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Volumn 73, Issue 7, 1999, Pages 6104-6110

Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; N ACETYL BETA GLUCOSAMINIDASE; OLIGOMER; OLIGOSACCHARIDE; SWAINSONINE; VIRUS GLYCOPROTEIN;

EID: 0032994359     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.7.6104-6110.1999     Document Type: Article
Times cited : (273)

References (54)
  • 1
    • 0023245732 scopus 로고
    • Expression of the Saccharomyces cerevisiae glycoprotein invertase in mouse fibroblasts: Glycosylation, secretion, and enzymatic activity
    • Bergh, M., C. Cepko, D. Wolf, and P. Rabbins. 1987. Expression of the Saccharomyces cerevisiae glycoprotein invertase in mouse fibroblasts: glycosylation, secretion, and enzymatic activity. Proc. Natl. Acad. Sci. USA 84: 3570-3574.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3570-3574
    • Bergh, M.1    Cepko, C.2    Wolf, D.3    Rabbins, P.4
  • 2
    • 0022787110 scopus 로고
    • Data appraisal, evaluation and display for synchrotron radiation experiments: Hardware and software
    • Boulin, C., R. Kempf, M. H. J. Koch, and S. M. Mclaughlin. 1986. Data appraisal, evaluation and display for synchrotron radiation experiments: hardware and software. Nucl. Instrum. Methods A249:399-407.
    • (1986) Nucl. Instrum. Methods , vol.A249 , pp. 399-407
    • Boulin, C.1    Kempf, R.2    Koch, M.H.J.3    Mclaughlin, S.M.4
  • 3
  • 4
    • 0025015320 scopus 로고
    • Purification and analysis of infectious virions and native non-structural antigens from cells infected with tick-borne encephalitis virus
    • Crooks, A. J., J. M. Lee, A. B. Dowsett, and J. R. Stephenson. 1990. Purification and analysis of infectious virions and native non-structural antigens from cells infected with tick-borne encephalitis virus. J. Chromatogr. 502: 59-68.
    • (1990) J. Chromatogr. , vol.502 , pp. 59-68
    • Crooks, A.J.1    Lee, J.M.2    Dowsett, A.B.3    Stephenson, J.R.4
  • 5
    • 0028650344 scopus 로고
    • The NS1 protein of tick-borne encephalitis virus forms multimeric species upon secretion from the host cell
    • Crooks, A. J., J. M. Lee, L. M. Easterbrook, A. V. Timofeev, and J. R. Stephenson. 1994. The NS1 protein of tick-borne encephalitis virus forms multimeric species upon secretion from the host cell. J. Gen. Virol. 75:3453-3460.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3453-3460
    • Crooks, A.J.1    Lee, J.M.2    Easterbrook, L.M.3    Timofeev, A.V.4    Stephenson, J.R.5
  • 7
    • 0027304942 scopus 로고
    • Differences between cell membrane fusion activities of two dengue type-1 isolates reflect modifications of viral structure
    • Desprès, P., M.-P. Frenkiel, and V. Deubel. 1993. Differences between cell membrane fusion activities of two dengue type-1 isolates reflect modifications of viral structure. Virology 196:209-219.
    • (1993) Virology , vol.196 , pp. 209-219
    • Desprès, P.1    Frenkiel, M.-P.2    Deubel, V.3
  • 8
    • 0025801963 scopus 로고
    • Characterization of yellow fever virus proteins E and NS1 expressed in Vero and Spodoptera frugiperda cells
    • Desprès, P., M. Girard, and M. Bouloy. 1991. Characterization of yellow fever virus proteins E and NS1 expressed in Vero and Spodoptera frugiperda cells. J. Gen. Virol. 72:1331-1342.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1331-1342
    • Desprès, P.1    Girard, M.2    Bouloy, M.3
  • 9
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., R. A. Lamb, J. K. Rose, and A. Helenius. 1993. Folding and assembly of viral membrane proteins. Virology 193:545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 10
    • 0342511969 scopus 로고    scopus 로고
    • Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions
    • Dubuisson, J. M., T. Decamps, and P. Vachette. 1997. Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions. J. Appl. Crystalogr. 30:49-54.
    • (1997) J. Appl. Crystalogr. , vol.30 , pp. 49-54
    • Dubuisson, J.M.1    Decamps, T.2    Vachette, P.3
  • 11
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein, A. D. 1991. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J. 5:3055-3063.
