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Volumn 81, Issue 4, 2007, Pages 1879-1887

Deterministic, compensatory mutational events in the capsid of foot-and-mouth disease virus in response to the introduction of mutations found in viruses from persistent infections

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTATION; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CYTOLYSIS; FOOT AND MOUTH DISEASE VIRUS; GENE CLUSTER; GENETIC CONSERVATION; GENOTYPE PHENOTYPE CORRELATION; NONHUMAN; PERSISTENT VIRUS INFECTION; PRIORITY JOURNAL; VIRION; VIRUS CAPSID; VIRUS CELL INTERACTION; VIRUS GENOME; VIRUS MUTANT; VIRUS MUTATION; VIRUS REPLICATION; VIRUS VIRULENCE;

EID: 33846784067     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01899-06     Document Type: Article
Times cited : (24)

References (60)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • Acharya, R., E. Fry, D. Stuart, G. Fox, D. Rowlands, and F. Brown. 1989. The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å 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
    • 0035168149 scopus 로고    scopus 로고
    • Coxsackievirus A9 VP mutants with enhanced or hindered A particle formation and decreased infectivity
    • Airaksinen, A., M. Roivainen, and T. Hovi. 2001. Coxsackievirus A9 VP mutants with enhanced or hindered A particle formation and decreased infectivity. J. Virol. 75:952-960.
    • (2001) J. Virol , vol.75 , pp. 952-960
    • Airaksinen, A.1    Roivainen, M.2    Hovi, T.3
  • 3
    • 0027411107 scopus 로고
    • Suppression of protein structure destabilizing mutations in Bacillus thuringiensis delta-endotoxins by second site mutations
    • Almond, B. D., and D. H. Dean. 1993. Suppression of protein structure destabilizing mutations in Bacillus thuringiensis delta-endotoxins by second site mutations. Biochemistry 32:1040-1046.
    • (1993) Biochemistry , vol.32 , pp. 1040-1046
    • Almond, B.D.1    Dean, D.H.2
  • 5
    • 0025231512 scopus 로고
    • How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases
    • Blacklow, S. C., and J. R. Knowles. 1990. How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases. Biochemistry 29:4099-4108.
    • (1990) Biochemistry , vol.29 , pp. 4099-4108
    • Blacklow, S.C.1    Knowles, J.R.2
  • 6
    • 0030042461 scopus 로고    scopus 로고
    • Second-site reversion of a structural defect in bacteriophage T4 lysozyme
    • Bouvier, S. E., and A. R. Poteete. 1996. Second-site reversion of a structural defect in bacteriophage T4 lysozyme. FASEB J. 10:159-163.
    • (1996) FASEB J , vol.10 , pp. 159-163
    • Bouvier, S.E.1    Poteete, A.R.2
  • 7
    • 0027141517 scopus 로고
    • Long-range structural effects in a second-site revenant of a mutant dihydrofolate reductase
    • Brown, K. A., E. E. Howell, and J. Kraut. 1993. Long-range structural effects in a second-site revenant of a mutant dihydrofolate reductase. Proc. Natl. Acad. Sci. USA 90:11753-11756.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11753-11756
    • Brown, K.A.1    Howell, E.E.2    Kraut, J.3
  • 8
    • 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
    • Bubeck, D., D. J. Filman, N. Cheng, A. C. Steven, J. M. Hogle, and D. M. Belnap. 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
  • 9
    • 33745943265 scopus 로고    scopus 로고
    • Structural tolerance versus functional intolerance to mutation of hydrophobic core residues surrounding cavities in a parvovirus capsid
    • Carreira, A., and M. G. Mateu. 2006. Structural tolerance versus functional intolerance to mutation of hydrophobic core residues surrounding cavities in a parvovirus capsid. J. Mol. Biol. 360:1081-1093.
    • (2006) J. Mol. Biol , vol.360 , pp. 1081-1093
    • Carreira, A.1    Mateu, M.G.2
  • 10
    • 33744918278 scopus 로고    scopus 로고
    • Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein
    • Chanel-Vos, C., and M. Kielian. 2006. Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein. J. Virol. 80:6115-6122.
    • (2006) J. Virol , vol.80 , pp. 6115-6122
    • Chanel-Vos, C.1    Kielian, M.2
  • 11
    • 0034003379 scopus 로고    scopus 로고
    • Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation. J. Virol. 74:4273-4283.
