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Volumn 78, Issue 3, 2014, Pages 418-437

Picornavirus morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALANINE; BUTHIONINE SULFOXIMINE; CAPSID PROTEIN; ENTEROVIRUS 2C ATPASE; GELDANAMYCIN; GLUTATHIONE; GUANIDINE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HYDANTOIN; MYRISTIC ACID; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 2C ATPASE; NUCLEOSIDE ANALOG; POLYPROTEIN; PROTEIN P1; PY 11; RNA; UNCLASSIFIED DRUG; VIRUS ENZYME; ANTIVIRUS AGENT; VIRUS RNA;

EID: 84907219219     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00012-14     Document Type: Review
Times cited : (179)

References (219)
  • 3
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 A resolution
    • Hogle JM, Chow M, Filman DJ. 1985. Three-dimensional structure of poliovirus at 2.9 A resolution. Science 229:1358-1365. http://dx.doi.org/10.1126/science.2994218.
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 5
    • 79952042139 scopus 로고    scopus 로고
    • Virion structure
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Fry EE, Stuart DI. 2010. Virion structure, p 59-72. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 59-72
    • Fry, E.E.1    Stuart, D.I.2
  • 6
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li Q, Yafal AG, Lee YM, Hogle J, Chow M. 1994. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J. Virol. 68:3965-3970.
    • (1994) J. Virol. , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.3    Hogle, J.4    Chow, M.5
  • 7
    • 0027133067 scopus 로고
    • Genetics of poliovirus
    • Wimmer E, Hellen CU, Cao X. 1993. Genetics of poliovirus. Annu. Rev. Genet. 27:353-436. http://dx.doi.org/10.1146/annurev.ge.27.120193.002033.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 353-436
    • Wimmer, E.1    Hellen, C.U.2    Cao, X.3
  • 8
    • 79952039453 scopus 로고    scopus 로고
    • Genome organization and encoded proteins
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Palmenberg A, Neubauer D, Skern T. 2010. Genome organization and encoded proteins, p 3-18. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 3-18
    • Palmenberg, A.1    Neubauer, D.2    Skern, T.3
  • 9
    • 84860530379 scopus 로고    scopus 로고
    • Receptors
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Bergelson JM. 2010. Receptors, p 73-86. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 73-86
    • Bergelson, J.M.1
  • 10
    • 80054008048 scopus 로고    scopus 로고
    • Cell entry: A biochemical and structural perspective
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Levy HC, Bostina M, Filman DJ, Hogle JM. 2010. Cell entry: a biochemical and structural perspective, p 87-104. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 87-104
    • Levy, H.C.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 11
    • 79952038041 scopus 로고    scopus 로고
    • Translation and protein processing
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Martinez-Salaz E, Ryan MD. 2010. Translation and protein processing, p 141-161. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 141-161
    • Martinez-Salaz, E.1    Ryan, M.D.2
  • 12
    • 0018136863 scopus 로고
    • Poliovirus single-stranded RNA and double-stranded RNA: Differential infectivity in enucleate cells
    • Detjen BM, Lucas J, Wimmer E. 1978. Poliovirus single-stranded RNA and double-stranded RNA: differential infectivity in enucleate cells. J. Virol. 27:582-586.
    • (1978) J. Virol. , vol.27 , pp. 582-586
    • Detjen, B.M.1    Lucas, J.2    Wimmer, E.3
  • 13
    • 79952039623 scopus 로고    scopus 로고
    • Remodeling cellular membranes
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Van Kuppeveld F, Belov G, Ehrenfeld E. 2010. Remodeling cellular membranes, p 181-193. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 181-193
    • Van Kuppeveld, F.1    Belov, G.2    Ehrenfeld, E.3
  • 14
    • 84903966620 scopus 로고    scopus 로고
    • Genome replication II: The process
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Kirkegaard K, Semler BL. 2010. Genome replication II: the process, p 127-140. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 127-140
    • Kirkegaard, K.1    Semler, B.L.2
  • 15
    • 79955427084 scopus 로고    scopus 로고
    • Genome replication I: The players
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Rozovics JM, Semler BL. 2010. Genome replication I: the players, p 107-126. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 107-126
    • Rozovics, J.M.1    Semler, B.L.2
  • 16
    • 0032554886 scopus 로고    scopus 로고
    • Protein-primed RNA synthesis by purified poliovirus RNA polymerase
    • Paul AV, van Boom JH, Filippov D, Wimmer E. 1998. Protein-primed RNA synthesis by purified poliovirus RNA polymerase. Nature 393:280-284. http://dx.doi.org/10.1038/30529.
    • (1998) Nature , vol.393 , pp. 280-284
    • Paul, A.V.1    Van Boom, J.H.2    Filippov, D.3    Wimmer, E.4
  • 18
    • 84881623229 scopus 로고    scopus 로고
    • How positive-strand RNA viruses benefit from autophagosome maturation
    • Richards AL, Jackson WT. 2013. How positive-strand RNA viruses benefit from autophagosome maturation. J. Virol. 87:9966-9972. http://dx.doi.org/10.1128/JVI.00460-13.
    • (2013) J. Virol. , vol.87 , pp. 9966-9972
    • Richards, A.L.1    Jackson, W.T.2
  • 19
    • 84862523248 scopus 로고    scopus 로고
    • Hepatitis A virus
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Feng Z, Lemon SM. 2010. Hepatitis A virus, p 383-396. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 383-396
    • Feng, Z.1    Lemon, S.M.2
  • 20
    • 77957916790 scopus 로고    scopus 로고
    • Direct interaction between two viral proteins, the nonstructural protein 2C and the capsid protein VP3, is required for enterovirus morphogenesis
    • Liu Y, Wang C, Mueller S, Paul AV, Wimmer E, Jiang P. 2010. Direct interaction between two viral proteins, the nonstructural protein 2C and the capsid protein VP3, is required for enterovirus morphogenesis. PLoS Pathog. 6:e1001066. http://dx.doi.org/10.1371/journal.ppat.1001066.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001066
    • Liu, Y.1    Wang, C.2    Mueller, S.3    Paul, A.V.4    Wimmer, E.5    Jiang, P.6
  • 21
    • 84866177871 scopus 로고    scopus 로고
    • Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/ 2CATPase interactions are essential for morphogenesis
    • Wang C, Jiang P, Sand C, Paul AV, Wimmer E. 2012. Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/ 2CATPase interactions are essential for morphogenesis. J. Virol. 86:9964-9975. http://dx.doi.org/10.1128/JVI.00914-12.
    • (2012) J. Virol. , vol.86 , pp. 9964-9975
    • Wang, C.1    Jiang, P.2    Sand, C.3    Paul, A.V.4    Wimmer, E.5
  • 24
    • 33748698840 scopus 로고    scopus 로고
    • Glutathione is required for efficient production of infectious picornavirus virions
    • Smith AD, Dawson H. 2006. Glutathione is required for efficient production of infectious picornavirus virions. Virology 353:258-267. http://dx.doi.org/10.1016/j.virol.2006.06.012.
    • (2006) Virology , vol.353 , pp. 258-267
    • Smith, A.D.1    Dawson, H.2
  • 25
    • 0037332360 scopus 로고    scopus 로고
    • The 5=-end sequence of the genome of Aichi virus, a picornavirus, contains an element critical for viral RNA encapsidation
    • Sasaki J, Taniguchi K. 2003. The 5=-end sequence of the genome of Aichi virus, a picornavirus, contains an element critical for viral RNA encapsidation. J. Virol. 77:3542-3548. http://dx.doi.org/10.1128/JVI.77.6.3542-3548.2003.
    • (2003) J. Virol. , vol.77 , pp. 3542-3548
    • Sasaki, J.1    Taniguchi, K.2
  • 26
    • 0141789704 scopus 로고    scopus 로고
    • Aichi virus leader protein is involved in viral RNA replication and encapsidation
    • Sasaki J, Nagashima S, Taniguchi K. 2003. Aichi virus leader protein is involved in viral RNA replication and encapsidation. J. Virol. 77:10799-10807. http://dx.doi.org/10.1128/JVI.77.20.10799-10807.2003.
    • (2003) J. Virol. , vol.77 , pp. 10799-10807
    • Sasaki, J.1    Nagashima, S.2    Taniguchi, K.3
  • 27
    • 53349165985 scopus 로고    scopus 로고
    • The unique role of domain 2A of the hepatitis A virus precursor polypeptide P1-2A in viral morphogenesis
    • Morace G, Kusov Y, Dzagurov G, Beneduce F, Gauss-Muller V. 2008. The unique role of domain 2A of the hepatitis A virus precursor polypeptide P1-2A in viral morphogenesis. BMB Rep. 41:678-683. http://dx.doi.org/10.5483/BMBRep.2008.41.9.678.
    • (2008) BMB Rep. , vol.41 , pp. 678-683
    • Morace, G.1    Kusov, Y.2    Dzagurov, G.3    Beneduce, F.4    Gauss-Muller, V.5
  • 29
    • 0023043280 scopus 로고
    • A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
    • Toyoda H, Nicklin MJ, Murray MG, Anderson CW, Dunn JJ, Studier FW, Wimmer E. 1986. A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein. Cell 45:761-770. http://dx.doi.org/10.1016/0092-8674(86)90790-7.
    • (1986) Cell , vol.45 , pp. 761-770
    • Toyoda, H.1    Nicklin, M.J.2    Murray, M.G.3    Anderson, C.W.4    Dunn, J.J.5    Studier, F.W.6    Wimmer, E.7
  • 31
    • 0029026646 scopus 로고
    • Myristoyl modification of viral proteins: Assays to assess functional roles
    • Chow M, Moscufo N. 1995. Myristoyl modification of viral proteins: assays to assess functional roles. Methods Enzymol. 250:495-509. http://dx.doi.org/10.1016/0076-6879(95)50093-6.
    • (1995) Methods Enzymol. , vol.250 , pp. 495-509
    • Chow, M.1    Moscufo, N.2
  • 32
    • 0023198719 scopus 로고
    • Myristylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M, Newman JF, Filman D, Hogle JM, Rowlands DJ, Brown F. 1987. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature 327:482-486. http://dx.doi.org/10.1038/327482a0.
    • (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
  • 33
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller R, Vignuzzi M, Andino R, Frydman J. 2007. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 21:195- 205. http://dx.doi.org/10.1101/gad.1505307.
    • (2007) Genes Dev. , vol.21 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 34
    • 0026525537 scopus 로고
    • Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells
    • Macejak DG, Sarnow P. 1992. Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells. J. Virol. 66: 1520-1527.
    • (1992) J. Virol. , vol.66 , pp. 1520-1527
    • Macejak, D.G.1    Sarnow, P.2
  • 35
    • 0023224697 scopus 로고
    • Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins
    • Ypma-Wong MF, Semler BL. 1987. Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins. J. Virol. 61:3181-3189.
