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Volumn 13, Issue 7, 2003, Pages 539-548

N-glycan structures of human transferrin produced by Lymantria dispar (gypsy moth) cells using the LdMNPV expression system

Author keywords

Baculovirus; Gypsy moth; Insect cells; Lymantria dispar nucleopolyhedrovirus; N glycan

Indexed keywords

2 AMINOPYRIDINE; ASPARAGINE; BOVINE SERUM ALBUMIN; FUCOSE; GLYCAN; MANNOSE; N ACETYLGALACTOSAMINE; POLYHEDRIN; RECOMBINANT PROTEIN; TRANSFERRIN;

EID: 0037819506     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwg071     Document Type: Article
Times cited : (26)

References (52)
  • 1
    • 0033902975 scopus 로고    scopus 로고
    • N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: Effects of mammalian galactosyltransferase
    • Ailor, E., Takahashi, N., Tsukamoto, Y., Masuda, K., Rahman, B.A., Jarvis, D.L., Lee, Y.C., and Betenbaugh, M.J. (2000) N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: effects of mammalian galactosyltransferase. Glycobiology, 10, 837-847.
    • (2000) Glycobiology , vol.10 , pp. 837-847
    • Ailor, E.1    Takahashi, N.2    Tsukamoto, Y.3    Masuda, K.4    Rahman, B.A.5    Jarvis, D.L.6    Lee, Y.C.7    Betenbaugh, M.J.8
  • 2
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altman, F., Schwihla, S., Staudacher, E., and Gloessl, J. (1995a) Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem., 270, 17344-17349.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17344-17349
    • Altman, F.1    Schwihla, S.2    Staudacher, E.3    Gloessl, J.4
  • 3
    • 0028926641 scopus 로고
    • Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity
    • Altmann, F., Schweiszer, S., and Weber, C. (1995b) Kinetic comparison of peptide: N-glycosidases F and A reveals several differences in substrate specificity. Glycoconj. J., 12, 84-93.
    • (1995) Glycoconj. J. , vol.12 , pp. 84-93
    • Altmann, F.1    Schweiszer, S.2    Weber, C.3
  • 4
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann, F., Staudacher, E., Wilson, I.B., and Marz, L. (1999) Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J., 16, 109-123.
    • (1999) Glycoconj. J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    Marz, L.4
  • 5
    • 0036910585 scopus 로고    scopus 로고
    • Expression and functional characterization of a nucleotide sugar transporter from Drosophila melanogaster: Relevance to protein glycosylation in insect cell expression systems
    • Aumiller, J.J. and Jarvis, D.L. (2002) Expression and functional characterization of a nucleotide sugar transporter from Drosophila melanogaster: relevance to protein glycosylation in insect cell expression systems. Protein Expr. Purif., 26, 438-448.
    • (2002) Protein Expr. Purif. , vol.26 , pp. 438-448
    • Aumiller, J.J.1    Jarvis, D.L.2
  • 7
    • 0029758219 scopus 로고    scopus 로고
    • Characterization of the Lymantria dispar nucleopolyhedrovirus 25K FP gene
    • Bischoff, D.S. and Slavicek, J.M. (1996) Characterization of the Lymantria dispar nucleopolyhedrovirus 25K FP gene. J. Gen. Virol., 77(8), 1913-1923.
    • (1996) J. Gen. Virol. , vol.77 , Issue.8 , pp. 1913-1923
    • Bischoff, D.S.1    Slavicek, J.M.2
  • 8
    • 0035817416 scopus 로고    scopus 로고
    • Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases
    • Breitbach, K. and Jarvis, D.L. (2001) Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases. Biotechnol. Bioeng., 74, 230-239.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 230-239
    • Breitbach, K.1    Jarvis, D.L.2
  • 9
    • 0019873857 scopus 로고
    • Isolation and characterization of mosquito cell membrane glycoproteins
    • Butters, T.D. and Hughes, R.C. (1981) Isolation and characterization of mosquito cell membrane glycoproteins. Biochim. Biophys. Acta, 640, 655-671.
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 655-671
    • Butters, T.D.1    Hughes, R.C.2
  • 10
    • 0030856740 scopus 로고    scopus 로고
    • Detailed studies on substrate structure requirements of glycoamidases A and F
    • Fan, J.-Q. and Lee, Y.C. (1997) Detailed studies on substrate structure requirements of glycoamidases A and F. J. Biol. Chem., 272, 27058-27064.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27058-27064
    • Fan, J.-Q.1    Lee, Y.C.2
  • 11
    • 0035735890 scopus 로고    scopus 로고
    • N- and O-linked oligosaccharides of allergenic glycoproteins
    • Fotisch, K. and Vieths, S. (2001) N- and O-linked oligosaccharides of allergenic glycoproteins. Glycoconj. J., 18, 373-390.