    • (2000) J. Virol , vol.74 , pp. 4273-4283
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 12
    • 0343170500 scopus 로고
    • Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine-isoleucine replacement at position 57
    • Das, G., D. R. Hickey, D. McLendon, G. McLendon, and F. Sherman. 1989. Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine-isoleucine replacement at position 57. Proc. Natl. Acad. Sci. USA 86:496-499.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 496-499
    • Das, G.1    Hickey, D.R.2    McLendon, D.3    McLendon, G.4    Sherman, F.5
  • 13
    • 0022392249 scopus 로고
    • Establishment of cell lines persistently infected with foot-and-mouth disease virus
    • de la Torre, J. C., M. Dávila, F. Sobrino, J. Ortín, and E. Domingo. 1985. Establishment of cell lines persistently infected with foot-and-mouth disease virus. Virology 145:24-35.
    • (1985) Virology , vol.145 , pp. 24-35
    • de la Torre, J.C.1    Dávila, M.2    Sobrino, F.3    Ortín, J.4    Domingo, E.5
  • 15
    • 0030945684 scopus 로고    scopus 로고
    • Second-site reversion of a dysfunctional mutation in a conserved region of the tobacco mosaic tobamovirus movement protein
    • Deom, C. M., and X. Z. He. 1997. Second-site reversion of a dysfunctional mutation in a conserved region of the tobacco mosaic tobamovirus movement protein. Virology 232:13-18.
    • (1997) Virology , vol.232 , pp. 13-18
    • Deom, C.M.1    He, X.Z.2
  • 16
    • 0025036307 scopus 로고
    • Unique amino acid substitutions in the capsid proteins of foot-and-mouth disease virus from a persistent infection in cell culture
    • Díez, J., M. Dávila, C. Escarmís, M. G. Mateu, J. Domínguez, J. J. Pérez, E. Giralt, J. A. Melero, and E. Domingo. 1990. Unique amino acid substitutions in the capsid proteins of foot-and-mouth disease virus from a persistent infection in cell culture. J. Virol. 64:5519-5528.
    • (1990) J. Virol , vol.64 , pp. 5519-5528
    • Díez, J.1    Dávila, M.2    Escarmís, C.3    Mateu, M.G.4    Domínguez, J.5    Pérez, J.J.6    Giralt, E.7    Melero, J.A.8    Domingo, E.9
  • 17
    • 30644478836 scopus 로고    scopus 로고
    • ed, Quasispecies. Concepts and implications for virology. Springer, New York, NY. Curr. Top. Microbiol. Immunol. 299
    • Domingo, E., (ed.). 2006. Current topics in microbiology and immunology, vol. 299. Quasispecies. Concepts and implications for virology. Springer, New York, NY. Curr. Top. Microbiol. Immunol. 299:51-82.
    • (2006) Current topics in microbiology and immunology , vol.299 , pp. 51-82
  • 18
    • 0030747157 scopus 로고    scopus 로고
    • RNA virus mutations and fitness for survival
    • Domingo, E., and J. J. Holland. 1997. RNA virus mutations and fitness for survival. Annu. Rev. Microbiol. 51:151-178.
    • (1997) Annu. Rev. Microbiol , vol.51 , pp. 151-178
    • Domingo, E.1    Holland, J.J.2
  • 19
    • 0002482572 scopus 로고    scopus 로고
    • Viral quasispecies and fitness variations
    • E. Domingo, R. G. Webster, and J. J. Holland ed, Academic Press, San Diego, CA
    • Domingo, E., C. Escarmís, L. Menéndez-Arias, and J. J. Holland. 1999. Viral quasispecies and fitness variations, p. 141-161. In E. Domingo, R. G. Webster, and J. J. Holland (ed.), Origin and evolution of viruses. Academic Press, San Diego, CA.
    • (1999) Origin and evolution of viruses , pp. 141-161
    • Domingo, E.1    Escarmís, C.2    Menéndez-Arias, L.3    Holland, J.J.4
  • 21
    • 3543028670 scopus 로고    scopus 로고
    • A compensatory double mutation of the alanine-86 to leucine mutant located in the hinge region of the iron-sulfur protein of the yeast cytochrome bel complex
    • Ebert, C. E., and D. S. Beattie. 2004. A compensatory double mutation of the alanine-86 to leucine mutant located in the hinge region of the iron-sulfur protein of the yeast cytochrome bel complex. Arch. Biochem. Biophys. 429:16-22.