    • (1987) J. Virol. , vol.61 , pp. 3181-3189
    • Ypma-Wong, M.F.1    Semler, B.L.2
  • 36
    • 70350312842 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus assembly: Processing of recombinant capsid precursor by exogenous protease induces self-assembly of pentamers in vitro in a myristoylation-dependent manner
    • Goodwin S, Tuthill 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. http://dx.doi.org/10.1128/JVI.01263-09.
    • (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
  • 37
    • 0027164245 scopus 로고
    • Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4
    • Tesar M, Jia XY, Summers DF, Ehrenfeld E. 1993. Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4. Virology 194:616-626. http://dx.doi.org/10.1006/viro.1993.1301.
    • (1993) Virology , vol.194 , pp. 616-626
    • Tesar, M.1    Jia, X.Y.2    Summers, D.F.3    Ehrenfeld, E.4
  • 38
    • 0036310386 scopus 로고    scopus 로고
    • Analysis of deletion mutants indicates that the 2A polypeptide of hepatitis A virus participates in virion morphogenesis
    • Cohen L, Benichou D, Martin A. 2002. Analysis of deletion mutants indicates that the 2A polypeptide of hepatitis A virus participates in virion morphogenesis. J. Virol. 76:7495-7505. http://dx.doi.org/10.1128/JVI.76.15.7495-7505.2002.
    • (2002) J. Virol. , vol.76 , pp. 7495-7505
    • Cohen, L.1    Benichou, D.2    Martin, A.3
  • 39
    • 77950421701 scopus 로고    scopus 로고
    • Fine-tuning translation kinetics selection as the driving force of codon usage bias in the hepatitis A virus capsid
    • Aragones L, Guix S, Ribes E, Bosch A, Pinto RM. 2010. Fine-tuning translation kinetics selection as the driving force of codon usage bias in the hepatitis A virus capsid. PLoS Pathog. 6:e1000797. http://dx.doi.org/10.1371/journal.ppat.1000797.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000797
    • Aragones, L.1    Guix, S.2    Ribes, E.3    Bosch, A.4    Pinto, R.M.5
  • 40
    • 0026633957 scopus 로고
    • Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles
    • Ansardi DC, Porter DC, Morrow CD. 1992. Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles. J. Virol. 66:4556-4563.
    • (1992) J. Virol. , vol.66 , pp. 4556-4563
    • Ansardi, D.C.1    Porter, D.C.2    Morrow, C.D.3
  • 41
    • 0026550736 scopus 로고
    • Myristate modification does not function as a membrane association signal during poliovirus capsid assembly
    • Lee YM, Chow M. 1992. Myristate modification does not function as a membrane association signal during poliovirus capsid assembly. Virology 187:814-820. http://dx.doi.org/10.1016/0042-6822(92)90485-8.
    • (1992) Virology , vol.187 , pp. 814-820
    • Lee, Y.M.1    Chow, M.2
  • 42
    • 0039000097 scopus 로고    scopus 로고
    • The amino-terminal nine amino acid sequence of poliovirus capsid VP4 protein is sufficient to confer N-myristoylation and targeting to detergent-insoluble membranes
    • Martin-Belmonte F, Lopez-Guerrero JA, Carrasco L, Alonso MA. 2000. The amino-terminal nine amino acid sequence of poliovirus capsid VP4 protein is sufficient to confer N-myristoylation and targeting to detergent-insoluble membranes. Biochemistry 39:1083-1090. http://dx.doi.org/10.1021/bi992132e.
    • (2000) Biochemistry , vol.39 , pp. 1083-1090
    • Martin-Belmonte, F.1    Lopez-Guerrero, J.A.2    Carrasco, L.3    Alonso, M.A.4
  • 43
    • 0025936844 scopus 로고
    • An assembly defect as a result of an attenuating mutation in the capsid proteins of the poliovirus type 3 vaccine strain
    • Macadam AJ, Ferguson G, Arnold C, Minor PD. 1991. An assembly defect as a result of an attenuating mutation in the capsid proteins of the poliovirus type 3 vaccine strain. J. Virol. 65:5225-5231.
    • (1991) J. Virol. , vol.65 , pp. 5225-5231
    • Macadam, A.J.1    Ferguson, G.2    Arnold, C.3    Minor, P.D.4
  • 44
    • 0027315290 scopus 로고
    • Synthesis and assembly of hepatitis A virus-specific proteins in BS-C-1 cells
    • Borovec SV, Anderson DA. 1993. Synthesis and assembly of hepatitis A virus-specific proteins in BS-C-1 cells. J. Virol. 67:3095-3102.
    • (1993) J. Virol. , vol.67 , pp. 3095-3102
    • Borovec, S.V.1    Anderson, D.A.2
  • 45
    • 0033582489 scopus 로고    scopus 로고
    • Intrinsic signals for the assembly of hepatitis A virus particles. Role of structural proteins VP4 and 2A
    • Probst C, Jecht M, Gauss-Muller V. 1999. Intrinsic signals for the assembly of hepatitis A virus particles. Role of structural proteins VP4 and 2A. J. Biol. Chem. 274:4527-4531.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4527-4531
    • Probst, C.1    Jecht, M.2    Gauss-Muller, V.3
  • 46
    • 0028970382 scopus 로고
    • RNA binding properties of poliovirus subviral particles
    • Nugent CI, Kirkegaard K. 1995. RNA binding properties of poliovirus subviral particles. J. Virol. 69:13-22.
    • (1995) J. Virol. , vol.69 , pp. 13-22
    • Nugent, C.I.1    Kirkegaard, K.2
  • 47
    • 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. 2000. Cell-free synthesis of poliovirus: 14S subunits are the key intermediates in the encapsidation of poliovirus RNA. J. Gen. Virol. 81:2751-2754. http://dx.doi.org/10.1099/vir.0.17247-0.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2751-2754
    • Verlinden, Y.1    Cuconati, A.2    Wimmer, E.3    Rombaut, B.4
  • 48
    • 0019810316 scopus 로고
    • Differences between poliovirus empty capsids formed in vivo and those formed in vitro: A role for the morphopoietic factor
    • Putnak JR, Phillips BA. 1981. Differences between poliovirus empty capsids formed in vivo and those formed in vitro: a role for the morphopoietic factor. J. Virol. 40:173-183.
    • (1981) J. Virol. , vol.40 , pp. 173-183
    • Putnak, J.R.1    Phillips, B.A.2
  • 49
    • 0019870688 scopus 로고
    • Picornaviral structure and assembly
    • Putnak JR, Phillips BA. 1981. Picornaviral structure and assembly. Microbiol. Rev. 45:287-315.
    • (1981) Microbiol. Rev. , vol.45 , pp. 287-315
    • Putnak, J.R.1    Phillips, B.A.2
  • 50
    • 0025277444 scopus 로고
    • New evidence for the precursor role of 14 S subunits in poliovirus morphogenesis
    • Rombaut B, Vrijsen R, Boeye A. 1990. New evidence for the precursor role of 14 S subunits in poliovirus morphogenesis. Virology 177:411-414. http://dx.doi.org/10.1016/0042-6822(90)90502-I.
    • (1990) Virology , vol.177 , pp. 411-414
    • Rombaut, B.1    Vrijsen, R.2    Boeye, A.3
  • 51
    • 0028795216 scopus 로고
    • Poliovirus subviral particles associated with progeny RNA in the replication complex
    • Pfister T, Egger D, Bienz K. 1995. Poliovirus subviral particles associated with progeny RNA in the replication complex. J. Gen. Virol. 76 (Part 1) : 63-71.
    • (1995) J. Gen. Virol. , vol.76 , pp. 63-71
    • Pfister, T.1    Egger, D.2    Bienz, K.3
  • 52
    • 33645094787 scopus 로고
    • Identification of poliovirus particles of different antigenicity by specific agglutination as seen in the electron microscope
    • Hummeler K, Anderson TF, Brown RA. 1962. Identification of poliovirus particles of different antigenicity by specific agglutination as seen in the electron microscope. Virology 16:84-90. http://dx.doi.org/10.1016/0042-6822(62)90205-2.
    • (1962) Virology , vol.16 , pp. 84-90
    • Hummeler, K.1    Anderson, T.F.2    Brown, R.A.3
  • 53
    • 50549204819 scopus 로고
    • Quantitative study of the formation of poliovirus antigens in infected HeLa cells
    • Scharff MD, Levintow L. 1963. Quantitative study of the formation of poliovirus antigens in infected HeLa cells. Virology 19:491-500. http://dx.doi.org/10.1016/0042-6822(63)90043-6.
    • (1963) Virology , vol.19 , pp. 491-500
    • Scharff, M.D.1    Levintow, L.2
  • 54
    • 0019512309 scopus 로고
    • Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids
    • Marongiu ME, Pani A, Corrias MV, Sau M, La Colla P. 1981. Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids. J. Virol. 39:341-347.
    • (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
  • 55
    • 0019906645 scopus 로고
    • A pH-dependent antigenic conversion of empty capsids of poliovirus studied with the aid of monoclonal antibodies to N and H antigen
    • Rombaut B, Vrijsen R, Brioen P, Boeye A. 1982. A pH-dependent antigenic conversion of empty capsids of poliovirus studied with the aid of monoclonal antibodies to N and H antigen. Virology 122:215-218. http://dx.doi.org/10.1016/0042-6822(82)90393-2.
    • (1982) Virology , vol.122 , pp. 215-218
    • Rombaut, B.1    Vrijsen, R.2    Brioen, P.3    Boeye, A.4
  • 56
    • 0020041699 scopus 로고
    • Poliovirus empty capsid morphogenesis: Evidence for conformational differences between self- and extract-assembled empty capsids
    • Putnak JR, Phillips BA. 1982. Poliovirus empty capsid morphogenesis: evidence for conformational differences between self- and extract-assembled empty capsids. J. Virol. 41:792-800.
    • (1982) J. Virol. , vol.41 , pp. 792-800
    • Putnak, J.R.1    Phillips, B.A.2
  • 57
    • 0002881434 scopus 로고
    • The replication of picornaviruses
    • Levy HB (ed), Marcel Dekker, New York, NY
    • Baltimore D. 1969. The replication of picornaviruses, p 103-176. In Levy HB (ed), The biochemistry of viruses. Marcel Dekker, New York, NY.
    • (1969) The Biochemistry of Viruses , pp. 103-176
    • Baltimore, D.1
  • 58
    • 0015817915 scopus 로고
    • Morphogenesis of poliovirus. II. Demonstration of a new intermediate, the proviron
    • Fernandez-Tomas CB, Baltimore D. 1973. Morphogenesis of poliovirus. II. Demonstration of a new intermediate, the proviron. J. Virol. 12:1122-1130.
