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Volumn 160, Issue 1, 2015, Pages

Three-dimensional structure of foot-and-mouth disease virus and its biological functions

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN;

EID: 84924085675     PISSN: 03048608     EISSN: 14328798     Source Type: Journal    
DOI: 10.1007/s00705-014-2278-x     Document Type: Review
Times cited : (40)

References (150)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution
    • COI: 1:CAS:528:DyaL1MXhsFWjsLY%3D
    • Acharya R, Fry E, Stuart D, Fox G, Rowlands D, Brown F (1989) The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution. Nature 337:709–716
    • (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
    • 77958122066 scopus 로고    scopus 로고
    • A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape
    • Agudo R, Ferrer-Orta C, Arias A, de la Higuera I, Perales C, Perez-Luque R, Verdaguer N, Domingo E (2010) A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape. PLoS Pathog 6:e1001072
    • (2010) PLoS Pathog , vol.6 , pp. e1001072
    • Agudo, R.1    Ferrer-Orta, C.2    Arias, A.3    de la Higuera, I.4    Perales, C.5    Perez-Luque, R.6    Verdaguer, N.7    Domingo, E.8
  • 3
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire M, Chernaia MM, Malcolm BA, James MN (1994) Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369:72–76
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.4
  • 6
    • 70349540640 scopus 로고    scopus 로고
    • Structure and dynamics of the GH loop of the foot-and-mouth disease virus capsid
    • COI: 1:CAS:528:DC%2BD1MXht1WrtbnK
    • Azuma H, Yoneda S (2009) Structure and dynamics of the GH loop of the foot-and-mouth disease virus capsid. J Mol Graph Model 28:278–286
    • (2009) J Mol Graph Model , vol.28 , pp. 278-286
    • Azuma, H.1    Yoneda, S.2
  • 7
    • 0034777116 scopus 로고    scopus 로고
    • Interaction of picornavirus 2C polypeptide with the viral negative-strand RNA
    • COI: 1:CAS:528:DC%2BD3MXotlanur0%3D
    • Banerjee R, Dasgupta A (2001) Interaction of picornavirus 2C polypeptide with the viral negative-strand RNA. J Gen Virol 82:2621–2627
    • (2001) J Gen Virol , vol.82 , pp. 2621-2627
    • Banerjee, R.1    Dasgupta, A.2
  • 8
    • 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
    • COI: 1:CAS:528:DC%2BD3cXptlCksg%3D%3D
    • Baranowski E, Ruiz-Jarabo CM, Sevilla N, Andreu D, Beck E, Domingo E (2000) Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: flexibility in aphthovirus receptor usage. J Virol 74:1641–1647
    • (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
  • 9
    • 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 A resolution
    • COI: 1:CAS:528:DyaK2MXit1yjsrc%3D
    • Basavappa R, Syed R, Flore O, Icenogle JP, Filman DJ, Hogle JM (1994) Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution. Protein Sci 3:1651–1669
    • (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
  • 10
    • 0038364155 scopus 로고    scopus 로고
    • Viral internal ribosome entry site structures segregate into two distinct morphologies
    • COI: 1:CAS:528:DC%2BD3sXktV2nsb0%3D
    • Beales LP, Holzenburg A, Rowlands DJ (2003) Viral internal ribosome entry site structures segregate into two distinct morphologies. J Virol 77:6574–6579
    • (2003) J Virol , vol.77 , pp. 6574-6579
    • Beales, L.P.1    Holzenburg, A.2    Rowlands, D.J.3
  • 14
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • COI: 1:CAS:528:DC%2BD3cXkvVGm
    • Belsham GJ, McInerney GM, Ross-Smith N (2000) Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J Virol 74:272–280
    • (2000) J Virol , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 15
    • 10644274416 scopus 로고    scopus 로고
    • Translation and replication of FMDV RNA
    • COI: 1:CAS:528:DC%2BD2MXitVeksbc%3D
    • Belsham GJ (2005) Translation and replication of FMDV RNA. Curr Top Microbiol Immunol 288:43–70
    • (2005) Curr Top Microbiol Immunol , vol.288 , pp. 43-70
    • Belsham, G.J.1
  • 16
    • 84857069862 scopus 로고    scopus 로고
    • Formation of higher-order foot-and-mouth disease virus 3D(pol) complexes is dependent on elongation activity
    • COI: 1:CAS:528:DC%2BC38XitVKmtLk%3D
    • Bentham M, Holmes K, Forrest S, Rowlands DJ, Stonehouse NJ (2012) Formation of higher-order foot-and-mouth disease virus 3D(pol) complexes is dependent on elongation activity. J Virol 86:2371–2374
    • (2012) J Virol , vol.86 , pp. 2371-2374
    • Bentham, M.1    Holmes, K.2    Forrest, S.3    Rowlands, D.J.4    Stonehouse, N.J.5
  • 17
    • 64049110136 scopus 로고    scopus 로고
    • Human rhinovirus type 2 uncoating at the plasma membrane is not affected by a pH gradient but is affected by the membrane potential
    • COI: 1:CAS:528:DC%2BD1MXktlSisr0%3D
    • Berka U, Khan A, Blaas D, Fuchs R (2009) Human rhinovirus type 2 uncoating at the plasma membrane is not affected by a pH gradient but is affected by the membrane potential. J Virol 83:3778–3787
    • (2009) J Virol , vol.83 , pp. 3778-3787
    • Berka, U.1    Khan, A.2    Blaas, D.3    Fuchs, R.4
  • 18
    • 20744436958 scopus 로고    scopus 로고
    • Early events in integrin alphavbeta6-mediated cell entry of foot-and-mouth disease virus
    • COI: 1:CAS:528:DC%2BD2MXlslGisr0%3D
    • Berryman S, Clark S, Monaghan P, Jackson T (2005) Early events in integrin alphavbeta6-mediated cell entry of foot-and-mouth disease virus. J Virol 79:8519–8534
    • (2005) J Virol , vol.79 , pp. 8519-8534
    • Berryman, S.1    Clark, S.2    Monaghan, P.3    Jackson, T.4
  • 19
    • 84880681051 scopus 로고    scopus 로고
    • Positively charged residues at the five-fold symmetry axis of cell culture-adapted foot-and-mouth disease virus permit novel receptor interactions
    • COI: 1:CAS:528:DC%2BC3sXhtFCmtbnL
    • Berryman S, Clark S, Kakker NK, Silk R, Seago J, Wadsworth J, Chamberlain K, Knowles NJ, Jackson T (2013) Positively charged residues at the five-fold symmetry axis of cell culture-adapted foot-and-mouth disease virus permit novel receptor interactions. J Virol 87:8735–8744
    • (2013) J Virol , vol.87 , pp. 8735-8744
    • Berryman, S.1    Clark, S.2    Kakker, N.K.3    Silk, R.4    Seago, J.5    Wadsworth, J.6    Chamberlain, K.7    Knowles, N.J.8    Jackson, T.9
  • 20
    • 0025236535 scopus 로고
    • Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region
    • COI: 1:CAS:528:DyaK3cXitFekt7c%3D
    • Bienz K, Egger D, Troxler M, Pasamontes L (1990) Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region. J Virol 64:1156–1163
    • (1990) J Virol , vol.64 , pp. 1156-1163
    • Bienz, K.1    Egger, D.2    Troxler, M.3    Pasamontes, L.4
  • 21
    • 22844440428 scopus 로고    scopus 로고
    • Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy
    • Birtley JR, Curry S (2005) Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy. Acta Crystallogr Sect D Biol Crystallogr 61:646–650
    • (2005) Acta Crystallogr Sect D Biol Crystallogr , vol.61 , pp. 646-650
    • Birtley, J.R.1    Curry, S.2
  • 22
    • 15744372994 scopus 로고    scopus 로고
    • Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity
    • COI: 1:CAS:528:DC%2BD2MXisVyjtrw%3D
    • Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S (2005) Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity. J Biol Chem 280:11520–11527
    • (2005) J Biol Chem , vol.280 , pp. 11520-11527
    • Birtley, J.R.1    Knox, S.R.2    Jaulent, A.M.3    Brick, P.4    Leatherbarrow, R.J.5    Curry, S.6
  • 23
    • 36048987028 scopus 로고    scopus 로고
    • NMR solution structures of the apo and peptide-inhibited human rhinovirus 3C protease (Serotype 14): structural and dynamic comparison
    • COI: 1:CAS:528:DC%2BD2sXhtFOitbzP
    • Bjorndahl TC, Andrew LC, Semenchenko V, Wishart DS (2007) NMR solution structures of the apo and peptide-inhibited human rhinovirus 3C protease (Serotype 14): structural and dynamic comparison. Biochemistry 46:12945–12958
    • (2007) Biochemistry , vol.46 , pp. 12945-12958
    • Bjorndahl, T.C.1    Andrew, L.C.2    Semenchenko, V.3    Wishart, D.S.4
  • 24
    • 0029846866 scopus 로고    scopus 로고
    • Cleavage site analysis in picornaviral polyproteins: discovering cellular targets by neural networks
    • COI: 1:CAS:528:DyaK28XntVKqtLs%3D
    • Blom N, Hansen J, Blaas D, Brunak S (1996) Cleavage site analysis in picornaviral polyproteins: discovering cellular targets by neural networks. Protein Sci 5:2203–2216
    • (1996) Protein Sci , vol.5 , pp. 2203-2216
    • Blom, N.1    Hansen, J.2    Blaas, D.3    Brunak, S.4
  • 25
    • 0037405104 scopus 로고    scopus 로고
    • Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH
    • COI: 1:CAS:528:DC%2BD3sXjtFyrsr4%3D
    • Brabec M, Baravalle G, Blaas D, Fuchs R (2003) Conformational changes, plasma membrane penetration, and infection by human rhinovirus type 2: role of receptors and low pH. J Virol 77:5370–5377
    • (2003) J Virol , vol.77 , pp. 5370-5377
    • Brabec, M.1    Baravalle, G.2    Blaas, D.3    Fuchs, R.4
  • 26
    • 0012481667 scopus 로고
    • Dissociation of foot-and-mouth disease virus into its nucleic acid and protein components
    • COI: 1:CAS:528:DyaF38XktVKntrg%3D
    • Brown F, Cartwright B (1961) Dissociation of foot-and-mouth disease virus into its nucleic acid and protein components. Nature 192:1163–1164
    • (1961) Nature , vol.192 , pp. 1163-1164
    • Brown, F.1    Cartwright, B.2
  • 27
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • COI: 1:CAS:528:DC%2BD2MXkvFCmsLk%3D
    • Bubeck D, Filman DJ, Cheng N, Steven AC, Hogle JM, Belnap DM (2005) The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J Virol 79:7745–7755
    • (2005) J Virol , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3    Steven, A.C.4    Hogle, J.M.5    Belnap, D.M.6
  • 28
    • 33748929004 scopus 로고    scopus 로고
    • Specificity of the VP1 GH loop of foot-and-mouth disease virus for alphav integrins
    • COI: 1:CAS:528:DC%2BD28XhtVWgt7%2FL
    • Burman A, Clark S, Abrescia NG, Fry EE, Stuart DI, Jackson T (2006) Specificity of the VP1 GH loop of foot-and-mouth disease virus for alphav integrins. J Virol 80:9798–9810
    • (2006) J Virol , vol.80 , pp. 9798-9810
    • Burman, A.1    Clark, S.2    Abrescia, N.G.3    Fry, E.E.4    Stuart, D.I.5    Jackson, T.6
  • 29
    • 84892469578 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction shows poliovirus 135S particles poised for membrane interaction and RNA release
    • COI: 1:CAS:528:DC%2BC2cXlsVylsL8%3D
    • Butan C, Filman DJ, Hogle JM (2014) Cryo-electron microscopy reconstruction shows poliovirus 135S particles poised for membrane interaction and RNA release. J Virol 88:1758–1770
    • (2014) J Virol , vol.88 , pp. 1758-1770
    • Butan, C.1    Filman, D.J.2    Hogle, J.M.3
  • 30
    • 65449181209 scopus 로고    scopus 로고
    • Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
    • COI: 1:CAS:528:DC%2BD1MXltlChtLk%3D
    • Cao Y, Lu Z, Sun J, Bai X, Sun P, Bao H, Chen Y, Guo J, Li D, Liu X, Liu Z (2009) Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs. Veterinary Microbiol 137:10–17
    • (2009) Veterinary Microbiol , vol.137 , pp. 10-17
    • Cao, Y.1    Lu, Z.2    Sun, J.3    Bai, X.4    Sun, P.5    Bao, H.6    Chen, Y.7    Guo, J.8    Li, D.9    Liu, X.10    Liu, Z.11
  • 31
    • 0019226319 scopus 로고
    • Serological and immunological relations between the 146S and 12S particles of foot-and-mouth disease virus
    • COI: 1:STN:280:DyaL3M7hvV2isA%3D%3D
    • Cartwright B, Chapman WG, Brown F (1980) Serological and immunological relations between the 146S and 12S particles of foot-and-mouth disease virus. J Gen Virol 50:369–375
    • (1980) J Gen Virol , vol.50 , pp. 369-375
    • Cartwright, B.1    Chapman, W.G.2    Brown, F.3
  • 32
    • 34848832896 scopus 로고    scopus 로고
    • Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR
    • COI: 1:CAS:528:DC%2BD2sXhtFemtbbJ
    • Cencic R, Mayer C, Juliano MA, Juliano L, Konrat R, Kontaxis G, Skern T (2007) Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR. J Mol Biol 373:1071–1087
    • (2007) J Mol Biol , vol.373 , pp. 1071-1087
    • Cencic, R.1    Mayer, C.2    Juliano, M.A.3    Juliano, L.4    Konrat, R.5    Kontaxis, G.6    Skern, T.7
  • 33
    • 0024077613 scopus 로고
    • Processing and assembly of foot-and-mouth disease virus proteins using subgenomic RNA
    • COI: 1:CAS:528:DyaL1MXmtFSlsLg%3D
    • Clarke BE, Sangar DV (1988) Processing and assembly of foot-and-mouth disease virus proteins using subgenomic RNA. J Gen Virol 69(Pt 9):2313–2325
    • (1988) J Gen Virol , vol.69 , pp. 2313-2325
    • Clarke, B.E.1    Sangar, D.V.2
  • 34
    • 0028917761 scopus 로고
    • Viral RNA modulates the acid sensitivity of foot-and-mouth disease virus capsids
    • COI: 1:CAS:528:DyaK2MXislWrtb4%3D
    • Curry S, Abrams CC, Fry E, Crowther JC, Belsham GJ, Stuart DI, King AM (1995) Viral RNA modulates the acid sensitivity of foot-and-mouth disease virus capsids. J Virol 69:430–438
    • (1995) J Virol , vol.69 , pp. 430-438
    • Curry, S.1    Abrams, C.C.2    Fry, E.3    Crowther, J.C.4    Belsham, G.J.5    Stuart, D.I.6    King, A.M.7
  • 35
    • 0029643960 scopus 로고    scopus 로고
    • Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicity
    • COI: 1:CAS:528:DyaK28XhtlSiurc%3D
    • Curry S, Fry E, Blakemore W, Abu-Ghazaleh R, Jackson T, King A, Lea S, Newman J, Rowlands D, Stuart D (1996) Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicity. Structure 4:135–145
    • (1996) Structure , vol.4 , pp. 135-145
    • 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    Rowlands, D.9    Stuart, D.10
  • 36
    • 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
    • COI: 1:CAS:528:DyaK2sXnsVGnsLs%3D
    • Curry S, Fry E, Blakemore W, Abu-Ghazaleh R, Jackson T, King A, Lea S, Newman J, Stuart D (1997) 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 71:9743–9752
    • (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
  • 37
    • 34250837503 scopus 로고    scopus 로고
    • Structural analysis of foot-and-mouth disease virus 3C protease: a viable target for antiviral drugs?