    • (2004) Arch. Biochem. Biophys , vol.429 , pp. 16-22
    • Ebert, C.E.1    Beattie, D.S.2
  • 23
    • 33744457709 scopus 로고    scopus 로고
    • A novel method for detecting intramolecular coevolution: Adding a further dimension to selective constraints analysis
    • Fares, M. A., and S. A. A. Travers. 2006. A novel method for detecting intramolecular coevolution: adding a further dimension to selective constraints analysis. Genetics 173:9-21.
    • (2006) Genetics , vol.173 , pp. 9-21
    • Fares, M.A.1    Travers, S.A.A.2
  • 24
    • 0024316730 scopus 로고
    • Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus
    • Filman, D. J., R. Syed, M. Chow, A. J. Macadam, P. D. Minor, and J. M. Hogle. 1989. Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. EMBO J. 8:1567-1579.
    • (1989) EMBO J , vol.8 , pp. 1567-1579
    • Filman, D.J.1    Syed, R.2    Chow, M.3    Macadam, A.J.4    Minor, P.D.5    Hogle, J.M.6
  • 25
    • 0028560446 scopus 로고
    • Second-site suppressor mutations at glycine 218 and histidine 245 in the alpha subunit of F1F0 ATP synthase in Escherichia coli
    • Hartzog, P. E., and B. D. Cain. 1994. Second-site suppressor mutations at glycine 218 and histidine 245 in the alpha subunit of F1F0 ATP synthase in Escherichia coli. J. Biol. Chem. 269:32313-32317.
    • (1994) J. Biol. Chem , vol.269 , pp. 32313-32317
    • Hartzog, P.E.1    Cain, B.D.2
  • 26
    • 0009404164 scopus 로고
    • Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins
    • Jarvik, J., and D. Botstein. 1975. Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins. Proc. Natl. Acad. Sci. USA 72:2738-2742.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2738-2742
    • Jarvik, J.1    Botstein, D.2
  • 27
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • Joerger, A. C., M. D. Allen, and A. R. Fersht. 2004. Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J. Biol. Chem. 279:1291-1296.
    • (2004) J. Biol. Chem , vol.279 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 29
    • 0023701043 scopus 로고
    • Second-site revertants of Escherichia coli trp represser mutants
    • Klig, L. S., D. L. Oxender, and C. Yanofsky. 1988. Second-site revertants of Escherichia coli trp represser mutants. Genetics 120:651-655.
    • (1988) Genetics , vol.120 , pp. 651-655
    • Klig, L.S.1    Oxender, D.L.2    Yanofsky, C.3
  • 31
    • 9444269272 scopus 로고    scopus 로고
    • Compensated deleterious mutations in insect genomes
    • Kulathinal, R. J., B. R. Bettencourt, and D. L. Hartl. 2004. Compensated deleterious mutations in insect genomes. Science 306:1553-1554.
    • (2004) Science , vol.306 , pp. 1553-1554
    • Kulathinal, R.J.1    Bettencourt, B.R.2    Hartl, D.L.3
  • 33
    • 0034872867 scopus 로고    scopus 로고
    • Second-site, intragenic alterations in the gene encoding subunit II of cytochrome c oxidase from yeast can suppress two different missense mutations
    • Machingo, Q., M. Mazourek, and W. Cameron. 2001. Second-site, intragenic alterations in the gene encoding subunit II of cytochrome c oxidase from yeast can suppress two different missense mutations. Curr. Genet. 39:297-304.
    • (2001) Curr. Genet , vol.39 , pp. 297-304
    • Machingo, Q.1    Mazourek, M.2    Cameron, W.3
  • 35
    • 0142039882 scopus 로고    scopus 로고
    • Complete alanine scanning of intersubunit interfaces in a foot-and-mouth disease virus capsid reveals critical contributions of many side chains to particle stability and viral function
    • Mateo, R., A. Díaz, E. Baranowski, and M. G. Mateu. 2003. Complete alanine scanning of intersubunit interfaces in a foot-and-mouth disease virus capsid reveals critical contributions of many side chains to particle stability and viral function. J. Biol. Chem. 278:41019-41027.
    • (2003) J. Biol. Chem , vol.278 , pp. 41019-41027
    • Mateo, R.1    Díaz, A.2    Baranowski, E.3    Mateu, M.G.4
  • 36
    • 0033616825 scopus 로고    scopus 로고
    • Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
    • Mateu, M. G., and A. R. Fersht. 1999. Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization. Proc. Natl. Acad. Sci. USA 96:3595-3599.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3595-3599
    • Mateu, M.G.1    Fersht, A.R.2
  • 37
    • 0034141471 scopus 로고    scopus 로고
    • Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
    • Nikolova, P. V., K. B. Wong, B. DeDecker, J. Henckel, and A. R. Fersht. 2000. Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. EMBO J. 19:370-378.
