메뉴 건너뛰기




Volumn 402, Issue 1, 2007, Pages 105-115

Towards abolition of immunogenic structures in insect cells: Characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core α1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme

Author keywords

Allergy; Anti (horseradish peroxidase); Fucosyltransferase (FucT); Honey bee (Apis mellifera); Lewis X; N glycan

Indexed keywords

ALLERGIES; ANTIGENS; BIOASSAY; BIODIVERSITY; DNA; ENZYMES; GENETIC ENGINEERING;

EID: 33846949412     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060964     Document Type: Article
Times cited : (26)

References (59)
  • 1
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core α1,3-fucosylated glycans and the requisite fucosyltransferase in Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope
    • Fabini, G., Freilinger, A., Altmann, F. and Wilson, I. B. H. (2001) Identification of core α1,3-fucosylated glycans and the requisite fucosyltransferase in Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J. Biol. Chem. 276, 28058-28067
    • (2001) J. Biol. Chem , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.B.H.4
  • 2
    • 0019470313 scopus 로고
    • Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunciamycin
    • Butters, T. D., Hughes, R. C. and Vischer, P. (1981) Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunciamycin. Biochim. Biophys. Acta 640, 672-686
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 672-686
    • Butters, T.D.1    Hughes, R.C.2    Vischer, P.3
  • 3
    • 0026596843 scopus 로고
    • Occurrence of sialic acids in Drosophila melanogaster
    • Roth, J., Kempt, A., Reuter, G., Schauer, R. and Gehring, W. J. (1992) Occurrence of sialic acids in Drosophila melanogaster. Science 256, 673-675
    • (1992) Science , vol.256 , pp. 673-675
    • Roth, J.1    Kempt, A.2    Reuter, G.3    Schauer, R.4    Gehring, W.J.5
  • 4
    • 0033526537 scopus 로고    scopus 로고
    • Constraints on the transport and glycosylation of recombinant IFN-γ in Chinese hamster ovary and insect cells
    • Hooker, A. D., Green, N. H., Baines, A. J., Bull, A. T., Jenkins, N., Strange, P. G. and James, D. C. (1999) Constraints on the transport and glycosylation of recombinant IFN-γ in Chinese hamster ovary and insect cells. Biotechnol. Bioeng. 63, 559-572
    • (1999) Biotechnol. Bioeng , vol.63 , pp. 559-572
    • Hooker, A.D.1    Green, N.H.2    Baines, A.J.3    Bull, A.T.4    Jenkins, N.5    Strange, P.G.6    James, D.C.7
  • 7
    • 0029933189 scopus 로고    scopus 로고
    • Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human β1,2-N-acetylglucosaminyltransferase I
    • Wagner, R., Liedtke, S., Kretzschmar, E., Geyer, H., Geyer, R. and Klenk, H. D. (1996) Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human β1,2-N-acetylglucosaminyltransferase I. Glycobiology 6, 165-175
    • (1996) Glycobiology , vol.6 , pp. 165-175
    • Wagner, R.1    Liedtke, S.2    Kretzschmar, E.3    Geyer, H.4    Geyer, R.5    Klenk, H.D.6
  • 8
    • 0033105027 scopus 로고    scopus 로고
    • Use of mannosamine for inducing the addition of outer arm N-acetylglucosamine onto N-linked oligosaccharides of recombinant proteins in insect cells
    • Donaldson, M., Wood, H. A., Kulakosky, P C. and Shuler, M. L. (1999) Use of mannosamine for inducing the addition of outer arm N-acetylglucosamine onto N-linked oligosaccharides of recombinant proteins in insect cells. Biotechnol. Prog. 15, 168-173
    • (1999) Biotechnol. Prog , vol.15 , pp. 168-173
    • Donaldson, M.1    Wood, H.A.2    Kulakosky, P.C.3    Shuler, M.L.4
  • 9
    • 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
  • 10
    • 33646178162 scopus 로고    scopus 로고
    • The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