    • (2001) Glycoconj. J. , vol.18 , pp. 373-390
    • Fotisch, K.1    Vieths, S.2
  • 12
    • 2242455924 scopus 로고    scopus 로고
    • Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans
    • Hollister, J., Grabenhorst, E., Nimtz, M., Conradt, H., and Jarvis, D.L. (2002) Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry, 41, 15093-15104.
    • (2002) Biochemistry , vol.41 , pp. 15093-15104
    • Hollister, J.1    Grabenhorst, E.2    Nimtz, M.3    Conradt, H.4    Jarvis, D.L.5
  • 13
    • 0035093068 scopus 로고    scopus 로고
    • Engineering lepidopteran insect cells for sialoglycoprotein production by genetic transformation with mammalian beta 1,4-galactosyltransferase and alpha 2,6-sialyltransferase genes
    • Hollister, J.R. and Jarvis, D.L. (2001) Engineering lepidopteran insect cells for sialoglycoprotein production by genetic transformation with mammalian beta 1,4-galactosyltransferase and alpha 2,6-sialyltransferase genes. Glycobiology, 11, 1-9.
    • (2001) Glycobiology , vol.11 , pp. 1-9
    • Hollister, J.R.1    Jarvis, D.L.2
  • 14
    • 0031775473 scopus 로고    scopus 로고
    • Stable expression of mammalian β-1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells
    • Hollister, J.R., Shaper, J.H., and Jarvis, D.L. (1998) Stable expression of mammalian β-1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells. Glycobiology, 8, 473-480.
    • (1998) Glycobiology , vol.8 , pp. 473-480
    • Hollister, J.R.1    Shaper, J.H.2    Jarvis, D.L.3
  • 15
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing
    • Hsieh, P. and Robbins, P.W. (1984) Regulation of asparagine-linked oligosaccharide processing. J. Biol. Chem., 259, 2375-2382.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 17
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins, N. and Curling, E.M. (1994) Glycosylation of recombinant proteins: problems and prospects. Enzyme Microb. Technol., 16, 354-364.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.2
  • 18
    • 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
  • 19
    • 0028236119 scopus 로고
    • Structure of the N-linked oligosaccharides of the membrane glycoproteins from three Lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
    • Kubelka, V., Altman, F., Kornfeld, G., and März, L. (1994) Structure of the N-linked oligosaccharides of the membrane glycoproteins from three Lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N). Arch. Biochem. Biophys., 308, 148-157.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 148-157
    • Kubelka, V.1    Altman, F.2    Kornfeld, G.3    März, L.4
  • 20
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • Kuroda, K., Geyer, H., Geyer, R., Doerfler, W., and Klenk, H.D. (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
  • 22
    • 0034625409 scopus 로고    scopus 로고
    • Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability
    • Lawrence, S.M., Huddleston, K.A., Pitts, L.R., Nguyen, N., Lee, Y.C., Vann, W.F., Coleman, T.A., and Betenbaugh, M.J. (2000) Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability. J. Biol. Chem., 275, 17869-17877.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17869-17877
    • Lawrence, S.M.1    Huddleston, K.A.2    Pitts, L.R.3    Nguyen, N.4    Lee, Y.C.5    Vann, W.F.6    Coleman, T.A.7    Betenbaugh, M.J.8
  • 24
    • 0000383273 scopus 로고
    • Protein glycosylation in insects
    • Montreuil, J., Vliegenthart, J.F.G., and Schachter, H. (Eds), Elsevier, Amsterdam, The Netherlands
    • März, L., Altman, F., Staudacher, E., and Kubelka, V. (1995) Protein glycosylation in insects. In Montreuil, J., Vliegenthart, J.F.G., and Schachter, H. (Eds), Glycoproteins. Elsevier, Amsterdam, The Netherlands, pp. 543-563.
    • (1995) Glycoproteins , pp. 543-563
    • März, L.1    Altman, F.2    Staudacher, E.3    Kubelka, V.4
  • 25
    • 0028950435 scopus 로고
    • Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography
    • Nakagawa, H., Kawamura, Y., Kato, K., Shimada, I., Arata, Y., and Takahashi, N. (1995) Identification of neutral and sialyl N-linked oligosaccharide structures from human serum glycoproteins using three kinds of high-performance liquid chromatography. Anal. Biochem., 226, 130-138.