    • (1991) FASEB J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 12
    • 0023161237 scopus 로고
    • Glycosylation inhibitors for N-linked glycoproteins
    • Elbein, A. D. 1987. Glycosylation inhibitors for N-linked glycoproteins. Methods Enzymol. 138:661-709.
    • (1987) Methods Enzymol. , vol.138 , pp. 661-709
    • Elbein, A.D.1
  • 13
    • 0031020410 scopus 로고    scopus 로고
    • The dengue virus nonstructural-1 protein (NS1) generates antibodies to common epitopes on human blood clotting, integrin/ adhesin proteins and binds to human endothelial cells: Potential implications in haemorrhagic fever pathogenesis
    • Falconar, A. K. I. 1997. The dengue virus nonstructural-1 protein (NS1) generates antibodies to common epitopes on human blood clotting, integrin/ adhesin proteins and binds to human endothelial cells: potential implications in haemorrhagic fever pathogenesis. Arch. Virol. 142:897-916.
    • (1997) Arch. Virol. , vol.142 , pp. 897-916
    • Falconar, A.K.I.1
  • 14
    • 0025605334 scopus 로고
    • Immunoaffinity purification of native dimer forms of the flavivirus nonstructural glycoprotein NS1
    • Falconar, A. K. I., and P. R. Young. 1990. Immunoaffinity purification of native dimer forms of the flavivirus nonstructural glycoprotein NS1. J. Virol. Methods 30:323-332.
    • (1990) J. Virol. Methods , vol.30 , pp. 323-332
    • Falconar, A.K.I.1    Young, P.R.2
  • 15
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2a cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • Falgout, B., and L. Markoff. 1995. Evidence that flavivirus NS1-NS2a cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum. J. Virol. 69:7232-7243.
    • (1995) J. Virol. , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 16
    • 0025350163 scopus 로고
    • Membrane association and secretion of the Japanese encephalitis virus NS1 protein from cells expressing NS1 cDNA
    • Fan, W., and P. W. Mason. 1990. Membrane association and secretion of the Japanese encephalitis virus NS1 protein from cells expressing NS1 cDNA. Virology 177:470-476.
    • (1990) Virology , vol.177 , pp. 470-476
    • Fan, W.1    Mason, P.W.2
  • 17
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K., and K. Simons. 1995. The role of N-glycans in the secretory pathway. Cell 81:309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 18
    • 0027094171 scopus 로고
    • Expression and secretion of Japanese encephalitis virus nonstructural protein NS1 by insect cells using a recombinant baculovirus
    • Flamand, M., V. Deubel, and M. Girard. 1992. Expression and secretion of Japanese encephalitis virus nonstructural protein NS1 by insect cells using a recombinant baculovirus. Virology 191:826-336.
    • (1992) Virology , vol.191 , pp. 826-1336
    • Flamand, M.1    Deubel, V.2    Girard, M.3
  • 19
    • 0021806683 scopus 로고
    • Examination of the immunological relationships between flaviviruses using yellow fever virus monoclonal antibodies
    • Gould, E. A., A. Buckley, N. Cammack, A. D. T. Barrett, J. C. S. Clegg, R. Ishak, and M. G. R. Varma. 1985. Examination of the immunological relationships between flaviviruses using yellow fever virus monoclonal antibodies. J. Gen. Virol. 66:1369-1382.
    • (1985) J. Gen. Virol. , vol.66 , pp. 1369-1382
    • Gould, E.A.1    Buckley, A.2    Cammack, N.3    Barrett, A.D.T.4    Clegg, J.C.S.5    Ishak, R.6    Varma, M.G.R.7
  • 20
    • 0022102238 scopus 로고
    • Secretion of high-mannose-type α1-proteinase inhibitor and α1-acid glycoprotein by primary cultures of rat hepatocytes in the presence of the mannosidase I inhibitor 1-deoxymannojirimycin
    • Gross, V., K. Steube, T.-A. Tran-Thi, W. McDowell, R. Schwarz, K. Decker, W. Gerok, and P. Heinrich. 1985. Secretion of high-mannose-type α1-proteinase inhibitor and α1-acid glycoprotein by primary cultures of rat hepatocytes in the presence of the mannosidase I inhibitor 1-deoxymannojirimycin. Eur. J. Biochem. 150:41-46.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 41-46
    • Gross, V.1    Steube, K.2    Tran-Thi, T.-A.3    McDowell, W.4    Schwarz, R.5    Decker, K.6    Gerok, W.7    Heinrich, P.8
  • 22
    • 0022235399 scopus 로고
    • Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding
    • Herve, G., M. F. Moody, P. Tauc, P. Vachette, and P. T. Jones. 1985 Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding. J. Mol. Biol. 185:189-199.