    • Léonard, R., Rendić, D., Rabouille, C., Wilson, I. B. H., Préat, T. and Altmann, F. (2006) The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing. J. Biol. Chem. 281, 4867-4875
    • (2006) J. Biol. Chem , vol.281 , pp. 4867-4875
    • Léonard, R.1    Rendić, D.2    Rabouille, C.3    Wilson, I.B.H.4    Préat, T.5    Altmann, F.6
  • 11
    • 0027426870 scopus 로고
    • Fucose α1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honey-bee venom allergic individuals
    • Tretter, V., Altmann, F., Kubelka, V., März, L. and Becker, W. M. (1993) Fucose α1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honey-bee 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    März, L.4    Becker, W.M.5
  • 13
    • 0026691179 scopus 로고
    • 2. The role of α1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • 2. The role of α1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem. J. 284, 377-380
    • (1992) Biochem. J , vol.284 , pp. 377-380
    • Prenner, C.1    Mach, L.2    Glössl, J.3    März, L.4
  • 14
    • 0025797046 scopus 로고
    • The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
    • Kurosaka, A., Yano, A., Itoh, N., Kuroda, Y., Nakagawa, T. and Kawasaki, T. (1991) The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. J. Biol. Chem. 266, 4168-4172
    • (1991) J. Biol. Chem , vol.266 , pp. 4168-4172
    • Kurosaka, A.1    Yano, A.2    Itoh, N.3    Kuroda, Y.4    Nakagawa, T.5    Kawasaki, T.6
  • 15
    • 14844312386 scopus 로고    scopus 로고
    • Sol i 1, the phospholipase allergen of imported fire ant venom
    • Hoffman, D. R., Sakell, R. H. and Schmidt, M. (2005) Sol i 1, the phospholipase allergen of imported fire ant venom. J. Allergy Clin. Immunol. 115, 611-616
    • (2005) J. Allergy Clin. Immunol , vol.115 , pp. 611-616
    • Hoffman, D.R.1    Sakell, R.H.2    Schmidt, M.3
  • 16
    • 0035217040 scopus 로고    scopus 로고
    • Antibody binding to venom carbohydrates is a frequent cause for double positivity to honey-bee and yellow jacket venom in patients with stinging-insect allergy
    • Hemmer, W., Focke, M., Kolarich, D., Wilson, I. B. H., Altmann, F., Wöhrl, S., Götz, M. and Jarisch, R. (2001) Antibody binding to venom carbohydrates is a frequent cause for double positivity to honey-bee and yellow jacket venom in patients with stinging-insect allergy. J. Allergy Clin. Immunol. 108, 1045-1052
    • (2001) J. Allergy Clin. Immunol , vol.108 , pp. 1045-1052
    • Hemmer, W.1    Focke, M.2    Kolarich, D.3    Wilson, I.B.H.4    Altmann, F.5    Wöhrl, S.6    Götz, M.7    Jarisch, R.8
  • 18
    • 0028915061 scopus 로고
    • The asparagine-linked carbohydrate of honey-bee venom hyaluronidase
    • Kubelka, V., Altmann, F. and März, L. (1995) The asparagine-linked carbohydrate of honey-bee venom hyaluronidase. Glycoconjug. J. 12, 77-83
    • (1995) Glycoconjug. J , vol.12 , pp. 77-83
    • Kubelka, V.1    Altmann, F.2    März, L.3
  • 19
    • 0141557676 scopus 로고    scopus 로고
    • Specific antibody responses to three schistosome-related carbohydrate structures in recently exposed immigrants and established residents in an area of Schistosoma mansoni endemicity
    • Naus, C. W. A., van Remoortere, A., Ouma, J. H., Kimani, G., Dunne, D. W., Kamerling, J. P., Deelder, A. M. and Hokke, C. H. (2003) Specific antibody responses to three schistosome-related carbohydrate structures in recently exposed immigrants and established residents in an area of Schistosoma mansoni endemicity. Infect. Immun. 71, 5676-5681
    • (2003) Infect. Immun , vol.71 , pp. 5676-5681
    • Naus, C.W.A.1    van Remoortere, A.2    Ouma, J.H.3    Kimani, G.4    Dunne, D.W.5    Kamerling, J.P.6    Deelder, A.M.7    Hokke, C.H.8