    • (1995) Anal. Biochem. , vol.226 , pp. 130-138
    • Nakagawa, H.1    Kawamura, Y.2    Kato, K.3    Shimada, I.4    Arata, Y.5    Takahashi, N.6
  • 26
    • 0030070842 scopus 로고    scopus 로고
    • Isolation and characterization of an insect cell line able to perform complex N-linked glycosylation on recombinant proteins
    • Ogonah, O.W., Freedman, R.B., Jenkins, N., Patel, K., and Rooney, B.C. (1996) Isolation and characterization of an insect cell line able to perform complex N-linked glycosylation on recombinant proteins. Biotechnol., 14, 197-202.
    • (1996) Biotechnol. , vol.14 , pp. 197-202
    • Ogonah, O.W.1    Freedman, R.B.2    Jenkins, N.3    Patel, K.4    Rooney, B.C.5
  • 27
    • 0031799347 scopus 로고    scopus 로고
    • A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis
    • Papac, D.I., Briggs, J.B., Chin, E.T., and Jones, A.J. (1998) A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis. Glycobiology, 8, 445-454.
    • (1998) Glycobiology , vol.8 , pp. 445-454
    • Papac, D.I.1    Briggs, J.B.2    Chin, E.T.3    Jones, A.J.4
  • 28
    • 0026691179 scopus 로고
    • The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of α-1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • Prenner, C., Mach, L., Glossl, J., and Marz, L. (1992) The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of α-1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem. J., 284(2), 377-380.
    • (1992) Biochem. J. , vol.284 , Issue.2 , pp. 377-380
    • Prenner, C.1    Mach, L.2    Glossl, J.3    Marz, L.4
  • 29
    • 0028220764 scopus 로고
    • Identification and characterization of the ecdysteroid UDP-glucosyltransferase gene of the Lymantria dispar multinucleocapsid nuclear polyhedrosis virus
    • Riegel, C.I., Lanner-Herrera, C., and Slavicek, J.M. (1994) Identification and characterization of the ecdysteroid UDP-glucosyltransferase gene of the Lymantria dispar multinucleocapsid nuclear polyhedrosis virus. J. Gen. Virol., 75(4), 829-838.
    • (1994) J. Gen. Virol. , vol.75 , Issue.4 , pp. 829-838
    • Riegel, C.I.1    Lanner-Herrera, C.2    Slavicek, J.M.3
  • 30
    • 0034701053 scopus 로고    scopus 로고
    • Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells
    • Rudd, P.M., Downing, A.K., Cadene, M., Harvey, D.J., Wormald, M.R., Weir, I., Dwek, R.A., Rifkin, D.B., and Gleizes, P.E. (2000) Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells. Biochemistry, 39, 1596-1603.
    • (2000) Biochemistry , vol.39 , pp. 1596-1603
    • Rudd, P.M.1    Downing, A.K.2    Cadene, M.3    Harvey, D.J.4    Wormald, M.R.5    Weir, I.6    Dwek, R.A.7    Rifkin, D.B.8    Gleizes, P.E.9
  • 31
    • 0034793949 scopus 로고    scopus 로고
    • Identification of a Lymantria dispar nucleopolyhedrovirus isolate that does not accumulate few-polyhedra mutants during extended serial passage in cell culture
    • Slavicek, J.M., Hayes-Plazolles, N., and Kelly, M.E. (2001) Identification of a Lymantria dispar nucleopolyhedrovirus isolate that does not accumulate few-polyhedra mutants during extended serial passage in cell culture. Biol. Con., 22, 159-168.
    • (2001) Biol. Con. , vol.22 , pp. 159-168
    • Slavicek, J.M.1    Hayes-Plazolles, N.2    Kelly, M.E.3
  • 32
    • 0001962451 scopus 로고
    • A manual of methods for baculovirus vectors and insect cell culture procedures
    • No. 1555
    • Summers, M.D. and Smith, G.E. (1987) A manual of methods for baculovirus vectors and insect cell culture procedures. TX Ag. Expt. Stn. Bull., No. 1555.
    • (1987) TX Ag. Expt. Stn. Bull.
    • Summers, M.D.1    Smith, G.E.2
  • 33
    • 0018116324 scopus 로고
    • Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages
    • Takahashi, N. and Nishibe, H. (1978) Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. J. Biochem. (Tokyo), 84, 1467-1473.