    • COI: 1:CAS:528:DC%2BD2sXls1Snsb0%3D
    • Curry S, Roque-Rosell N, Sweeney TR, Zunszain PA, Leatherbarrow RJ (2007) Structural analysis of foot-and-mouth disease virus 3C protease: a viable target for antiviral drugs? Biochem Soc Trans 35:594–598
    • (2007) Biochem Soc Trans , vol.35 , pp. 594-598
    • Curry, S.1    Roque-Rosell, N.2    Sweeney, T.R.3    Zunszain, P.A.4    Leatherbarrow, R.J.5
  • 38
    • 33749649170 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target
    • COI: 1:CAS:528:DC%2BD28XhtVygt77M
    • Curry S, Roque-Rosell N, Zunszain PA, Leatherbarrow RJ (2007) Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target. Int J Biochem Cell Biol 39:1–6
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1-6
    • Curry, S.1    Roque-Rosell, N.2    Zunszain, P.A.3    Leatherbarrow, R.J.4
  • 40
    • 32444446676 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response
    • de Los Santos T, de Avila Botton S, Weiblen R, Grubman MJ (2006) The leader proteinase of foot-and-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response. J Virol 80:1906–1914
    • (2006) J Virol , vol.80 , pp. 1906-1914
    • de Los Santos, T.1    de Avila Botton, S.2    Weiblen, R.3    Grubman, M.J.4
  • 42
    • 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
    • COI: 1:CAS:528:DyaL1MXhvVek
    • Devaney MA, Vakharia VN, Lloyd RE, Ehrenfeld E, Grubman MJ (1988) Leader protein of foot-and-mouth disease virus is required for cleavage of the p220 component of the cap-binding protein complex. J Virol 62:4407–4409
    • (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
  • 44
    • 38349152810 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alphavbeta6: implications for infectiousness
    • COI: 1:CAS:528:DC%2BD1cXhtFOku78%3D
    • Dicara D, Burman A, Clark S, Berryman S, Howard MJ, Hart IR, Marshall JF, Jackson T (2008) Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alphavbeta6: implications for infectiousness. J Virol 82:1537–1546
    • (2008) J Virol , vol.82 , pp. 1537-1546
    • Dicara, D.1    Burman, A.2    Clark, S.3    Berryman, S.4    Howard, M.J.5    Hart, I.R.6    Marshall, J.F.7    Jackson, T.8
  • 46
    • 0032792102 scopus 로고    scopus 로고
    • Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids
    • COI: 1:CAS:528:DyaK1MXlt1aqtLc%3D
    • Ellard FM, Drew J, Blakemore WE, Stuart DI, King AM (1999) Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids. J Gen Virol 80(Pt 8):1911–1918
    • (1999) J Gen Virol , vol.80 , pp. 1911-1918
    • Ellard, F.M.1    Drew, J.2    Blakemore, W.E.3    Stuart, D.I.4    King, A.M.5
  • 47
    • 78650261546 scopus 로고    scopus 로고
    • Structural analysis provides insights into the modular organization of picornavirus IRES
    • COI: 1:CAS:528:DC%2BC3cXhsF2isL7L
    • Fernandez N, Garcia-Sacristan A, Ramajo J, Briones C, Martinez-Salas E (2011) Structural analysis provides insights into the modular organization of picornavirus IRES. Virology 409:251–261
    • (2011) Virology , vol.409 , pp. 251-261
    • Fernandez, N.1    Garcia-Sacristan, A.2    Ramajo, J.3    Briones, C.4    Martinez-Salas, E.5
  • 48
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
    • COI: 1:CAS:528:DC%2BD2cXptFejtrg%3D
    • Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N (2004) Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J Biol Chem 279:47212–47221
    • (2004) J Biol Chem , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 49
    • 33644519317 scopus 로고    scopus 로고
    • The structure of a protein primer-polymerase complex in the initiation of genome replication
    • COI: 1:CAS:528:DC%2BD28Xhs1ersLo%3D
    • Ferrer-Orta C, Arias A, Agudo R, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N (2006) The structure of a protein primer-polymerase complex in the initiation of genome replication. EMBO J 25:880–888
    • (2006) EMBO J , vol.25 , pp. 880-888
    • Ferrer-Orta, C.1    Arias, A.2    Agudo, R.3    Perez-Luque, R.4    Escarmis, C.5    Domingo, E.6    Verdaguer, N.7
  • 52
    • 70549097349 scopus 로고    scopus 로고
    • Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase
    • COI: 1:CAS:528:DC%2BD1MXhsV2gs77L
    • Ferrer-Orta C, Agudo R, Domingo E, Verdaguer N (2009) Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase. Curr Opin Struct Biol 19:752–758
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 752-758
    • Ferrer-Orta, C.1    Agudo, R.2    Domingo, E.3    Verdaguer, N.4
  • 54
    • 18944384457 scopus 로고    scopus 로고
    • The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions
    • COI: 1:CAS:528:DC%2BD2MXksFyrt7s%3D
    • Foeger N, Kuehnel E, Cencic R, Skern T (2005) The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions. FEBS J 272:2602–2611
    • (2005) FEBS J , vol.272 , pp. 2602-2611
    • Foeger, N.1    Kuehnel, E.2    Cencic, R.3    Skern, T.4
  • 56
    • 21444433508 scopus 로고    scopus 로고
    • Structure of Foot-and-mouth disease virus serotype A10 61 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation
    • COI: 1:CAS:528:DC%2BD2MXlvF2ruro%3D
    • Fry EE, Newman JW, Curry S, Najjam S, Jackson T, Blakemore W, Lea SM, Miller L, Burman A, King AM, Stuart DI (2005) Structure of Foot-and-mouth disease virus serotype A10 61 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation. J Gen Virol 86:1909–1920
    • (2005) J Gen Virol , vol.86 , pp. 1909-1920
    • Fry, E.E.1    Newman, J.W.2    Curry, S.3    Najjam, S.4    Jackson, T.5    Blakemore, W.6    Lea, S.M.7    Miller, L.8    Burman, A.9    King, A.M.10    Stuart, D.I.11
  • 57
    • 10644278809 scopus 로고    scopus 로고
    • The structure of foot-and-mouth disease virus
    • COI: 1:CAS:528:DC%2BD2MXitVektr4%3D
    • Fry EE, Stuart DI, Rowlands DJ (2005) The structure of foot-and-mouth disease virus. Curr Top Microbiol Immunol 288:71–101
    • (2005) Curr Top Microbiol Immunol , vol.288 , pp. 71-101
    • Fry, E.E.1    Stuart, D.I.2    Rowlands, D.J.3
  • 58
    • 77956625541 scopus 로고    scopus 로고
    • Uncoating of human rhinoviruses
    • COI: 1:CAS:528:DC%2BC3cXht1Ols7fL
    • Fuchs R, Blaas D (2010) Uncoating of human rhinoviruses. Rev Med Virol 20:281–297
    • (2010) Rev Med Virol , vol.20 , pp. 281-297
    • Fuchs, R.1    Blaas, D.2
  • 59
    • 84857488318 scopus 로고    scopus 로고
    • Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid
    • COI: 1:CAS:528:DC%2BC38XhtVyisLc%3D
    • Garriga D, Pickl-Herk A, Luque D, Wruss J, Caston JR, Blaas D, Verdaguer N (2012) Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid. PLoS Pathog 8:e1002473
    • (2012) PLoS Pathog , vol.8 , pp. e1002473
    • Garriga, D.1    Pickl-Herk, A.2    Luque, D.3    Wruss, J.4    Caston, J.R.5    Blaas, D.6    Verdaguer, N.7
  • 60
    • 0035929633 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus leader proteinase: involvement of C-terminal residues in self-processing and cleavage of eIF4GI
    • COI: 1:CAS:528:DC%2BD3MXntFahsrg%3D
    • Glaser W, Cencic R, Skern T (2001) Foot-and-mouth disease virus leader proteinase: involvement of C-terminal residues in self-processing and cleavage of eIF4GI. J Biol Chem 276:35473–35481
    • (2001) J Biol Chem , vol.276 , pp. 35473-35481
    • Glaser, W.1    Cencic, R.2    Skern, T.3
  • 61