    • (1973) J. Virol. , vol.12 , pp. 1122-1130
    • Fernandez-Tomas, C.B.1    Baltimore, D.2
  • 59
    • 0015688306 scopus 로고
    • Morphogenesis of poliovirus. III. Formation of provirion in cell-free extracts
    • Fernandez-Tomas CB, Guttman N, Baltimore D. 1973. Morphogenesis of poliovirus. III. Formation of provirion in cell-free extracts. J. Virol. 12:1181-1183.
    • (1973) J. Virol. , vol.12 , pp. 1181-1183
    • Fernandez-Tomas, C.B.1    Guttman, N.2    Baltimore, D.3
  • 60
    • 0017736745 scopus 로고
    • Morphogenesis of poliovirus. IV. Existence of particles sedimenting at 150S and having the properties of provirion
    • Guttman N, Baltimore D. 1977. Morphogenesis of poliovirus. IV. Existence of particles sedimenting at 150S and having the properties of provirion. J. Virol. 23:363-367.
    • (1977) J. Virol. , vol.23 , pp. 363-367
    • Guttman, N.1    Baltimore, D.2
  • 62
    • 0025036493 scopus 로고
    • Morphogenesis of hepatitis A virus: Isolation and characterization of subviral particles
    • Anderson DA, Ross BC. 1990. Morphogenesis of hepatitis A virus: isolation and characterization of subviral particles. J. Virol. 64:5284-5289.
    • (1990) J. Virol. , vol.64 , pp. 5284-5289
    • Anderson, D.A.1    Ross, B.C.2
  • 63
    • 1242303700 scopus 로고    scopus 로고
    • Picornavirus structure overview
    • Semler BL, Wimmer E (ed), ASM Press, Washington, DC
    • Rossmann MG. 2002. Picornavirus structure overview, p 27-68. In Semler BL, Wimmer E (ed), Molecular biology of picornaviruses. ASM Press, Washington, DC.
    • (2002) Molecular Biology of Picornaviruses , pp. 27-68
    • Rossmann, M.G.1
  • 65
    • 0031713179 scopus 로고    scopus 로고
    • Complete nucleotide sequence and genetic organization of Aichi virus, a distinct member of the Picornaviridae associated with acute gastroenteritis in humans
    • Yamashita T, Sakae K, Tsuzuki H, Suzuki Y, Ishikawa N, Takeda N, Miyamura T, Yamazaki S. 1998. Complete nucleotide sequence and genetic organization of Aichi virus, a distinct member of the Picornaviridae associated with acute gastroenteritis in humans. J. Virol. 72:8408-8412.
    • (1998) J. Virol. , vol.72 , pp. 8408-8412
    • Yamashita, T.1    Sakae, K.2    Tsuzuki, H.3    Suzuki, Y.4    Ishikawa, N.5    Takeda, N.6    Miyamura, T.7    Yamazaki, S.8
  • 67
    • 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
    • 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. http://dx.doi.org/10.1002/pro.5560031005.
    • (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
  • 68
    • 0026017496 scopus 로고
    • Catalysis of poliovirus VP0 maturation cleavage is not mediated by serine 10 of VP2
    • Harber JJ, Bradley J, Anderson CW, Wimmer E. 1991. Catalysis of poliovirus VP0 maturation cleavage is not mediated by serine 10 of VP2. J. Virol. 65:326-334.
    • (1991) J. Virol. , vol.65 , pp. 326-334
    • Harber, J.J.1    Bradley, J.2    Anderson, C.W.3    Wimmer, E.4
  • 70
    • 0032881997 scopus 로고    scopus 로고
    • Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4
    • Hindiyeh M, Li QH, Basavappa R, Hogle JM, Chow M. 1999. Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4. J. Virol. 73:9072-9079.
    • (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
  • 71
    • 0029656107 scopus 로고    scopus 로고
    • Mouse adaptation determinants of poliovirus type 1 enhance viral uncoating
    • Couderc T, Delpeyroux F, Le Blay H, Blondel B. 1996. Mouse adaptation determinants of poliovirus type 1 enhance viral uncoating. J. Virol. 70:305-312.
    • (1996) J. Virol. , vol.70 , pp. 305-312
    • Couderc, T.1    Delpeyroux, F.2    Le Blay, H.3    Blondel, B.4
  • 72
    • 0025060763 scopus 로고
    • Mutations in VP1 of poliovirus specifically affect both encapsidation and release of viral RNA
    • Kirkegaard K. 1990. Mutations in VP1 of poliovirus specifically affect both encapsidation and release of viral RNA. J. Virol. 64:195-206.
    • (1990) J. Virol. , vol.64 , pp. 195-206
    • Kirkegaard, K.1
  • 73
    • 0025150548 scopus 로고
    • Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions
    • Compton SR, Nelsen B, Kirkegaard K. 1990. Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions. J. Virol. 64:4067-4075.
    • (1990) J. Virol. , vol.64 , pp. 4067-4075
    • Compton, S.R.1    Nelsen, B.2    Kirkegaard, K.3
  • 74
    • 18144402819 scopus 로고    scopus 로고
    • Stimulation of poliovirus synthesis in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CDpro
    • Franco D, Pathak HB, Cameron CE, Rombaut B, Wimmer E, Paul AV. 2005. Stimulation of poliovirus synthesis in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CDpro. J. Virol. 79:6358-6367. http://dx.doi.org/10.1128/JVI.79.10.6358-6367.2005.
    • (2005) J. Virol. , vol.79 , pp. 6358-6367
    • Franco, D.1    Pathak, H.B.2    Cameron, C.E.3    Rombaut, B.4    Wimmer, E.5    Paul, A.V.6
  • 75
    • 29144465066 scopus 로고    scopus 로고
    • Stimulation of poliovirus RNA synthesis and virus maturation in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CDpro
    • Franco D, Pathak HB, Cameron CE, Rombaut B, Wimmer E, Paul AV. 2005. Stimulation of poliovirus RNA synthesis and virus maturation in a HeLa cell-free in vitro translation-RNA replication system by viral protein 3CDpro. Virol. J. 2:86. http://dx.doi.org/10.1186/1743-422X-2-86.
    • (2005) Virol. J. , vol.2 , pp. 86
    • Franco, D.1    Pathak, H.B.2    Cameron, C.E.3    Rombaut, B.4    Wimmer, E.5    Paul, A.V.6
  • 76
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A, Paul AV, Wimmer E. 1991. Cell-free, de novo synthesis of poliovirus. Science 254:1647-1651. http://dx.doi.org/10.1126/science.1661029.
    • (1991) Science , vol.254 , pp. 1647-1651
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 77
    • 0027323262 scopus 로고
    • Effects of temperature and lipophilic agents on poliovirus formation and RNA synthesis in a cell-free system
    • Molla A, Paul AV, Wimmer E. 1993. Effects of temperature and lipophilic agents on poliovirus formation and RNA synthesis in a cell-free system. J. Virol. 67:5932-5938.
    • (1993) J. Virol. , vol.67 , pp. 5932-5938
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 78
    • 0036645722 scopus 로고    scopus 로고
    • Picornavirus-receptor interactions
    • Rossmann MG, He Y, Kuhn RJ. 2002. Picornavirus-receptor interactions. Trends Microbiol. 10:324-331. http://dx.doi.org/10.1016/S0966-842X(02)02383-1.
    • (2002) Trends Microbiol. , vol.10 , pp. 324-331
    • Rossmann, M.G.1    He, Y.2    Kuhn, R.J.3
  • 79
    • 0028278231 scopus 로고
    • Decay-accelerating factor (CD55), a glycosylphosphatidylinositolanchored complement regulatory protein, is a receptor for several echoviruses
    • Bergelson JM, Chan M, Solomon KR, St John NF, Lin H, Finberg RW. 1994. Decay-accelerating factor (CD55), a glycosylphosphatidylinositolanchored complement regulatory protein, is a receptor for several echoviruses. Proc. Natl. Acad. Sci. U. S. A. 91:6245-6248. http://dx.doi.org/10.1073/pnas.91.13.6245.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6245-6248
    • Bergelson, J.M.1    Chan, M.2    Solomon, K.R.3    St John, N.F.4    Lin, H.5    Finberg, R.W.6
  • 84
    • 0024591695 scopus 로고
    • The structure of antiviral agents that inhibit uncoating when complexed with viral capsids
    • Rossmann MG. 1989. The structure of antiviral agents that inhibit uncoating when complexed with viral capsids. Antiviral Res. 11:3-13. http://dx.doi.org/10.1016/0166-3542(89)90016-8.
    • (1989) Antiviral Res. , vol.11 , pp. 3-13
    • Rossmann, M.G.1
  • 88
    • 84974671810 scopus 로고
    • Committee on Typing of the National Foundation of Infantile Paralysis
    • Salk JE. 1951. Committee on Typing of the National Foundation of Infantile Paralysis. Am. J. Hyg. 54:191-274.
    • (1951) Am. J. Hyg. , vol.54 , pp. 191-274
    • Salk, J.E.1
  • 89
    • 0030912887 scopus 로고    scopus 로고
    • Efficient encapsidation of human immunodeficiency virus type 1 vectors and further characterization of cis elements required for encapsidation
    • McBride MS, Schwartz MD, Panganiban AT. 1997. Efficient encapsidation of human immunodeficiency virus type 1 vectors and further characterization of cis elements required for encapsidation. J. Virol. 71:4544-4554.
    • (1997) J. Virol. , vol.71 , pp. 4544-4554
    • McBride, M.S.1    Schwartz, M.D.2    Panganiban, A.T.3
  • 90
    • 0026706346 scopus 로고
    • Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome
    • Bartenschlager R, Schaller H. 1992. Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome. EMBO J. 11:3413-3420.
    • (1992) EMBO J. , vol.11 , pp. 3413-3420
    • Bartenschlager, R.1    Schaller, H.2
  • 92
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • 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
  • 93
    • 0008467451 scopus 로고
    • A chimeric plasmid from cDNA clones of poliovirus and coxsackievirus produces a recombinant virus that is temperature-sensitive
    • Semler BL, Johnson VH, Tracy S. 1986. A chimeric plasmid from cDNA clones of poliovirus and coxsackievirus produces a recombinant virus that is temperature-sensitive. Proc. Natl. Acad. Sci. U. S. A. 83:1777- 1781. http://dx.doi.org/10.1073/pnas.83.6.1777.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 1777-1781
    • Semler, B.L.1    Johnson, V.H.2    Tracy, S.3
  • 94
    • 0023854102 scopus 로고
    • Defined recombinants of poliovirus and coxsackievirus: Sequence-specific deletions and functional substitutions in the 5=-noncoding regions of viral RNAs
    • Johnson VH, Semler BL. 1988. Defined recombinants of poliovirus and coxsackievirus: sequence-specific deletions and functional substitutions in the 5=-noncoding regions of viral RNAs. Virology 162:47-57. http://dx.doi.org/10.1016/0042-6822(88)90393-5.
