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Volumn 4-4, Issue , 2008, Pages 821-838

Glycobiology of viruses

Author keywords

Alkyl glycosides; Disaccharide; Nucleophiles; Oligosaccharides; Regioselectivity

Indexed keywords

ANTIBODIES; BIOCHEMISTRY; CARBOHYDRATES; CELL MEMBRANES; CHAINS; CYTOLOGY; ENZYME ACTIVITY; GLYCOPROTEINS; NUCLEOPHILES; OLIGOSACCHARIDES; REGIOSELECTIVITY;

EID: 1242334091     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527618255.ch89     Document Type: Chapter
Times cited : (9)

References (61)
  • 1
    • 0028693193 scopus 로고
    • Viruses as model systems in cell biology
    • R. W. Compans, P. C. Roberts, Viruses as model systems in cell biology, Methods Cell Biol., 1994, 43, 3-42.
    • (1994) Methods Cell Biol. , vol.43 , pp. 3-42
    • Compans, R.W.1    Roberts, P.C.2
  • 2
    • 0029123983 scopus 로고
    • Virus entry and release in polarized epithelial cells
    • R. W. Compans, Virus entry and release in polarized epithelial cells, Curr. Top. Microbiol. Immunol., 1995, 202, 209-219.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.202 , pp. 209-219
    • Compans, R.W.1
  • 3
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • R. W. Doms, R. A. Lamb, J. K. Rose, A. Helenius, Folding and assembly of viral membrane proteins, Virology, 1993, 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
  • 4
    • 0027984858 scopus 로고
    • Entry and uncoating of enveloped viruses
    • M. Lanzrein, A. Schlegel, C. Kempf, Entry and uncoating of enveloped viruses, Biochem. J., 1994, 302, 313-320.
    • (1994) Biochem. J. , vol.302 , pp. 313-320
    • Lanzrein, M.1    Schlegel, A.2    Kempf, C.3
  • 5
    • 0028506208 scopus 로고
    • The Jeanne Manery Fisher Memorial Lecture 1994. Molecular biology of rubella virus structural proteins
    • S. Gillam, The Jeanne Manery Fisher Memorial Lecture 1994. Molecular biology of rubella virus structural proteins, Biochem. Cell Biol., 1994, 72, 349-356.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 349-356
    • Gillam, S.1
  • 6
    • 0030407682 scopus 로고    scopus 로고
    • Maturation and assembly of retroviral glycoproteins
    • D. Einfeld, Maturation and assembly of retroviral glycoproteins, Curr. Top. Microbiol. Immunol, 1996, 214, 133-176.
    • (1996) Curr. Top. Microbiol. Immunol , vol.214 , pp. 133-176
    • Einfeld, D.1
  • 7
    • 0026520248 scopus 로고
    • Viral glycoprotein heterogeneity-enhancement of functional diversity
    • I. T. Schulze, I. D. Manger, Viral glycoprotein heterogeneity-enhancement of functional diversity, Glycoconjugate J., 1992, 9, 63-66.
    • (1992) Glycoconjugate J. , vol.9 , pp. 63-66
    • Schulze, I.T.1    Manger, I.D.2
  • 8
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A. Varki, Biological roles of oligosaccharides: all of the theories are correct, Glycobiology, 1993, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 9
    • 0032560488 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors as potential broad based anti-viral agents
    • A. Mehta, N. Zitzmann, P. M. Rudd, T. M. Block, R. A. Dwek, Alpha-glucosidase inhibitors as potential broad based anti-viral agents, FEBS Lett., 1998, 430, 17-22.
    • (1998) FEBS Lett. , vol.430 , pp. 17-22
    • Mehta, A.1    Zitzmann, N.2    Rudd, P.M.3    Block, T.M.4    Dwek, R.A.5
  • 10
    • 0026642422 scopus 로고
    • Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size
    • K. Munk, E. Pritzer, E. Kretzschmar, B. Gutte, W. Garten, H. D. Klenk, Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size, Glycobiology, 1992, 2, 233-240.