    • 70350312842 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus assembly: processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner
    • COI: 1:CAS:528:DC%2BD1MXhsVSmtL%2FE
    • Goodwin S, Tuthill TJ, Arias A, Killington RA, Rowlands DJ (2009) Foot-and-mouth disease virus assembly: processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner. J Virol 83:11275–11282
    • (2009) J Virol , vol.83 , pp. 11275-11282
    • Goodwin, S.1    Tuthill, T.J.2    Arias, A.3    Killington, R.A.4    Rowlands, D.J.5
  • 62
    • 31144445870 scopus 로고    scopus 로고
    • Mechanisms of action of ribavirin against distinct viruses
    • COI: 1:CAS:528:DC%2BD28XhslWruro%3D
    • Graci JD, Cameron CE (2006) Mechanisms of action of ribavirin against distinct viruses. Rev Med Virol 16:37–48
    • (2006) Rev Med Virol , vol.16 , pp. 37-48
    • Graci, J.D.1    Cameron, C.E.2
  • 63
    • 1842457807 scopus 로고    scopus 로고
    • Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro
    • COI: 1:CAS:528:DC%2BD2cXis1KltrY%3D
    • Gradi A, Foeger N, Strong R, Svitkin YV, Sonenberg N, Skern T, Belsham GJ (2004) Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro. J Virol 78:3271–3278
    • (2004) J Virol , vol.78 , pp. 3271-3278
    • Gradi, A.1    Foeger, N.2    Strong, R.3    Svitkin, Y.V.4    Sonenberg, N.5    Skern, T.6    Belsham, G.J.7
  • 64
    • 2042459160 scopus 로고    scopus 로고
    • Foot-and-mouth disease
    • COI: 1:CAS:528:DC%2BD2cXktl2isrg%3D
    • Grubman MJ, Baxt B (2004) Foot-and-mouth disease. Clin Microbiol Rev 17:465–493
    • (2004) Clin Microbiol Rev , vol.17 , pp. 465-493
    • Grubman, M.J.1    Baxt, B.2
  • 65
    • 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
    • COI: 1:CAS:528:DyaK1MXksVCmtw%3D%3D
    • Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T (1998) Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition. EMBO J 17:7469–7479
    • (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
  • 66
    • 0034613018 scopus 로고    scopus 로고
    • Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes
    • COI: 1:CAS:528:DC%2BD3cXnsFGlu7g%3D
    • Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T (2000) Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes. J Mol Biol 302:1227–1240
    • (2000) J Mol Biol , vol.302 , pp. 1227-1240
    • Guarne, A.1    Hampoelz, B.2    Glaser, W.3    Carpena, X.4    Tormo, J.5    Fita, I.6    Skern, T.7
  • 67
    • 0002709844 scopus 로고    scopus 로고
    • Swiss-PdbViewer: a fast and easy-to-use PDB viewer for Macintosh and PC
    • Guex N, Peitsch MC (1996) Swiss-PdbViewer: a fast and easy-to-use PDB viewer for Macintosh and PC. Protein Data Bank Quarterly Newsletter 77
    • (1996) Protein Data Bank Quarterly Newsletter , pp. 77
    • Guex, N.1    Peitsch, M.C.2
  • 68
    • 84880173237 scopus 로고    scopus 로고
    • Assembly and characterization of foot-and-mouth disease virus empty capsid particles expressed within mammalian cells
    • COI: 1:CAS:528:DC%2BC3sXht12gs7vM
    • Gullberg M, Muszynski B, Organtini LJ, Ashley RE, Hafenstein SL, Belsham GJ, Polacek C (2013) Assembly and characterization of foot-and-mouth disease virus empty capsid particles expressed within mammalian cells. J Gen Virol 94:1769–1779
    • (2013) J Gen Virol , vol.94 , pp. 1769-1779
    • Gullberg, M.1    Muszynski, B.2    Organtini, L.J.3    Ashley, R.E.4    Hafenstein, S.L.5    Belsham, G.J.6    Polacek, C.7
  • 69
    • 84879815475 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus-like particles produced by a SUMO fusion protein system in Escherichia coli induce potent protective immune responses in guinea pigs, swine and cattle
    • COI: 1:CAS:528:DC%2BC3sXht1ersLbP
    • Guo HC, Sun SQ, Jin Y, Yang SL, Wei YQ, Sun DH, Yin SH, Ma JW, Liu ZX, Guo JH, Luo JX, Yin H, Liu XT, Liu DX (2013) Foot-and-mouth disease virus-like particles produced by a SUMO fusion protein system in Escherichia coli induce potent protective immune responses in guinea pigs, swine and cattle. Veterinary Res 44:48
    • (2013) Veterinary Res , vol.44 , pp. 48
    • Guo, H.C.1    Sun, S.Q.2    Jin, Y.3    Yang, S.L.4    Wei, Y.Q.5    Sun, D.H.6    Yin, S.H.7    Ma, J.W.8    Liu, Z.X.9    Guo, J.H.10    Luo, J.X.11    Yin, H.12    Liu, X.T.13    Liu, D.X.14
  • 70
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • COI: 1:CAS:528:DC%2BD38XovFCnsrk%3D
    • Hedstrom L (2002) Serine protease mechanism and specificity. Chem Rev 102:4501–4524
    • (2002) Chem Rev , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 72
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop
    • COI: 1:CAS:528:DyaK2sXislKmtb8%3D
    • Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI (1997) Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop. EMBO J 16:1492–1500
    • (1997) EMBO J , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brookes, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.I.10
  • 73
    • 0034010674 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin alpha5beta1: influence of the leucine residue within the RGDL motif on selectivity of integrin binding
    • COI: 1:CAS:528:DC%2BD3cXjtFWksL8%3D
    • Jackson T, Blakemore W, Newman JW, Knowles NJ, Mould AP, Humphries MJ, King AM (2000) Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin alpha5beta1: influence of the leucine residue within the RGDL motif on selectivity of integrin binding. J Gen Virol 81:1383–1391
    • (2000) J Gen Virol , vol.81 , pp. 1383-1391
    • Jackson, T.1    Blakemore, W.2    Newman, J.W.3    Knowles, N.J.4    Mould, A.P.5    Humphries, M.J.6    King, A.M.7
  • 74
    • 0033625053 scopus 로고    scopus 로고
    • The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus
    • COI: 1:CAS:528:DC%2BD3cXjsVKgtbs%3D
    • Jackson T, Sheppard D, Denyer M, Blakemore W, King AM (2000) The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus. J Virol 74:4949–4956
    • (2000) J Virol , vol.74 , pp. 4949-4956
    • Jackson, T.1    Sheppard, D.2    Denyer, M.3    Blakemore, W.4    King, A.M.5
  • 75
    • 0036007134 scopus 로고    scopus 로고
    • Integrin alphavbeta1 is a receptor for foot-and-mouth disease virus
    • COI: 1:CAS:528:DC%2BD38XnvFCntw%3D%3D
    • Jackson T, Mould AP, Sheppard D, King AM (2002) Integrin alphavbeta1 is a receptor for foot-and-mouth disease virus. J Virol 76:935–941
    • (2002) J Virol , vol.76 , pp. 935-941
    • Jackson, T.1    Mould, A.P.2    Sheppard, D.3    King, A.M.4
  • 76
    • 2442671781 scopus 로고    scopus 로고
    • Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infection
    • COI: 1:CAS:528:DC%2BD2cXjsVKisrw%3D
    • Jackson T, Clark S, Berryman S, Burman A, Cambier S, Mu D, Nishimura S, King AM (2004) Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infection. J Virol 78:4533–4540
    • (2004) J Virol , vol.78 , pp. 4533-4540
    • Jackson, T.1    Clark, S.2    Berryman, S.3    Burman, A.4    Cambier, S.5    Mu, D.6    Nishimura, S.7    King, A.M.8
  • 77
    • 84889032990 scopus 로고    scopus 로고
    • Foot-and-mouth disease: past, present and future
    • Jamal SM, Belsham GJ (2013) Foot-and-mouth disease: past, present and future. Veterinary Res 44:116
    • (2013) Veterinary Res , vol.44 , pp. 116
    • Jamal, S.M.1    Belsham, G.J.2
  • 78
    • 45749103230 scopus 로고    scopus 로고