    • (1988) Virology , vol.162 , pp. 47-57
    • Johnson, V.H.1    Semler, B.L.2
  • 95
    • 79960384228 scopus 로고    scopus 로고
    • The making of a picornavirus
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Wimmer E, Paul AV. 2010. The making of a picornavirus, p 33-55. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 33-55
    • Wimmer, E.1    Paul, A.V.2
  • 96
    • 0043169497 scopus 로고    scopus 로고
    • Analysis of the cloverleaf element in a human rhinovirus type 14/poliovirus chimera: Correlation of subdomain D structure, ternary protein complex formation and virus replication
    • Rieder E, Xiang W, Paul A, Wimmer E. 2003. Analysis of the cloverleaf element in a human rhinovirus type 14/poliovirus chimera: correlation of subdomain D structure, ternary protein complex formation and virus replication. J. Gen. Virol. 84:2203-2216. http://dx.doi.org/10.1099/vir.0.19013-0.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2203-2216
    • Rieder, E.1    Xiang, W.2    Paul, A.3    Wimmer, E.4
  • 97
    • 0015049892 scopus 로고
    • Defective interfering particles of poliovirus. I. Isolation and physical properties
    • Cole CN, Smoler D, Wimmer E, Baltimore D. 1971. Defective interfering particles of poliovirus. I. Isolation and physical properties. J. Virol. 7:478-485.
    • (1971) J. Virol. , vol.7 , pp. 478-485
    • Cole, C.N.1    Smoler, D.2    Wimmer, E.3    Baltimore, D.4
  • 98
    • 0018415607 scopus 로고
    • Defective interfering particles of poliovirus: Mapping of the deletion and evidence that the deletions in the genomes of DI(1), (2) and (3) are located in the same region
    • Nomoto A, Jacobson A, Lee YF, Dunn J, Wimmer E. 1979. Defective interfering particles of poliovirus: mapping of the deletion and evidence that the deletions in the genomes of DI(1), (2) and (3) are located in the same region. J. Mol. Biol. 128:179-196. http://dx.doi.org/10.1016/0022-2836(79)90125-6.
    • (1979) J. Mol. Biol. , vol.128 , pp. 179-196
    • Nomoto, A.1    Jacobson, A.2    Lee, Y.F.3    Dunn, J.4    Wimmer, E.5
  • 99
    • 0023003082 scopus 로고
    • Primary structure of poliovirus defective-interfering particle genomes and possible generation mechanisms of the particles
    • Kuge S, Saito I, Nomoto A. 1986. Primary structure of poliovirus defective-interfering particle genomes and possible generation mechanisms of the particles. J. Mol. Biol. 192:473-487. http://dx.doi.org/10.1016/0022-2836(86)90270-6.
    • (1986) J. Mol. Biol. , vol.192 , pp. 473-487
    • Kuge, S.1    Saito, I.2    Nomoto, A.3
  • 100
    • 0028136217 scopus 로고
    • Coupling between genome translation and replication in an RNA virus
    • Novak JE, Kirkegaard K. 1994. Coupling between genome translation and replication in an RNA virus. Genes Dev. 8:1726-1737. http://dx.doi.org/10.1101/gad.8.14.1726.
    • (1994) Genes Dev. , vol.8 , pp. 1726-1737
    • Novak, J.E.1    Kirkegaard, K.2
  • 101
    • 0022302658 scopus 로고
    • Isolation and characterization of defective-interfering particles of poliovirus Sabin 1 strain
    • Kajigaya S, Arakawa H, Kuge S, Koi T, Imura N, Nomoto A. 1985. Isolation and characterization of defective-interfering particles of poliovirus Sabin 1 strain. Virology 142:307-316. http://dx.doi.org/10.1016/0042-6822(85)90339-3.
    • (1985) Virology , vol.142 , pp. 307-316
    • Kajigaya, S.1    Arakawa, H.2    Kuge, S.3    Koi, T.4    Imura, N.5    Nomoto, A.6
  • 102
    • 0032579846 scopus 로고    scopus 로고
    • Demonstration of the specificity of poliovirus encapsidation using a novel replicon which encodes enzymatically active firefly luciferase
    • Porter DC, Ansardi DC, Wang J, McPherson S, Moldoveanu Z, Morrow CD. 1998. Demonstration of the specificity of poliovirus encapsidation using a novel replicon which encodes enzymatically active firefly luciferase. Virology 243:1-11. http://dx.doi.org/10.1006/viro.1998.9046.
    • (1998) Virology , vol.243 , pp. 1-11
    • Porter, D.C.1    Ansardi, D.C.2    Wang, J.3    McPherson, S.4    Moldoveanu, Z.5    Morrow, C.D.6
  • 104
    • 0028859870 scopus 로고
    • Encapsidation of poliovirus replicons encoding the complete human immunodeficiency virus type 1 gag gene by using a complementation system which provides the P1 capsid protein in trans
    • Porter DC, Ansardi DC, Morrow CD. 1995. Encapsidation of poliovirus replicons encoding the complete human immunodeficiency virus type 1 gag gene by using a complementation system which provides the P1 capsid protein in trans. J. Virol. 69:1548-1555.
    • (1995) J. Virol. , vol.69 , pp. 1548-1555
    • Porter, D.C.1    Ansardi, D.C.2    Morrow, C.D.3
  • 105
    • 0026627865 scopus 로고
    • A poliovirus replicon containing the chloramphenicol acetyltransferase gene can be used to study the replication and encapsidation of poliovirus RNA
    • Percy N, Barclay WS, Sullivan M, Almond JW. 1992. A poliovirus replicon containing the chloramphenicol acetyltransferase gene can be used to study the replication and encapsidation of poliovirus RNA. J. Virol. 66:5040-5046.
    • (1992) J. Virol. , vol.66 , pp. 5040-5046
    • Percy, N.1    Barclay, W.S.2    Sullivan, M.3    Almond, J.W.4
  • 106
    • 0034003829 scopus 로고    scopus 로고
    • Identification of a cis-acting replication element within the poliovirus coding region
    • Goodfellow I, Chaudhry Y, Richardson A, Meredith J, Almond JW, Barclay W, Evans DJ. 2000. Identification of a cis-acting replication element within the poliovirus coding region. J. Virol. 74:4590-4600. http://dx.doi.org/10.1128/JVI.74.10.4590-4600.2000.
    • (2000) J. Virol. , vol.74 , pp. 4590-4600
    • Goodfellow, I.1    Chaudhry, Y.2    Richardson, A.3    Meredith, J.4    Almond, J.W.5    Barclay, W.6    Evans, D.J.7
  • 107
    • 0242415195 scopus 로고    scopus 로고
    • A "slide-back" mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus
    • Paul AV, Yin J, Mugavero J, Rieder E, Liu Y, Wimmer E. 2003. A "slide-back" mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus. J. Biol. Chem. 278:43951-43960. http://dx.doi.org/10.1074/jbc.M307441200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43951-43960
    • Paul, A.V.1    Yin, J.2    Mugavero, J.3    Rieder, E.4    Liu, Y.5    Wimmer, E.6
  • 108
    • 0001856730 scopus 로고    scopus 로고
    • Possible unifying mechanism of picornavirus genome replication
    • Semler BL, Wimmer E (ed), ASM Press, Washington, DC
    • Paul AV. 2002. Possible unifying mechanism of picornavirus genome replication, p 227-246. In Semler BL, Wimmer E (ed), Molecular biology of picornaviruses. ASM Press, Washington, DC.
    • (2002) Molecular Biology of Picornaviruses , pp. 227-246
    • Paul, A.V.1
  • 109
    • 0035945235 scopus 로고    scopus 로고
    • Conserved RNA secondary structures in Picornaviridae genomes
    • Witwer C, Rauscher S, Hofacker IL, Stadler PF. 2001. Conserved RNA secondary structures in Picornaviridae genomes. Nucleic Acids Res. 29: 5079-5089. http://dx.doi.org/10.1093/nar/29.24.5079.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 5079-5089
    • Witwer, C.1    Rauscher, S.2    Hofacker, I.L.3    Stadler, P.F.4
  • 110
    • 84865994677 scopus 로고    scopus 로고
    • Identification of two functionally redundant RNA elements in the coding sequence of poliovirus using computer-generated design
    • Song Y, Liu Y, Ward CB, Mueller S, Futcher B, Skiena S, Paul AV, Wimmer E. 2012. Identification of two functionally redundant RNA elements in the coding sequence of poliovirus using computer-generated design. Proc. Natl. Acad. Sci. U. S. A. 109:14301-14307. http://dx.doi.org/10.1073/pnas.1211484109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14301-14307
    • Song, Y.1    Liu, Y.2    Ward, C.B.3    Mueller, S.4    Futcher, B.5    Skiena, S.6    Paul, A.V.7    Wimmer, E.8
  • 111
    • 33748923860 scopus 로고    scopus 로고
    • Reduction of the rate of poliovirus protein synthesis through large-scale codon deoptimization causes attenuation of viral virulence by lowering specific infectivity
    • Mueller S, Papamichail D, Coleman JR, Skiena S, Wimmer E. 2006. Reduction of the rate of poliovirus protein synthesis through large-scale codon deoptimization causes attenuation of viral virulence by lowering specific infectivity. J. Virol. 80:9687-9696. http://dx.doi.org/10.1128/JVI.00738-06.
    • (2006) J. Virol. , vol.80 , pp. 9687-9696
    • Mueller, S.1    Papamichail, D.2    Coleman, J.R.3    Skiena, S.4    Wimmer, E.5
  • 112
    • 46449120581 scopus 로고    scopus 로고
    • Virus attenuation by genome-scale changes in codon pair bias
    • Coleman JR, Papamichail D, Skiena S, Futcher B, Wimmer E, Mueller S. 2008. Virus attenuation by genome-scale changes in codon pair bias. Science 320:1784-1787. http://dx.doi.org/10.1126/science.1155761.
    • (2008) Science , vol.320 , pp. 1784-1787
    • Coleman, J.R.1    Papamichail, D.2    Skiena, S.3    Futcher, B.4    Wimmer, E.5    Mueller, S.6
  • 113
    • 0033755326 scopus 로고    scopus 로고
    • Genetic and biochemical studies of poliovirus cis-acting replication element cre in relation to VPg uridylylation
    • Rieder E, Paul AV, Kim DW, van Boom JH, Wimmer E. 2000. Genetic and biochemical studies of poliovirus cis-acting replication element cre in relation to VPg uridylylation. J. Virol. 74:10371-10380. http://dx.doi.org/10.1128/JVI.74.22.10371-10380.2000.