    • (1985) J. Mol. Biol. , vol.185 , pp. 189-199
    • Herve, G.1    Moody, M.F.2    Tauc, P.3    Vachette, P.4    Jones, P.T.5
  • 24
    • 0028194854 scopus 로고
    • Glycosidase inhibitors in study of glycoconjugates
    • Kaushal, G. P., and A. D. Elbein. 1994. Glycosidase inhibitors in study of glycoconjugates. Methods Enzymol. 230:316-329.
    • (1994) Methods Enzymol. , vol.230 , pp. 316-329
    • Kaushal, G.P.1    Elbein, A.D.2
  • 26
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata, A. 1992. Structures and functions of the sugar chains of glycoproteins. Eur. J. Biochem. 209:483-501.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 483-501
    • Kobata, A.1
  • 27
    • 0032427728 scopus 로고    scopus 로고
    • N-glycosylation of a baculovirus-expressed recombinant glycoprotein in three insect cell lines
    • Kulakosky, P. C., M. L. Shuler, and H. A. Wood. 1998. N-Glycosylation of a baculovirus-expressed recombinant glycoprotein in three insect cell lines. In Vitro Cell. Dev. Biol. 34:101-108.
    • (1998) In Vitro Cell. Dev. Biol. , vol.34 , pp. 101-108
    • Kulakosky, P.C.1    Shuler, M.L.2    Wood, H.A.3
  • 28
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • Kuroda, K., H. Geyer, R. Geyer, W. Doerfler, and H.-D. Klenk. 1990 The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector. Virology 174:418-429.
    • (1990) Virology , vol.174 , pp. 418-429
    • Kuroda, K.1    Geyer, H.2    Geyer, R.3    Doerfler, W.4    Klenk, H.-D.5
  • 29
    • 0024552542 scopus 로고
    • The synthesis and maturation of a non-structural extracellular antigen from tick-borne encephalitis virus and its relationship to the intracellular NS1 protein
    • Lee, J. M., A. J. Crooks, and J. R. Stephenson. 1989. The synthesis and maturation of a non-structural extracellular antigen from tick-borne encephalitis virus and its relationship to the intracellular NS1 protein. J. Gen. Virol. 70:335-343.
    • (1989) J. Gen. Virol. , vol.70 , pp. 335-343
    • Lee, J.M.1    Crooks, A.J.2    Stephenson, J.R.3
  • 30
    • 0026064102 scopus 로고
    • Preparation of Japanese encephalitis virus nonstructural protein NS1 obtained from culture fluid of JEV-infected Vero cells
    • Lee, T., K. Watanabe, C. Aizawa, A. Nomoto, and H. Hashimoto. 1991. Preparation of Japanese encephalitis virus nonstructural protein NS1 obtained from culture fluid of JEV-infected Vero cells. Arch. Virol. 116:253-260.
    • (1991) Arch. Virol. , vol.116 , pp. 253-260
    • Lee, T.1    Watanabe, K.2    Aizawa, C.3    Nomoto, A.4    Hashimoto, H.5
  • 31
    • 0030774240 scopus 로고    scopus 로고
    • trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication
    • Lindenbach, B. D., and C. M. Rice. 1997. trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication. J. Virol. 71:9608-9617.
    • (1997) J. Virol. , vol.71 , pp. 9608-9617
    • Lindenbach, B.D.1    Rice, C.M.2
  • 32
    • 0029941322 scopus 로고    scopus 로고
    • Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication
    • Mackenzie, J. M., M. K. Jones, and P. R. Young. 1996. Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication. Virology 220:232-240.
    • (1996) Virology , vol.220 , pp. 232-240
    • Mackenzie, J.M.1    Jones, M.K.2    Young, P.R.3
  • 33
    • 0024502091 scopus 로고
    • Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells
    • Mason, P. W. 1989. Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells. Virology 169:354-364.
