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Volumn 396, Issue 6706, 1998, Pages 92-96

Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE; HEMAGGLUTININ;

EID: 0032487864     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/23974     Document Type: Article
Times cited : (194)

References (30)
  • 1
    • 0025984385 scopus 로고
    • Structure and function of the HEF glycoprotein of influenza C virus
    • Herrler, G. & Klenk, H.-D. Structure and function of the HEF glycoprotein of influenza C virus. Adv. Virus Res. 40, 213-234 (1991).
    • (1991) Adv. Virus Res. , vol.40 , pp. 213-234
    • Herrler, G.1    Klenk, H.-D.2
  • 2
    • 0028936579 scopus 로고
    • A novel variant of the catalytic triad in the Streptomyces scabies esterase
    • Wei, Y. et al. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nature Struct. Biol. 2, 218-223 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 218-223
    • Wei, Y.1
  • 3
    • 0031021088 scopus 로고    scopus 로고
    • Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer
    • Ho, Y. S. et al. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature 385, 89-93 (1997).
    • (1997) Nature , vol.385 , pp. 89-93
    • Ho, Y.S.1
  • 4
    • 0024094778 scopus 로고
    • Sequence of mouse hepatitis virus A59 mRNA 2: Indications for RNA recombination between coronaviruses and influenza C virus
    • Luytjes, W., Bredenbeek, P. J., Noten, A. F., Horzinek, M. C. & Spaan, W. J. Sequence of mouse hepatitis virus A59 mRNA 2: indications for RNA recombination between coronaviruses and influenza C virus. Virology 166, 415-422 (1988).
    • (1988) Virology , vol.166 , pp. 415-422
    • Luytjes, W.1    Bredenbeek, P.J.2    Noten, A.F.3    Horzinek, M.C.4    Spaan, W.J.5
  • 6
    • 0026708107 scopus 로고
    • A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme
    • Herrler, C. et al. A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J. Biol. Chem. 267, 12501-12505 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 12501-12505
    • Herrler, C.1
  • 7
    • 1042308180 scopus 로고    scopus 로고
    • Synthesis and inhibitory properties of a thiomethylmercuric sialic acid with application to the X-ray structure determination of 9-O-acetylsialic acid esterase from influenza C virus
    • Fitz, W., Rosenthal, P. B. & Wong, C.-H. Synthesis and inhibitory properties of a thiomethylmercuric sialic acid with application to the X-ray structure determination of 9-O-acetylsialic acid esterase from influenza C virus. Biorg. Med. Chem. 4, 1349-1353 (1996).
    • (1996) Biorg. Med. Chem. , vol.4 , pp. 1349-1353
    • Fitz, W.1    Rosenthal, P.B.2    Wong, C.-H.3
  • 8
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography
    • Eisen, M. B., Sabesan, S., Skehel, J. J. & Wiley, D. C. Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography. Virology 232, 19-31 (1997).
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 9
    • 0023915219 scopus 로고
    • Structure of the influenza haemagglutinin complexed with its receptor, sialic acid
    • Weis, W. et al. Structure of the influenza haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426-431 (1988).
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1
  • 10
    • 0020595851 scopus 로고
    • Single amino-acid substitutions in influenza haemagglutinin change receptor binding specificity
    • Rogers, G. N. et al. Single amino-acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature 304, 76-78 (1983).
    • (1983) Nature , vol.304 , pp. 76-78
    • Rogers, G.N.1
  • 11
    • 0023002952 scopus 로고
    • Influenza C virus uses 9-O-acetyl-N-acetylneuaminic acid as a high affinity receptor determinant for attachment to cells
    • Rogers, G. N., Herrler, G., Paulson, J. C. & Klenk, H.-D. Influenza C virus uses 9-O-acetyl-N-acetylneuaminic acid as a high affinity receptor determinant for attachment to cells. J. Biol. Chem, 261, 5947-5951 (1986).
    • (1986) J. Biol. Chem , vol.261 , pp. 5947-5951
    • Rogers, G.N.1    Herrler, G.2    Paulson, J.C.3    Klenk, H.-D.4
  • 12
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 13
    • 0028874050 scopus 로고
    • The crystal structure of bluetongue virus VP7
    • Grimes, J., Basak, A. K., Roy, P. & Stuart, D. The crystal structure of bluetongue virus VP7. Nature 373, 167-170 (1995).
    • (1995) Nature , vol.373 , pp. 167-170
    • Grimes, J.1    Basak, A.K.2    Roy, P.3    Stuart, D.4
  • 14
    • 0015990842 scopus 로고
    • Identification of biological activities of paramyxovirus giycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus
    • Scheid, A. & Choppin, P. Identification of biological activities of paramyxovirus giycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57, 475-490 (1974).
    • (1974) Virology , vol.57 , pp. 475-490
    • Scheid, A.1    Choppin, P.2
  • 15
    • 0026567492 scopus 로고
    • Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region
    • Pollard, S. R., Rosa, M. D., Rosa, J. J. & Wiley, D. C. Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region. EMBO J. 11, 585-591 (1992).
    • (1992) EMBO J. , vol.11 , pp. 585-591
    • Pollard, S.R.1    Rosa, M.D.2    Rosa, J.J.3    Wiley, D.C.4
  • 16
    • 0030730243 scopus 로고    scopus 로고
    • Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein
    • Wyatt, R. et al. Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J. Virol. 71, 9722-9731 (1997).
    • (1997) J. Virol. , vol.71 , pp. 9722-9731
    • Wyatt, R.1
  • 17
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth, E., Olshevsky, U., Furman, C. & Sodroski, J. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65, 2119-2123 (1991).
    • (1991) J. Virol. , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 18
    • 0020035202 scopus 로고
    • Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion
    • Skehel, J. J. et al. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl Acad. Sci. USA 79, 968-972 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 968-972
    • Skehel, J.J.1
  • 19
    • 0030500468 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoprotein
    • Rosenthal, P. B. et al. Crystallization and preliminary X-ray diffraction studies of the influenza C virus glycoprotein. Acta Crystallogr. D 52, 1041-1045 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 1041-1045
    • Rosenthal, P.B.1
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0028103275 scopus 로고
    • Collaborative Computational Project No. 4, the CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project No. 4, the CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 23
    • 0019860994 scopus 로고
    • Correlation of DNA exonic regions with protein structural units in haemoglobin
    • Go, M. Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature 291, 90-92 (1981).
    • (1981) Nature , vol.291 , pp. 90-92
    • Go, M.1
  • 24
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Hohn, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Hohn, L.1    Sander, C.2
  • 26
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. Ribbon models of macromolecules. J. Mol. Graph. Modelg 5, 103-106 (1987).
    • (1987) J. Mol. Graph. Modelg , vol.5 , pp. 103-106
    • Carson, M.1
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 28
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript which includes greatly enhanced coloring capabilities
    • Esnouf, R. M. An extensively modified version of Molscript which includes greatly enhanced coloring capabilities. J. Mol. Graph. Modelg 15, 132-134 (1997).
    • (1997) J. Mol. Graph. Modelg , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 29
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 276, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 30
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S. V. SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. Modelg 11, 134-138 (1993).
    • (1993) J. Mol. Graph. Modelg , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.