    • (1992) Glycobiology , vol.2 , pp. 233-240
    • Munk, K.1    Pritzer, E.2    Kretzschmar, E.3    Gutte, B.4    Garten, W.5    Klenk, H.D.6
  • 11
    • 0024780756 scopus 로고
    • Molecular biology of Friend viral erythroleukemia
    • D. Kabat, Molecular biology of Friend viral erythroleukemia, Curr. Top. Microbiol. Immunol., 1989, 148, 1-42.
    • (1989) Curr. Top. Microbiol. Immunol. , vol.148 , pp. 1-42
    • Kabat, D.1
  • 12
    • 0028970073 scopus 로고
    • Erythroleukaemia induction by the Friend spleen focus-forming virus
    • S. K. Ruscetti, Erythroleukaemia induction by the Friend spleen focus-forming virus, Baillieres Clin. Haematol., 1995, 8, 225-247.
    • (1995) Baillieres Clin. Haematol. , vol.8 , pp. 225-247
    • Ruscetti, S.K.1
  • 13
    • 0031927203 scopus 로고    scopus 로고
    • Moloney murine leukemia virus envelope protein sub-units, gp70 and Pr15E, form a stable disulfide-linked complex
    • D. J. Opstelten, M. Wallin, H. Garoff, Moloney murine leukemia virus envelope protein sub-units, gp70 and Pr15E, form a stable disulfide-linked complex, J. Virol., 1998, 72, 6537-6545.
    • (1998) J. Virol. , vol.72 , pp. 6537-6545
    • Opstelten, D.J.1    Wallin, M.2    Garoff, H.3
  • 14
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of retroviral transmembrane protein: P15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein
    • A. Rein, J. Mirro, J. G. Haynes, S. M. Ernst, K. Nagashima, Function of the cytoplasmic domain of retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein, J. Virol., 1994, 68, 1773-1781.
    • (1994) J. Virol. , vol.68 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 15
    • 0344890777 scopus 로고
    • in H. Hanafusa, A. Pinter, M. E. Pullman (Eds.): Academic Press, New York
    • A. Pinter, in H. Hanafusa, A. Pinter, M. E. Pullman (Eds.): Retroviruses and disease, Academic Press, New York 1989, pp. 20-39.
    • (1989) Retroviruses and disease , pp. 20-39
    • Pinter, A.1
  • 17
    • 1842294027 scopus 로고    scopus 로고
    • The critical N-linked glycan of murine leukemia virus envelope protein promotes both folding of the C-terminal domains of the precursor polyprotein and stability of the postcleavage envelope complex
    • Z. Li, A. Pinter, S. C. Kayman, The critical N-linked glycan of murine leukemia virus envelope protein promotes both folding of the C-terminal domains of the precursor polyprotein and stability of the postcleavage envelope complex, J. Virol., 1997, 71, 7012-7019.
    • (1997) J. Virol. , vol.71 , pp. 7012-7019
    • Li, Z.1    Pinter, A.2    Kayman, S.C.3
  • 18
    • 0026684601 scopus 로고
    • Mutational analysis of the N-linked glycosylation sites of the SU envelope protein of Moloney murine leukemia virus
    • R. H. Felkner, M. J. Roth, Mutational analysis of the N-linked glycosylation sites of the SU envelope protein of Moloney murine leukemia virus, J. Virol., 1992, 66, 4258-4264.
    • (1992) J. Virol. , vol.66 , pp. 4258-4264
    • Felkner, R.H.1    Roth, M.J.2
  • 19
    • 0025134793 scopus 로고
    • Glycosylation of the envelope glycoprotein from a polytropic murine retrovirus in two different host cells
    • H. Geyer, R. Kempf, H.-H. Schott, R. Geyer, Glycosylation of the envelope glycoprotein from a polytropic murine retrovirus in two different host cells, Eur. J. Biochem., 1990, 193, 855-862.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 855-862
    • Geyer, H.1    Kempf, R.2    Schott, H.-H.3    Geyer, R.4
  • 20
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • H. Feldmann, S. T. Nichol, H. D. Klenk, C. J. Peters, A. Sanchez, Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein, Virology, 1994, 199, 469-473.
