M.A.1    Racaniello, V.R.2    Dunn, G.3    Cooper, J.4    Minor, P.D.5    Almond, J.W.6
  • 294
    • 0031427632 scopus 로고    scopus 로고
    • RNA determinants of picornavirus cap-independent translation initiation
    • Stewart S.R., Semler B.L. RNA determinants of picornavirus cap-independent translation initiation. Semin. Virol. 8:1997;242-255.
    • (1997) Semin. Virol. , vol.8 , pp. 242-255
    • Stewart, S.R.1    Semler, B.L.2
  • 295
    • 0022453797 scopus 로고
    • A second protease of foot-and-mouth disease virus
    • Strebel K., Beck E. A second protease of foot-and-mouth disease virus. J. Virol. 58:1986;893-899.
    • (1986) J. Virol. , vol.58 , pp. 893-899
    • Strebel, K.1    Beck, E.2
  • 296
    • 0019990849 scopus 로고
    • Location and characterization of the antigenic portion of the FMDV immunizing protein
    • Strohmaier K., Franze R., Adam K.H. Location and characterization of the antigenic portion of the FMDV immunizing protein. J. Gen. Virol. 59:1982;295-306.
    • (1982) J. Gen. Virol. , vol.59 , pp. 295-306
    • Strohmaier, K.1    Franze, R.2    Adam, K.H.3
  • 298
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles
    • Suhy D.A., Giddings T.H. Jr, Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74:2000;8953-8965.
    • (2000) J. Virol. , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings T.H., Jr.2    Kirkegaard, K.3
  • 299
    • 0022448122 scopus 로고
    • Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin
    • Tamkun J.W., DeSimone D.W., Fonda D., Patel R.S., Buck C., Horwitz A.F., Hynes R.O. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell. 46:1986;271-282.
    • (1986) Cell , vol.46 , pp. 271-282
    • Tamkun, J.W.1    DeSimone, D.W.2    Fonda, D.3    Patel, R.S.4    Buck, C.5    Horwitz, A.F.6    Hynes, R.O.7
  • 300
    • 0025099730 scopus 로고
    • Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3
    • Tesar M., Marquardt O. Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3. Virology. 174:1990;364-374.
    • (1990) Virology , vol.174 , pp. 364-374
    • Tesar, M.1    Marquardt, O.2
  • 301
    • 0024724957 scopus 로고
    • Serological probes for some foot-and-mouth disease virus nonstructural proteins
    • Tesar M., Berger H.G., Marquardt O. Serological probes for some foot-and-mouth disease virus nonstructural proteins. Virus Genes. 3:1989;29-44.
    • (1989) Virus Genes , vol.3 , pp. 29-44
    • Tesar, M.1    Berger, H.G.2    Marquardt, O.3
  • 302
    • 0035087397 scopus 로고    scopus 로고
    • Requirements for assembly of poliovirus replication complexes and negative-strand RNA synthesis
    • Teterina N.L., Egger D., Bienz K., Brown D.M., Semler B.L., Ehrenfeld E. Requirements for assembly of poliovirus replication complexes and negative-strand RNA synthesis. J. Virol. 75:2001;3841-3850.
    • (2001) J. Virol. , vol.75 , pp. 3841-3850
    • Teterina, N.L.1    Egger, D.2    Bienz, K.3    Brown, D.M.4    Semler, B.L.5    Ehrenfeld, E.6
  • 303
    • 0030802760 scopus 로고    scopus 로고
    • Replication-competent picornaviruses with complete genomic RNA 3′ noncoding region deletions
    • Todd S., Towner J.S., Brown D.M., Semler B.L. Replication-competent picornaviruses with complete genomic RNA 3′ noncoding region deletions. J. Virol. 71:1997;8868-8874.
    • (1997) J. Virol. , vol.71 , pp. 8868-8874
    • Todd, S.1    Towner, J.S.2    Brown, D.M.3    Semler, B.L.4
  • 304
    • 0035039737 scopus 로고    scopus 로고
    • Kinetic analysis of the effect of poliovirus receptor on viral uncoating: The receptor as a catalyst
    • Tsang S.K., McDermott B.M., Racaniello V.R., Hogle J.M. Kinetic analysis of the effect of poliovirus receptor on viral uncoating: the receptor as a catalyst. J. Virol. 75:2001;4984-4989.
