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Volumn 23, Issue 7, 2013, Pages 778-796

Mucin-type proteins produced in the Trichoplusia ni and Spodoptera frugiperda insect cell lines carry novel O-glycans with phosphocholine and sulfate substitutions

Author keywords

insect cells; mass spectrometry; O glycosylation; phosphocholine; sulfate

Indexed keywords

GALACTURONIC ACID; GLUCURONIC ACID; GLYCAN DERIVATIVE; HEXOSE; HEXURONIC ACID; HYBRID PROTEIN; MUCIN TYPE PROTEIN; N ACETYLGALACTOSAMINE; OLIGOSACCHARIDE; P SELECTIN GLYCOPROTEIN LIGAND 1; PHOSPHORYLCHOLINE; PROTEIN; SULFATE; UNCLASSIFIED DRUG;

EID: 84882778713     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt015     Document Type: Article
Times cited : (20)

References (86)
  • 1
    • 0015855908 scopus 로고
    • The purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein
    • Allen AK, Neuberger A. 1973. The purification and properties of the lectin from potato tubers, a hydroxyproline-containing glycoprotein. Biochem J. 135:307-314.
    • (1973) Biochem J. , vol.135 , pp. 307-314
    • Allen, A.K.1    Neuberger, A.2
  • 2
    • 33846187538 scopus 로고    scopus 로고
    • The role of protein glycosylation in allergy
    • Altmann F. 2007. The role of protein glycosylation in allergy. Int Arch Allergy Immunol. 142:99-115.
    • (2007) Int Arch Allergy Immunol. , vol.142 , pp. 99-115
    • Altmann, F.1
  • 3
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann F, Staudacher E, Wilson IB, 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
  • 4
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki K, Perlman M, Lim JM, Cantu R, Wells L, Tiemeyer M. 2007. Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo. J Biol Chem. 282:9127-9142.
    • (2007) J Biol Chem. , vol.282 , pp. 9127-9142
    • Aoki, K.1    Perlman, M.2    Lim, J.M.3    Cantu, R.4    Wells, L.5    Tiemeyer, M.6
  • 5
    • 57149096197 scopus 로고    scopus 로고
    • The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling
    • Aoki K, Porterfield M, Lee SS, Dong B, Nguyen K, McGlamry KH, Tiemeyer M. 2008. The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling. J Biol Chem. 283:30385-30400.
    • (2008) J Biol Chem. , vol.283 , pp. 30385-30400
    • Aoki, K.1    Porterfield, M.2    Lee, S.S.3    Dong, B.4    Nguyen, K.5    McGlamry, K.H.6    Tiemeyer, M.7
  • 6
    • 77956162735 scopus 로고    scopus 로고
    • The glycomics of glycan glucuronylation in Drosophila melanogaster
    • Aoki K, Tiemeyer M. 2010. The glycomics of glycan glucuronylation in Drosophila melanogaster. Methods Enzymol. 480:297-321.
    • (2010) Methods Enzymol. , vol.480 , pp. 297-321
    • Aoki, K.1    Tiemeyer, M.2
  • 7
    • 0038243176 scopus 로고    scopus 로고
    • A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins
    • Aumiller JJ, Hollister JR, Jarvis DL. 2003. A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins. Glycobiology. 13:497-507.
    • (2003) Glycobiology. , vol.13 , pp. 497-507
    • Aumiller, J.J.1    Hollister, J.R.2    Jarvis, D.L.3
  • 8
    • 42749085119 scopus 로고    scopus 로고
    • Glucuronic acid can extend O-linked core 1 glycans, but it contributes only weakly to the negative surface charge of Drosophila melanogaster Schneider-2 cells
    • Breloy I, Schwientek T, Lehr S, Hanisch FG. 2008. Glucuronic acid can extend O-linked core 1 glycans, but it contributes only weakly to the negative surface charge of Drosophila melanogaster Schneider-2 cells. FEBS Lett. 582:1593-1598.
    • (2008) FEBS Lett. , vol.582 , pp. 1593-1598
    • Breloy, I.1    Schwientek, T.2    Lehr, S.3    Hanisch, F.G.4
  • 10
    • 0027194326 scopus 로고
    • Characterization of two different glycosylated domains from the insoluble mucin complex of rat small intestine
    • Carlstedt I, Herrmann A, Karlsson H, Sheehan J, Fransson LA, Hansson GC. 1993. Characterization of two different glycosylated domains from the insoluble mucin complex of rat small intestine. J Biol Chem. 268:18771-18781.
    • (1993) J Biol Chem. , vol.268 , pp. 18771-18781