  • 20
    • 0242609139 scopus 로고    scopus 로고
    • Vaccination-induced protection of lambs against the parasitic nematode Haemonchus contortus correlates with high IgG antibody responses to the LDNF glycan antigen
    • Vervelde, L., Bakker, N., Kooyman, F. N. J., Cornelissen, A. W. C. A., Bank, C. M. C., Nyame, A. K., Cummings, R. D. and van Die, I. (2003) Vaccination-induced protection of lambs against the parasitic nematode Haemonchus contortus correlates with high IgG antibody responses to the LDNF glycan antigen. Glycobiology 13, 795-804
    • (2003) Glycobiology , vol.13 , pp. 795-804
    • Vervelde, L.1    Bakker, N.2    Kooyman, F.N.J.3    Cornelissen, A.W.C.A.4    Bank, C.M.C.5    Nyame, A.K.6    Cummings, R.D.7    van Die, I.8
  • 21
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D. J. and Lowe, J. B. (2003) Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 23
    • 3042691090 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis
    • Kannagi, R., Izawa, M., Koike, T., Miyazaki, K. and Kimura, N. (2004) Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis. Cancer Sci. 95, 377-384
    • (2004) Cancer Sci , vol.95 , pp. 377-384
    • Kannagi, R.1    Izawa, M.2    Koike, T.3    Miyazaki, K.4    Kimura, N.5
  • 24
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P. M., Deleury, E., Davies, G. J. and Henrissat, B. (2003) An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328, 307-317
    • (2003) J. Mol. Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 25
    • 0025799819 scopus 로고
    • GDP-fucose: β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc) -Asn-peptide) α1→3-fucosyltransferase activity in honey-bee (Apis mellifera) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine
    • Staudacher, E., Altmann, F., Glössl, J., März, L., Schachter, H., Kamerling, J. P., Hård, K. and Vliegenthart, J. F. G. (1991) GDP-fucose: β-N-acetylglucosamine (Fuc to (Fucα1→6GlcNAc) -Asn-peptide) α1→3-fucosyltransferase activity in honey-bee (Apis mellifera) venom glands. The difucosylation of asparagine-bound N-acetylglucosamine. Eur. J. Biochem. 199, 745-751
    • (1991) Eur. J. Biochem , vol.199 , pp. 745-751
    • Staudacher, E.1    Altmann, F.2    Glössl, J.3    März, L.4    Schachter, H.5    Kamerling, J.P.6    Hård, K.7    Vliegenthart, J.F.G.8
  • 26
    • 0026734854 scopus 로고
    • Distinct N-glycan fucosylation potentials of three lepidopteran cell lines
    • Staudacher, E., Kubelka, V. and März, L. (1992) Distinct N-glycan fucosylation potentials of three lepidopteran cell lines. Eur. J. Biochem. 207, 987-993
    • (1992) Eur. J. Biochem , vol.207 , pp. 987-993
    • Staudacher, E.1    Kubelka, V.2    März, L.3
  • 27
    • 33645641542 scopus 로고    scopus 로고
    • Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells
    • Rendic, D., Linder, A., Paschinger, K., Borth, N., Wilson, I. B. H. and Fabini, G. (2006) Modulation of neural carbohydrate epitope expression in Drosophila melanogaster cells. J. Biol. Chem. 281, 3343-3353
    • (2006) J. Biol. Chem , vol.281 , pp. 3343-3353
    • Rendic, D.1    Linder, A.2    Paschinger, K.3    Borth, N.4    Wilson, I.B.H.5    Fabini, G.6
  • 29
    • 9644270354 scopus 로고    scopus 로고
    • Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans
    • Paschinger, K., Rendić, D., Lochnit, G., Jantsch, V. and Wilson, I. B. H. (2004) Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans. J. Biol. Chem. 279, 49588-49598
    • (2004) J. Biol. Chem , vol.279 , pp. 49588-49598
    • Paschinger, K.1    Rendić, D.2    Lochnit, G.3    Jantsch, V.4    Wilson, I.B.H.5
  • 30
    • 0025971614 scopus 로고