    • (2001) J. Virol. , vol.75 , pp. 4984-4989
    • Tsang, S.K.1    McDermott, B.M.2    Racaniello, V.R.3    Hogle, J.M.4
  • 305
    • 0023197987 scopus 로고
    • Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts
    • Vakharia V.N., Devaney M.A., Moore D.M., Dunn J.J., Grubman M.J. Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts. J. Virol. 61:1987;3199-3207.
    • (1987) J. Virol. , vol.61 , pp. 3199-3207
    • Vakharia, V.N.1    Devaney, M.A.2    Moore, D.M.3    Dunn, J.J.4    Grubman, M.J.5
  • 306
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • van Kuppeveld F.J., Hoenderop J.G., Smeets R.L., Willems P.H., Dijkman H.B., Galama J.M., Melchers W.J. Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J. 16:1997;3519-3532.
    • (1997) EMBO J. , vol.16 , pp. 3519-3532
    • Van Kuppeveld, F.J.1    Hoenderop, J.G.2    Smeets, R.L.3    Willems, P.H.4    Dijkman, H.B.5    Galama, J.M.6    Melchers, W.J.7
  • 308
    • 0029867609 scopus 로고    scopus 로고
    • Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus
    • Verdaguer N., Mateu M.G., Bravo J., Domingo E., Fita I. Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus. J. Mol. Biol. 256:1996;364-376.
    • (1996) J. Mol. Biol. , vol.256 , pp. 364-376
    • Verdaguer, N.1    Mateu, M.G.2    Bravo, J.3    Domingo, E.4    Fita, I.5
  • 309
    • 0031963629 scopus 로고    scopus 로고
    • A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: Implications for intratypic antigenic variation
    • Verdaguer N., Sevilla N., Valero M.L., Stuart D., Brocchi E., Andreu D., Giralt E., Domingo E., Mateu M.G., Fita I. A similar pattern of interaction for different antibodies with a major antigenic site of foot-and-mouth disease virus: implications for intratypic antigenic variation. J. Virol. 72:1998;739-748.
    • (1998) J. Virol. , vol.72 , pp. 739-748
    • Verdaguer, N.1    Sevilla, N.2    Valero, M.L.3    Stuart, D.4    Brocchi, E.5    Andreu, D.6    Giralt, E.7    Domingo, E.8    Mateu, M.G.9    Fita, I.10
  • 310
    • 0033766542 scopus 로고    scopus 로고
    • Cell-free synthesis of poliovirus: 14S subunits are the key intermediates in the encapsidation of poliovirus RNA
    • Verlinden Y., Cuconati A., Wimmer E., Rombaut B. Cell-free synthesis of poliovirus: 14S subunits are the key intermediates in the encapsidation of poliovirus RNA. J. Gen. Virol. 81:(Pt. 11):2000;2751-2754.
    • (2000) J. Gen. Virol. , vol.81 , Issue.PART 11 , pp. 2751-2754
    • Verlinden, Y.1    Cuconati, A.2    Wimmer, E.3    Rombaut, B.4
  • 311
    • 0024279635 scopus 로고
    • 3D gene of foot-and-mouth disease virus. Conservation by convergence of average sequences
    • Villaverde A., Martinez-Salas E., Domingo E. 3D gene of foot-and-mouth disease virus. Conservation by convergence of average sequences. J. Mol. Biol. 204:1988;771-776.
    • (1988) J. Mol. Biol. , vol.204 , pp. 771-776
    • Villaverde, A.1    Martinez-Salas, E.2    Domingo, E.3
  • 312
    • 0029766940 scopus 로고    scopus 로고
    • Intracellular membrane proliferation in E. coli induced by foot-and mouth- disease virus 3A gene products
    • Weber S., Granzow H., Weiland F., Marquardt O. Intracellular membrane proliferation in E. coli induced by foot-and mouth- disease virus 3A gene products. Virus Genes. 12:1996;5-14.
    • (1996) Virus Genes , vol.12 , pp. 5-14
    • Weber, S.1    Granzow, H.2    Weiland, F.3    Marquardt, O.4
  • 313
    • 0020047410 scopus 로고
    • Genome-linked proteins of viruses
    • Wimmer E. Genome-linked proteins of viruses. Cell. 28:1982;199-201.