    • (2000) J. Virol. , vol.74 , pp. 10371-10380
    • Rieder, E.1    Paul, A.V.2    Kim, D.W.3    Van Boom, J.H.4    Wimmer, E.5
  • 114
    • 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 EV, Poperechny KV, Maslova SV, Melchers WJ, Slot HJ, Agol VI. 1996. 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. 15:5428-5436.
    • (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
  • 115
    • 24644461482 scopus 로고    scopus 로고
    • An authentic 3= noncoding region is necessary for efficient poliovirus replication
    • Brown DM, Cornell CT, Tran GP, Nguyen JH, Semler BL. 2005. An authentic 3= noncoding region is necessary for efficient poliovirus replication. J. Virol. 79:11962-11973. http://dx.doi.org/10.1128/JVI.79.18.11962-11973.2005.
    • (2005) J. Virol. , vol.79 , pp. 11962-11973
    • Brown, D.M.1    Cornell, C.T.2    Tran, G.P.3    Nguyen, J.H.4    Semler, B.L.5
  • 116
    • 33745174889 scopus 로고    scopus 로고
    • Polyadenylation of genomic RNA and initiation of antigenomic RNA in a positive-strand RNA virus are controlled by the same cis-element
    • van Ooij MJ, Polacek C, Glaudemans DH, Kuijpers J, van Kuppeveld FJ, Andino R, Agol VI, Melchers WJ. 2006. Polyadenylation of genomic RNA and initiation of antigenomic RNA in a positive-strand RNA virus are controlled by the same cis-element. Nucleic Acids Res. 34:2953-2965. http://dx.doi.org/10.1093/nar/gkl349.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2953-2965
    • Van Ooij, M.J.1    Polacek, C.2    Glaudemans, D.H.3    Kuijpers, J.4    Van Kuppeveld, F.J.5    Andino, R.6    Agol, V.I.7    Melchers, W.J.8
  • 117
    • 0028824892 scopus 로고
    • The 3′ untranslated region of picornavirus RNA: Features required for efficient genome replication
    • Rohll JB, Moon DH, Evans DJ, Almond JW. 1995. The 3′ untranslated region of picornavirus RNA: features required for efficient genome replication. J. Virol. 69:7835-7844.
    • (1995) J. Virol. , vol.69 , pp. 7835-7844
    • Rohll, J.B.1    Moon, D.H.2    Evans, D.J.3    Almond, J.W.4
  • 118
    • 0030802760 scopus 로고    scopus 로고
    • Replicationcompetent picornaviruses with complete genomic RNA 3′ noncoding region deletions
    • Todd S, Towner JS, Brown DM, Semler BL. 1997. Replicationcompetent picornaviruses with complete genomic RNA 3′ noncoding region deletions. J. Virol. 71:8868-8874.
    • (1997) J. Virol. , vol.71 , pp. 8868-8874
    • Todd, S.1    Towner, J.S.2    Brown, D.M.3    Semler, B.L.4
  • 119
    • 18744377196 scopus 로고    scopus 로고
    • 5′-terminal deletions occur in coxsackievirus B3 during replication in murine hearts and cardiac myocyte cultures and correlate with encapsidation of negative-strand viral RNA
    • Kim KS, Tracy S, Tapprich W, Bailey J, Lee CK, Kim K, Barry WH, Chapman NM. 2005. 5′-terminal deletions occur in coxsackievirus B3 during replication in murine hearts and cardiac myocyte cultures and correlate with encapsidation of negative-strand viral RNA. J. Virol. 79:7024-7041. http://dx.doi.org/10.1128/JVI.79.11.7024-7041.2005.
    • (2005) J. Virol. , vol.79 , pp. 7024-7041
    • Kim, K.S.1    Tracy, S.2    Tapprich, W.3    Bailey, J.4    Lee, C.K.5    Kim, K.6    Barry, W.H.7    Chapman, N.M.8
  • 120
    • 0028925901 scopus 로고
    • Poliovirus protein 2C contains two regions involved in RNA binding activity
    • Rodriguez PL, Carrasco L. 1995. Poliovirus protein 2C contains two regions involved in RNA binding activity. J. Biol. Chem. 270:10105-10112. http://dx.doi.org/10.1074/jbc.270.17.10105.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10105-10112
    • Rodriguez, P.L.1    Carrasco, L.2
  • 121
    • 0028331981 scopus 로고
    • Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C
    • Paul AV, Molla A, Wimmer E. 1994. Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C. Virology 199:188-199. http://dx.doi.org/10.1006/viro.1994.1111.
    • (1994) Virology , vol.199 , pp. 188-199
    • Paul, A.V.1    Molla, A.2    Wimmer, E.3
  • 122
    • 0023724339 scopus 로고
    • Isolation of poliovirus 2C mutants defective in viral RNA synthesis
    • Li JP, Baltimore D. 1988. Isolation of poliovirus 2C mutants defective in viral RNA synthesis. J. Virol. 62:4016-4021.
    • (1988) J. Virol. , vol.62 , pp. 4016-4021
    • Li, J.P.1    Baltimore, D.2
  • 123
    • 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 KW, Wimmer E. 2000. A cysteine-rich motif in poliovirus protein 2C(ATPase) is involved in RNA replication and binds zinc in vitro. J. Virol. 74:334-343. http://dx.doi.org/10.1128/JVI.74.1.334-343.2000.
    • (2000) J. Virol. , vol.74 , pp. 334-343
    • Pfister, T.1    Jones, K.W.2    Wimmer, E.3
  • 124
    • 0022623016 scopus 로고
    • Guanidine-selected mutants of poliovirus: Mapping of point mutations to polypeptide 2C
    • Pincus SE, Diamond DC, Emini EA, Wimmer E. 1986. Guanidine-selected mutants of poliovirus: mapping of point mutations to polypeptide 2C. J. Virol. 57:638-646.
    • (1986) J. Virol. , vol.57 , pp. 638-646
    • Pincus, S.E.1    Diamond, D.C.2    Emini, E.A.3    Wimmer, E.4
  • 125
    • 0026769791 scopus 로고
    • Genetic analysis of an NTP-binding motif in poliovirus polypeptide 2C
    • Mirzayan C, Wimmer E. 1992. Genetic analysis of an NTP-binding motif in poliovirus polypeptide 2C. Virology 189:547-555. http://dx.doi.org/10.1016/0042-6822(92)90578-D.
    • (1992) Virology , vol.189 , pp. 547-555
    • Mirzayan, C.1    Wimmer, E.2
  • 126
    • 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. 1999. Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. J. Biol. Chem. 274:6992-7001. http://dx.doi.org/10.1074/jbc.274.11.6992.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6992-7001
    • Pfister, T.1    Wimmer, E.2
  • 127
    • 0025213458 scopus 로고
    • An intragenic revertant of a poliovirus 2C mutant has an uncoating defect
    • Li JP, Baltimore D. 1990. An intragenic revertant of a poliovirus 2C mutant has an uncoating defect. J. Virol. 64:1102-1107.
    • (1990) J. Virol. , vol.64 , pp. 1102-1107
    • Li, J.P.1    Baltimore, D.2
  • 128
    • 0030725538 scopus 로고    scopus 로고
    • Induction of intracellular membrane rearrangements by HAV proteins 2C and 2BC
    • Teterina NL, Bienz K, Egger D, Gorbalenya AE, Ehrenfeld E. 1997. Induction of intracellular membrane rearrangements by HAV proteins 2C and 2BC. Virology 237:66-77. http://dx.doi.org/10.1006/viro.1997.8775.
    • (1997) Virology , vol.237 , pp. 66-77
    • Teterina, N.L.1    Bienz, K.2    Egger, D.3    Gorbalenya, A.E.4    Ehrenfeld, E.5
  • 129
    • 0030807887 scopus 로고    scopus 로고
    • Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells
    • Teterina NL, Gorbalenya AE, Egger D, Bienz K, Ehrenfeld E. 1997. Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells. J. Virol. 71:8962-8972.
    • (1997) J. Virol. , vol.71 , pp. 8962-8972
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 130
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho MW, Teterina N, Egger D, Bienz K, Ehrenfeld E. 1994. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202:129-145. http://dx.doi.org/10.1006/viro.1994.1329.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 131
    • 0029814801 scopus 로고    scopus 로고
    • Membrane permeabilization by poliovirus proteins 2B and 2BC
    • Aldabe R, Barco A, Carrasco L. 1996. Membrane permeabilization by poliovirus proteins 2B and 2BC. J. Biol. Chem. 271:23134-23137. http://dx.doi.org/10.1074/jbc.271.38.23134.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23134-23137
    • Aldabe, R.1    Barco, A.2    Carrasco, L.3
  • 132
    • 0030765991 scopus 로고    scopus 로고
    • Poliovirus 2C region functions during encapsidation of viral RNA
    • Vance LM, Moscufo N, Chow M, Heinz BA. 1997. Poliovirus 2C region functions during encapsidation of viral RNA. J. Virol. 71:8759-8765.
    • (1997) J. Virol. , vol.71 , pp. 8759-8765
    • Vance, L.M.1    Moscufo, N.2    Chow, M.3    Heinz, B.A.4
  • 133
    • 34547599626 scopus 로고    scopus 로고
    • Complete protein linkage map between the P2 and P3 non-structural proteins of poliovirus
    • Yin J, Liu Y, Wimmer E, Paul AV. 2007. Complete protein linkage map between the P2 and P3 non-structural proteins of poliovirus. J. Gen. Virol. 88:2259-2267. http://dx.doi.org/10.1099/vir.0.82795-0.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2259-2267
    • Yin, J.1    Liu, Y.2    Wimmer, E.3    Paul, A.V.4
  • 134
    • 79955398622 scopus 로고    scopus 로고
    • Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells
    • Teterina NL, Pinto Y, Weaver JD, Jensen KS, Ehrenfeld E. 2011. Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells. J. Virol. 85:4284-4296. http://dx.doi.org/10.1128/JVI.02398-10.
    • (2011) J. Virol. , vol.85 , pp. 4284-4296
    • Teterina, N.L.1    Pinto, Y.2    Weaver, J.D.3    Jensen, K.S.4    Ehrenfeld, E.5
  • 135
    • 4143118915 scopus 로고    scopus 로고
    • Regulation of poliovirus 3C protease by the 2C polypeptide
    • Banerjee R, Weidman MK, Echeverri A, Kundu P, Dasgupta A. 2004. Regulation of poliovirus 3C protease by the 2C polypeptide. J. Virol. 78:9243-9256. http://dx.doi.org/10.1128/JVI.78.17.9243-9256.2004.