    • (2000) EMBO J , vol.19 , pp. 370-378
    • Nikolova, P.V.1    Wong, K.B.2    DeDecker, B.3    Henckel, J.4    Fersht, A.R.5
  • 38
    • 0032804864 scopus 로고    scopus 로고
    • Increased fitness of drug-resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy
    • Nijhuis, M., R. Schuurman, D. de Jong, J. Erickson, E. Gustchina, J. Albert, P. Schipper, S. Gulnik, and C. A. Boucher. 1999. Increased fitness of drug-resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy. AIDS 13:2349-2359.
    • (1999) AIDS , vol.13 , pp. 2349-2359
    • Nijhuis, M.1    Schuurman, R.2    de Jong, D.3    Erickson, J.4    Gustchina, E.5    Albert, J.6    Schipper, P.7    Gulnik, S.8    Boucher, C.A.9
  • 39
    • 0344348869 scopus 로고    scopus 로고
    • Second-site reversion of a human immunodeficiency virus type 1 reverse transcriptase mutant that restores enzyme function and replication capacity
    • Olivares, I., V. Sánchez-Merino, M. A. Martínez, E. Domingo, C. López-Galíndez, and L. Menéndez-Arias. 1999. Second-site reversion of a human immunodeficiency virus type 1 reverse transcriptase mutant that restores enzyme function and replication capacity. J. Virol. 73:6293-6298.
    • (1999) J. Virol , vol.73 , pp. 6293-6298
    • Olivares, I.1    Sánchez-Merino, V.2    Martínez, M.A.3    Domingo, E.4    López-Galíndez, C.5    Menéndez-Arias, L.6
  • 40
    • 2942704147 scopus 로고    scopus 로고
    • Tryptophan scanning mutagenesis of aromatic residues within the polymerase domain of HIV-1 reverse transcriptase: Critical role of Phe-130 for p51 function and second-site revertant restoring viral replication capacity
    • Olivares, I., M. Gutiérrez-Rivas, C. López- Galíndez, and L. Menéndez-Arias. 2004. Tryptophan scanning mutagenesis of aromatic residues within the polymerase domain of HIV-1 reverse transcriptase: critical role of Phe-130 for p51 function and second-site revertant restoring viral replication capacity. Virology 324:400-411.
    • (2004) Virology , vol.324 , pp. 400-411
    • Olivares, I.1    Gutiérrez-Rivas, M.2    López- Galíndez, C.3    Menéndez-Arias, L.4
  • 41
    • 0030926508 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 matrix revertants: Effects on virus assembly, Gag processing, and Env incorporation into virions
    • Ono, A., M. Huang, and E. O. Freed. 1997. Characterization of human immunodeficiency virus type 1 matrix revertants: effects on virus assembly, Gag processing, and Env incorporation into virions. J. Virol. 71:4409-4418.
    • (1997) J. Virol , vol.71 , pp. 4409-4418
    • Ono, A.1    Huang, M.2    Freed, E.O.3
  • 42
    • 0029896360 scopus 로고    scopus 로고
    • Kinetic characterization of human immunodeficiency virus type-1 protease-resistant variants
    • Pazhanisamy, S., C. M. Stuver, A. B. Cullinan, N. Margolin, B. G. Rao, and D. J. Livingston. 1996. Kinetic characterization of human immunodeficiency virus type-1 protease-resistant variants. J. Biol. Chem. 271:17979-17985.
    • (1996) J. Biol. Chem , vol.271 , pp. 17979-17985
    • Pazhanisamy, S.1    Stuver, C.M.2    Cullinan, A.B.3    Margolin, N.4    Rao, B.G.5    Livingston, D.J.6
  • 43
    • 0035881966 scopus 로고    scopus 로고
    • Mutations at amino acid positions 63, 189, and 396 of human immunodeficiency virus type 1 reverse transcriptase (RT) partially restore the DNA polymerase activity of a Trp229Tyr mutant RT
    • Pelemans, H., R. Esnouf, K. L. Min, M. Parniak, E. De Clercq, and J. Balzarini. 2001. Mutations at amino acid positions 63, 189, and 396 of human immunodeficiency virus type 1 reverse transcriptase (RT) partially restore the DNA polymerase activity of a Trp229Tyr mutant RT. Virology 287:143-150.