    • (1982) Cell , vol.28 , pp. 199-201
    • Wimmer, E.1
  • 314
    • 0029766556 scopus 로고    scopus 로고
    • Equine rhinovirus serotypes 1 and 2: Relationship to each other and to aphthoviruses and cardioviruses
    • Wutz G., Auer H., Nowotny N., Grosse B., Skern T., Kuechler E. Equine rhinovirus serotypes 1 and 2: relationship to each other and to aphthoviruses and cardioviruses. J. Gen. Virol. 77:1996;1719-1730.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1719-1730
    • Wutz, G.1    Auer, H.2    Nowotny, N.3    Grosse, B.4    Skern, T.5    Kuechler, E.6
  • 315
    • 0029044382 scopus 로고
    • Interaction between the 5′-terminal cloverleaf and 3AB/3CDpro of poliovirus is essential for RNA replication
    • Xiang W., Harris K.S., Alexander L., Wimmer E. Interaction between the 5′-terminal cloverleaf and 3AB/3CDpro of poliovirus is essential for RNA replication. J. Virol. 69:1995;3658-3667.
    • (1995) J. Virol. , vol.69 , pp. 3658-3667
    • Xiang, W.1    Harris, K.S.2    Alexander, L.3    Wimmer, E.4
  • 316
    • 0031947053 scopus 로고    scopus 로고
    • Complete protein linkage map of poliovirus P3 proteins: Interaction of polymerase 3Dpol with VPg and with genetic variants of 3AB
    • Xiang W., Cuconati A., Hope D., Kirkegaard K., Wimmer E. Complete protein linkage map of poliovirus P3 proteins: interaction of polymerase 3Dpol with VPg and with genetic variants of 3AB. J. Virol. 72:1998;6732-6741.
    • (1998) J. Virol. , vol.72 , pp. 6732-6741
    • Xiang, W.1    Cuconati, A.2    Hope, D.3    Kirkegaard, K.4    Wimmer, E.5
  • 318
    • 0023259037 scopus 로고
    • Neutralization of foot-and-mouth disease virus can be mediated through any of at least three separate antigenic sites
    • Xie Q.C., McCahon D., Crowther J.R., Belsham G.J., McCullough K.C. Neutralization of foot-and-mouth disease virus can be mediated through any of at least three separate antigenic sites. J. Gen. Virol. 68:1987;1637-1647.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1637-1647
    • Xie, Q.C.1    McCahon, D.2    Crowther, J.R.3    Belsham, G.J.4    McCullough, K.C.5
  • 319
    • 0018379080 scopus 로고
    • Morphogenesis of foot-and-mouth disease virus. I. Role of procapsids as virion precursors
    • Yafal A.G., Palma E.L. Morphogenesis of foot-and-mouth disease virus. I. Role of procapsids as virion precursors. J. Virol. 30:1979;643-649.
    • (1979) J. Virol. , vol.30 , pp. 643-649
    • Yafal, A.G.1    Palma, E.L.2
  • 320
    • 0031458316 scopus 로고    scopus 로고
    • Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro
    • Yalamanchili P., Weidman K., Dasgupta A. Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro. Virology. 239:1997;176-185.
    • (1997) Virology , vol.239 , pp. 176-185
    • Yalamanchili, P.1    Weidman, K.2    Dasgupta, A.3
  • 321
    • 0033604756 scopus 로고    scopus 로고
    • Epidemiological characteristics and financial costs of the 1997 foot-and-mouth disease epidemic in Taiwan
    • Yang P.C., Chu R.M., Chung W.B., Sung H.T. Epidemiological characteristics and financial costs of the 1997 foot-and-mouth disease epidemic in Taiwan. Vet. Rec. 145:1999;731-734.
    • (1999) Vet. Rec. , vol.145 , pp. 731-734
    • Yang, P.C.1    Chu, R.M.2    Chung, W.B.3    Sung, H.T.4
  • 322
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong M.F., Dewalt P.G., Johnson V.H., Lamb J.G., Semler B.L. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology. 166:1988;265-270.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.L.5
  • 323
    • 0025353397 scopus 로고
    • Infectious foot-and-mouth disease virus derived from a cloned full-length cDNA
    • Zibert A., Maass G., Strebel K., Falk M.M., Beck E. Infectious foot-and-mouth disease virus derived from a cloned full-length cDNA. J. Virol. 64:1990;2467-2473.
    • (1990) J. Virol. , vol.64 , pp. 2467-2473
    • Zibert, A.1    Maass, G.2    Strebel, K.3    Falk, M.M.4    Beck, E.5
  • 324
    • 0029008576 scopus 로고
    • Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin
    • Ziegler E., Borman A.M., Kirchweger R., Skern T., Kean K.M. Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin. J. Virol. 69:1995;3465-3474.
    • (1995) J. Virol. , vol.69 , pp. 3465-3474
    • Ziegler, E.1    Borman, A.M.2    Kirchweger, R.3    Skern, T.4    Kean, K.M.5


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