    • Flexibility in the donor substrate specificity of β 1,4-galactosyltransferase: Application in the synthesis of complex carbohydrates
    • Palcic, M. M. and Hindsgaul, O. (1991) Flexibility in the donor substrate specificity of β 1,4-galactosyltransferase: application in the synthesis of complex carbohydrates. Glycobiology 1, 205-209
    • (1991) Glycobiology , vol.1 , pp. 205-209
    • Palcic, M.M.1    Hindsgaul, O.2
  • 31
    • 24044466162 scopus 로고    scopus 로고
    • Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates
    • Paschinger, K., Staudacher, E., Stemmer, U., Fabini, G. and Wilson, I. B. H. (2005) Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates. Glycobiology 15, 463-474
    • (2005) Glycobiology , vol.15 , pp. 463-474
    • Paschinger, K.1    Staudacher, E.2    Stemmer, U.3    Fabini, G.4    Wilson, I.B.H.5
  • 32
    • 0031883033 scopus 로고    scopus 로고
    • HPLC method for the determination of Fuc to Asn-linked GlcNAc fucosyltransferases
    • Roitinger, A., Leiter, H., Staudacher, E. and Altmann, F. (1998) HPLC method for the determination of Fuc to Asn-linked GlcNAc fucosyltransferases. Glycoconjug. J. 15, 89-91
    • (1998) Glycoconjug. J , vol.15 , pp. 89-91
    • Roitinger, A.1    Leiter, H.2    Staudacher, E.3    Altmann, F.4
  • 33
    • 0035744550 scopus 로고    scopus 로고
    • Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase
    • Wilson, I. B. H. (2001) Identification of a cDNA encoding a plant Lewis-type α1,4-fucosyltransferase, Glycoconjug. J. 18, 439-447
    • (2001) Glycoconjug. J , vol.18 , pp. 439-447
    • Wilson, I.B.H.1
  • 35
    • 0031596341 scopus 로고    scopus 로고
    • Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts
    • Wilson, I. B. H., Harthill, J. E., Mullin, N. P., Ashford, D. A. and Altmann, F. (1998) Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts. Glycobiology 8, 651-661
    • (1998) Glycobiology , vol.8 , pp. 651-661
    • Wilson, I.B.H.1    Harthill, J.E.2    Mullin, N.P.3    Ashford, D.A.4    Altmann, F.5
  • 36
    • 13444288238 scopus 로고    scopus 로고
    • Identification of Lewis x structures of the cell adhesion molecule CEACAM1 from human granulocytes
    • Lucka, L., Fernando, M., Grunow, D., Kannicht, C., Horst, A. K., Nollau, P. and Wagener, C. (2005) Identification of Lewis x structures of the cell adhesion molecule CEACAM1 from human granulocytes. Glycobiology 15, 87-100
    • (2005) Glycobiology , vol.15 , pp. 87-100
    • Lucka, L.1    Fernando, M.2    Grunow, D.3    Kannicht, C.4    Horst, A.K.5    Nollau, P.6    Wagener, C.7
  • 38
    • 0031909680 scopus 로고    scopus 로고
    • Conserved structural features in eukaryotic and prokaryotic fucosyltransferases
    • Breton, C., Oriol, R. and Imberty, A. (1998) Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. Glycobiology 8, 87-94
    • (1998) Glycobiology , vol.8 , pp. 87-94
    • Breton, C.1    Oriol, R.2    Imberty, A.3
  • 39
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria
    • Oriol, R., Mollicone, R., Cailleau, A., Balanzino, L. and Breton, C. (1999) Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates, and bacteria. Glycobiology 9, 323-334
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 40
    • 16544370449 scopus 로고    scopus 로고
    • A genetic and structural analysis of the N-glycosylation capabilities of rice and other monocotyledons
    • Léonard, R., Kolarich, D., Paschinger, K., Altmann, F. and Wilson, I. B. H. (2004) A genetic and structural analysis of the N-glycosylation capabilities of rice and other monocotyledons. Plant Mol. Biol. 55, 631-644
    • (2004) Plant Mol. Biol , vol.55 , pp. 631-644
    • Léonard, R.1    Kolarich, D.2    Paschinger, K.3    Altmann, F.4    Wilson, I.B.H.5
  • 41