    • The coming of age of virus-like particle vaccines
    • COI: 1:CAS:528:DC%2BD1cXls1ait78%3D
    • Jennings GT, Bachmann MF (2008) The coming of age of virus-like particle vaccines. Biol Chem 389:521–536
    • (2008) Biol Chem , vol.389 , pp. 521-536
    • Jennings, G.T.1    Bachmann, M.F.2
  • 79
    • 0034036079 scopus 로고    scopus 로고
    • Structures of virus and virus-like particles
    • COI: 1:CAS:528:DC%2BD3cXivFWgtb8%3D
    • Johnson JE, Chiu W (2000) Structures of virus and virus-like particles. Curr Opin Struct Biol 10:229–235
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 229-235
    • Johnson, J.E.1    Chiu, W.2
  • 80
    • 84873689836 scopus 로고    scopus 로고
    • Candidate RNA structures for domain 3 of the foot-and-mouth-disease virus internal ribosome entry site
    • COI: 1:CAS:528:DC%2BC3sXhvV2mt7g%3D
    • Jung S, Schlick T (2013) Candidate RNA structures for domain 3 of the foot-and-mouth-disease virus internal ribosome entry site. Nucleic Acids Res 41:1483–1495
    • (2013) Nucleic Acids Res , vol.41 , pp. 1483-1495
    • Jung, S.1    Schlick, T.2
  • 81
    • 0025875756 scopus 로고
    • Proteoglycans: structures and interactions
    • COI: 1:CAS:528:DyaK3MXlsFeitLg%3D
    • Kjellen L, Lindahl U (1991) Proteoglycans: structures and interactions. Annu Rev Biochem 60:443–475
    • (1991) Annu Rev Biochem , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 82
    • 0032699505 scopus 로고    scopus 로고
    • Echovirus 9 strain barty non-structural protein 2C has NTPase activity
    • COI: 1:CAS:528:DyaK1MXns1agsbk%3D
    • Klein M, Eggers HJ, Nelsen-Salz B (1999) Echovirus 9 strain barty non-structural protein 2C has NTPase activity. Virus Res 65:155–160
    • (1999) Virus Res , vol.65 , pp. 155-160
    • Klein, M.1    Eggers, H.J.2    Nelsen-Salz, B.3
  • 84
    • 0029644937 scopus 로고
    • Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67
    • COI: 1:CAS:528:DyaK2MXmvVyrsrc%3D
    • Lea S, Abu-Ghazaleh R, Blakemore W, Curry S, Fry E, Jackson T, King A, Logan D, Newman J, Stuart D (1995) Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67. Structure 3:571–580
    • (1995) Structure , vol.3 , pp. 571-580
    • Lea, S.1    Abu-Ghazaleh, R.2    Blakemore, W.3    Curry, S.4    Fry, E.5    Jackson, T.6    King, A.7    Logan, D.8    Newman, J.9    Stuart, D.10
  • 85
    • 84869214041 scopus 로고    scopus 로고
    • In vitro assembly of an empty picornavirus capsid follows a dodecahedral path
    • COI: 1:CAS:528:DC%2BC38Xhs1yksb%2FM
    • Li C, Wang JC, Taylor MW, Zlotnick A (2012) In vitro assembly of an empty picornavirus capsid follows a dodecahedral path. J Virol 86:13062–13069
    • (2012) J Virol , vol.86 , pp. 13062-13069
    • Li, C.1    Wang, J.C.2    Taylor, M.W.3    Zlotnick, A.4
  • 86
    • 0035913956 scopus 로고    scopus 로고
    • Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot-and-mouth disease virus 3C protease: identification of the eIF4AI cleavage site
    • COI: 1:CAS:528:DC%2BD3MXnslWrtrw%3D
    • Li W, Ross-Smith N, Proud CG, Belsham GJ (2001) Cleavage of translation initiation factor 4AI (eIF4AI) but not eIF4AII by foot-and-mouth disease virus 3C protease: identification of the eIF4AI cleavage site. FEBS Lett 507:1–5
    • (2001) FEBS Lett , vol.507 , pp. 1-5
    • Li, W.1    Ross-Smith, N.2    Proud, C.G.3    Belsham, G.J.4
  • 87
    • 79952083641 scopus 로고    scopus 로고
    • FMD subunit vaccine produced using a silkworm-baculovirus expression system: protective efficacy against two type Asia1 isolates in cattle
    • COI: 1:CAS:528:DC%2BC3MXjs12itLg%3D
    • Li Z, Yin X, Yi Y, Li X, Li B, Lan X, Zhang Z, Liu J (2011) FMD subunit vaccine produced using a silkworm-baculovirus expression system: protective efficacy against two type Asia1 isolates in cattle. Veterinary Microbiol 149:99–103
    • (2011) Veterinary Microbiol , vol.149 , pp. 99-103
    • Li, Z.1    Yin, X.2    Yi, Y.3    Li, X.4    Li, B.5    Lan, X.6    Zhang, Z.7    Liu, J.8
  • 90
    • 0037109209 scopus 로고    scopus 로고
    • IRES-driven translation is stimulated separately by the FMDV 3′-NCR and poly(A) sequences
    • COI: 1:CAS:528:DC%2BD38Xot1Cju7s%3D
    • Lopez de Quinto S, Saiz M, de la Morena D, Sobrino F, Martinez-Salas E (2002) IRES-driven translation is stimulated separately by the FMDV 3′-NCR and poly(A) sequences. Nucleic Acids Res 30:4398–4405
    • (2002) Nucleic Acids Res , vol.30 , pp. 4398-4405
    • Lopez de Quinto, S.1    Saiz, M.2    de la Morena, D.3    Sobrino, F.4    Martinez-Salas, E.5
  • 91
    • 80054000375 scopus 로고    scopus 로고
    • Enterovirus 71 and coxsackievirus A16 3C proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design
    • COI: 1:CAS:528:DC%2BC3MXhtlWiurvI
    • Lu G, Qi J, Chen Z, Xu X, Gao F, Lin D, Qian W, Liu H, Jiang H, Yan J, Gao GF (2011) Enterovirus 71 and coxsackievirus A16 3C proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design. J Virol 85:10319–10331
    • (2011) J Virol , vol.85 , pp. 10319-10331
    • Lu, G.1    Qi, J.2    Chen, Z.3    Xu, X.4    Gao, F.5    Lin, D.6    Qian, W.7    Liu, H.8    Jiang, H.9    Yan, J.10    Gao, G.F.11
  • 92
    • 62849083315 scopus 로고    scopus 로고
    • Protection of guinea pigs and swine by a recombinant adenovirus expressing O serotype of foot-and-mouth disease virus whole capsid and 3C protease
    • COI: 1:CAS:528:DC%2BD1cXhsVKls7nI
    • Lu Z, Bao H, Cao Y, Sun P, Guo J, Li P, Bai X, Chen Y, Xie B, Li D, Liu Z, Xie Q (2008) Protection of guinea pigs and swine by a recombinant adenovirus expressing O serotype of foot-and-mouth disease virus whole capsid and 3C protease. Vaccine 26(Suppl 6):G48–53
    • (2008) Vaccine , vol.26 , pp. G48-G53
    • Lu, Z.1    Bao, H.2    Cao, Y.3    Sun, P.4    Guo, J.5    Li, P.6    Bai, X.7    Chen, Y.8    Xie, B.9    Li, D.10    Liu, Z.11    Xie, Q.12
  • 93
    • 84878071509 scopus 로고    scopus 로고
    • Analysis of SAT type foot-and-mouth disease virus capsid proteins and the identification of putative amino acid residues affecting virus stability
    • Maree FF, Blignaut B, de Beer TA, Rieder E (2013) Analysis of SAT type foot-and-mouth disease virus capsid proteins and the identification of putative amino acid residues affecting virus stability. PLoS ONE 8:e61612
    • (2013) PLoS ONE , vol.8 , pp. e61612
    • Maree, F.F.1    Blignaut, B.2    de Beer, T.A.3    Rieder, E.4
  • 94
    • 35648989044 scopus 로고    scopus 로고
    • Productive entry of type C foot-and-mouth disease virus into susceptible cultured cells requires clathrin and is dependent on the presence of plasma membrane cholesterol
    • COI: 1:CAS:528:DC%2BD2sXht1Krsr%2FK
    • Martin-Acebes MA, Gonzalez-Magaldi M, Sandvig K, Sobrino F, Armas-Portela R (2007) Productive entry of type C foot-and-mouth disease virus into susceptible cultured cells requires clathrin and is dependent on the presence of plasma membrane cholesterol. Virology 369:105–118
    • (2007) Virology , vol.369 , pp. 105-118
    • Martin-Acebes, M.A.1    Gonzalez-Magaldi, M.2    Sandvig, K.3    Sobrino, F.4    Armas-Portela, R.5
  • 95
    • 77649155795 scopus 로고    scopus 로고
    • A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition
    • COI: 1:CAS:528:DC%2BC3cXjt1eisL4%3D