    • (1994) Virology , vol.199 , pp. 469-473
    • Feldmann, H.1    Nichol, S.T.2    Klenk, H.D.3    Peters, C.J.4    Sanchez, A.5
  • 21
    • 0030733467 scopus 로고    scopus 로고
    • Host-cell-specific glycosylation of HIV-2 envelope glycoprotein
    • S. Liedtke, R. Geyer, H. Geyer, Host-cell-specific glycosylation of HIV-2 envelope glycoprotein, Glycoconj. J., 1997, 14, 785-793.
    • (1997) Glycoconj. J. , vol.14 , pp. 785-793
    • Liedtke, S.1    Geyer, R.2    Geyer, H.3
  • 22
    • 0023807495 scopus 로고
    • Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells
    • T. Mizuochi, M. W. Spellman, M. Larkin, J. Solomon, L. J. Basa, T. Feizi, Carbohydrate structures of the human-immunodeficiency-virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese-hamster ovary cells, Biochem. J., 1988, 254, 599-603.
    • (1988) Biochem. J. , vol.254 , pp. 599-603
    • Mizuochi, T.1    Spellman, M.W.2    Larkin, M.3    Solomon, J.4    Basa, L.J.5    Feizi, T.6
  • 23
    • 0025374887 scopus 로고
    • Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues
    • T. Mizuochi, T. J. Matthews, M. Kato, J. Hamako, K. Titani, J. Solomon, T. Feizi, Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues, J. Biol.Chem., 1990, 265, 8519-8524.
    • (1990) J. Biol.Chem. , vol.265 , pp. 8519-8524
    • Mizuochi, T.1    Matthews, T.J.2    Kato, M.3    Hamako, J.4    Titani, K.5    Solomon, J.6    Feizi, T.7
  • 24
    • 0024232268 scopus 로고
    • Structural characterization by chromatographic profiling of the oligosaccharides of human immunodeficiency virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese hamster ovary cells
    • T. Mizuochi, M. W. Spellman, M. Larkin, J. Solomon, L. J. Basa, T. Feizi, Structural characterization by chromatographic profiling of the oligosaccharides of human immunodeficiency virus (HIV) recombinant envelope glycoprotein gp120 produced in Chinese hamster ovary cells, Biomed. Chromatogr., 1988, 2, 260-270.
    • (1988) Biomed. Chromatogr. , vol.2 , pp. 260-270
    • Mizuochi, T.1    Spellman, M.W.2    Larkin, M.3    Solomon, J.4    Basa, L.J.5    Feizi, T.6
  • 25
    • 0028798328 scopus 로고
    • Cell surface activation of the erythropoietin receptor by Friend spleen focus-forming virus gp55
    • J. P. Li, H. O. Hu, Q. T. Niu, C. Fang, Cell surface activation of the erythropoietin receptor by Friend spleen focus-forming virus gp55, J. Virol., 1995, 69, 1714-1719.
    • (1995) J. Virol. , vol.69 , pp. 1714-1719
    • Li, J.P.1    Hu, H.O.2    Niu, Q.T.3    Fang, C.4
  • 26
    • 2642651104 scopus 로고    scopus 로고
    • An array of novel murine spleen focus-forming viruses that activate the erythropoietin receptor
    • E. Gomez-Lucia, Y. Zhi, M. Nabavi, W. Zhang, D. Kabat, M. E. Hoatlin, An array of novel murine spleen focus-forming viruses that activate the erythropoietin receptor, J. Virol., 1998, 72, 3742-3750.
    • (1998) J. Virol. , vol.72 , pp. 3742-3750
    • Gomez-Lucia, E.1    Zhi, Y.2    Nabavi, M.3    Zhang, W.4    Kabat, D.5    Hoatlin, M.E.6
  • 27
    • 0026070065 scopus 로고
    • Friend virus-induced erythroleukemia and the multistage nature of cancer
    • Y. Ben-David, A. Bernstein, Friend virus-induced erythroleukemia and the multistage nature of cancer, Cell, 1991, 66, 831-834.
