메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12146-12159

Fixation of oligosaccharides to a surface may increase the susceptibility to human parainfluenza virus 1, 2, or 3 hemagglutinin-neuraminidase

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; GLYCOPROTEIN; HN PROTEIN; N ACETYLNEURAMINIC ACID; OLIGOSACCHARIDE;

EID: 81255123479     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05537-11     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 0032732835 scopus 로고    scopus 로고
    • Virus-receptor interactions of human parainfluenza viruses types 1, 2 and 3
    • Ah-Tye, C., S. Schwartz, K. Huberman, E. Carlin, and A. Moscona. 1999. Virus-receptor interactions of human parainfluenza viruses types 1, 2 and 3. Microb. Pathog. 27:329-336.
    • (1999) Microb. Pathog. , vol.27 , pp. 329-336
    • Ah-Tye, C.1    Schwartz, S.2    Huberman, K.3    Carlin, E.4    Moscona, A.5
  • 2
    • 33750970829 scopus 로고    scopus 로고
    • Identification of ligand specificities for glycan-binding proteins using glycan arrays
    • Alvarez, R. A., and O. Blixt. 2006. Identification of ligand specificities for glycan-binding proteins using glycan arrays. Methods Enzymol. 415:292-310.
    • (2006) Methods Enzymol , vol.415 , pp. 292-310
    • Alvarez, R.A.1    Blixt, O.2
  • 3
    • 81255214348 scopus 로고    scopus 로고
    • Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein
    • 16 August, doi:10.1093/glycob/cwr112
    • Alymova, I. V., et al. 16 August 2011. Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein. Glycobiology. doi:10.1093/glycob/cwr112.
    • (2011) Glycobiology
    • Alymova, I.V.1
  • 4
    • 34547114495 scopus 로고    scopus 로고
    • Human parainfluenza viruses hPIV1 and hPIV3 bind oligosaccharides with α2-3-linked sialic acids that are distinct from those bound by H5 avian influenza virus hemagglutinin
    • Amonsen, M., D. F. Smith, R. D. Cummings, and G. M. Air. 2007. Human parainfluenza viruses hPIV1 and hPIV3 bind oligosaccharides with α2-3-linked sialic acids that are distinct from those bound by H5 avian influenza virus hemagglutinin. J. Virol. 81:8341-8345.
    • (2007) J. Virol. , vol.81 , pp. 8341-8345
    • Amonsen, M.1    Smith, D.F.2    Cummings, R.D.3    Air, G.M.4
  • 5
    • 33748513031 scopus 로고    scopus 로고
    • Mutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutinin-neuraminidase protein
    • Bousse, T., and T. Takimoto. 2006. Mutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutinin-neuraminidase protein. J. Virol. 80:9009-9016.
    • (2006) J. Virol. , vol.80 , pp. 9009-9016
    • Bousse, T.1    Takimoto, T.2
  • 6
    • 23744432758 scopus 로고    scopus 로고
    • Terminal sialic acid residues on human glycophorin A are recognized by porcine kupffer cells
    • Burlak, C., L. M. Twining, and M. A. Rees. 2005. Terminal sialic acid residues on human glycophorin A are recognized by porcine kupffer cells. Transplantation 80:344-352.
    • (2005) Transplantation , vol.80 , pp. 344-352
    • Burlak, C.1    Twining, L.M.2    Rees, M.A.3
  • 7
    • 0028037160 scopus 로고
    • Analysis of the primary T-cell response to Sendai virus infection in C57BL/6 mice: CD4+ T-cell recognition is directed predominantly to the hemagglutinin-neuraminidase glycoprotein
    • Cole, G. A., et al. 1994. Analysis of the primary T-cell response to Sendai virus infection in C57BL/6 mice: CD4+ T-cell recognition is directed predominantly to the hemagglutinin-neuraminidase glycoprotein. J. Virol. 68: 6863-6870.
