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Volumn 83, Issue 17, 2009, Pages 8482-8491

Impact of quaternary organization on the antigenic structure of the tick-borne encephalitis virus envelope glycoprotein E

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; EPITOPE; GLYCOPROTEIN E; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; GLYCOPROTEIN E, FLAVIVIRUS; VIRUS ANTIBODY; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 69249221492     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00660-09     Document Type: Article
Times cited : (40)

References (55)
  • 1
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • DOI 10.1038/337709a0
    • 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. (Pubitemid 19064726)
    • (1989) Nature , vol.337 , Issue.6209 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 2
    • 0028024309 scopus 로고
    • Expression of cloned envelope protein genes from the flavivirus tick-borne encephalitis virus in mammalian cells and random mutagenesis by PCR
    • Allison, S. L., C. W. Mandl, C. Kunz, and F. X. Heinz. 1994. Expression of cloned envelope protein genes from the flavivirus tick-borne encephalitis virus in mammalian cells and random mutagenesis by PCR. Virus Genes 8:187-198.
    • (1994) Virus Genes , vol.8 , pp. 187-198
    • Allison, S.L.1    Mandl, C.W.2    Kunz, C.3    Heinz, F.X.4
  • 3
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein e
    • Allison, S. L., J. Schalich, K. Stiasny, C. W. Mandl, and F. X. Heinz. 2001. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 75:4268-4275.
    • (2001) J. Virol. , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 4
    • 0142060900 scopus 로고    scopus 로고
    • Two distinct size classes of immature and mature subviral particles from tick-borne encephalitis virus
    • Allison, S. L., Y. J. Tao, G. O'Riordain, C. W. Mandl, S. C. Harrison, and F. X. Heinz. 2003. Two distinct size classes of immature and mature subviral particles from tick-borne encephalitis virus. J. Virol. 77:11357-11366.
    • (2003) J. Virol. , vol.77 , pp. 11357-11366
    • Allison, S.L.1    Tao, Y.J.2    O'Riordain, G.3    Mandl, C.W.4    Harrison, S.C.5    Heinz, F.X.6
  • 6
    • 0028877602 scopus 로고
    • Structural features of the reactions between antibodies and protein antigens
    • Braden, B. C., and R. J. Poljak. 1995. Structural features of the reactions between antibodies and protein antigens. FASEB J. 9:9-16.
    • (1995) FASEB J. , vol.9 , pp. 9-16
    • Braden, B.C.1    Poljak, R.J.2
  • 7
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • DOI 10.1038/sj.emboj.7600064
    • Bressanelli, S., K. Stiasny, S. L. Allison, E. A. Stura, S. Duquerroy, J. Lescar, F. X. Heinz, and F. A. Rey. 2004. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23:728-738. (Pubitemid 38425440)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6    Heinz, F.X.7    Rey, F.A.8
  • 8
    • 0025064577 scopus 로고
    • An analysis of the properties of monoclonal antibodies directed to epitopes on influenza virus hemagglutinin
    • Brown, L. E., J. M. Murray, D. O. White, and D. C. Jackson. 1990. An analysis of the properties of monoclonal antibodies directed to epitopes on influenza virus hemagglutinin. Arch. Virol. 114:1-26.
    • (1990) Arch. Virol. , vol.114 , pp. 1-26
    • Brown, L.E.1    Murray, J.M.2    White, D.O.3    Jackson, D.C.4
  • 9
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • DOI 10.1006/viro.1999.0172
    • Corver, J., A. Ortiz, S. L. Allison, J. Schalich, F. X. Heinz, and J. Wilschut. 2000. Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology 269:37-46. (Pubitemid 30183167)
    • (2000) Virology , vol.269 , Issue.1 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 10
    • 34047178962 scopus 로고    scopus 로고
    • A detailed mutagenesis study of flavivirus cross-reactive epitopes using West Nile virus-like particles
    • Crill, W. D., N. B. Trainor, and G. J. Chang. 2007. A detailed mutagenesis study of flavivirus cross-reactive epitopes using West Nile virus-like particles. J. Gen. Virol. 88:1169-1174.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1169-1174
    • Crill, W.D.1    Trainor, N.B.2    Chang, G.J.3
  • 11
    • 52049125010 scopus 로고    scopus 로고
    • The structural immunology of antibody protection against West Nile virus
    • Diamond, M. S., T. C. Pierson, and D. H. Fremont. 2008. The structural immunology of antibody protection against West Nile virus. Immunol. Rev. 225:212-225.