    • (1991) Cell , vol.66 , pp. 831-834
    • Ben-David, Y.1    Bernstein, A.2
  • 28
    • 0023840524 scopus 로고
    • Carbohydrate structure of glycoprotein 52 encoded by the polycythemia-inducing strain of Friend spleen focus-forming virus
    • K.-H. Strube, H.-H. Schott, R. Geyer, Carbohydrate structure of glycoprotein 52 encoded by the polycythemia-inducing strain of Friend spleen focus-forming virus, J. Biol. Chem., 1988, 263, 3762-3771.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3762-3771
    • Strube, K.-H.1    Schott, H.-H.2    Geyer, R.3
  • 29
    • 0028067011 scopus 로고
    • Glycosylation of glycoprotein 55 encoded by the anaemia-inducing strain of Friend spleen focus-forming virus
    • J. Völker, H. Geyer, R. Geyer, Glycosylation of glycoprotein 55 encoded by the anaemia-inducing strain of Friend spleen focus-forming virus, Glycoconj. J., 1994, 11, 133-139.
    • (1994) Glycoconj. J. , vol.11 , pp. 133-139
    • Völker, J.1    Geyer, H.2    Geyer, R.3
  • 30
    • 0024581643 scopus 로고
    • Carbohydrate structure of glycoprotein 65 encoded by the polycythemia-inducing strain of Friend spleen focus-forming virus
    • K.-H. Strube, R. Geyer, Carbohydrate structure of glycoprotein 65 encoded by the polycythemia-inducing strain of Friend spleen focus-forming virus, Eur. J. Biochem., 1989, 179, 441-450.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 441-450
    • Strube, K.-H.1    Geyer, R.2
  • 31
    • 0027486632 scopus 로고
    • Glycosylation pattern and processing of envelope gene products encoded by glycosylation mutants of Friend spleen focus-forming virus
    • A. Freis, S. Rau, R. W. Friedrich, R. Geyer, Glycosylation pattern and processing of envelope gene products encoded by glycosylation mutants of Friend spleen focus-forming virus, Glycobiology, 1993, 3, 465-473.
    • (1993) Glycobiology , vol.3 , pp. 465-473
    • Freis, A.1    Rau, S.2    Friedrich, R.W.3    Geyer, R.4
  • 32
    • 0027500535 scopus 로고
    • The role of gp55 N-glycosylation in pathogenesis of Friend spleen focus-forming virus
    • S. Rau, R. Geyer, R. W. Friedrich, The role of gp55 N-glycosylation in pathogenesis of Friend spleen focus-forming virus, J. Gen. Virol., 1993, 74, 699-705.
    • (1993) J. Gen. Virol. , vol.74 , pp. 699-705
    • Rau, S.1    Geyer, R.2    Friedrich, R.W.3
  • 33
    • 0027511719 scopus 로고
    • Erythropoietin receptor (EpoR)-dependent mito-genicity of spleen focus-forming virus correlates with viral pathogenicity and processing of env protein but not with formation of gp52-EpoR complexes in the endoplasmic reticulum
    • Y. Wang, S. C. Kayman, J. P. Li, A. Pinter, Erythropoietin receptor (EpoR)-dependent mito-genicity of spleen focus-forming virus correlates with viral pathogenicity and processing of env protein but not with formation of gp52-EpoR complexes in the endoplasmic reticulum, J. Virol., 1993, 67, 1322-1327.
    • (1993) J. Virol. , vol.67 , pp. 1322-1327
    • Wang, Y.1    Kayman, S.C.2    Li, J.P.3    Pinter, A.4
  • 35
    • 0027407071 scopus 로고
    • Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein
    • C. Will, E. Mühlberger, D. Linder, W. Slenczka, H. D. Klenk, H. Feldmann, Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein, J. Virol., 1993, 67, 1203-1210.
    • (1993) J. Virol. , vol.67 , pp. 1203-1210
    • Will, C.1    Mühlberger, E.2    Linder, D.3    Slenczka, W.4    Klenk, H.D.5    Feldmann, H.6
  • 37
    • 0028872697 scopus 로고
    • The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus
    • S. Becker, M. Spiess, H. D. Klenk, The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus, J. Gen. Virol., 1995, 76, 393-399.
    • (1995) J. Gen. Virol. , vol.76 , pp. 393-399
    • Becker, S.1    Spiess, M.2    Klenk, H.D.3
  • 38
    • 0032615793 scopus 로고    scopus 로고
    • Molecular pathogenesis and filovirus infections: Role of macrophages and endothelial cells
    • H. J. Schnittler, H. Feldmann, Molecular pathogenesis and filovirus infections: Role of macrophages and endothelial cells, Curr. Top. Microbiol. Immunol, 1998, 235, 175-204.