    • Carlstedt, I.1    Herrmann, A.2    Karlsson, H.3    Sheehan, J.4    Fransson, L.A.5    Hansson, G.C.6
  • 11
    • 34848927484 scopus 로고    scopus 로고
    • The GlycanBuilder: A fast, intuitive and flexible software tool for building and displaying glycan structures
    • Ceroni A, Dell A, Haslam SM. 2007. The GlycanBuilder: A fast, intuitive and flexible software tool for building and displaying glycan structures. Source Code Biol Med. 2:3.
    • (2007) Source Code Biol Med. , vol.2 , pp. 3
    • Ceroni, A.1    Dell, A.2    Haslam, S.M.3
  • 12
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni A, Maass K, Geyer H, Geyer R, Dell A, Haslam SM. 2008. GlycoWorkbench: A tool for the computer-assisted annotation of mass spectra of glycans. J Proteome Res. 7:1650-1659.
    • (2008) J Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 13
    • 22544463401 scopus 로고    scopus 로고
    • N-Glycans of Caenorhabditis elegans are specific to developmental stages
    • Cipollo JF, Awad AM, Costello CE, Hirschberg CB. 2005. N-Glycans of Caenorhabditis elegans are specific to developmental stages. J Biol Chem. 280:26063-26072.
    • (2005) J Biol Chem. , vol.280 , pp. 26063-26072
    • Cipollo, J.F.1    Awad, A.M.2    Costello, C.E.3    Hirschberg, C.B.4
  • 14
    • 0348209615 scopus 로고    scopus 로고
    • The fine structure of Caenorhabditis elegans N-glycans
    • Cipollo JF, Costello CE, Hirschberg CB. 2002. The fine structure of Caenorhabditis elegans N-glycans. J Biol Chem. 277:49143-49157.
    • (2002) J Biol Chem. , vol.277 , pp. 49143-49157
    • Cipollo, J.F.1    Costello, C.E.2    Hirschberg, C.B.3
  • 15
    • 84857455818 scopus 로고    scopus 로고
    • Recombinant protein vaccines produced in insect cells
    • Cox MM. 2012. Recombinant protein vaccines produced in insect cells. Vaccine. 30:1759-1766.
    • (2012) Vaccine. , vol.30 , pp. 1759-1766
    • Cox, M.M.1
  • 16
    • 0035876914 scopus 로고    scopus 로고
    • A filarial nematode-secreted phosphorylcholine-containing glycoprotein uncouples the B cell antigen receptor from extracellular signal-regulated kinase-mitogen-activated protein kinase by promoting the surface Ig-mediated recruitment of Src homology 2 domain-containing tyrosine phosphatase-1 and Pac-1 mitogen-activated kinase-phosphatase
    • Deehan MR, Harnett W, Harnett MM. 2001. A filarial nematode-secreted phosphorylcholine-containing glycoprotein uncouples the B cell antigen receptor from extracellular signal-regulated kinase-mitogen-activated protein kinase by promoting the surface Ig-mediated recruitment of Src homology 2 domain-containing tyrosine phosphatase-1 and Pac-1 mitogen-activated kinase-phosphatase. J Immunol. 166:7462-7468.
    • (2001) J Immunol. , vol.166 , pp. 7462-7468
    • Deehan, M.R.1    Harnett, W.2    Harnett, M.M.3
  • 17
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon B, Costello CE. 1988. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj J. 5:397-400.
    • (1988) Glycoconj J. , vol.5 , pp. 397-400
    • Domon, B.1    Costello, C.E.2
  • 18
    • 70449710875 scopus 로고    scopus 로고
    • Expression systems for therapeutic glycoprotein production
    • Durocher Y, Butler M. 2009. Expression systems for therapeutic glycoprotein production. Curr Opin Biotechnol. 20:700-707.
    • (2009) Curr Opin Biotechnol. , vol.20 , pp. 700-707
    • Durocher, Y.1    Butler, M.2
  • 19
    • 79955928801 scopus 로고    scopus 로고
    • Structural characterization of complex O-linked glycans from insect-derived material
    • Garenaux E, Maes E, Leveque S, Brassart C, Guerardel Y. 2011. Structural characterization of complex O-linked glycans from insect-derived material. Carbohydr Res. 346:1093-1104.
    • (2011) Carbohydr Res. , vol.346 , pp. 1093-1104
    • Garenaux, E.1    Maes, E.2    Leveque, S.3    Brassart, C.4    Guerardel, Y.5
  • 20
    • 84860912187 scopus 로고    scopus 로고
    • Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation
    • Ghaderi D, Zhang M, Hurtado-Ziola N, Varki A. 2012. Production platforms for biotherapeutic glycoproteins. Occurrence, impact, and challenges of non-human sialylation. Biotechnol Genet Eng Rev. 28:147-175.
    • (2012) Biotechnol Genet Eng Rev. , vol.28 , pp. 147-175
    • Ghaderi, D.1    Zhang, M.2    Hurtado-Ziola, N.3    Varki, A.4
  • 21
    • 0026847353 scopus 로고
    • Large-scale insect cell culture
    • Goosen MF. 1992. Large-scale insect cell culture. Curr Opin Biotechnol. 3:99-104.
    • (1992) Curr Opin Biotechnol. , vol.3 , pp. 99-104
    • Goosen, M.F.1
  • 22
    • 37049229755 scopus 로고
    • Induction of polyhedral bodies in ovarian tissues of the tussock moth in vitro
    • Grace TD. 1958. Induction of polyhedral bodies in ovarian tissues of the tussock moth in vitro. Science. 128:249-250.
    • (1958) Science. , vol.128 , pp. 249-250
    • Grace, T.D.1
  • 23
    • 0035396643 scopus 로고    scopus 로고
    • The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: Identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides
    • Guerardel Y, Balanzino L, Maes E, Leroy Y, Coddeville B, Oriol R, Strecker G. 2001. The nematode Caenorhabditis elegans synthesizes unusual O-linked glycans: Identification of glucose-substituted mucin-type O-glycans and short chondroitin-like oligosaccharides. Biochem J. 357:167-182.
    • (2001) Biochem J. , vol.357 , pp. 167-182
    • Guerardel, Y.1    Balanzino, L.2    Maes, E.3    Leroy, Y.4    Coddeville, B.5    Oriol, R.6    Strecker, G.7
  • 25
    • 36148929103 scopus 로고    scopus 로고
    • A new generation of carbohydratebased therapeutics: Recombinant mucin-type fusion proteins as versatile inhibitors of protein-carbohydrate interactions
    • Gustafsson A, Holgersson J. 2006. A new generation of carbohydratebased therapeutics: Recombinant mucin-type fusion proteins as versatile inhibitors of protein-carbohydrate interactions. Expert Opin Drug Discovery. 1:161-178.
    • (2006) Expert Opin Drug Discovery. , vol.1 , pp. 161-178
    • Gustafsson, A.1    Holgersson, J.2
  • 27
    • 0027346497 scopus 로고
    • Gas chromatography and gas chromatographymass spectrometry of glycoprotein oligosaccharides
    • Hansson GC, Karlsson H. 1993. Gas chromatography and gas chromatographymass spectrometry of glycoprotein oligosaccharides. Methods Mol Biol. 14:47-54.
    • (1993) Methods Mol Biol. , vol.14 , pp. 47-54
    • Hansson, G.C.1    Karlsson, H.2
  • 28
    • 0027405920 scopus 로고
    • Structure of the asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein
    • Hard K, Van Doorn JM, Thomas-Oates JE, Kamerling JP, Van der Horst DJ. 1993. Structure of the asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein. Biochemistry. 32:766-775.
    • (1993) Biochemistry. , vol.32 , pp. 766-775
    • Hard, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van Der Horst, D.J.5
  • 29
    • 45749093792 scopus 로고    scopus 로고
    • Therapeutic immunomodulators from nematode parasites
    • Harnett W, Harnett MM. 2008. Therapeutic immunomodulators from nematode parasites. Expert Rev Mol Med. 10:e18.
    • (2008) Expert Rev Mol Med. , vol.10
    • Harnett, W.1    Harnett, M.M.2
  • 30
    • 0037302799 scopus 로고    scopus 로고
    • Structural/functional aspects of ES-62-A secreted immunomodulatory phosphorylcholine-containing filarial nematode glycoprotein
    • Harnett W, Harnett MM, Byron O. 2003. Structural/functional aspects of ES-62-a secreted immunomodulatory phosphorylcholine-containing filarial nematode glycoprotein. Curr Protein Pept Sci. 4:59-71.
    • (2003) Curr Protein Pept Sci. , vol.4 , pp. 59-71
    • Harnett, W.1    Harnett, M.M.2    Byron, O.3
  • 32
    • 74549165574 scopus 로고    scopus 로고
    • The therapeutic potential of the filarial nematode-derived immunomodulator, ES-62 in inflammatory disease
    • Harnett MM, Melendez AJ, Harnett W. 2010. The therapeutic potential of the filarial nematode-derived immunomodulator, ES-62 in inflammatory disease. Clin Exp Immunol. 159:256-267.
    • (2010) Clin Exp Immunol. , vol.159 , pp. 256-267
    • Harnett, M.M.1    Melendez, A.J.2    Harnett, W.3