    • (2008) Immunol. Rev. , vol.225 , pp. 212-225
    • Diamond, M.S.1    Pierson, T.C.2    Fremont, D.H.3
  • 13
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • DOI 10.1016/0022-1759(85)90044-4
    • Friguet, B., A. F. Chaffotte, L. Djavadi-Ohaniance, and M. E. Goldberg. 1985. Measurements of the true affinity constant in solution of antigenantibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77:305-319. (Pubitemid 15103678)
    • (1985) Journal of Immunological Methods , vol.77 , Issue.2 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Ohaniance, L.D.3    Goldberg, M.E.4
  • 14
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz, R., K. Stiasny, and F. X. Heinz. 2008. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J. Cell Biol. 183:353-361.
    • (2008) J. Cell Biol. , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 15
    • 8644255116 scopus 로고    scopus 로고
    • Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein
    • Goncalvez, A. P., R. H. Purcell, and C. J. Lai. 2004. Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein. J. Virol. 78:12919-12928.
    • (2004) J. Virol. , vol.78 , pp. 12919-12928
    • Goncalvez, A.P.1    Purcell, R.H.2    Lai, C.J.3
  • 16
    • 34548627957 scopus 로고    scopus 로고
    • Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus
    • Gromowski, G. D., and A. D. Barrett. 2007. Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus. Virology 366:349-360.
    • (2007) Virology , vol.366 , pp. 349-360
    • Gromowski, G.D.1    Barrett, A.D.2
  • 17
    • 0024593180 scopus 로고
    • Epitope model of tick-borne encephalitis virus envelope glycoprotein E: Analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH
    • DOI 10.1016/0042-6822(89)90044-5
    • Guirakhoo, F., F. X. Heinz, and C. Kunz. 1989. Epitope model of tick-borne encephalitis virus envelope glycoprotein E: analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH. Virology 169:90-99. (Pubitemid 19080151)
    • (1989) Virology , vol.169 , Issue.1 , pp. 90-99
    • Guirakhoo, F.1    Heinz, F.X.2    Kunz, C.3
  • 18
    • 0019997281 scopus 로고
    • Monoclonal antibodies to the structural glycoprotein of tick-borne encephalitis virus
    • Heinz, F. X., R. Berger, O. Majdic, W. Knapp, and C. Kunz. 1982. Monoclonal antibodies to the structural glycoprotein of tick-borne encephalitis virus. Infect. Immun. 37:869-874.
    • (1982) Infect. Immun. , vol.37 , pp. 869-874
    • Heinz, F.X.1    Berger, R.2    Majdic, O.3    Knapp, W.4    Kunz, C.5
  • 19
    • 0019835410 scopus 로고
    • Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: Comparison with other flaviviruses
    • Heinz, F. X., and C. Kunz. 1981. Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: comparison with other flaviviruses. J. Gen. Virol. 57:263-274.
    • (1981) J. Gen. Virol. , vol.57 , pp. 263-274
    • Heinz, F.X.1    Kunz, C.2
  • 20
    • 0021345838 scopus 로고
    • Antibodyinduced conformational changes result in enhanced avidity of antibodies to different antigenic sites on the tick-borne encephalitis virus glycoprotein
    • Heinz, F. X., C. Mandl, R. Berger, W. Tuma, and C. Kunz. 1984. Antibodyinduced conformational changes result in enhanced avidity of antibodies to different antigenic sites on the tick-borne encephalitis virus glycoprotein. Virology 133:25-34.
    • (1984) Virology , vol.133 , pp. 25-34
    • Heinz, F.X.1    Mandl, C.2    Berger, R.3    Tuma, W.4    Kunz, C.5
  • 21
    • 0026094713 scopus 로고
    • The flavivirus envelope protein E: Isolation of a soluble form from tick-borne encephalitis virus and its crystallization
    • Heinz, F. X., C. W. Mandl, H. Holzmann, C. Kunz, B. A. Harris, F. Rey, and S. C. Harrison. 1991. The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization. J. Virol. 65:5579-5583.