    • (2001) Virology , vol.287 , pp. 143-150
    • Pelemans, H.1    Esnouf, R.2    Min, K.L.3    Parniak, M.4    De Clercq, E.5    Balzarini, J.6
  • 44
    • 21044438202 scopus 로고    scopus 로고
    • The rate of compensatory mutation in the DNA bacteriophage ΦX174
    • Poon, A., and L. Chao. 2005. The rate of compensatory mutation in the DNA bacteriophage ΦX174. Genetics 170:989-999.
    • (2005) Genetics , vol.170 , pp. 989-999
    • Poon, A.1    Chao, L.2
  • 45
    • 0030671578 scopus 로고    scopus 로고
    • Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations
    • Poteete, A. R., D. Rennell, S. E. Bouvier, and L. W. Hardy. 1997. Alteration of T4 lysozyme structure by second-site reversion of deleterious mutations. Protein Sci. 6:2418-2425.
    • (1997) Protein Sci , vol.6 , pp. 2418-2425
    • Poteete, A.R.1    Rennell, D.2    Bouvier, S.E.3    Hardy, L.W.4
  • 46
    • 0024226784 scopus 로고
    • Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion
    • Regan, L., L. Buxbaum, K. Hill, and P. Schimmel. 1988. Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion. J. Biol. Chem. 263:18598-18600.
    • (1988) J. Biol. Chem , vol.263 , pp. 18598-18600
    • Regan, L.1    Buxbaum, L.2    Hill, K.3    Schimmel, P.4
  • 47
    • 1542267838 scopus 로고    scopus 로고
    • Role of interfacial amino acid residues in assembly, stability and conformation of a spherical virus capsid
    • Reguera, J., A. Carreira, L. Riolobos, J. M. Almendral, and M. G. Mateu. 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
  • 48
    • 0042208058 scopus 로고    scopus 로고
    • Second-site suppressor mutations for the serine 202 to phenylalanine substitution within the interdomain loop of the tetracycline efflux protein Tet(C)
    • Sapunaric, F. M., and S. B. Levy. 2003. Second-site suppressor mutations for the serine 202 to phenylalanine substitution within the interdomain loop of the tetracycline efflux protein Tet(C). J. Biol. Chem. 278:28588-28592.
    • (2003) J. Biol. Chem , vol.278 , pp. 28588-28592
    • Sapunaric, F.M.1    Levy, S.B.2
  • 49
    • 0029794374 scopus 로고    scopus 로고
    • Evolution of a persistent aphthovirus in cytolytic infections: Partial reversion of phenotypic traits accompanied by genetic diversification
    • Sevilla, N., and E. Domingo. 1996. Evolution of a persistent aphthovirus in cytolytic infections: partial reversion of phenotypic traits accompanied by genetic diversification. J. Virol. 70:6617-6624.
    • (1996) J. Virol , vol.70 , pp. 6617-6624
    • Sevilla, N.1    Domingo, E.2
  • 50
    • 4644305750 scopus 로고    scopus 로고
    • Isolation and characterization of poliovirus mutants resistant to heating at 50°C for 30 min
    • Shiomi, H., T. Urasawa, S. Urasawa, N. Kobayashi, S. Abe, and K. Taniguchi. 2004. Isolation and characterization of poliovirus mutants resistant to heating at 50°C for 30 min. J. Med. Virol. 74:484-491.
    • (2004) J. Med. Virol , vol.74 , pp. 484-491
    • Shiomi, H.1    Urasawa, T.2    Urasawa, S.3    Kobayashi, N.4    Abe, S.5    Taniguchi, K.6
  • 51
    • 0020544508 scopus 로고
    • Multiple genetic variants arise in the course of replication of foot-and-mouth disease virus
    • Sobrino, F., M. Dávila, J. Ortín, and E. Domingo. 1983. Multiple genetic variants arise in the course of replication of foot-and-mouth disease virus. Virology 128:310-318.
    • (1983) Virology , vol.128 , pp. 310-318
    • Sobrino, F.1    Dávila, M.2    Ortín, J.3    Domingo, E.4
  • 52
    • 0034612275 scopus 로고    scopus 로고
    • Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase
    • Tachedjian, G., H. E. Aronson, and S. P. Goff. 2000. Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase. Proc. Natl. Acad. Sci. USA 97:6334-6339.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6334-6339
    • Tachedjian, G.1    Aronson, H.E.2    Goff, S.P.3
  • 53
    • 33746190694 scopus 로고    scopus 로고
    • Compensatory capsid protein mutations in cucumber mosaic virus confer systematic infectivity in squash (Cucurbita pepo)
    • Thompson, J. R., S. Doun, and K. L. Perry. 2006. Compensatory capsid protein mutations in cucumber mosaic virus confer systematic infectivity in squash (Cucurbita pepo). J. Virol. 80:7740-7743.