    • (1994) J. Virol. , vol.68 , pp. 6863-6870
    • Cole, G.A.1
  • 8
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 9
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell, S., T. Takimoto, A. Portner, and G. Taylor. 2000. Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 7:1068-1074.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 10
    • 4143064852 scopus 로고    scopus 로고
    • Gangliosides and N-glycoproteins function as Newcastle disease virus receptors
    • Ferreira, L., E. Villar, and I. Munoz-Barroso. 2004. Gangliosides and N-glycoproteins function as Newcastle disease virus receptors. Int. J. Biochem. Cell Biol. 36:2344-2356.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2344-2356
    • Ferreira, L.1    Villar, E.2    Munoz-Barroso, I.3
  • 11
    • 0024260839 scopus 로고
    • The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500-megahertz 1H NMR spectroscopy
    • Green, E. D., G. Adelt, J. U. Baenziger, S. Wilson, and H. Van Halbeek. 1988. The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500-megahertz 1H NMR spectroscopy. J. Biol. Chem. 263:18253-18268.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18253-18268
    • Green, E.D.1    Adelt, G.2    Baenziger, J.U.3    Wilson, S.4    Van Halbeek, H.5
  • 12
    • 0034469926 scopus 로고    scopus 로고
    • The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA
    • Greengard, O., N. Poltoratskaia, E. Leikina, J. Zimmerberg, and A. Moscona. 2000. The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA. J. Virol. 74:11108-11114.
    • (2000) J. Virol. , vol.74 , pp. 11108-11114
    • Greengard, O.1    Poltoratskaia, N.2    Leikina, E.3    Zimmerberg, J.4    Moscona, A.5
  • 13
    • 0030863626 scopus 로고    scopus 로고
    • Antigenic structure, function, and evolution of the hemagglutinin-neuraminidase protein of human parainfluenza virus type 1
    • Henrickson, K. J., and L. L. Savatski. 1997. Antigenic structure, function, and evolution of the hemagglutinin-neuraminidase protein of human parainfluenza virus type 1. J. Infect. Dis. 176:867-875.
    • (1997) J. Infect. Dis. , vol.176 , pp. 867-875
    • Henrickson, K.J.1    Savatski, L.L.2
  • 14
    • 0026738671 scopus 로고
    • Genetic variation and evolution of human parainfluenza virus type 1 hemagglutinin neuraminidase: analysis of 12 clinical isolates
    • Henrickson, K. J., and L. L. Savatski. 1992. Genetic variation and evolution of human parainfluenza virus type 1 hemagglutinin neuraminidase: analysis of 12 clinical isolates. J. Infect. Dis. 166:995-1005.
    • (1992) J. Infect. Dis. , vol.166 , pp. 995-1005
    • Henrickson, K.J.1    Savatski, L.L.2
  • 15
    • 0030023812 scopus 로고    scopus 로고
    • Two distinct human parainfluenza virus type 1 genotypes detected during the 1991 Milwaukee epidemic
    • Henrickson, K. J., and L. L. Savatski. 1996. Two distinct human parainfluenza virus type 1 genotypes detected during the 1991 Milwaukee epidemic. J. Clin. Microbiol. 34:695-700.
    • (1996) J. Clin. Microbiol. , vol.34 , pp. 695-700
    • Henrickson, K.J.1    Savatski, L.L.2
  • 16
    • 0026485550 scopus 로고
    • The mapping by high-pH anion-exchange chromatography with pulsed amperometric detection and capillary electrophoresis of the carbohydrate moieties of human plasma alpha 1-acid glycoprotein
    • Hermentin, P., et al. 1992. The mapping by high-pH anion-exchange chromatography with pulsed amperometric detection and capillary electrophoresis of the carbohydrate moieties of human plasma alpha 1-acid glycoprotein. Anal. Biochem. 206:419-429.