    • (1998) Curr. Top. Microbiol. Immunol , vol.235 , pp. 175-204
    • Schnittler, H.J.1    Feldmann, H.2
  • 40
  • 41
    • 0031774859 scopus 로고    scopus 로고
    • Structure and glycosylation patterns of surface proteins from woodchuck hepatitis virus
    • T. K. Tolle, D. Glebe, M. Linder, D. Linder, S. Schmitt, R. Geyer, W. H. Gerlich, Structure and glycosylation patterns of surface proteins from woodchuck hepatitis virus, J. Virol., 1998, 72, 9978-9985.
    • (1998) J. Virol. , vol.72 , pp. 9978-9985
    • Tolle, T.K.1    Glebe, D.2    Linder, M.3    Linder, D.4    Schmitt, S.5    Geyer, R.6    Gerlich, W.H.7
  • 43
    • 0028859149 scopus 로고
    • Novel transmembrane topology of the hepatitis B virus envelope proteins
    • R. Prange, R. E. Streeck, Novel transmembrane topology of the hepatitis B virus envelope proteins, EMBO J, 1995, 14, 247-256.
    • (1995) EMBO J , vol.14 , pp. 247-256
    • Prange, R.1    Streeck, R.E.2
  • 44
    • 0026034960 scopus 로고
    • The role of envelope proteins in hepatitis B virus assembly
    • V. Bruss, D. Ganem, The role of envelope proteins in hepatitis B virus assembly, Proc. Natl Acad. Sci. U. S. A., 1991, 88, 1059-1063.
    • (1991) Proc. Natl Acad. Sci. U. S. A. , vol.88 , pp. 1059-1063
    • Bruss, V.1    Ganem, D.2
  • 45
    • 0031058830 scopus 로고    scopus 로고
    • Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion
    • A. Mehta, X. Lu, T. M. Block, B. S. Blumberg, R. A. Dwek, Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion, Proc. Natl Acad. Sci. U. S. A., 1997, 94, 1822-1827.
    • (1997) Proc. Natl Acad. Sci. U. S. A. , vol.94 , pp. 1822-1827
    • Mehta, A.1    Lu, X.2    Block, T.M.3    Blumberg, B.S.4    Dwek, R.A.5
  • 46
    • 0028872090 scopus 로고
    • Evidence that N-linked glycosylation is necessary for hepatitis B virus secretion
    • X. Lu, A. Mehta, R. A. Dwek, T. Butters, T. Block, Evidence that N-linked glycosylation is necessary for hepatitis B virus secretion, Virology, 1995, 213, 660-665.
    • (1995) Virology , vol.213 , pp. 660-665
    • Lu, X.1    Mehta, A.2    Dwek, R.A.3    Butters, T.4    Block, T.5
  • 47
    • 0031975746 scopus 로고    scopus 로고
    • Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles
    • M. Werr, R. Prange, Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles, J. Virol., 1998, 72, 778-782.
    • (1998) J. Virol. , vol.72 , pp. 778-782
    • Werr, M.1    Prange, R.2
  • 48
    • 0030964918 scopus 로고    scopus 로고
    • Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited
    • X. Lu, A. Mehta, M. Dadmarz, R. A. Dwek, B. S. Blumberg, T. M. Block, Aberrant trafficking of hepatitis B virus glycoproteins in cells in which N-glycan processing is inhibited, Proc. Natl Acad. Sci. U. S. A., 1997, 94, 2380-2385.
    • (1997) Proc. Natl Acad. Sci. U. S. A. , vol.94 , pp. 2380-2385
    • Lu, X.1    Mehta, A.2    Dadmarz, M.3    Dwek, R.A.4    Blumberg, B.S.5    Block, T.M.6
  • 51
    • 0021401355 scopus 로고
    • The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein E1
    • H. Niemann, R. Geyer, H.-D. Klenk, D. Linder, S. Stirm, M. Wirth, The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein E1, EMBO J., 1984, 3, 665-670.