    • (2004) J. Virol. , vol.78 , pp. 9243-9256
    • Banerjee, R.1    Weidman, M.K.2    Echeverri, A.3    Kundu, P.4    Dasgupta, A.5
  • 137
    • 84897380301 scopus 로고    scopus 로고
    • Phosphatidylinositol-4 kinase III beta and oxysterolbinding protein accumulate unesterified cholesterol on poliovirusinduced membrane structure
    • Arita M. 2014. Phosphatidylinositol-4 kinase III beta and oxysterolbinding protein accumulate unesterified cholesterol on poliovirusinduced membrane structure. Microbiol. Immunol. 58:239-256. http://dx.doi.org/10.1111/1348-0421.12144.
    • (2014) Microbiol. Immunol. , vol.58 , pp. 239-256
    • Arita, M.1
  • 138
    • 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 SE, Wimmer E. 1986. Production of guanidine-resistant and -dependent poliovirus mutants from cloned cDNA: mutations in polypeptide 2C are directly responsible for altered guanidine sensitivity. J. Virol. 60:793-796.
    • (1986) J. Virol. , vol.60 , pp. 793-796
    • Pincus, S.E.1    Wimmer, E.2
  • 139
    • 0023105743 scopus 로고
    • Guanidine-dependent mutants of poliovirus: Identification of three classes with different growth requirements
    • Pincus SE, Rohl H, Wimmer E. 1987. Guanidine-dependent mutants of poliovirus: identification of three classes with different growth requirements. Virology 157:83-88. http://dx.doi.org/10.1016/0042-6822(87)90316-3.
    • (1987) Virology , vol.157 , pp. 83-88
    • Pincus, S.E.1    Rohl, H.2    Wimmer, E.3
  • 140
    • 27144546976 scopus 로고    scopus 로고
    • Vaccine-derived polioviruses and the endgame strategy for global polio eradication
    • Kew OM, Sutter RW, de Gourville EM, Dowdle WR, Pallansch MA. 2005. Vaccine-derived polioviruses and the endgame strategy for global polio eradication. Annu. Rev. Microbiol. 59:587-635. http://dx.doi.org/10.1146/annurev.micro.58.030603.123625.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 587-635
    • Kew, O.M.1    Sutter, R.W.2    De Gourville, E.M.3    Dowdle, W.R.4    Pallansch, M.A.5
  • 141
    • 34547142736 scopus 로고    scopus 로고
    • Evidence for emergence of diverse polioviruses from C-cluster coxsackie A viruses and implications for global poliovirus eradication
    • Jiang P, Faase JA, Toyoda H, Paul A, Wimmer E, Gorbalenya AE. 2007. Evidence for emergence of diverse polioviruses from C-cluster coxsackie A viruses and implications for global poliovirus eradication. Proc. Natl. Acad. Sci. U. S. A. 104:9457-9462. http://dx.doi.org/10.1073/pnas.0700451104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9457-9462
    • Jiang, P.1    Faase, J.A.2    Toyoda, H.3    Paul, A.4    Wimmer, E.5    Gorbalenya, A.E.6
  • 142
    • 0029398842 scopus 로고
    • Molecular dissection of the multifunctional poliovirus RNA-binding protein 3AB
    • Xiang W, Cuconati A, Paul AV, Cao X, Wimmer E. 1995. Molecular dissection of the multifunctional poliovirus RNA-binding protein 3AB. RNA 1:892-904.
    • (1995) RNA , vol.1 , pp. 892-904
    • Xiang, W.1    Cuconati, A.2    Paul, A.V.3    Cao, X.4    Wimmer, E.5
  • 143
    • 0033960579 scopus 로고    scopus 로고
    • Interactions of viral protein 3CD and poly(rC) binding protein with the 5′ untranslated region of the poliovirus genome
    • Gamarnik AV, Andino R. 2000. Interactions of viral protein 3CD and poly(rC) binding protein with the 5′ untranslated region of the poliovirus genome. J. Virol. 74:2219-2226. http://dx.doi.org/10.1128/JVI.74.5.2219-2226.2000.
    • (2000) J. Virol. , vol.74 , pp. 2219-2226
    • Gamarnik, A.V.1    Andino, R.2
  • 144
    • 0033766003 scopus 로고    scopus 로고
    • Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg
    • Paul AV, Rieder E, Kim DW, van Boom JH, Wimmer E. 2000. Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg. J. Virol. 74:10359-10370. http://dx.doi.org/10.1128/JVI.74.22.10359-10370.2000.
    • (2000) J. Virol. , vol.74 , pp. 10359-10370
    • Paul, A.V.1    Rieder, E.2    Kim, D.W.3    Van Boom, J.H.4    Wimmer, E.5
  • 145
    • 38149020712 scopus 로고    scopus 로고
    • Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex
    • Shen M, Reitman ZJ, Zhao Y, Moustafa I, Wang Q, Arnold JJ, Pathak HB, Cameron CE. 2008. Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex. J. Biol. Chem. 283:875-888. http://dx.doi.org/10.1074/jbc.M707907200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 875-888
    • Shen, M.1    Reitman, Z.J.2    Zhao, Y.3    Moustafa, I.4    Wang, Q.5    Arnold, J.J.6    Pathak, H.B.7    Cameron, C.E.8
  • 146
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong MF, Dewalt PG, Johnson VH, Lamb JG, Semler BL. 1988. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology 166:265-270. http://dx.doi.org/10.1016/0042-6822(88)90172-9.
    • (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
  • 147
    • 0028364693 scopus 로고
    • Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B
    • Schultheiss T, Kusov YY, Gauss-Muller V. 1994. Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B. Virology 198:275-281. http://dx.doi.org/10.1006/viro.1994.1030.
    • (1994) Virology , vol.198 , pp. 275-281
    • Schultheiss, T.1    Kusov, Y.Y.2    Gauss-Muller, V.3
  • 149
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228:111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 151
    • 0025082005 scopus 로고
    • Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles
    • Marc D, Masson G, Girard M, van der Werf S. 1990. Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles. J. Virol. 64:4099-4107.
    • (1990) J. Virol. , vol.64 , pp. 4099-4107
    • Marc, D.1    Masson, G.2    Girard, M.3    Van Der Werf, S.4
  • 152
    • 0025773025 scopus 로고
    • Myristoylation is important at multiple stages in poliovirus assembly
    • 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
  • 155
    • 84876448042 scopus 로고    scopus 로고
    • (+)RNA viruses rewire cellular pathways to build replication organelles
    • Belov GA, van Kuppeveld FJ. 2012. (+)RNA viruses rewire cellular pathways to build replication organelles. Curr. Opin. Virol. 2:740-747. http://dx.doi.org/10.1016/j.coviro.2012.09.006.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 740-747
    • Belov, G.A.1    Van Kuppeveld, F.J.2
  • 157
    • 33846594517 scopus 로고    scopus 로고
    • Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm
    • Kirkegaard K, Jackson WT. 2005. Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm. Autophagy 1:182-184. http://dx.doi.org/10.4161/auto.1.3.2065.
    • (2005) Autophagy , vol.1 , pp. 182-184
    • Kirkegaard, K.1    Jackson, W.T.2
  • 158
    • 57149096870 scopus 로고    scopus 로고
    • A critical role of a cellular membrane traffic protein in poliovirus RNA replication
    • Belov GA, Feng Q, Nikovics K, Jackson CL, Ehrenfeld E. 2008. A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog. 4:e1000216. http://dx.doi.org/10.1371/journal.ppat.1000216.
    • (2008) PLoS Pathog. , vol.4 , pp. e1000216
    • Belov, G.A.1    Feng, Q.2    Nikovics, K.3    Jackson, C.L.4    Ehrenfeld, E.5
  • 159
    • 0026519212 scopus 로고
    • Structural and functional characterization of the poliovirus replication complex
    • Bienz K, Egger D, Pfister T, Troxler M. 1992. Structural and functional characterization of the poliovirus replication complex. J. Virol. 66:2740-2747.
    • (1992) J. Virol. , vol.66 , pp. 2740-2747
    • Bienz, K.1    Egger, D.2    Pfister, T.3    Troxler, M.4
  • 160
    • 14744283953 scopus 로고    scopus 로고
    • Intracellular location and translocation of silent and active poliovirus replication complexes
    • Egger D, Bienz K. 2005. Intracellular location and translocation of silent and active poliovirus replication complexes. J. Gen. Virol. 86:707-718. http://dx.doi.org/10.1099/vir.0.80442-0.
    • (2005) J. Gen. Virol. , vol.86 , pp. 707-718
    • Egger, D.1    Bienz, K.2
  • 161
    • 80455132064 scopus 로고    scopus 로고
    • The transformation of enterovirus replication structures: A three-dimensional study of single- and doublemembrane compartments
    • Limpens RW, van der Schaar HM, Kumar D, Koster AJ, Snijder EJ, van Kuppeveld FJ, Barcena M. 2011. The transformation of enterovirus replication structures: a three-dimensional study of single- and doublemembrane compartments. mBio 2(5):00166-11. http://dx.doi.org/10.1128/mBio.00166-11.
    • (2011) mBio , vol.2 , Issue.5 , pp. 00166-00211
    • Limpens, R.W.1    Van Der Schaar, H.M.2    Kumar, D.3    Koster, A.J.4    Snijder, E.J.5    Van Kuppeveld, F.J.6    Barcena, M.7
  • 162
    • 0026716484 scopus 로고
    • Immunocytochemical localization of capsid-related particles in subcellular fractions of poliovirus-infected cells
    • Pfister T, Pasamontes L, Troxler M, Egger D, Bienz K. 1992. Immunocytochemical localization of capsid-related particles in subcellular fractions of poliovirus-infected cells. Virology 188:676-684. http://dx.doi.org/10.1016/0042-6822(92)90522-Q.
    • (1992) Virology , vol.188 , pp. 676-684
    • Pfister, T.1    Pasamontes, L.2    Troxler, M.3    Egger, D.4    Bienz, K.5
  • 163
    • 84878515366 scopus 로고    scopus 로고
    • Behind closed membranes: The secret lives of picornaviruses?
    • Richards AL, Jackson WT. 2013. Behind closed membranes: the secret lives of picornaviruses? PLoS Pathog. 9:e1003262. http://dx.doi.org/10.1371/journal.ppat.1003262.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003262
    • Richards, A.L.1    Jackson, W.T.2
  • 164
    • 84870776595 scopus 로고    scopus 로고
    • Intracellular vesicle acidification promotes maturation of infectious poliovirus particles
    • Richards AL, Jackson WT. 2012. Intracellular vesicle acidification promotes maturation of infectious poliovirus particles. PLoS Pathog. 8:e1003046. http://dx.doi.org/10.1371/journal.ppat.1003046.