    • (1992) Anal. Biochem. , vol.206 , pp. 419-429
    • Hermentin, P.1
  • 17
    • 0028118587 scopus 로고
    • Human parainfluenza virus type 1 evolution combines cocirculation of strains and development of geographically restricted lineages
    • Hetherington, S. V., A. S. Watson, R. A. Scroggs, and A. Portner. 1994. Human parainfluenza virus type 1 evolution combines cocirculation of strains and development of geographically restricted lineages. J. Infect. Dis. 169:248-252.
    • (1994) J. Infect. Dis. , vol.169 , pp. 248-252
    • Hetherington, S.V.1    Watson, A.S.2    Scroggs, R.A.3    Portner, A.4
  • 18
    • 0028884662 scopus 로고
    • Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle
    • Huberman, K., R. W. Peluso, and A. Moscona. 1995. Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle. Virology 214:294-300.
    • (1995) Virology , vol.214 , pp. 294-300
    • Huberman, K.1    Peluso, R.W.2    Moscona, A.3
  • 19
    • 0035132884 scopus 로고    scopus 로고
    • Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity
    • Iorio, R. M., et al. 2001. Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity. J. Virol. 75:1918-1927.
    • (2001) J. Virol. , vol.75 , pp. 1918-1927
    • Iorio, R.M.1
  • 20
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
    • Lawrence, M. C., et al. 2004. Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J. Mol. Biol. 335:1343-1357.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1343-1357
    • Lawrence, M.C.1
  • 21
    • 0025847406 scopus 로고
    • Location of amino acid residues important for the structure and biological function of the haemagglutinin-neuraminidase glycoprotein of Sendai virus by analysis of escape mutants
    • Lyn, D., M. B. Mazanec, J. G. Nedrud, and A. Portner. 1991. Location of amino acid residues important for the structure and biological function of the haemagglutinin-neuraminidase glycoprotein of Sendai virus by analysis of escape mutants. J. Gen. Virol. 72:817-824.
    • (1991) J. Gen. Virol. , vol.72 , pp. 817-824
    • Lyn, D.1    Mazanec, M.B.2    Nedrud, J.G.3    Portner, A.4
  • 22
    • 0028841210 scopus 로고
    • Cooperative neuraminidase activity in a paramyxovirus
    • Mahon, P. J., R. Deng, A. M. Mirza, and R. M. Iorio. 1995. Cooperative neuraminidase activity in a paramyxovirus. Virology 213:241-244.
    • (1995) Virology , vol.213 , pp. 241-244
    • Mahon, P.J.1    Deng, R.2    Mirza, A.M.3    Iorio, R.M.4
  • 23
    • 55249102446 scopus 로고    scopus 로고
    • Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion
    • Mahon, P. J., A. M. Mirza, T. A. Musich, and R. M. Iorio. 2008. Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion. J. Virol. 82:10386-10396.
    • (2008) J. Virol. , vol.82 , pp. 10386-10396
    • Mahon, P.J.1    Mirza, A.M.2    Musich, T.A.3    Iorio, R.M.4
  • 24
    • 0019501239 scopus 로고
    • Inhibition of the neuraminidase of paramyxoviruses by halide ions: a possible means of modulating the two activities of the HN protein
    • Merz, D. C., P. Prehm, A. Scheid, and P. W. Choppin. 1981. Inhibition of the neuraminidase of paramyxoviruses by halide ions: a possible means of modulating the two activities of the HN protein. Virology 112:296-305.
    • (1981) Virology , vol.112 , pp. 296-305
    • Merz, D.C.1    Prehm, P.2    Scheid, A.3    Choppin, P.W.4
  • 25
    • 0026726805 scopus 로고
    • Fusion properties of cells infected with human parainfluenza virus type 3: receptor requirements for viral spread and virus-mediated membrane fusion
    • Moscona, A., and R. W. Peluso. 1992. Fusion properties of cells infected with human parainfluenza virus type 3: receptor requirements for viral spread and virus-mediated membrane fusion. J. Virol. 66:6280-6287.