    • Martin-Acebes MA, Rincon V, Armas-Portela R, Mateu MG, Sobrino F (2010) A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid lability and confer resistance to acid-dependent uncoating inhibition. J Virol 84:2902–2912
    • (2010) J Virol , vol.84 , pp. 2902-2912
    • Martin-Acebes, M.A.1    Rincon, V.2    Armas-Portela, R.3    Mateu, M.G.4    Sobrino, F.5
  • 96
    • 79952407319 scopus 로고    scopus 로고
    • A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance
    • COI: 1:CAS:528:DC%2BC3MXhtVWks7rN
    • Martin-Acebes MA, Vazquez-Calvo A, Rincon V, Mateu MG, Sobrino F (2011) A single amino acid substitution in the capsid of foot-and-mouth disease virus can increase acid resistance. J Virol 85:2733–2740
    • (2011) J Virol , vol.85 , pp. 2733-2740
    • Martin-Acebes, M.A.1    Vazquez-Calvo, A.2    Rincon, V.3    Mateu, M.G.4    Sobrino, F.5
  • 97
    • 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
    • COI: 1:CAS:528:DyaK2sXktF2rur8%3D
    • Martinez MA, Verdaguer N, Mateu MG, Domingo E (1997) 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 94:6798–6802
    • (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
  • 98
    • 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
    • COI: 1:CAS:528:DyaK2cXjtF2isL0%3D
    • Mason PW, Rieder E, Baxt B (1994) 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 91:1932–1936
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1932-1936
    • Mason, P.W.1    Rieder, E.2    Baxt, B.3
  • 99
    • 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
    • COI: 1:CAS:528:DC%2BD38XntFGks78%3D
    • Mason PW, Bezborodova SV, Henry TM (2002) 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 76:9686–9694
    • (2002) J Virol , vol.76 , pp. 9686-9694
    • Mason, P.W.1    Bezborodova, S.V.2    Henry, T.M.3
  • 100
    • 0037232731 scopus 로고    scopus 로고
    • Molecular basis of pathogenesis of FMDV
    • COI: 1:CAS:528:DC%2BD3sXjtF2ntg%3D%3D
    • Mason PW, Grubman MJ, Baxt B (2003) Molecular basis of pathogenesis of FMDV. Virus Res 91:9–32
    • (2003) Virus Res , vol.91 , pp. 9-32
    • Mason, P.W.1    Grubman, M.J.2    Baxt, B.3
  • 101
    • 57349125715 scopus 로고    scopus 로고
    • Engineering viable foot-and-mouth disease viruses with increased thermostability as a step in the development of improved vaccines
    • COI: 1:CAS:528:DC%2BD1cXhsVymsL%2FI
    • Mateo R, Luna E, Rincon V, Mateu MG (2008) Engineering viable foot-and-mouth disease viruses with increased thermostability as a step in the development of improved vaccines. J Virol 82:12232–12240
    • (2008) J Virol , vol.82 , pp. 12232-12240
    • Mateo, R.1    Luna, E.2    Rincon, V.3    Mateu, M.G.4
  • 102
    • 0029972140 scopus 로고    scopus 로고
    • Systematic replacement of amino acid residues within an Arg-Gly-Asp-containing loop of foot-and-mouth disease virus and effect on cell recognition
    • COI: 1:CAS:528:DyaK28XjtlGjtLc%3D
    • Mateu MG, Valero ML, Andreu D, Domingo E (1996) Systematic replacement of amino acid residues within an Arg-Gly-Asp-containing loop of foot-and-mouth disease virus and effect on cell recognition. J Biol Chem 271:12814–12819
    • (1996) J Biol Chem , vol.271 , pp. 12814-12819
    • Mateu, M.G.1    Valero, M.L.2    Andreu, D.3    Domingo, E.4
  • 104
    • 42449117554 scopus 로고    scopus 로고
    • Residue L143 of the foot-and-mouth disease virus leader proteinase is a determinant of cleavage specificity
    • COI: 1:CAS:528:DC%2BD1cXltVOmtbc%3D
    • Mayer C, Neubauer D, Nchinda AT, Cencic R, Trompf K, Skern T (2008) Residue L143 of the foot-and-mouth disease virus leader proteinase is a determinant of cleavage specificity. J Virol 82:4656–4659
    • (2008) J Virol , vol.82 , pp. 4656-4659
    • Mayer, C.1    Neubauer, D.2    Nchinda, A.T.3    Cencic, R.4    Trompf, K.5    Skern, T.6
  • 105
    • 0035047433 scopus 로고    scopus 로고
    • Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virus
    • COI: 1:CAS:528:DC%2BD3MXivFOkt78%3D
    • Miller LC, Blakemore W, Sheppard D, Atakilit A, King AM, Jackson T (2001) Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virus. J Virol 75:4158–4164
    • (2001) J Virol , vol.75 , pp. 4158-4164
    • Miller, L.C.1    Blakemore, W.2    Sheppard, D.3    Atakilit, A.4    King, A.M.5    Jackson, T.6
  • 106
    • 0025773025 scopus 로고
    • Myristoylation is important at multiple stages in poliovirus assembly
    • COI: 1:CAS:528:DyaK3MXit1Gnurc%3D
    • Moscufo N, Simons J, Chow M (1991) Myristoylation is important at multiple stages in poliovirus assembly. J Virol 65:2372–2380
    • (1991) J Virol , vol.65 , pp. 2372-2380
    • Moscufo, N.1    Simons, J.2    Chow, M.3
  • 107
    • 33748943522 scopus 로고    scopus 로고
    • Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication
    • COI: 1:CAS:528:DC%2BD28XhtVWgt7zI
    • Nayak A, Goodfellow IG, Woolaway KE, Birtley J, Curry S, Belsham GJ (2006) Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. J Virol 80:9865–9875
    • (2006) J Virol , vol.80 , pp. 9865-9875
    • Nayak, A.1    Goodfellow, I.G.2    Woolaway, K.E.3    Birtley, J.4    Curry, S.5    Belsham, G.J.6
  • 108
    • 2642681650 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus virulent for cattle utilizes the integrin alpha(v)beta3 as its receptor
    • COI: 1:CAS:528:DyaK1cXis1Khsrk%3D
    • Neff S, Sa-Carvalho D, Rieder E, Mason PW, Blystone SD, Brown EJ, Baxt B (1998) Foot-and-mouth disease virus virulent for cattle utilizes the integrin alpha(v)beta3 as its receptor. J Virol 72:3587–3594
    • (1998) J Virol , vol.72 , pp. 3587-3594
    • Neff, S.1    Sa-Carvalho, D.2    Rieder, E.3    Mason, P.W.4    Blystone, S.D.5    Brown, E.J.6    Baxt, B.7
  • 110
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • COI: 1:CAS:528:DyaK1cXotFSksLs%3D
    • Nugent CI, Johnson KL, Sarnow P, Kirkegaard K (1999) Functional coupling between replication and packaging of poliovirus replicon RNA. J Virol 73:427–435
    • (1999) J Virol , vol.73 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 111
    • 0242331746 scopus 로고    scopus 로고
    • Receptor priming of major group human rhinoviruses for uncoating and entry at mild low-pH environments
    • COI: 1:CAS:528:DC%2BD3sXovVansb0%3D
    • Nurani G, Lindqvist B, Casasnovas JM (2003) Receptor priming of major group human rhinoviruses for uncoating and entry at mild low-pH environments. J Virol 77:11985–11991
    • (2003) J Virol , vol.77 , pp. 11985-11991
    • Nurani, G.1    Lindqvist, B.2    Casasnovas, J.M.3
  • 112
    • 20744438160 scopus 로고    scopus 로고
    • Analysis of foot-and-mouth disease virus internalization events in cultured cells
    • O’Donnell V, LaRocco M, Duque H, Baxt B (2005) Analysis of foot-and-mouth disease virus internalization events in cultured cells. J Virol 79:8506–8518
    • (2005) J Virol , vol.79 , pp. 8506-8518
    • O’Donnell, V.1    LaRocco, M.2    Duque, H.3    Baxt, B.4
  • 113
    • 50949121523 scopus 로고    scopus 로고
    • Heparan sulfate-binding foot-and-mouth disease virus enters cells via caveola-mediated endocytosis
    • O’Donnell V, Larocco M, Baxt B (2008) Heparan sulfate-binding foot-and-mouth disease virus enters cells via caveola-mediated endocytosis. J Virol 82:9075–9085
    • (2008) J Virol , vol.82 , pp. 9075-9085
