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Volumn 7, Issue , 2002, Pages 31-47

Influenza virus surface glycoproteins, haemagglutinin and neuraminidase: a personal account

(1)  Laver, Graeme a  

a NONE   (Australia)

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EID: 5644230147     PISSN: 01687069     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0168-7069(02)07003-9     Document Type: Article
Times cited : (4)

References (47)
  • 1
    • 0002171713 scopus 로고
    • The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus
    • G.K. Hirst The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus Science 94 1941 22 23
    • (1941) Science , vol.94 , pp. 22-23
    • Hirst, G.K.1
  • 2
    • 0011508818 scopus 로고
    • Studies on the neuraminidase of influenza virus. 1. Separation and some properties of the enzyme from Asian and PR8 strains
    • L.W. Mayron B. Robert R.J. Winzler M.E. Rafelson Studies on the neuraminidase of influenza virus. 1. Separation and some properties of the enzyme from Asian and PR8 strains Arch Biochem Biophys 92 1961 475 483
    • (1961) Arch Biochem Biophys , vol.92 , pp. 475-483
    • Mayron, L.W.1    Robert, B.2    Winzler, R.J.3    Rafelson, M.E.4
  • 3
    • 0011422769 scopus 로고
    • The structural relationship of sialidase to the influenza virus surface
    • H. Noll T. Aoyagi J. Orlando The structural relationship of sialidase to the influenza virus surface Virology 18 1962 154 157
    • (1962) Virology , vol.18 , pp. 154-157
    • Noll, H.1    Aoyagi, T.2    Orlando, J.3
  • 4
    • 7344233616 scopus 로고
    • The structure of influenza viruses. 2. Disruption of the virus particle and separation of neuraminidase activity
    • W.G. Laver The structure of influenza viruses. 2. Disruption of the virus particle and separation of neuraminidase activity Virology 20 1963 251 262
    • (1963) Virology , vol.20 , pp. 251-262
    • Laver, W.G.1
  • 5
    • 0013899915 scopus 로고
    • Influenza virus subunit vaccines: immunogenicity and lack of toxicity for rabbits of ether- and detergent-disrupted virus
    • R.G. Webster W.G. Laver Influenza virus subunit vaccines: immunogenicity and lack of toxicity for rabbits of ether- and detergent-disrupted virus J Immunol 96 1966 596
    • (1966) J Immunol , vol.96 , pp. 596
    • Webster, R.G.1    Laver, W.G.2
  • 6
    • 12244268998 scopus 로고
    • The structure and composition of the myxoviruses 1. Electron microscope studies of the structure of myxovirus particles by negative staining techniques
    • R.W. Horne A.P. Waterson P. Wildy A.E. Farnham The structure and composition of the myxoviruses 1. Electron microscope studies of the structure of myxovirus particles by negative staining techniques Virology 11 1960 79 98
    • (1960) Virology , vol.11 , pp. 79-98
    • Horne, R.W.1    Waterson, A.P.2    Wildy, P.3    Farnham, A.E.4
  • 7
    • 0001325936 scopus 로고
    • Structural studies on the protein subunits from three strains of influenza virus
    • W.G. Laver Structural studies on the protein subunits from three strains of influenza virus J Mol Biol 9 1964 109 124
    • (1964) J Mol Biol , vol.9 , pp. 109-124
    • Laver, W.G.1
  • 8
    • 0014515235 scopus 로고
    • Morphology of the isolated haemagglutinin and neuraminidase subunits of influenza virus
    • W.G. Laver R.C. Valentine Morphology of the isolated haemagglutinin and neuraminidase subunits of influenza virus Virology 38 1969 105 119
    • (1969) Virology , vol.38 , pp. 105-119
    • Laver, W.G.1    Valentine, R.C.2
  • 10
    • 0015062851 scopus 로고
    • The polypeptide composition of influenza A viruses
    • J.J. Skehel G.C. Schild The polypeptide composition of influenza A viruses Virology 44 1971 396 408
    • (1971) Virology , vol.44 , pp. 396-408
    • Skehel, J.J.1    Schild, G.C.2
  • 11
    • 0015099556 scopus 로고
    • Separation of two polypeptide chains from the haemagglutinin subunit of influenza virus