    • (2012) PLoS Pathog. , vol.8 , pp. e1003046
    • Richards, A.L.1    Jackson, W.T.2
  • 166
    • 33644615778 scopus 로고    scopus 로고
    • Identification of AHBA biosynthetic genes related to geldanamycin biosynthesis in Streptomyces hygroscopicus 17997
    • He W, Wu L, Gao Q, Du Y, Wang Y. 2006. Identification of AHBA biosynthetic genes related to geldanamycin biosynthesis in Streptomyces hygroscopicus 17997. Curr. Microbiol. 52:197-203. http://dx.doi.org/10.1007/s00284-005-0203-y.
    • (2006) Curr. Microbiol. , vol.52 , pp. 197-203
    • He, W.1    Wu, L.2    Gao, Q.3    Du, Y.4    Wang, Y.5
  • 167
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, Akinaga S, Soga S, Sullivan W, Stensgard B, Toft D, Neckers LM. 1998. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 3:100-108. http://dx.doi.org/10.1379/1466-1268(1998)003〈0100:ARBTTN〉2.3.CO;2.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 168
    • 78651252353 scopus 로고    scopus 로고
    • Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly
    • Jirasko V, Montserret R, Lee JY, Gouttenoire J, Moradpour D, Penin F, Bartenschlager R. 2010. Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. PLoS Pathog. 6:e1001233. http://dx.doi.org/10.1371/journal.ppat.1001233.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001233
    • Jirasko, V.1    Montserret, R.2    Lee, J.Y.3    Gouttenoire, J.4    Moradpour, D.5    Penin, F.6    Bartenschlager, R.7
  • 169
    • 79952038244 scopus 로고    scopus 로고
    • Overview of taxonomy
    • Ehrenfeld E, Domingo E, Roos RP (ed), ASM Press, Washington, DC
    • Knowles NJ, Hovi T, King MQ, Stanway G. 2010. Overview of taxonomy, p 19-32. In Ehrenfeld E, Domingo E, Roos RP (ed), The picornaviruses. ASM Press, Washington, DC.
    • (2010) The Picornaviruses , pp. 19-32
    • Knowles, N.J.1    Hovi, T.2    King, M.Q.3    Stanway, G.4
  • 170
    • 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. 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
  • 171
    • 0024322439 scopus 로고
    • Icosahedral RNA virus structure
    • Rossmann MG, Johnson JE. 1989. Icosahedral RNA virus structure. Annu. Rev. Biochem. 58:533-573. http://dx.doi.org/10.1146/annurev.bi.58.070189.002533.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 533-573
    • Rossmann, M.G.1    Johnson, J.E.2
  • 172
    • 1242326207 scopus 로고    scopus 로고
    • Poliovirus receptors and cell entry
    • Semler BL, Wimmer E (ed), ASM Press, Washington, DC
    • Hogle JM, Rancaniello VR. 2002. Poliovirus receptors and cell entry, p 71-84. In Semler BL, Wimmer E (ed), Molecular biology of picornaviruses. ASM Press, Washington, DC.
    • (2002) Molecular Biology of Picornaviruses , pp. 71-84
    • Hogle, J.M.1    Rancaniello, V.R.2
  • 174
    • 0031762554 scopus 로고    scopus 로고
    • The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication
    • McKnight KL, Lemon SM. 1998. The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication. RNA 4:1569-1584. http://dx.doi.org/10.1017/S1355838298981006.
    • (1998) RNA , vol.4 , pp. 1569-1584
    • McKnight, K.L.1    Lemon, S.M.2
  • 176
    • 34547734952 scopus 로고    scopus 로고
    • Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus
    • Jones CT, Murray CL, Eastman DK, Tassello J, Rice CM. 2007. Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus. J. Virol. 81:8374-8383. http://dx.doi.org/10.1128/JVI.00690-07.
    • (2007) J. Virol. , vol.81 , pp. 8374-8383
    • Jones, C.T.1    Murray, C.L.2    Eastman, D.K.3    Tassello, J.4    Rice, C.M.5
  • 177
    • 84876520299 scopus 로고    scopus 로고
    • Hepatitis C virus proteins: From structure to function
    • Moradpour D, Penin F. 2013. Hepatitis C virus proteins: from structure to function. Curr. Top. Microbiol. Immunol. 369:113-142. http://dx.doi.org/10.1007/978-3-642-27340-7-5.
    • (2013) Curr. Top. Microbiol. Immunol. , vol.369 , pp. 113-142
    • Moradpour, D.1    Penin, F.2
  • 178
    • 78651399012 scopus 로고    scopus 로고
    • The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly
    • Phan T, Kohlway A, Dimberu P, Pyle AM, Lindenbach BD. 2011. The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly. J. Virol. 85:1193-1204. http://dx.doi.org/10.1128/JVI.01889-10.
    • (2011) J. Virol. , vol.85 , pp. 1193-1204
    • Phan, T.1    Kohlway, A.2    Dimberu, P.3    Pyle, A.M.4    Lindenbach, B.D.5
  • 179
    • 69249231061 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protein contributes to virus particle assembly via opposing epistatic interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes
    • Phan T, Beran RK, Peters C, Lorenz IC, Lindenbach BD. 2009. Hepatitis C virus NS2 protein contributes to virus particle assembly via opposing epistatic interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes. J. Virol. 83:8379-8395. http://dx.doi.org/10.1128/JVI.00891-09.
    • (2009) J. Virol. , vol.83 , pp. 8379-8395
    • Phan, T.1    Beran, R.K.2    Peters, C.3    Lorenz, I.C.4    Lindenbach, B.D.5
  • 180
    • 47749092840 scopus 로고    scopus 로고
    • NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly
    • Ma Y, Yates J, Liang Y, Lemon SM, Yi M. 2008. NS3 helicase domains involved in infectious intracellular hepatitis C virus particle assembly. J. Virol. 82:7624-7639. http://dx.doi.org/10.1128/JVI.00724-08.
    • (2008) J. Virol. , vol.82 , pp. 7624-7639
    • Ma, Y.1    Yates, J.2    Liang, Y.3    Lemon, S.M.4    Yi, M.5
  • 181
    • 0035032324 scopus 로고    scopus 로고
    • Coupling between replication and packaging of flavivirus RNA: Evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus
    • Khromykh AA, Varnavski AN, Sedlak PL, Westaway EG. 2001. Coupling between replication and packaging of flavivirus RNA: evidence derived from the use of DNA-based full-length cDNA clones of Kunjin virus. J. Virol. 75:4633-4640. http://dx.doi.org/10.1128/JVI.75.10.4633-4640.2001.
    • (2001) J. Virol. , vol.75 , pp. 4633-4640
    • Khromykh, A.A.1    Varnavski, A.N.2    Sedlak, P.L.3    Westaway, E.G.4
  • 183
    • 0026441615 scopus 로고
    • Replication complexes associated with the morphogenesis of rubella virus
    • Lee JY, Marshall JA, Bowden DS. 1992. Replication complexes associated with the morphogenesis of rubella virus. Arch. Virol. 122:95-106. http://dx.doi.org/10.1007/BF01321120.
    • (1992) Arch. Virol. , vol.122 , pp. 95-106
    • Lee, J.Y.1    Marshall, J.A.2    Bowden, D.S.3
  • 184
    • 80052131312 scopus 로고    scopus 로고
    • Mouse hepatic cells support assembly of infectious hepatitis C virus particles
    • Long G, Hiet MS, Windisch MP, Lee JY, Lohmann V, Bartenschlager R. 2011. Mouse hepatic cells support assembly of infectious hepatitis C virus particles. Gastroenterology 141:1057-1066. http://dx.doi.org/10.1053/j.gastro.2011.06.010.
    • (2011) Gastroenterology , vol.141 , pp. 1057-1066
    • Long, G.1    Hiet, M.S.2    Windisch, M.P.3    Lee, J.Y.4    Lohmann, V.5    Bartenschlager, R.6
  • 186
    • 0037219512 scopus 로고    scopus 로고
    • Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope
    • Op De Beeck A, Molenkamp R, Caron M, Ben Younes A, Bredenbeek P, Dubuisson J. 2003. Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope. J. Virol. 77:813-820. http://dx.doi.org/10.1128/JVI.77.2.813-820.2003.
    • (2003) J. Virol. , vol.77 , pp. 813-820
    • Op De Beeck, A.1    Molenkamp, R.2    Caron, M.3    Ben Younes, A.4    Bredenbeek, P.5    Dubuisson, J.6
  • 187
    • 7644232918 scopus 로고    scopus 로고
    • The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals
    • Op De Beeck A, Rouille Y, Caron M, Duvet S, Dubuisson J. 2004. The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals. J. Virol. 78:12591-12602. http://dx.doi.org/10.1128/JVI.78.22.12591-12602.2004.
    • (2004) J. Virol. , vol.78 , pp. 12591-12602
    • Op De Beeck, A.1    Rouille, Y.2    Caron, M.3    Duvet, S.4    Dubuisson, J.5
  • 188
    • 84858973962 scopus 로고    scopus 로고
    • The coronavirus E protein: Assembly and beyond
    • Ruch TR, Machamer CE. 2012. The coronavirus E protein: assembly and beyond. Viruses 4:363-382. http://dx.doi.org/10.3390/v4030363.
    • (2012) Viruses , vol.4 , pp. 363-382
    • Ruch, T.R.1    Machamer, C.E.2
  • 190
    • 0021322863 scopus 로고
    • Replication of coronavirus MHVA59 in sac- cells: Determination of the first site of budding of progeny virions
    • Tooze J, Tooze S, Warren G. 1984. Replication of coronavirus MHVA59 in sac- cells: determination of the first site of budding of progeny virions. Eur. J. Cell Biol. 33:281-293.
    • (1984) Eur. J. Cell Biol. , vol.33 , pp. 281-293
    • Tooze, J.1    Tooze, S.2    Warren, G.3
  • 192
    • 49149113893 scopus 로고    scopus 로고
    • Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles
    • Masaki T, Suzuki R, Murakami K, Aizaki H, Ishii K, Murayama A, Date T, Matsuura Y, Miyamura T, Wakita T, Suzuki T. 2008. Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles. J. Virol. 82:7964-7976. http://dx.doi.org/10.1128/JVI.00826-08.
    • (2008) J. Virol. , vol.82 , pp. 7964-7976
    • Masaki, T.1    Suzuki, R.2    Murakami, K.3    Aizaki, H.4    Ishii, K.5    Murayama, A.6    Date, T.7    Matsuura, Y.8    Miyamura, T.9    Wakita, T.10    Suzuki, T.11
  • 193
    • 84884283137 scopus 로고    scopus 로고
    • The ins and outs of hepatitis C virus entry and assembly
    • Lindenbach BD, Rice CM. 2013. The ins and outs of hepatitis C virus entry and assembly. Nat. Rev. Microbiol. 11:688-700. http://dx.doi.org/10.1038/nrmicro3098.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 688-700
    • Lindenbach, B.D.1    Rice, C.M.2
  • 194
    • 81255200368 scopus 로고    scopus 로고
    • A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus
    • Jones DM, Atoom AM, Zhang X, Kottilil S, Russell RS. 2011. A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus. J. Virol. 85:12351-12361. http://dx.doi.org/10.1128/JVI.05313-11.