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 1467-1473
    • Takahashi, N.1    Nishibe, H.2
  • 34
    • 0001632932 scopus 로고
    • Analysis of N-linked oligosaccharides: Application of glycoamidase A
    • Takahashi, N. and Muramatsu, T. (Eds.), CRC Press, Boca Raton, FL
    • Takahashi, N. and Tomiya, N. (1992) Analysis of N-linked oligosaccharides: application of glycoamidase A. In: Takahashi, N. and Muramatsu, T. (Eds.), Handbook of endoglycosidases and glycoamidases. CRC Press, Boca Raton, FL, pp. 199-332.
    • (1992) Handbook of Endoglycosidases and Glycoamidases , pp. 199-332
    • Takahashi, N.1    Tomiya, N.2
  • 35
    • 12444251262 scopus 로고    scopus 로고
    • Elution coordinate database for 2-D/3-D sugar map
    • Online document available at www.gak.co.jp/fcca
    • Takahashi, N. and Tomiya, N. (1998) Elution coordinate database for 2-D/3-D sugar map. Online document available at www.gak.co.jp/fcca.
    • (1998)
    • Takahashi, N.1    Tomiya, N.2
  • 36
    • 0028957151 scopus 로고
    • Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides
    • Takahashi, N., Nakagawa, H., Fujikawa, K., Kawamura, Y., and Tomiya, N. (1995) Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides. Anal. Biochem., 226, 139-146.
    • (1995) Anal. Biochem. , vol.226 , pp. 139-146
    • Takahashi, N.1    Nakagawa, H.2    Fujikawa, K.3    Kawamura, Y.4    Tomiya, N.5
  • 38
    • 0032533672 scopus 로고    scopus 로고
    • Contribution of component monosaccharides to the coordinates of neutral and sialyl pyridylaminated N-glycans on a two-dimensional sugar map
    • Tomiya, N. and Takahashi, N. (1998) Contribution of component monosaccharides to the coordinates of neutral and sialyl pyridylaminated N-glycans on a two-dimensional sugar map. Anal. Biochem., 264, 204-210.
    • (1998) Anal. Biochem. , vol.264 , pp. 204-210
    • Tomiya, N.1    Takahashi, N.2
  • 39
    • 0023948708 scopus 로고
    • Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
    • Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y., and Takahashi, N. (1988) Analyses of N-linked oligosaccharides using a two-dimensional mapping technique. Anal. Biochem., 171, 73-90.
    • (1988) Anal. Biochem. , vol.171 , pp. 73-90
    • Tomiya, N.1    Awaya, J.2    Kurono, M.3    Endo, S.4    Arata, Y.5    Takahashi, N.6
  • 40
    • 0026029982 scopus 로고
    • Calculated two-dimensional sugar map of pyridylaminated oligosaccharides: Elucidation of the jack bean alpha-mannosidase digestion pathway of Man9GlcNAc2
    • Tomiya, N., Lee, Y.C., Yoshida, T., Wada, Y., Awaya, J., Kurono, M., and Takahashi, N. (1991) Calculated two-dimensional sugar map of pyridylaminated oligosaccharides: elucidation of the jack bean alpha-mannosidase digestion pathway of Man9GlcNAc2. Anal. Biochem., 193, 90-100.
    • (1991) Anal. Biochem. , vol.193 , pp. 90-100
    • Tomiya, N.1    Lee, Y.C.2    Yoshida, T.3    Wada, Y.4    Awaya, J.5    Kurono, M.6    Takahashi, N.7
  • 41
    • 0037234667 scopus 로고    scopus 로고
    • Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian β-1,4-galactosyltransferase and β-1,2-N-acetylglucosaminyltransferase II
    • Tomiya, N., Howe, D., Aumiller, J.J., Pathak, M., Park, J., Palter, K., Jarvis, D.L., Betenbaugh, M.J., and Lee, Y.C. (2003) Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian β-1,4-galactosyltransferase and β-1,2-N-acetylglucosaminyltransferase II. Glycobiology, 13, 23-34.
    • (2003) Glycobiology , vol.13 , pp. 23-34
    • Tomiya, N.1    Howe, D.2    Aumiller, J.J.3    Pathak, M.4    Park, J.5    Palter, K.6    Jarvis, D.L.7    Betenbaugh, M.J.8    Lee, Y.C.9
  • 42
    • 0025923253 scopus 로고
    • 4-(N-acetyl-betaglucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1-3 to the asparagine-linked N-acetylglucosamine residue
    • 4-(N-acetyl-betaglucosaminyl)asparagine amidase F cannot release glycans with fucose attached α1-3 to the asparagine-linked N-acetylglucosamine residue. Eur. J. Biochem., 199, 647-652.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 43
    • 0027426870 scopus 로고
    • Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals
    • Tretter, V., Altmann, F., Kubelka, V., Marz, L., and Becker, W.M. (1993) Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int. Arch. Allergy Immunol., 102, 259-266.