    • (1984) EMBO J. , vol.3 , pp. 665-670
    • Niemann, H.1    Geyer, R.2    Klenk, H.-D.3    Linder, D.4    Stirm, S.5    Wirth, M.6
  • 52
    • 0019494758 scopus 로고
    • Carbohydrate structures of HVJ (Sendai virus) glycoproteins
    • H. Yoshima, M. Nakanishi, Y. Okada, A. Kobata, Carbohydrate structures of HVJ (Sendai virus) glycoproteins, J. Biol. Chem., 1981, 256, 5355-5361.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5355-5361
    • Yoshima, H.1    Nakanishi, M.2    Okada, Y.3    Kobata, A.4
  • 53
    • 0021399497 scopus 로고
    • Structure of the major oligosaccharides in the fusion glycoprotein of Newcastle disease virus
    • S. Diabaté, R. Geyer, S. Stirm, Structure of the major oligosaccharides in the fusion glycoprotein of Newcastle disease virus, Eur. J. Biochem., 1984, 139, 329-336.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 329-336
    • Diabaté, S.1    Geyer, R.2    Stirm, S.3
  • 54
    • 0017865285 scopus 로고
    • Carbohydrate structure of vesicular stomatitis virus glycoprotein
    • C. L. Reading, E. E. Penhoet, C. E. Ballou, Carbohydrate structure of vesicular stomatitis virus glycoprotein, J. Biol. Chem., 1978, 253, 5600-5612.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5600-5612
    • Reading, C.L.1    Penhoet, E.E.2    Ballou, C.E.3
  • 55
    • 0023186088 scopus 로고
    • Carbohydrates of influenza virus. Structure of the oligosaccharides linked to asparagines 406 and 478 in the hemagglutinin of fowl plague virus, strain Dutch
    • R. Geyer, S. Diabaté, H. Geyer, H. D. Klenk, H. Niemann, S. Stirm, Carbohydrates of influenza virus. Structure of the oligosaccharides linked to asparagines 406 and 478 in the hemagglutinin of fowl plague virus, strain Dutch, Glycoconj. J., 1987, 4, 17-32.
    • (1987) Glycoconj. J. , pp. 17-32
    • Geyer, R.1    Diabaté, S.2    Geyer, H.3    Klenk, H.D.4    Niemann, H.5    Stirm, S.6
  • 56
    • 0022137782 scopus 로고
    • Carbohydrates of influenza virus. Structural elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional 1H n.m.r. and methylation analysis
    • W. Keil, R. Geyer, J. Dabrowski, U. Dabrowski, H. Niemann, S. Stirm, H. D. Klenk, Carbohydrates of influenza virus. Structural elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional 1H n.m.r. and methylation analysis, EMBO J., 1985, 4, 2711-2720.
    • (1985) EMBO J. , vol.4 , pp. 2711-2720
    • Keil, W.1    Geyer, R.2    Dabrowski, J.3    Dabrowski, U.4    Niemann, H.5    Stirm, S.6    Klenk, H.D.7
  • 57
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120
    • H. Geyer, C. Holschbach, G. Hunsmann, J. Schneider, Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120, J. Biol. Chem., 1988, 263, 11760-11767.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11760-11767
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3    Schneider, J.4
  • 58
    • 0028017964 scopus 로고
    • Oligosaccharide profiles of HIV-2 external glycoprotein: Dependence on host cells and virus isolates
    • S. Liedtke, M. Adamski, R. Geyer, A. Pfützner, H. Rübsamen-Waigmann, H. Geyer, Oligosaccharide profiles of HIV-2 external glycoprotein: Dependence on host cells and virus isolates, Glycobiology, 1994, 4, 477-484.
    • (1994) Glycobiology , vol.4 , pp. 477-484
    • Liedtke, S.1    Adamski, M.2    Geyer, R.3    Pfützner, A.4    Rübsamen-Waigmann, H.5    Geyer, H.6
  • 59
    • 0025327470 scopus 로고
    • Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)
    • H. Holschbach, J. Schneider, H. Geyer, Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys), Biochem. J., 1990, 267, 759-766.
    • (1990) Biochem. J. , vol.267 , pp. 759-766
    • Holschbach, H.1    Schneider, J.2    Geyer, H.3


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