    • W.G. Laver Separation of two polypeptide chains from the haemagglutinin subunit of influenza virus Virology 45 1971 275 288
    • (1971) Virology , vol.45 , pp. 275-288
    • Laver, W.G.1
  • 12
    • 0013965776 scopus 로고
    • Identification in a recombinant influenza virus of structural proteins derived from both parents
    • W.G. Laver E.D. Kilbourne Identification in a recombinant influenza virus of structural proteins derived from both parents Virology 30 1966 493 501
    • (1966) Virology , vol.30 , pp. 493-501
    • Laver, W.G.1    Kilbourne, E.D.2
  • 13
    • 0014872140 scopus 로고
    • Antigenic hybrids of influenza A viruses with surface antigens to order
    • R.G. Webster Antigenic hybrids of influenza A viruses with surface antigens to order Virology 42 1970 633 642
    • (1970) Virology , vol.42 , pp. 633-642
    • Webster, R.G.1
  • 14
    • 0013979301 scopus 로고
    • Functional significance of sialidase during influenza virus multiplication
    • J.T. Seto R. Rott Functional significance of sialidase during influenza virus multiplication Virology 30 1966 731 737
    • (1966) Virology , vol.30 , pp. 731-737
    • Seto, J.T.1    Rott, R.2
  • 15
    • 0014103687 scopus 로고
    • Preparation and properties of antibody directed specifically against the neuraminidase of influenza virus
    • R.G. Webster W.G. Laver Preparation and properties of antibody directed specifically against the neuraminidase of influenza virus J Immunology 99 1967 49 55
    • (1967) J Immunology , vol.99 , pp. 49-55
    • Webster, R.G.1    Laver, W.G.2
  • 16
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • P. Palese M. Ueda K. Tobita R.W. Compans Characterization of temperature sensitive influenza virus mutants defective in neuraminidase Virology 61 1974 397 410
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Ueda, M.2    Tobita, K.3    Compans, R.W.4
  • 17
    • 0014014226 scopus 로고
    • Isolation of a low molecular weight sialidase (neuraminidase) from influenza virus
    • J.T. Seto R. Drzeniek R. Rott Isolation of a low molecular weight sialidase (neuraminidase) from influenza virus Biochim Biophys Acta 113 1966 402 404
    • (1966) Biochim Biophys Acta , vol.113 , pp. 402-404
    • Seto, J.T.1    Drzeniek, R.2    Rott, R.3
  • 18
    • 0018092715 scopus 로고
    • Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N2 influenza virus strains
    • W.G. Laver Crystallization and peptide maps of neuraminidase “heads” from H2N2 and H3N2 influenza virus strains Virology 86 1978 78 87
    • (1978) Virology , vol.86 , pp. 78-87
    • Laver, W.G.1
  • 19
    • 0017880301 scopus 로고
    • Preliminary crystallographic data for influenza virus neuraminidase “heads”
    • C.E. Wright W.G. Laver Preliminary crystallographic data for influenza virus neuraminidase “heads” J Mol Biol 120 1978 133 136
    • (1978) J Mol Biol , vol.120 , pp. 133-136
    • Wright, C.E.1    Laver, W.G.2
  • 20
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • J.N. Varghese W.G. Laver P.M. Colman Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution Nature 303 1983 35 40
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 22
    • 0016244226 scopus 로고
    • Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetyl neuraminic acid (FANA)
    • P. Palese J.L. Schulman G. Bodo P. Meindl Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetyl neuraminic acid (FANA) Virology 59 1974 490 498
    • (1974) Virology , vol.59 , pp. 490-498
    • Palese, P.1    Schulman, J.L.2    Bodo, G.3    Meindl, P.4
  • 23
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • M. Von Itzstein Rational design of potent sialidase-based inhibitors of influenza virus replication Nature 363 1993 418 423
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, M.1
  • 24
    • 0014723402 scopus 로고
    • Antibodies to influenza viruses (including the human A2/Asian/57 strain) in sera from Australian Shearwaters (Puffinus pacificus)