    • (1991) J. Virol. , vol.65 , pp. 5579-5583
    • Heinz, F.X.1    Mandl, C.W.2    Holzmann, H.3    Kunz, C.4    Harris, B.A.5    Rey, F.6    Harrison, S.C.7
  • 22
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein e by the heterodimeric association with protein prM
    • DOI 10.1006/viro.1994.1013
    • Heinz, F. X., K. Stiasny, G. Puschner-Auer, H. Holzmann, S. L. Allison, C. W. Mandl, and C. Kunz. 1994. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198:109-117. (Pubitemid 124018767)
    • (1994) Virology , vol.198 , Issue.1 , pp. 109-117
    • Heinz, F.X.1    Stiasny, K.2    Puschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6    Kunz, C.7
  • 23
    • 0031014304 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice
    • Holzmann, H., K. Stiasny, M. Ecker, C. Kunz, and F. X. Heinz. 1997. Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J. Gen. Virol. 78:31-37.
    • (1997) J. Gen. Virol. , vol.78 , pp. 31-37
    • Holzmann, H.1    Stiasny, K.2    Ecker, M.3    Kunz, C.4    Heinz, F.X.5
  • 24
    • 0029140422 scopus 로고
    • Tick-borne encephalitis virus envelope protein E-specific monoclonal antibodies for the study of low pH-induced conformational changes and immature virions
    • Holzmann, H., K. Stiasny, H. York, F. Dorner, C. Kunz, and F. X. Heinz. 1995. Tick-borne encephalitis virus envelope protein E-specific monoclonal antibodies for the study of low pH-induced conformational changes and immature virions. Arch. Virol. 140:213-221.
    • (1995) Arch. Virol. , vol.140 , pp. 213-221
    • Holzmann, H.1    Stiasny, K.2    York, H.3    Dorner, F.4    Kunz, C.5    Heinz, F.X.6
  • 28
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • Laemmli, U. K., and M. Favre. 1973. Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80:575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 29
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Li, Y., H. Li, F. Yang, S. J. Smith-Gill, and R. A. Mariuzza. 2003. X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol. 10:482-488.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 30
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Lindenbach, B. D., H. J. Thiel, and C. M. Rice. 2006. Flaviviridae: the viruses and their replication, p. 1101-1152. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2006) Fields Virology, 5th Ed. , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 32
    • 0024548815 scopus 로고
    • Antigenic structure of the flavivirus envelope protein e at the molecular level, using tick-borne encephalitis virus as a model
    • Mandl, C. W., F. Guirakhoo, H. Holzmann, F. X. Heinz, and C. Kunz. 1989. Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J. Virol. 63:564-571.
    • (1989) J. Virol. , vol.63 , pp. 564-571
    • Mandl, C.W.1    Guirakhoo, F.2    Holzmann, H.3    Heinz, F.X.4    Kunz, C.5
  • 33
    • 0023811062 scopus 로고
    • Sequence of the structural proteins of tick-borne encephalitis virus (western subtype) and comparative analysis with other flaviviruses
    • Mandl, C. W., F. X. Heinz, and C. Kunz. 1988. Sequence of the structural proteins of tick-borne encephalitis virus (western subtype) and comparative analysis with other flaviviruses. Virology 166:197-205.
    • (1988) Virology , vol.166 , pp. 197-205
    • Mandl, C.W.1    Heinz, F.X.2    Kunz, C.3
  • 34
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2003. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA 100:6986-6991.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 35
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • DOI 10.1038/nature02165
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2004. Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319. (Pubitemid 38133652)
    • (2004) Nature , vol.427 , Issue.6972 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 36
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • DOI 10.1128/JVI.79.2.1223-1231.2005
    • Modis, Y., S. Ogata, D. Clements, and S. C. Harrison. 2005. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79:1223-1231. (Pubitemid 40053904)
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 38
    • 33751223215 scopus 로고    scopus 로고
    • Crystal structure of the West Nile virus envelope glycoprotein
    • DOI 10.1128/JVI.01125-06
    • Nybakken, G. E., C. A. Nelson, B. R. Chen, M. S. Diamond, and D. H. Fremont. 2006. Crystal structure of the West Nile virus envelope glycoprotein. J. Virol. 80:11467-11474. (Pubitemid 44788862)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11467-11474
    • Nybakken, G.E.1    Nelson, C.A.2    Chen, B.R.3    Diamond, M.S.4    Fremont, D.H.5
  • 41
    • 0023906499 scopus 로고
    • Three-dimensional structure of poliovirus serotype 1 neutralizing determinants
    • Page, G. S., A. G. Mosser, J. M. Hogle, D. J. Filman, R. R. Rueckert, and M. Chow. 1988. Three-dimensional structure of poliovirus serotype 1 neutralizing determinants. J. Virol. 62:1781-1794.