    • (2011) J. Virol. , vol.85 , pp. 12351-12361
    • Jones, D.M.1    Atoom, A.M.2    Zhang, X.3    Kottilil, S.4    Russell, R.S.5
  • 195
    • 78651249671 scopus 로고    scopus 로고
    • Dimerization-driven interaction of hepatitis C virus core protein with NS3 helicase
    • Mousseau G, Kota S, Takahashi V, Frick DN, Strosberg AD. 2011. Dimerization-driven interaction of hepatitis C virus core protein with NS3 helicase. J. Gen. Virol. 92:101-111. http://dx.doi.org/10.1099/vir.0.023325-0.
    • (2011) J. Gen. Virol. , vol.92 , pp. 101-111
    • Mousseau, G.1    Kota, S.2    Takahashi, V.3    Frick, D.N.4    Strosberg, A.D.5
  • 196
    • 41149101538 scopus 로고    scopus 로고
    • Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions
    • Patkar CG, Kuhn RJ. 2008. Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions. J. Virol. 82:3342-3352. http://dx.doi.org/10.1128/JVI.02447-07.
    • (2008) J. Virol. , vol.82 , pp. 3342-3352
    • Patkar, C.G.1    Kuhn, R.J.2
  • 197
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer BM, Rice CM. 2002. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J. Virol. 76:4773-4784. http://dx.doi.org/10.1128/JVI.76.10.4773-4784.2002.
    • (2002) J. Virol. , vol.76 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 200
    • 84875782703 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis virus nsP2 protein regulates packaging of the viral genome into infectious virions
    • Kim DY, Atasheva S, Frolova EI, Frolov I. 2013. Venezuelan equine encephalitis virus nsP2 protein regulates packaging of the viral genome into infectious virions. J. Virol. 87:4202-4213. http://dx.doi.org/10.1128/JVI.03142-12.
    • (2013) J. Virol. , vol.87 , pp. 4202-4213
    • Kim, D.Y.1    Atasheva, S.2    Frolova, E.I.3    Frolov, I.4
  • 201
    • 84865305540 scopus 로고    scopus 로고
    • A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes
    • Groat-Carmona AM, Orozco S, Friebe P, Payne A, Kramer L, Harris E. 2012. A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes. Virology 432:511-526. http://dx.doi.org/10.1016/j.virol.2012.06.028.
    • (2012) Virology , vol.432 , pp. 511-526
    • Groat-Carmona, A.M.1    Orozco, S.2    Friebe, P.3    Payne, A.4    Kramer, L.5    Harris, E.6
  • 202
    • 79961205984 scopus 로고    scopus 로고
    • Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution
    • Kim DY, Firth AE, Atasheva S, Frolova EI, Frolov I. 2011. Conservation of a packaging signal and the viral genome RNA packaging mechanism in alphavirus evolution. J. Virol. 85:8022-8036. http://dx.doi.org/10.1128/JVI.00644-11.
    • (2011) J. Virol. , vol.85 , pp. 8022-8036
    • Kim, D.Y.1    Firth, A.E.2    Atasheva, S.3    Frolova, E.I.4    Frolov, I.5
  • 203
    • 0029887660 scopus 로고    scopus 로고
    • Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction
    • Liu Z, Yang D, Qiu Z, Lim KT, Chong P, Gillam S. 1996. Identification of domains in rubella virus genomic RNA and capsid protein necessary for specific interaction. J. Virol. 70:2184-2190.
    • (1996) J. Virol. , vol.70 , pp. 2184-2190
    • Liu, Z.1    Yang, D.2    Qiu, Z.3    Lim, K.T.4    Chong, P.5    Gillam, S.6
  • 204
    • 84876319689 scopus 로고    scopus 로고
    • Functional analysis of the murine coronavirus genomic RNA packaging signal
    • Kuo L, Masters PS. 2013. Functional analysis of the murine coronavirus genomic RNA packaging signal. J. Virol. 87:5182-5192. http://dx.doi.org/10.1128/JVI.00100-13.
    • (2013) J. Virol. , vol.87 , pp. 5182-5192
    • Kuo, L.1    Masters, P.S.2
  • 206
    • 27644584130 scopus 로고    scopus 로고
    • Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent
    • Hsieh PK, Chang SC, Huang CC, Lee TT, Hsiao CW, Kou YH, Chen IY, Chang CK, Huang TH, Chang MF. 2005. Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent. J. Virol. 79:13848-13855. http://dx.doi.org/10.1128/JVI.79.22.13848-13855.2005.
    • (2005) J. Virol. , vol.79 , pp. 13848-13855
    • Hsieh, P.K.1    Chang, S.C.2    Huang, C.C.3    Lee, T.T.4    Hsiao, C.W.5    Kou, Y.H.6    Chen, I.Y.7    Chang, C.K.8    Huang, T.H.9    Chang, M.F.10
  • 208
    • 70349634804 scopus 로고    scopus 로고
    • Knockdown of autophagy-related gene decreases the production of infectious hepatitisCvirus particles
    • Tanida I, Fukasawa M, Ueno T, Kominami E, Wakita T, Hanada K. 2009. Knockdown of autophagy-related gene decreases the production of infectious hepatitisCvirus particles. Autophagy 5:937-945. http://dx.doi.org/10.4161/auto.5.7.9243.
    • (2009) Autophagy , vol.5 , pp. 937-945
    • Tanida, I.1    Fukasawa, M.2    Ueno, T.3    Kominami, E.4    Wakita, T.5    Hanada, K.6
  • 209
    • 68949117729 scopus 로고    scopus 로고
    • The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity
    • Parent R, Qu X, Petit MA, Beretta L. 2009. The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity. Hepatology 49:1798-1809. http://dx.doi.org/10.1002/hep.22852.
    • (2009) Hepatology , vol.49 , pp. 1798-1809
    • Parent, R.1    Qu, X.2    Petit, M.A.3    Beretta, L.4
  • 211
    • 84866154404 scopus 로고    scopus 로고
    • Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assembly
    • Neveu G, Barouch-Bentov R, Ziv-Av A, Gerber D, Jacob Y, Einav S. 2012. Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assembly. PLoS Pathog. 8:e1002845. http://dx.doi.org/10.1371/journal.ppat.1002845.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002845
    • Neveu, G.1    Barouch-Bentov, R.2    Ziv-Av, A.3    Gerber, D.4    Jacob, Y.5    Einav, S.6
  • 212
    • 84869019846 scopus 로고    scopus 로고
    • Hepatitis C virus (HCV) induces formation of stress granules whose proteins regulate HCV RNA replication and virus assembly and egress
    • Garaigorta U, Heim MH, Boyd B, Wieland S, Chisari FV. 2012. Hepatitis C virus (HCV) induces formation of stress granules whose proteins regulate HCV RNA replication and virus assembly and egress. J. Virol. 86:11043-11056. http://dx.doi.org/10.1128/JVI.07101-11.
    • (2012) J. Virol. , vol.86 , pp. 11043-11056
    • Garaigorta, U.1    Heim, M.H.2    Boyd, B.3    Wieland, S.4    Chisari, F.V.5
  • 214
    • 34848917602 scopus 로고    scopus 로고
    • Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A
    • Hunt TA, Urbanowski MD, Kakani K, Law LM, Brinton MA, Hobman TC. 2007. Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A. Cell. Microbiol. 9:2756-2766. http://dx.doi.org/10.1111/j.1462-5822.2007.01046.x.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2756-2766
    • Hunt, T.A.1    Urbanowski, M.D.2    Kakani, K.3    Law, L.M.4    Brinton, M.A.5    Hobman, T.C.6
  • 215
    • 78650603909 scopus 로고    scopus 로고
    • Interaction between the yellow fever virus nonstructural protein NS3 and the host protein Alix contributes to the release of infectious particles
    • Carpp LN, Galler R, Bonaldo MC. 2011. Interaction between the yellow fever virus nonstructural protein NS3 and the host protein Alix contributes to the release of infectious particles. Microbes Infect. 13:85-95. http://dx.doi.org/10.1016/j.micinf.2010.10.010.
    • (2011) Microbes Infect. , vol.13 , pp. 85-95
    • Carpp, L.N.1    Galler, R.2    Bonaldo, M.C.3
  • 216
    • 78751511080 scopus 로고    scopus 로고
    • Envelope lipid-packing as a critical factor for the biological activity and stability of alphavirus particles isolated from mammalian and mosquito cells
    • Sousa IP, Jr, Carvalho CA, Ferreira DF, Weissmuller G, Rocha GM, Silva JL, Gomes AM. 2011. Envelope lipid-packing as a critical factor for the biological activity and stability of alphavirus particles isolated from mammalian and mosquito cells. J. Biol. Chem. 286:1730-1736. http://dx.doi.org/10.1074/jbc.M110.198002.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1730-1736
    • Sousa, I.P.1    Carvalho, C.A.2    Ferreira, D.F.3    Weissmuller, G.4    Rocha, G.M.5    Silva, J.L.6    Gomes, A.M.7
  • 217
    • 0018159248 scopus 로고
    • Chemical cross-linking of proteins of Semliki Forest virus: Virus particles and plasma membranes from BHK-21 cells treated with colchicine or dibucaine
    • Richardson CD, Vance DE. 1978. Chemical cross-linking of proteins of Semliki Forest virus: virus particles and plasma membranes from BHK-21 cells treated with colchicine or dibucaine. J. Virol. 28:193-198.
    • (1978) J. Virol. , vol.28 , pp. 193-198
    • Richardson, C.D.1    Vance, D.E.2
  • 218
    • 0017810501 scopus 로고
    • The effect of colchicine and dibucaine on the morphogenesis of Semliki Forest virus
    • Richardson CD, Vance DE. 1978. The effect of colchicine and dibucaine on the morphogenesis of Semliki Forest virus. J. Biol. Chem. 253:4584-4589.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4584-4589
    • Richardson, C.D.1    Vance, D.E.2
  • 219
    • 2142773504 scopus 로고    scopus 로고
    • Polioviruses (Picornaviridae): Molecular biology
    • Granoff WA (ed), Academic Press, New York, NY
    • Pfister T, Mirzayan C, Wimmer E. 1999. Polioviruses (Picornaviridae): molecular biology, p 1330-1348. In Granoff WA (ed), The encyclopedia of virology, 2nd ed. Academic Press, New York, NY.
    • (1999) The Encyclopedia of Virology, 2nd Ed. , pp. 1330-1348
    • Pfister, T.1    Mirzayan, C.2    Wimmer, E.3


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