    • C.A. Dasen W.G. Laver Antibodies to influenza viruses (including the human A2/Asian/57 strain) in sera from Australian Shearwaters ( Puffinus pacificus ) Bull WHO 42 1970 885 889
    • (1970) Bull WHO , vol.42 , pp. 885-889
    • Dasen, C.A.1    Laver, W.G.2
  • 25
    • 0015581509 scopus 로고
    • Isolation of a type A influenza virus from an Australian pelagic bird
    • J.C. Downie W.G. Laver Isolation of a type A influenza virus from an Australian pelagic bird Virology 51 1973 259 269
    • (1973) Virology , vol.51 , pp. 259-269
    • Downie, J.C.1    Laver, W.G.2
  • 27
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • C.U. Kim W. Lew M.A. Williams H. Lui L. Zhang S. Swaminathan N. Bischofberger M.S. Chen D.B. Mendel C.Y. Tai W.G. Laver R.C. Stevens Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity J Am Chem Soc 119 1997 681 690
    • (1997) J Am Chem Soc , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Lui, H.4    Zhang, L.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10    Laver, W.G.11    Stevens, R.C.12
  • 30
    • 0027292125 scopus 로고
    • Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3 dehydro-N-acetyl neuraminic acid
    • P.J. Bossart-Whittaker M. Carson Y.S. Babu C.D. Smith W.G. Laver G.M. Air Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3 dehydro-N-acetyl neuraminic acid J Mol Biol 232 1993 1069 1083
    • (1993) J Mol Biol , vol.232 , pp. 1069-1083
    • Bossart-Whittaker, P.J.1    Carson, M.2    Babu, Y.S.3    Smith, C.D.4    Laver, W.G.5    Air, G.M.6
  • 31
    • 0033603627 scopus 로고    scopus 로고
    • Drug development in space?
    • W.G. Laver Drug development in space? Science 284 1999 2089
    • (1999) Science , vol.284 , pp. 2089
    • Laver, W.G.1
  • 32
    • 50549185249 scopus 로고
    • The structure of influenza viruses. I. N-Terminal amino acid analyses
    • W.G. Laver The structure of influenza viruses. I. N-Terminal amino acid analyses Virology 19 1962 18 32
    • (1962) Virology , vol.19 , pp. 18-32
    • Laver, W.G.1
  • 34
    • 0014251161 scopus 로고
    • Selection of antigenic mutants of influenza viruses. Isolation and peptide mapping of their haemagglutinating proteins
    • W.G. Laver R.G. Webster Selection of antigenic mutants of influenza viruses. Isolation and peptide mapping of their haemagglutinating proteins Virology 34 1968 193 202
    • (1968) Virology , vol.34 , pp. 193-202
    • Laver, W.G.1    Webster, R.G.2
  • 35
    • 0017345454 scopus 로고
    • Electron microscopy of antibodies bound to isolated influenza haemagglutinin
    • N.G. Wrigley W.G. Laver J.C. Downie Electron microscopy of antibodies bound to isolated influenza haemagglutinin J Mol Biol 109 1977 405 421
    • (1977) J Mol Biol , vol.109 , pp. 405-421
    • Wrigley, N.G.1    Laver, W.G.2    Downie, J.C.3
  • 36
    • 84909648524 scopus 로고
    • The delineation of antigenic determinants of the haemagglutinin of influenza A viruses by means of monoclonal antibodies
    • W. Gerhard The delineation of antigenic determinants of the haemagglutinin of influenza A viruses by means of monoclonal antibodies Fourth ed. W.G. Laver H. Bachmeyer R. Weil Topics in Infectious Diseases 3 1977 Springer-Verlag 15 24
    • (1977) , pp. 15-24
    • Gerhard, W.1
  • 37
    • 0018451569 scopus 로고
    • Antigenic drift in Type A influenza virus: peptide mapping and antigenic analysis of A/PR/8/34 (H0N1) variants selected with monoclonal antibodies
    • W.G. Laver W. Gerhard R.G. Webster M.E. Frankel G.M. Air Antigenic drift in Type A influenza virus: peptide mapping and antigenic analysis of A/PR/8/34 (H0N1) variants selected with monoclonal antibodies Fourth ed. Proc Natl Acad Sci USA 76 1979 1425 1429
    • (1979) , pp. 1425-1429
    • Laver, W.G.1    Gerhard, W.2    Webster, R.G.3    Frankel, M.E.4    Air, G.M.5
  • 38
    • 0018668683 scopus 로고
    • Antigenic drift in Type A influenza virus. Sequence differences in the haemagglutinin of Hong Kong (H3N2) variants selected with monoclonal hybridoma antibodies