    • (1992) J. Virol. , vol.66 , pp. 6280-6287
    • Moscona, A.1    Peluso, R.W.2
  • 26
    • 0025941857 scopus 로고
    • Fusion properties of cells persistently infected with human parainfluenza virus type 3: participation of hemagglutinin-neuraminidase in membrane fusion
    • Moscona, A., and R. W. Peluso. 1991. Fusion properties of cells persistently infected with human parainfluenza virus type 3: participation of hemagglutinin-neuraminidase in membrane fusion. J. Virol. 65:2773-2777.
    • (1991) J. Virol. , vol.65 , pp. 2773-2777
    • Moscona, A.1    Peluso, R.W.2
  • 27
    • 67449093027 scopus 로고    scopus 로고
    • Human parainfluenza virus infection of the airway epithelium: viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity
    • Palermo, L. M., et al. 2009. Human parainfluenza virus infection of the airway epithelium: viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity. J. Virol. 83:6900-6908.
    • (2009) J. Virol. , vol.83 , pp. 6900-6908
    • Palermo, L.M.1
  • 28
    • 33947363286 scopus 로고    scopus 로고
    • A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism
    • Porotto, M., M. Fornabaio, G. E. Kellogg, and A. Moscona. 2007. A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism. J. Virol. 81:3216-3228.
    • (2007) J. Virol. , vol.81 , pp. 3216-3228
    • Porotto, M.1    Fornabaio, M.2    Kellogg, G.E.3    Moscona, A.4
  • 29
    • 13444270795 scopus 로고    scopus 로고
    • Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein
    • Porotto, M., M. Murrell, O. Greengard, L. Doctor, and A. Moscona. 2005. Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein. J. Virol. 79:2383-2392. VOL. 85, 2011 HN PREFERS SUBSTRATES ON A SURFACE 12159
    • (2005) J. Virol. , vol.79 , pp. 2383-2392
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Doctor, L.4    Moscona, A.5
  • 30
    • 0016712387 scopus 로고
    • A temperature-sensitive mutant of Sendai virus with an altered hemagglutinin-neuraminidase polypeptide: consequences for virus assembly and cytopathology
    • Portner, A., R. A. Scroggs, P. S. Marx, and D. W. Kingsbury. 1975. A temperature-sensitive mutant of Sendai virus with an altered hemagglutinin-neuraminidase polypeptide: consequences for virus assembly and cytopathology. Virology 67:179-187.
    • (1975) Virology , vol.67 , pp. 179-187
    • Portner, A.1    Scroggs, R.A.2    Marx, P.S.3    Kingsbury, D.W.4
  • 31
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate
    • Potier, M., L. Mameli, M. Belisle, L. Dallaire, and S. B. Melancon. 1979. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl- alpha-D-N-acetylneuraminate) substrate. Anal. Biochem. 94:287-296.
    • (1979) Anal. Biochem. , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 32
    • 33645453800 scopus 로고    scopus 로고
    • Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus
    • Ryan, C., et al. 2006. Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus. Glycoconj. J. 23:135-141.
    • (2006) Glycoconj. J. , vol.23 , pp. 135-141
    • Ryan, C.1
  • 33
    • 54949158207 scopus 로고    scopus 로고
    • The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin
    • Schonfeld, D. L., R. B. Ravelli, U. Mueller, and A. Skerra. 2008. The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. J. Mol. Biol. 384:393-405.
    • (2008) J. Mol. Biol. , vol.384 , pp. 393-405
    • Schonfeld, D.L.1    Ravelli, R.B.2    Mueller, U.3    Skerra, A.4
  • 34
    • 0020616962 scopus 로고
    • Biological consequences of neuraminidase deficiency in Newcastle disease virus
    • Smith, G. W., and L. E. Hightower. 1983. Biological consequences of neuraminidase deficiency in Newcastle disease virus. J. Virol. 47:385-391.