    • (1989) Virology , vol.169 , pp. 354-364
    • Mason, P.W.1
  • 34
    • 0031041235 scopus 로고    scopus 로고
    • The glycosylation of the influenza A virus hemagglutinin by mammalian cells - A site-specific study
    • Mir-Sheraki, S. Y., D. A. Ashford, D. J. Harvey, R. A. Dwek, and I. T. Schulze. 1997. The glycosylation of the influenza A virus hemagglutinin by mammalian cells - a site-specific study. J. Biol. Chem. 272:4027-4036.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4027-4036
    • Mir-Sheraki, S.Y.1    Ashford, D.A.2    Harvey, D.J.3    Dwek, R.A.4    Schulze, I.T.5
  • 35
    • 0001925194 scopus 로고    scopus 로고
    • Flaviviruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Monath, T. P., and F. X. Heinz. 1996. Flaviviruses, p. 961-1034. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, vol. 1. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , vol.1 , pp. 961-1034
    • Monath, T.P.1    Heinz, F.X.2
  • 36
    • 0030218225 scopus 로고    scopus 로고
    • Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: Effects on virus replication and mouse neurovirulence
    • Muylaert, I. R., T. J. Chambers, R. Galler, and C. M. Rice. 1996. Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: Effects on virus replication and mouse neurovirulence. Virology 222:159-168.
    • (1996) Virology , vol.222 , pp. 159-168
    • Muylaert, I.R.1    Chambers, T.J.2    Galler, R.3    Rice, C.M.4
  • 37
    • 0031060332 scopus 로고    scopus 로고
    • Genetic analysis of yellow fever virus NS1 protein: Identification of a temperature-sensitive mutation which blocks RNA accumulation
    • Muylaert, I. R., R. Galler, and C. M. Rice. 1997. Genetic analysis of yellow fever virus NS1 protein: identification of a temperature-sensitive mutation which blocks RNA accumulation. J. Virol. 71:291-298.
    • (1997) J. Virol. , vol.71 , pp. 291-298
    • Muylaert, I.R.1    Galler, R.2    Rice, C.M.3
  • 39
    • 0027255002 scopus 로고
    • Chimeric tick-borne encephalitis and dengue type 4 viruses: Effects of mutations on neurovirulence in mice
    • Pletnev, A. G., M. Bray, and C.-J. Lai. 1993. Chimeric tick-borne encephalitis and dengue type 4 viruses: effects of mutations on neurovirulence in mice. J. Virol. 67:4956-4963.
    • (1993) J. Virol. , vol.67 , pp. 4956-4963
    • Pletnev, A.G.1    Bray, M.2    Lai, C.-J.3
  • 40
    • 0026080606 scopus 로고
    • Glycosylation and secretion of yellow fever virus nonstructural protein NS1
    • Post, P. R., R. Carvalho, and R. Galler. 1990. Glycosylation and secretion of yellow fever virus nonstructural protein NS1. Virus Res. 18:291-302.
    • (1990) Virus Res. , vol.18 , pp. 291-302
    • Post, P.R.1    Carvalho, R.2    Galler, R.3
  • 41
    • 0027209027 scopus 로고
    • The effects of site-directed mutagenesis on the dimerization and secretion of the NS1 protein specified by dengue virus
    • Pryor, M. J., and P. J. Wright. 1993. The effects of site-directed mutagenesis on the dimerization and secretion of the NS1 protein specified by dengue virus. Virology 194:769-780.
    • (1993) Virology , vol.194 , pp. 769-780
    • Pryor, M.J.1    Wright, P.J.2
  • 42
    • 0028345969 scopus 로고
    • Glycosylation mutants of dengue virus NS1 protein
    • Pryor, M. J., and P. J. Wright. 1994. Glycosylation mutants of dengue virus NS1 protein. J. Gen. Virol. 75:1183-1187.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1183-1187
    • Pryor, M.J.1    Wright, P.J.2
  • 43
    • 0026701015 scopus 로고
    • Nonselective utilization of the endomannosidase pathway for processing glycoproteins by human hepatoma (HepG2) cells
    • Rabouille, C., and R. Spiro. 1992. Nonselective utilization of the endomannosidase pathway for processing glycoproteins by human hepatoma (HepG2) cells. J. Biol. Chem. 267:11573-11578.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11573-11578
    • Rabouille, C.1    Spiro, R.2
  • 44
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, vol. 1. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , vol.1 , pp. 931-959
    • Rice, C.M.1
  • 45
    • 0025373742 scopus 로고
    • Cell surface expression of yellow fever virus nonstructural glycoprotein NS1: Consequences of interaction with antibody
    • Schlesinger, J. J., M. W. Brandriss, J. R. Putnak, and E. E. Walsh. 1990. Cell surface expression of yellow fever virus nonstructural glycoprotein NS1: consequences of interaction with antibody. J. Gen. Virol. 71:593-599.