    • 0033618435 scopus 로고    scopus 로고
    • Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn- linked GlcNAc α1,3-fucosyltransferase from mung beans
    • Leiter, H., Mucha, J., Staudacher, E., Grimm, R., Glössl, J. and Altmann, F. (1999) Purification, cDNA cloning, and expression of GDP-L-Fuc:Asn- linked GlcNAc α1,3-fucosyltransferase from mung beans. J. Biol. Chem. 274, 21830-21839
    • (1999) J. Biol. Chem , vol.274 , pp. 21830-21839
    • Leiter, H.1    Mucha, J.2    Staudacher, E.3    Grimm, R.4    Glössl, J.5    Altmann, F.6
  • 43
    • 0020121682 scopus 로고
    • Antibodies to horseradish peroxidase as specific neuronal markers in Drosophila and in grasshopper embryos
    • Jan, L. Y. and Jan, Y. N. (1982) Antibodies to horseradish peroxidase as specific neuronal markers in Drosophila and in grasshopper embryos. Proc. Natl. Acad. Sci. U.S.A. 79, 2700-2704
    • (1982) Proc. Natl. Acad. Sci. U.S.A , vol.79 , pp. 2700-2704
    • Jan, L.Y.1    Jan, Y.N.2
  • 44
    • 0001378198 scopus 로고
    • Patterns of larval food production by hypopharyngeal glands in adult worker honey bees
    • Knecht, D. and Kaatz, H. H. (1990) Patterns of larval food production by hypopharyngeal glands in adult worker honey bees. Apidologie 21, 457-468
    • (1990) Apidologie , vol.21 , pp. 457-468
    • Knecht, D.1    Kaatz, H.H.2
  • 45
    • 0030695026 scopus 로고    scopus 로고
    • Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honey-bee Apis mellifera L
    • Ohashi, K., Natori, S. and Kubo, T. (1997) Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honey-bee Apis mellifera L. Eur. J. Biochem. 249, 797-802
    • (1997) Eur. J. Biochem , vol.249 , pp. 797-802
    • Ohashi, K.1    Natori, S.2    Kubo, T.3
  • 47
    • 0030029692 scopus 로고    scopus 로고
    • Change in the expression of hypopharyngeal-gland proteins of the worker honey-bees (Apis mellifera L.) with age and/or role
    • Kubo, T., Sasaki, M., Nakamura, J., Sasagawa, H., Ohashi, K., Takeuchi, H. and Natori, S. (1996) Change in the expression of hypopharyngeal-gland proteins of the worker honey-bees (Apis mellifera L.) with age and/or role. J. Biochem. (Tokyo) 119, 291-295
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 291-295
    • Kubo, T.1    Sasaki, M.2    Nakamura, J.3    Sasagawa, H.4    Ohashi, K.5    Takeuchi, H.6    Natori, S.7
  • 48
    • 0005134824 scopus 로고    scopus 로고
    • Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honey-bee (Apis mellifera L.)
    • Ohashi, K., Natori, S. and Kubo, T. (1999) Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honey-bee (Apis mellifera L.). Eur. J. Biochem. 265, 127-133
    • (1999) Eur. J. Biochem , vol.265 , pp. 127-133
    • Ohashi, K.1    Natori, S.2    Kubo, T.3
  • 49
    • 84945629485 scopus 로고
    • Invertase in the hypopharyngeal glands of the honey-bee
    • Simpson, J., Riedel, I. B. M. and Wilding, M. (1968) Invertase in the hypopharyngeal glands of the honey-bee. J. Apic. Res. 7, 127-133
    • (1968) J. Apic. Res , vol.7 , pp. 127-133
    • Simpson, J.1    Riedel, I.B.M.2    Wilding, M.3
  • 50
    • 0034296913 scopus 로고    scopus 로고
    • Structural features of N-glycans linked to royal jelly glycoproteins: Structures of high-mannose type, hybrid type, and biantennary type glycans
    • Kimura, Y., Miyagi, C., Kimura, M., Nitoda, T., Kawai, N. and Sugimoto, H. (2000) Structural features of N-glycans linked to royal jelly glycoproteins: structures of high-mannose type, hybrid type, and biantennary type glycans. Biosci. Biotechnol. Biochem. 64, 2109-2120
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , pp. 2109-2120
    • Kimura, Y.1    Miyagi, C.2    Kimura, M.3    Nitoda, T.4    Kawai, N.5    Sugimoto, H.6
  • 51