    • O’Donnell, V.1    Larocco, M.2    Baxt, B.3
  • 114
    • 20444422895 scopus 로고    scopus 로고
    • Rapid protection of cattle from direct challenge with foot-and-mouth disease virus (FMDV) by a single inoculation with an adenovirus-vectored FMDV subunit vaccine
    • COI: 1:CAS:528:DC%2BD2MXltFCmu7k%3D
    • Pacheco JM, Brum MC, Moraes MP, Golde WT, Grubman MJ (2005) Rapid protection of cattle from direct challenge with foot-and-mouth disease virus (FMDV) by a single inoculation with an adenovirus-vectored FMDV subunit vaccine. Virology 337:205–209
    • (2005) Virology , vol.337 , pp. 205-209
    • Pacheco, J.M.1    Brum, M.C.2    Moraes, M.P.3    Golde, W.T.4    Grubman, M.J.5
  • 115
    • 11844282166 scopus 로고    scopus 로고
    • Metabolism and antiviral activity of ribavirin
    • COI: 1:CAS:528:DC%2BD2MXkvFeisg%3D%3D
    • Parker WB (2005) Metabolism and antiviral activity of ribavirin. Virus Res 107:165–171
    • (2005) Virus Res , vol.107 , pp. 165-171
    • Parker, W.B.1
  • 117
    • 0030089428 scopus 로고    scopus 로고
    • The solution structure of the immunodominant and cell receptor binding regions of foot-and-mouth disease virus serotype A, variant A
    • COI: 1:CAS:528:DyaK28Xit1aru7w%3D
    • Pegna M, Molinari H, Zetta L, Gibbons WA, Brown F, Rowlands D, Siligardi G, Mascagni P (1996) The solution structure of the immunodominant and cell receptor binding regions of foot-and-mouth disease virus serotype A, variant A. J Peptide Sci 2:75–90
    • (1996) J Peptide Sci , vol.2 , pp. 75-90
    • Pegna, M.1    Molinari, H.2    Zetta, L.3    Gibbons, W.A.4    Brown, F.5    Rowlands, D.6    Siligardi, G.7    Mascagni, P.8
  • 118
    • 0033525205 scopus 로고    scopus 로고
    • Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide
    • COI: 1:CAS:528:DyaK1MXhtVemtrY%3D
    • Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S (1999) Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide. J Biol Chem 274:3686–3692
    • (1999) J Biol Chem , vol.274 , pp. 3686-3692
    • Petit, M.C.1    Benkirane, N.2    Guichard, G.3    Du, A.P.4    Marraud, M.5    Cung, M.T.6    Briand, J.P.7    Muller, S.8
  • 119
    • 64249093351 scopus 로고    scopus 로고
    • Molecular characterization of a foot-and-mouth disease virus containing a 57-nucleotide insertion in the 3′ untranslated region
    • COI: 1:CAS:528:DC%2BD1MXktV2gsb8%3D
    • Piccone ME, Pauszek S, Pacheco J, Rieder E, Kramer E, Rodriguez LL (2009) Molecular characterization of a foot-and-mouth disease virus containing a 57-nucleotide insertion in the 3′ untranslated region. Arch Virol 154:671–676
    • (2009) Arch Virol , vol.154 , pp. 671-676
    • Piccone, M.E.1    Pauszek, S.2    Pacheco, J.3    Rieder, E.4    Kramer, E.5    Rodriguez, L.L.6
  • 122
    • 1542267838 scopus 로고    scopus 로고
    • Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid
    • COI: 1:CAS:528:DC%2BD2cXitlWiu7o%3D
    • Reguera J, Carreira A, Riolobos L, Almendral JM, Mateu MG (2004) Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid. Proc Natl Acad Sci USA 101:2724–2729
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2724-2729
    • Reguera, J.1    Carreira, A.2    Riolobos, L.3    Almendral, J.M.4    Mateu, M.G.5
  • 123
    • 0029841919 scopus 로고    scopus 로고
    • Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus
    • COI: 1:CAS:528:DyaK28XlslGrsr8%3D
    • Rieder E, Berinstein A, Baxt B, Kang A, Mason PW (1996) Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus. Proc Natl Acad Sci USA 93:10428–10433
    • (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
  • 124
    • 0027537974 scopus 로고
    • Poliovirus protein 2C has ATPase and GTPase activities
    • COI: 1:CAS:528:DyaK3sXisFWitLs%3D
    • Rodriguez PL, Carrasco L (1993) Poliovirus protein 2C has ATPase and GTPase activities. J Biol Chem 268:8105–8110
    • (1993) J Biol Chem , vol.268 , pp. 8105-8110
    • Rodriguez, P.L.1    Carrasco, L.2
  • 125
    • 64049103834 scopus 로고    scopus 로고
    • Attenuated foot-and-mouth disease virus RNA carrying a deletion in the 3′ noncoding region can elicit immunity in swine
    • Rodriguez Pulido M, Sobrino F, Borrego B, Saiz M (2009) Attenuated foot-and-mouth disease virus RNA carrying a deletion in the 3′ noncoding region can elicit immunity in swine. J Virol 83:3475–3485
    • (2009) J Virol , vol.83 , pp. 3475-3485
    • Rodriguez Pulido, M.1    Sobrino, F.2    Borrego, B.3    Saiz, M.4
  • 126
    • 0021269982 scopus 로고
    • Systematic nomenclature of picornavirus proteins
    • COI: 1:CAS:528:DyaL2cXks1yqtL8%3D
    • Rueckert RR, Wimmer E (1984) Systematic nomenclature of picornavirus proteins. J Virol 50:957–959
    • (1984) J Virol , vol.50 , pp. 957-959
    • Rueckert, R.R.1    Wimmer, E.2
  • 127
    • 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
    • COI: 1:CAS:528:DyaK2sXjvVGqt7o%3D
    • Sa-Carvalho D, Rieder E, Baxt B, Rodarte R, Tanuri A, Mason PW (1997) Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle. J Virol 71:5115–5123
    • (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
  • 128
    • 0035170571 scopus 로고    scopus 로고
    • Deletion or substitution of the aphthovirus 3′ NCR abrogates infectivity and virus replication
    • COI: 1:CAS:528:DC%2BD3MXjtVGhug%3D%3D
    • Saiz M, Gomez S, Martinez-Salas E, Sobrino F (2001) Deletion or substitution of the aphthovirus 3′ NCR abrogates infectivity and virus replication. J Gen Virol 82:93–101
    • (2001) J Gen Virol , vol.82 , pp. 93-101
    • Saiz, M.1    Gomez, S.2    Martinez-Salas, E.3    Sobrino, F.4
  • 129
    • 30344446267 scopus 로고    scopus 로고
    • ATP hydrolysis and AMP kinase activities of nonstructural protein 2C of human parechovirus 1
    • COI: 1:CAS:528:DC%2BD28XivVyisw%3D%3D
    • Samuilova O, Krogerus C, Fabrichniy I, Hyypia T (2006) ATP hydrolysis and AMP kinase activities of nonstructural protein 2C of human parechovirus 1. J Virol 80:1053–1058
    • (2006) J Virol , vol.80 , pp. 1053-1058
    • Samuilova, O.1    Krogerus, C.2    Fabrichniy, I.3    Hyypia, T.4
  • 130
    • 84874058889 scopus 로고    scopus 로고
    • Virus-like particles produced in plants as potential vaccines
    • COI: 1:CAS:528:DC%2BC3sXis1Cjtb0%3D
    • Scotti N, Rybicki EP (2013) Virus-like particles produced in plants as potential vaccines. Expert Rev Vaccines 12:211–224
    • (2013) Expert Rev Vaccines , vol.12 , pp. 211-224
    • Scotti, N.1    Rybicki, E.P.2
  • 132
    • 33749069918 scopus 로고    scopus 로고
    • The 3′ end of the foot-and-mouth disease virus genome establishes two distinct long-range RNA-RNA interactions with the 5′ end region
    • COI: 1:CAS:528:DC%2BD28XhtVGlsLnE
    • Serrano P, Pulido MR, Saiz M, Martinez-Salas E (2006) The 3′ end of the foot-and-mouth disease virus genome establishes two distinct long-range RNA-RNA interactions with the 5′ end region. J Gen Virol 87:3013–3022
    • (2006) J Gen Virol , vol.87 , pp. 3013-3022
    • Serrano, P.1    Pulido, M.R.2    Saiz, M.3    Martinez-Salas, E.4
  • 133
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • COI: 1:CAS:528:DC%2BD2sXhtVehtb7M
    • Singleton MR, Dillingham MS, Wigley DB (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu Rev Biochem 76:23–50
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 134