    • (1990) J. Gen. Virol. , vol.71 , pp. 593-599
    • Schlesinger, J.J.1    Brandriss, M.W.2    Putnak, J.R.3    Walsh, E.E.4
  • 46
    • 0027050126 scopus 로고
    • Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes
    • Simsolo, R., J. Ong, and P. Kern. 1992. Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes. J. Lipid Res. 33:1777-1784.
    • (1992) J. Lipid Res. , vol.33 , pp. 1777-1784
    • Simsolo, R.1    Ong, J.2    Kern, P.3
  • 47
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagine-linked glycans: Purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino, A. L., and T. H. Plummer. 1994. Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods Enzymol. 230:44-57.
    • (1994) Methods Enzymol. , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer, T.H.2
  • 48
    • 0023161248 scopus 로고
    • Peptide-N-(N-acetyl-β-glucosaminyl) asparagine amidase and endo-N-acetylglucosaminidase from Flavobacterium meningosepticum
    • Tarentino, A. L., and T. H. Plummer. 1987. Peptide-N-(N-acetyl-β-glucosaminyl) asparagine amidase and endo-N-acetylglucosaminidase from Flavobacterium meningosepticum. Methods Enzymol. 138:770-778.
    • (1987) Methods Enzymol. , vol.138 , pp. 770-778
    • Tarentino, A.L.1    Plummer, T.H.2
  • 49
    • 0031733824 scopus 로고    scopus 로고
    • Lectins as chaperones in glycoprotein folding
    • Trombetta, E., and A. Helenius. 1998. Lectins as chaperones in glycoprotein folding. Curr. Opin. Struct. Biol. 8:587-592.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 587-592
    • Trombetta, E.1    Helenius, A.2
  • 50
    • 0023239916 scopus 로고
    • Variation in distribution of the three flavivirus-specified glycoproteins detected by immunofluorescence in infected Vero cells
    • Westaway, E. G., and M. R. Goodman. 1987. Variation in distribution of the three flavivirus-specified glycoproteins detected by immunofluorescence in infected Vero cells. Arch. Virol. 94:215-228.
    • (1987) Arch. Virol. , vol.94 , pp. 215-228
    • Westaway, E.G.1    Goodman, M.R.2
  • 51
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures
    • Westaway, E. G., J. M. Mackenzie, M. T. Kenney, M. K. Jones, and A. A. Khromykh. 1997. Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures. J. Virol. 71:6650-6661.
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 52
    • 0024345888 scopus 로고
    • Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization
    • Winkler, G., S. E. Maxwell, C. Ruemmler, and V. Stollar. 1989. Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization. Virology 171:302-305.
    • (1989) Virology , vol.171 , pp. 302-305
    • Winkler, G.1    Maxwell, S.E.2    Ruemmler, C.3    Stollar, V.4
  • 53
    • 0023857108 scopus 로고
    • Evidence that the mature form of the flavivirus nonstructural protein NS1 is a dimer
    • Winkler, G., V. B. Randolph, G. R. Cleaves, T. E. Ryan, and V. Stollar. 1988 Evidence that the mature form of the flavivirus nonstructural protein NS1 is a dimer. Virology 162:187-196.
    • (1988) Virology , vol.162 , pp. 187-196
    • Winkler, G.1    Randolph, V.B.2    Cleaves, G.R.3    Ryan, T.E.4    Stollar, V.5
  • 54
    • 0031908813 scopus 로고    scopus 로고
    • The role of site-specific N-glycosylation in secretion of soluble forms of rabies virus glycoprotein
    • Wojczyk, B., M. Stwora-Wojczyk, S. Shakin-Eshelman, W. Wunner, and S. Spitalnik. 1998. The role of site-specific N-glycosylation in secretion of soluble forms of rabies virus glycoprotein. Glycobiology 8:121-130.
    • (1998) Glycobiology , vol.8 , pp. 121-130
    • Wojczyk, B.1    Stwora-Wojczyk, M.2    Shakin-Eshelman, S.3    Wunner, W.4    Spitalnik, S.5


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