    • W.G. Laver G.M. Air R.G. Webster W. Gerhard C.W. Ward T.A.A. Dopheide Antigenic drift in Type A influenza virus. Sequence differences in the haemagglutinin of Hong Kong (H3N2) variants selected with monoclonal hybridoma antibodies Virology 98 1979 226 237
    • (1979) Virology , vol.98 , pp. 226-237
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Gerhard, W.4    Ward, C.W.5    Dopheide, T.A.A.6
  • 39
    • 0019512990 scopus 로고
    • The mechanism of antigenic drift in influenza virus. Amino acid sequence changes in an antigenically active region of Hong Kong (H3N2) influenza virus haemagglutinin
    • W.G. Laver G.M. Air R.G. Webster The mechanism of antigenic drift in influenza virus. Amino acid sequence changes in an antigenically active region of Hong Kong (H3N2) influenza virus haemagglutinin J Mol Biol 145 1981 339 361
    • (1981) J Mol Biol , vol.145 , pp. 339-361
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3
  • 40
    • 85112943142 scopus 로고
    • G. Laver G. Air Structure and Variation in Influenza Virus Fourth ed. Developments in Cell Biology Volume 5 1980 Elsevier/North-Holland Amsterdam
    • (1980)
  • 41
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • I.A. Wilson J.J. Skehel D.C. Wiley Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution Nature 289 1981 366 373
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 42
    • 0020050946 scopus 로고
    • Molecular mechanisms of variation in influenza virus
    • R.G. Webster W.G. Laver G.M. Air G.C. Schild Molecular mechanisms of variation in influenza virus Nature 296 1982 115 121
    • (1982) Nature , vol.296 , pp. 115-121
    • Webster, R.G.1    Laver, W.G.2    Air, G.M.3    Schild, G.C.4
  • 43
    • 85027792330 scopus 로고    scopus 로고
    • In Memoriam Chu Chi Ming
    • W.G. Laver R.G. Webster In Memoriam Chu Chi Ming Virology 255 1999 1
    • (1999) Virology , vol.255 , pp. 1
    • Laver, W.G.1    Webster, R.G.2
  • 44
    • 0014658728 scopus 로고
    • New criteria for the selection of influenza vaccine strains
    • S. Fazekas de St Groth New criteria for the selection of influenza vaccine strains Bull WHO 41 1969 651 657
    • (1969) Bull WHO , vol.41 , pp. 651-657
    • Fazekas de St Groth, S.1
  • 45
    • 0015338301 scopus 로고
    • Studies on the origin of pandemic influenza. 1. Antigenic analysis of A2 influenza viruses isolated before and after the appearance of Hong Kong influenza using antisera to the isolated haemagglutinin subunits
    • R.G. Webster W.G. Laver Studies on the origin of pandemic influenza. 1. Antigenic analysis of A2 influenza viruses isolated before and after the appearance of Hong Kong influenza using antisera to the isolated haemagglutinin subunits Virology 48 1972 433 444
    • (1972) Virology , vol.48 , pp. 433-444
    • Webster, R.G.1    Laver, W.G.2
  • 46
    • 0015336070 scopus 로고
    • Studies on the origin of pandemic influenza. 2. Peptide maps of the light and heavy polypeptide chains from the haemagglutinin subunits of A2 influenza viruses isolated before and after the appearance of Hong Kong influenza
    • W.G. Laver R.G. Webster Studies on the origin of pandemic influenza. 2. Peptide maps of the light and heavy polypeptide chains from the haemagglutinin subunits of A2 influenza viruses isolated before and after the appearance of Hong Kong influenza Virology 48 1972 445 455
    • (1972) Virology , vol.48 , pp. 445-455
    • Laver, W.G.1    Webster, R.G.2
  • 47
    • 0015578869 scopus 로고
    • Studies on the origin of pandemic influenza. 3. Evidence implicating duck and equine influenza viruses as possible progenitors of the Hong Kong strain of human influenza
    • W.G. Laver R.G. Webster Studies on the origin of pandemic influenza. 3. Evidence implicating duck and equine influenza viruses as possible progenitors of the Hong Kong strain of human influenza Virology 51 1973 383 391
    • (1973) Virology , vol.51 , pp. 383-391
    • Laver, W.G.1    Webster, R.G.2


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