    • 33845759346 scopus 로고    scopus 로고
    • Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis
    • COI: 1:CAS:528:DC%2BD28XhtlCgu7rI
    • Sweeney TR, Roque-Rosell N, Birtley JR, Leatherbarrow RJ, Curry S (2007) Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis. J Virol 81:115–124
    • (2007) J Virol , vol.81 , pp. 115-124
    • Sweeney, T.R.1    Roque-Rosell, N.2    Birtley, J.R.3    Leatherbarrow, R.J.4    Curry, S.5
  • 135
    • 77955294379 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a coordinated ATP hydrolysis mechanism
    • COI: 1:CAS:528:DC%2BC3cXpsFemsro%3D
    • Sweeney TR, Cisnetto V, Bose D, Bailey M, Wilson JR, Zhang X, Belsham GJ, Curry S (2010) Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a coordinated ATP hydrolysis mechanism. J Biol Chem 285:24347–24359
    • (2010) J Biol Chem , vol.285 , pp. 24347-24359
    • Sweeney, T.R.1    Cisnetto, V.2    Bose, D.3    Bailey, M.4    Wilson, J.R.5    Zhang, X.6    Belsham, G.J.7    Curry, S.8
  • 136
    • 30044452234 scopus 로고    scopus 로고
    • Testing the modularity of the N-terminal amphipathic helix conserved in picornavirus 2C proteins and hepatitis C NS5A protein
    • COI: 1:CAS:528:DC%2BD28XhvFKisA%3D%3D
    • Teterina NL, Gorbalenya AE, Egger D, Bienz K, Rinaudo MS, Ehrenfeld E (2006) Testing the modularity of the N-terminal amphipathic helix conserved in picornavirus 2C proteins and hepatitis C NS5A protein. Virology 344:453–467
    • (2006) Virology , vol.344 , pp. 453-467
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Rinaudo, M.S.5    Ehrenfeld, E.6
  • 137
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • COI: 1:CAS:528:DC%2BD2cXntFCnsrY%3D
    • Thompson AA, Peersen OB (2004) Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J 23:3462–3471
    • (2004) EMBO J , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 139
    • 0023197987 scopus 로고
    • Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts
    • COI: 1:CAS:528:DyaL1cXht1Kqsr0%3D
    • Vakharia VN, Devaney MA, Moore DM, Dunn JJ, Grubman MJ (1987) Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts. J Virol 61:3199–3207
    • (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
  • 140
    • 0032536161 scopus 로고    scopus 로고
    • Titration calculations of foot-and-mouth disease virus capsids and their stabilities as a function of pH
    • van Vlijmen HW, Curry S, Schaefer M, Karplus M (1998) Titration calculations of foot-and-mouth disease virus capsids and their stabilities as a function of pH. J Mol Biol 275:295–308
    • (1998) J Mol Biol , vol.275 , pp. 295-308
    • van Vlijmen, H.W.1    Curry, S.2    Schaefer, M.3    Karplus, M.4
  • 141
    • 0029019739 scopus 로고
    • Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction
    • COI: 1:CAS:528:DyaK2MXlsl2gsbY%3D
    • Verdaguer N, Mateu MG, Andreu D, Giralt E, Domingo E, Fita I (1995) Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction. EMBO J 14:1690–1696
    • (1995) EMBO J , vol.14 , pp. 1690-1696
    • Verdaguer, N.1    Mateu, M.G.2    Andreu, D.3    Giralt, E.4    Domingo, E.5    Fita, I.6
  • 142
    • 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
    • COI: 1:CAS:528:DyaK28Xht1Snsro%3D
    • Verdaguer N, Mateu MG, Bravo J, Domingo E, Fita I (1996) Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease virus. J Mol Biol 256:364–376
    • (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
  • 143
    • 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
    • COI: 1:CAS:528:DyaK1cXhvFegtA%3D%3D
    • Verdaguer N, Sevilla N, Valero ML, Stuart D, Brocchi E, Andreu D, Giralt E, Domingo E, Mateu MG, Fita I (1998) 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 72:739–748
    • (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
  • 144
    • 0033558734 scopus 로고    scopus 로고
    • Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation
    • COI: 1:CAS:528:DyaK1MXhsFGltr0%3D
    • Verdaguer N, Schoehn G, Ochoa WF, Fita I, Brookes S, King A, Domingo E, Mateu MG, Stuart D, Hewat EA (1999) Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation. Virology 255:260–268
    • (1999) Virology , vol.255 , pp. 260-268
    • Verdaguer, N.1    Schoehn, G.2    Ochoa, W.F.3    Fita, I.4    Brookes, S.5    King, A.6    Domingo, E.7    Mateu, M.G.8    Stuart, D.9    Hewat, E.A.10
  • 145
    • 0033766542 scopus 로고    scopus 로고
    • Cell-free synthesis of poliovirus: 14S subunits are the key intermediates in the encapsidation of poliovirus RNA
    • COI: 1:CAS:528:DC%2BD3cXnvFWgu7o%3D
    • Verlinden Y, Cuconati A, Wimmer E, Rombaut B (2000) Cell-free synthesis of poliovirus: 14S subunits are the key intermediates in the encapsidation of poliovirus RNA. J Gen Virol 81:2751–2754
    • (2000) J Gen Virol , vol.81 , pp. 2751-2754
    • Verlinden, Y.1    Cuconati, A.2    Wimmer, E.3    Rombaut, B.4
  • 146
    • 0035945235 scopus 로고    scopus 로고
    • Conserved RNA secondary structures in Picornaviridae genomes
    • COI: 1:CAS:528:DC%2BD38Xmslahuw%3D%3D
    • Witwer C, Rauscher S, Hofacker IL, Stadler PF (2001) Conserved RNA secondary structures in Picornaviridae genomes. Nucleic acids Res 29:5079–5089
    • (2001) Nucleic acids Res , vol.29 , pp. 5079-5089
    • Witwer, C.1    Rauscher, S.2    Hofacker, I.L.3    Stadler, P.F.4
  • 147
    • 79952537148 scopus 로고    scopus 로고
    • Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-foot-and-mouth disease pandemic in China
    • COI: 1:CAS:528:DC%2BC3cXoslelurw%3D
    • Wu Y, Lou Z, Miao Y, Yu Y, Dong H, Peng W, Bartlam M, Li X, Rao Z (2010) Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-foot-and-mouth disease pandemic in China. Protein Cell 1:491–500
    • (2010) Protein Cell , vol.1 , pp. 491-500
    • Wu, Y.1    Lou, Z.2    Miao, Y.3    Yu, Y.4    Dong, H.5    Peng, W.6    Bartlam, M.7    Li, X.8    Rao, Z.9
  • 148
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • COI: 1:CAS:528:DC%2BD38XivVWjsLo%3D
    • Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, Arnaout MA (2002) Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 296:151–155
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 149
    • 84874091416 scopus 로고    scopus 로고
    • Quantitative proteomics by amino acid labeling in foot-and-mouth disease virus (FMDV)-infected cells
    • COI: 1:CAS:528:DC%2BC38XhslWksbfJ
    • Ye Y, Yan G, Luo Y, Tong T, Liu X, Xin C, Liao M, Fan H (2013) Quantitative proteomics by amino acid labeling in foot-and-mouth disease virus (FMDV)-infected cells. J Proteome Res 12:363–377
    • (2013) J Proteome Res , vol.12 , pp. 363-377
    • Ye, Y.1    Yan, G.2    Luo, Y.3    Tong, T.4    Liu, X.5    Xin, C.6    Liao, M.7    Fan, H.8
  • 150
    • 73149105706 scopus 로고    scopus 로고
    • Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate
    • COI: 1:CAS:528:DC%2BC3cXjsValsQ%3D%3D
    • Zunszain PA, Knox SR, Sweeney TR, Yang J, Roque-Rosell N, Belsham GJ, Leatherbarrow RJ, Curry S (2010) Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate. J Mol Biol 395:375–389
    • (2010) J Mol Biol , vol.395 , pp. 375-389
    • Zunszain, P.A.1    Knox, S.R.2    Sweeney, T.R.3    Yang, J.4    Roque-Rosell, N.5    Belsham, G.J.6    Leatherbarrow, R.J.7    Curry, S.8


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