    • 0023475207 scopus 로고
    • Neural-specific carbohydrate moiety shared by many surface glycoproteins in Drosophila and grasshopper embryos
    • Snow, P. M., Patel, N. H., Harrelson, A. L. and Goodman, C. S. (1987) Neural-specific carbohydrate moiety shared by many surface glycoproteins in Drosophila and grasshopper embryos. J. Neurosci. 7, 4137-4144
    • (1987) J. Neurosci , vol.7 , pp. 4137-4144
    • Snow, P.M.1    Patel, N.H.2    Harrelson, A.L.3    Goodman, C.S.4
  • 52
    • 0037383779 scopus 로고    scopus 로고
    • Induction of neuron-specific glycosylation by Tollo/Toll-8, a Drosophila Toll-like receptor expressed in non-neural cells
    • Seppo, A., Matani, P., Sharrow, M. and Tiemeyer, M. (2003) Induction of neuron-specific glycosylation by Tollo/Toll-8, a Drosophila Toll-like receptor expressed in non-neural cells. Development 130, 1439-1448
    • (2003) Development , vol.130 , pp. 1439-1448
    • Seppo, A.1    Matani, P.2    Sharrow, M.3    Tiemeyer, M.4
  • 53
    • 17644415389 scopus 로고    scopus 로고
    • Age-dependent morphology and ultrastructure of the hypopharyngeal gland of Apis mellifera workers (Hymenoptera, Apidae)
    • Deseyn, J. and Billen, J. (2005) Age-dependent morphology and ultrastructure of the hypopharyngeal gland of Apis mellifera workers (Hymenoptera, Apidae). Apidologie 36, 49-57
    • (2005) Apidologie , vol.36 , pp. 49-57
    • Deseyn, J.1    Billen, J.2
  • 54
    • 4043068563 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a Lepidopteran insect β4-N- acetylgalactosaminyltransferase with broad substrate specificity, a functional role in glycoprotein biosynthesis, and a potential functional role in glycolipid biosynthesis
    • Vadaie, N. and Jarvis, D. L. (2004) Molecular cloning and functional characterization of a Lepidopteran insect β4-N- acetylgalactosaminyltransferase with broad substrate specificity, a functional role in glycoprotein biosynthesis, and a potential functional role in glycolipid biosynthesis. J. Biol. Chem. 279, 33501-33508
    • (2004) J. Biol. Chem , vol.279 , pp. 33501-33508
    • Vadaie, N.1    Jarvis, D.L.2
  • 55
    • 22444448589 scopus 로고    scopus 로고
    • Functional analysis of Drosophila β1,4-N-acetlygalactosaminyltransferases
    • Haines, N. and Irvine, K. D. (2005) Functional analysis of Drosophila β1,4-N-acetlygalactosaminyltransferases. Glycobiology 15, 335-346
    • (2005) Glycobiology , vol.15 , pp. 335-346
    • Haines, N.1    Irvine, K.D.2
  • 56
    • 0036707819 scopus 로고    scopus 로고
    • Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression studies in the mouse
    • Baboval, T. and Smith, F. I. (2002) Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression studies in the mouse. Mamm. Genome 13, 538-541
    • (2002) Mamm. Genome , vol.13 , pp. 538-541
    • Baboval, T.1    Smith, F.I.2
  • 58
    • 0028236119 scopus 로고
    • Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
    • Kubelka, V., Altmann, F., Kornfeld, G. and März, L. (1994) Structures 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    Altmann, F.2    Kornfeld, G.3    März, L.4
  • 59
    • 33748433786 scopus 로고    scopus 로고
    • Isolation and analysis of a baculovirus vector that supports recombinant glycoprotein sialylation by SfSWT-1 cells cultured in serum-free medium
    • Hill, D. R., Aumiller, J. J., Shi, X. and Jarvis, D. L. (2006) Isolation and analysis of a baculovirus vector that supports recombinant glycoprotein sialylation by SfSWT-1 cells cultured in serum-free medium. Biotechnol. Bioeng. 95, 37-47
    • (2006) Biotechnol. Bioeng , vol.95 , pp. 37-47
    • Hill, D.R.1    Aumiller, J.J.2    Shi, X.3    Jarvis, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.