    • (1983) J. Virol. , vol.47 , pp. 385-391
    • Smith, G.W.1    Hightower, L.E.2
  • 35
    • 0020054614 scopus 로고
    • Revertant analysis of a temperature-sensitive mutant of Newcastle disease virus with defective glycoproteins: implication of the fusion glycoprotein in cell killing and isolation of a neuraminidase-deficient hemagglutinating virus
    • Smith, G. W., and L. E. Hightower. 1982. Revertant analysis of a temperature-sensitive mutant of Newcastle disease virus with defective glycoproteins: implication of the fusion glycoprotein in cell killing and isolation of a neuraminidase-deficient hemagglutinating virus. J. Virol. 42:659-668.
    • (1982) J. Virol. , vol.42 , pp. 659-668
    • Smith, G.W.1    Hightower, L.E.2
  • 36
    • 84961040256 scopus 로고
    • Studies on fetuin, a glycoprotein of fetal serum. I. Isolation, chemical composition, and physiochemical properties
    • Spiro, R. G. 1960. Studies on fetuin, a glycoprotein of fetal serum. I. Isolation, chemical composition, and physiochemical properties. J. Biol. Chem. 235:2860-2869.
    • (1960) J. Biol. Chem. , vol.235 , pp. 2860-2869
    • Spiro, R.G.1
  • 37
    • 0016245734 scopus 로고
    • Structure of the O-glycosidically linked carbohydrate units of fetuin
    • Spiro, R. G., and V. D. Bhoyroo. 1974. Structure of the O-glycosidically linked carbohydrate units of fetuin. J. Biol. Chem. 249:5704-5717.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5704-5717
    • Spiro, R.G.1    Bhoyroo, V.D.2
  • 38
    • 0023616076 scopus 로고
    • Expression of the F and HN glycoproteins of human parainfluenza virus type 3 by recombinant vaccinia viruses: contributions of the individual proteins to host immunity
    • Spriggs, M. K., B. R. Murphy, G. A. Prince, R. A. Olmsted, and P. L. Collins. 1987. Expression of the F and HN glycoproteins of human parainfluenza virus type 3 by recombinant vaccinia viruses: contributions of the individual proteins to host immunity. J. Virol. 61:3416-3423.
    • (1987) J. Virol. , vol.61 , pp. 3416-3423
    • Spriggs, M.K.1    Murphy, B.R.2    Prince, G.A.3    Olmsted, R.A.4    Collins, P.L.5
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0032989659 scopus 로고    scopus 로고
    • Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain
    • Wang, Z., and R. M. Iorio. 1999. Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain. J. Gen. Virol. 80:749-753.
    • (1999) J. Gen. Virol. , vol.80 , pp. 749-753
    • Wang, Z.1    Iorio, R.M.2
  • 41
    • 0008128130 scopus 로고
    • The thiobarbituric acid assay of sialic acids
    • Warren, L. 1959. The thiobarbituric acid assay of sialic acids. J. Biol. Chem. 234:1971-1975.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1971-1975
    • Warren, L.1
  • 42
    • 0027768796 scopus 로고
    • Electrospray ionization-mass spectrometric analysis of serum transferrin isoforms in patients with carbohydrate-deficient glycoprotein syndrome
    • Yamashita, K., T. Ohkura, H. Ideo, K. Ohno, and M. Kanai. 1993. Electrospray ionization-mass spectrometric analysis of serum transferrin isoforms in patients with carbohydrate-deficient glycoprotein syndrome. J. Biochem. 114:766-769.
    • (1993) J. Biochem. , vol.114 , pp. 766-769
    • Yamashita, K.1    Ohkura, T.2    Ideo, H.3    Ohno, K.4    Kanai, M.5
  • 43
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemag-glutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan, P., et al. 2005. Structural studies of the parainfluenza virus 5 hemag-glutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803-815.
    • (2005) Structure , vol.13 , pp. 803-815
    • Yuan, P.1
  • 44
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion
    • Zaitsev, V., et al. 2004. Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J. Virol. 78: 3733-3741.
    • (2004) J. Virol. , vol.78 , pp. 3733-3741
    • Zaitsev, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.