    • (2006) J. Virol , vol.80 , pp. 7740-7743
    • Thompson, J.R.1    Doun, S.2    Perry, K.L.3
  • 54
    • 0032842518 scopus 로고    scopus 로고
    • Genomic nucleotide sequence of a foot-and-mouth disease virus clone and its persistent derivatives. Implications for the evolution of viral quasispecies during a persistent infection
    • Toja, M., C. Escarmís, and E. Domingo. 1999. Genomic nucleotide sequence of a foot-and-mouth disease virus clone and its persistent derivatives. Implications for the evolution of viral quasispecies during a persistent infection. Virus Res. 64:161-171.
    • (1999) Virus Res , vol.64 , pp. 161-171
    • Toja, M.1    Escarmís, C.2    Domingo, E.3
  • 55
    • 0028870352 scopus 로고
    • Characterization of an acid-resistant mutant of foot-and-mouth disease virus
    • Twomey, T., L. L. France, S. Hassard, T. G. Burrage, J. F. E. Newman, and F. Brown. 1995. Characterization of an acid-resistant mutant of foot-and-mouth disease virus. Virology 206:69-75.
    • (1995) Virology , vol.206 , pp. 69-75
    • Twomey, T.1    France, L.L.2    Hassard, S.3    Burrage, T.G.4    Newman, J.F.E.5    Brown, F.6
  • 56
    • 0033536578 scopus 로고    scopus 로고
    • Structural analysis of a non-contiguous second-site revertant in T4 lysozyme show that increasing the rigidity of a protein can enhance its stability
    • Wray, J. W., W. A. Baase, J. D. Lindstrom, L. H. Weaver, A. R. Poteete, and B. W. Matthews. 1999. Structural analysis of a non-contiguous second-site revertant in T4 lysozyme show that increasing the rigidity of a protein can enhance its stability. J. Mol. Biol. 292:1111-1120.
    • (1999) J. Mol. Biol , vol.292 , pp. 1111-1120
    • Wray, J.W.1    Baase, W.A.2    Lindstrom, J.D.3    Weaver, L.H.4    Poteete, A.R.5    Matthews, B.W.6
  • 57
    • 20244387096 scopus 로고    scopus 로고
    • Mutation patterns and structural correlates in human immunodeficiency virus type 1 protease following different protease inhibitor treatments
    • Wu, T. D., C. A. Schiffer, M. J. Gonzales, J. Taylor, R. Kantor, S. Chou, D. Israelski, A. R. Zolopa, W. F. Fessel, and R. W. Shafer. 2003. Mutation patterns and structural correlates in human immunodeficiency virus type 1 protease following different protease inhibitor treatments. J. Virol. 77:4836-4847.
    • (2003) J. Virol , vol.77 , pp. 4836-4847
    • Wu, T.D.1    Schiffer, C.A.2    Gonzales, M.J.3    Taylor, J.4    Kantor, R.5    Chou, S.6    Israelski, D.7    Zolopa, A.R.8    Fessel, W.F.9    Shafer, R.W.10
  • 59
    • 0034000244 scopus 로고    scopus 로고
    • A frequent, naturally occurring mutation (P130T) of human hepatitis B virus core antigen is compensatory for immature secretion phenotype of another frequent variant (I97L)
    • Yuan, T. T., and C. Shih. 2000. A frequent, naturally occurring mutation (P130T) of human hepatitis B virus core antigen is compensatory for immature secretion phenotype of another frequent variant (I97L). J. Virol. 74:4929-4932.
    • (2000) J. Virol , vol.74 , pp. 4929-4932
    • Yuan, T.T.1    Shih, C.2
  • 60
    • 0025353397 scopus 로고
    • Infectious foot-and-mouth disease virus derived from a cloned full-length cDNA
    • Zibert, A., G. Maass, K. Strebel, M. M. Falk, and E. Beck. 1990. Infectious foot-and-mouth disease virus derived from a cloned full-length cDNA. J. Virol. 64:2467-2473.
    • (1990) J. Virol , vol.64 , pp. 2467-2473
    • Zibert, A.1    Maass, G.2    Strebel, K.3    Falk, M.M.4    Beck, E.5


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