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 259-266
    • Tretter, V.1    Altmann, F.2    Kubelka, V.3    Marz, L.4    Becker, W.M.5
  • 44
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 45
    • 0027381117 scopus 로고
    • Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation
    • Voss, T., Ergulen, E., Ahorn, H., Kubelka, V., Sugiyama, K., Maurer-Fogy, I., and Glossl, J. (1993) Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation. Eur. J. Biochem., 217, 913-919.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 913-919
    • Voss, T.1    Ergulen, E.2    Ahorn, H.3    Kubelka, V.4    Sugiyama, K.5    Maurer-Fogy, I.6    Glossl, J.7
  • 46
    • 0029950110 scopus 로고    scopus 로고
    • N-Acetyl-beta-glucosaminidase accounts for differences in glycosylation of influenza virus hemagglutinin expressed in insect cells from a baculovirus vector
    • Wagner, R., Geyer, H., Geyer, R., and Klenk, H.D. (1996) N-Acetyl-beta-glucosaminidase accounts for differences in glycosylation of influenza virus hemagglutinin expressed in insect cells from a baculovirus vector. J. Virol., 70, 4103-4109.
    • (1996) J. Virol. , vol.70 , pp. 4103-4109
    • Wagner, R.1    Geyer, H.2    Geyer, R.3    Klenk, H.D.4
  • 47
    • 0037085295 scopus 로고    scopus 로고
    • Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under β-N-acetylglucosaminidase inhibition
    • Watanabe, S., Kokuho, T., Takahashi, H., Takahashi, M., Kubota, T., and Inumaru, S. (2002) Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under β-N-acetylglucosaminidase inhibition. J. Biol. Chem., 277, 5090-5093.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5090-5093
    • Watanabe, S.1    Kokuho, T.2    Takahashi, H.3    Takahashi, M.4    Kubota, T.5    Inumaru, S.6
  • 48
    • 0023199689 scopus 로고
    • Specific interaction of IgE antibodies with a carbohydrate epitope of honey bee venom phospholipase A2
    • Weber, A., Schroder, H., Thalberg, K., and Marz, L. (1987) Specific interaction of IgE antibodies with a carbohydrate epitope of honey bee venom phospholipase A2. Allergy, 42, 464-470.
    • (1987) Allergy , vol.42 , pp. 464-470
    • Weber, A.1    Schroder, H.2    Thalberg, K.3    Marz, L.4
  • 49
    • 0034958453 scopus 로고    scopus 로고
    • Analysis of Asn-linked glycans from vegetable foodstuffs: Widespread occurrence of Lewis a, core alpha 1,3-linked fucose and xylose substitutions
    • Wilson, I.B., Zeleny, R., Kolarich, D., Staudacher, E., Stroop, C.J., Kamerling, J.P., and Altmann, F. (2001) Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core alpha 1,3-linked fucose and xylose substitutions. Glycobiology, 11, 261-274.
    • (2001) Glycobiology , vol.11 , pp. 261-274
    • Wilson, I.B.1    Zeleny, R.2    Kolarich, D.3    Staudacher, E.4    Stroop, C.J.5    Kamerling, J.P.6    Altmann, F.7
  • 50
    • 0024592956 scopus 로고
    • Structures of the sugar chains of interferon-gamma produced by human myelomonocyte cell line HBL-38
    • Yamamoto, S., Hase, S., Fukuda, S., Sano, O., and Ikenaka, T. (1989) Structures of the sugar chains of interferon-gamma produced by human myelomonocyte cell line HBL-38. J. Biochem. (Tokyo), 105, 547-555.
    • (1989) J. Biochem. (Tokyo) , vol.105 , pp. 547-555
    • Yamamoto, S.1    Hase, S.2    Fukuda, S.3    Sano, O.4    Ikenaka, T.5
  • 52
    • 0026622925 scopus 로고
    • Genetic engineering of a Lymantria dispar nuclear polyhedrosis virus for expression of foreign genes
    • Yu, Z., Podgwaite, J.D., and Wood, H.A. (1992) Genetic engineering of a Lymantria dispar nuclear polyhedrosis virus for expression of foreign genes. J. Gen. Virol., 73(6), 1509-1514.
    • (1992) J. Gen. Virol. , vol.73 , Issue.6 , pp. 1509-1514
    • Yu, Z.1    Podgwaite, J.D.2    Wood, H.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.