    • (1988) J. Virol. , vol.62 , pp. 1781-1794
    • Page, G.S.1    Mosser, A.G.2    Hogle, J.M.3    Filman, D.J.4    Rueckert, R.R.5    Chow, M.6
  • 42
    • 56549118853 scopus 로고    scopus 로고
    • Molecular mechanisms of antibody- Mediated neutralisation of flavivirus infection
    • Pierson, T. C., and M. S. Diamond. 2008. Molecular mechanisms of antibody- mediated neutralisation of flavivirus infection. Expert Rev. Mol. Med. 10:e12.
    • (2008) Expert Rev. Mol. Med. , vol.10
    • Pierson, T.C.1    Diamond, M.S.2
  • 43
    • 50849120046 scopus 로고    scopus 로고
    • Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: Implications for vaccine development
    • Pierson, T. C., D. H. Fremont, R. J. Kuhn, and M. S. Diamond. 2008. Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: implications for vaccine development. Cell Host Microbe 4:229-238.
    • (2008) Cell Host Microbe , vol.4 , pp. 229-238
    • Pierson, T.C.1    Fremont, D.H.2    Kuhn, R.J.3    Diamond, M.S.4
  • 44
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 a resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 45
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • Roehrig, J. T. 2003. Antigenic structure of flavivirus proteins. Adv. Virus Res. 59:141-175.
    • (2003) Adv. Virus Res. , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 46
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica
    • DOI 10.1006/viro.1998.9200
    • Roehrig, J. T., R. A. Bolin, and R. G. Kelly. 1998. Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology 246:317-328. (Pubitemid 28384045)
    • (1998) Virology , vol.246 , Issue.2 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 47
    • 0028012338 scopus 로고
    • Antigenicity of the N8 influenza a virus neuraminidase: Existence of an epitope at the subunit interface of the neuraminidase
    • Saito, T., G. Taylor, W. G. Laver, Y. Kawaoka, and R. G. Webster. 1994. Antigenicity of the N8 influenza A virus neuraminidase: existence of an epitope at the subunit interface of the neuraminidase. J. Virol. 68:1790-1796. (Pubitemid 24065748)
    • (1994) Journal of Virology , vol.68 , Issue.3 , pp. 1790-1796
    • Saito, T.1    Taylor, G.2    Laver, W.G.3    Kawaoka, Y.4    Webster, R.G.5
  • 48
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, G. and C. Weissmann. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, G.1    Weissmann, C.2
  • 49
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich, J., S. L. Allison, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1996. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol. 70:4549-4557. (Pubitemid 26187453)
    • (1996) Journal of Virology , vol.70 , Issue.7 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 50
    • 0023250991 scopus 로고
    • Modification of an ELISA-based procedure for affinity determination: Correction necessary for use with bivalent antibody
    • Stevens, F. J. 1987. Modification of an ELISA-based procedure for affinity determination: correction necessary for use with bivalent antibody. Mol. Immunol. 24:1055-1060.
    • (1987) Mol. Immunol. , vol.24 , pp. 1055-1060
    • Stevens, F.J.1
  • 51
    • 33748948792 scopus 로고    scopus 로고
    • Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites
    • DOI 10.1128/JVI.00080-06
    • Stiasny, K., S. Kiermayr, H. Holzmann, and F. X. Heinz. 2006. Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J. Virol. 80:9557-9568. (Pubitemid 44435631)
    • (2006) Journal of Virology , vol.80 , Issue.19 , pp. 9557-9568
    • Stiasny, K.1    Kiermayr, S.2    Holzmann, H.3    Heinz, F.X.4


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