  • 34
    • 77956532465 scopus 로고    scopus 로고
    • Re-visiting the endogenous capacity for recombinant glycoprotein sialylation by baculovirus-infected Tn-4h and DpN1 cells
    • Hillar A, Jarvis DL. 2010. Re-visiting the endogenous capacity for recombinant glycoprotein sialylation by baculovirus-infected Tn-4h and DpN1 cells. Glycobiology. 20:1323-1330.
    • (2010) Glycobiology. , vol.20 , pp. 1323-1330
    • Hillar, A.1    Jarvis, D.L.2
  • 36
    • 0027346988 scopus 로고
    • Foreign gene expression in insect cells
    • Jarvis DL. 1993. Foreign gene expression in insect cells. Bioprocess Technol. 17:195-219.
    • (1993) Bioprocess Technol. , vol.17 , pp. 195-219
    • Jarvis, D.L.1
  • 37
    • 0038544334 scopus 로고    scopus 로고
    • Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
    • Jarvis DL. 2003. Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production. Virology. 310:1-7.
    • (2003) Virology. , vol.310 , pp. 1-7
    • Jarvis, D.L.1
  • 38
    • 0032190659 scopus 로고    scopus 로고
    • Engineering N-glycosylation pathways in the baculovirus-insect cell system
    • Jarvis DL, Kawar ZS, Hollister JR. 1998. Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr Opin Biotechnol. 9:528-533.
    • (1998) Curr Opin Biotechnol. , vol.9 , pp. 528-533
    • Jarvis, D.L.1    Kawar, Z.S.2    Hollister, J.R.3
  • 39
    • 0038458983 scopus 로고    scopus 로고
    • Effect of culture conditions on the degree of sialylation of a recombinant glycoprotein expressed in insect cells
    • Joosten CE, Shuler ML. 2003. Effect of culture conditions on the degree of sialylation of a recombinant glycoprotein expressed in insect cells. Biotechnol Prog. 19:739-749.
    • (2003) Biotechnol Prog. , vol.19 , pp. 739-749
    • Joosten, C.E.1    Shuler, M.L.2
  • 40
    • 2342527904 scopus 로고    scopus 로고
    • Structural determination of neutral O-linked oligosaccharide alditols by negative ion LC-electrospray-MSn
    • Karlsson NG, Schulz BL, Packer NH. 2004. Structural determination of neutral O-linked oligosaccharide alditols by negative ion LC-electrospray-MSn. J Am Soc Mass Spectrom. 15:659-672.
    • (2004) J Am Soc Mass Spectrom. , vol.15 , pp. 659-672
    • Karlsson, N.G.1    Schulz, B.L.2    Packer, N.H.3
  • 41
    • 0025111573 scopus 로고
    • Carbohydrate binding specificities of several poly-N-acetyllactosamine- binding lectins
    • Kawashima H, Sueyoshi S, Li H, Yamamoto K, Osawa T. 1990. Carbohydrate binding specificities of several poly-N-acetyllactosamine-binding lectins. Glycoconj J. 7:323-334.
    • (1990) Glycoconj J. , vol.7 , pp. 323-334
    • Kawashima, H.1    Sueyoshi, S.2    Li, H.3    Yamamoto, K.4    Osawa, T.5
  • 42
    • 80052566105 scopus 로고    scopus 로고
    • Sulfate migration in oligosaccharides induced by negative ion mode ion trap CID
    • Kenny DT, Issa SMA, Karlsson NG. 2012. Sulfate migration in oligosaccharides induced by negative ion mode ion trap CID. Rapid Commun Mass Spectrom. 25:2611-2618.
    • (2012) Rapid Commun Mass Spectrom. , vol.25 , pp. 2611-2618
    • Kenny, D.T.1    Issa, S.M.A.2    Karlsson, N.G.3
  • 43
    • 84863190461 scopus 로고    scopus 로고
    • Presence of terminal N-acetylgalactosamine beta1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: Involvement in Helicobacter pylori colonization
    • Kenny DT, Skoog EC, Linden SK, Struwe WB, Rudd PM, Karlsson NG. 2012. Presence of terminal N-acetylgalactosamine beta1-4N-acetylglucosamine residues on O-linked oligosaccharides from gastric MUC5AC: Involvement in Helicobacter pylori colonization? Glycobiology. 22:1077-1085.
    • (2012) Glycobiology. , vol.22 , pp. 1077-1085
    • Kenny, D.T.1    Skoog, E.C.2    Linden, S.K.3    Struwe, W.B.4    Rudd, P.M.5    Karlsson, N.G.6
  • 44
    • 62449088479 scopus 로고    scopus 로고
    • Sialylation in protostomes: A perspective from Drosophila genetics and biochemistry
    • Koles K, Repnikova E, Pavlova G, Korochkin LI, Panin VM. 2009. Sialylation in protostomes: A perspective from Drosophila genetics and biochemistry. Glycoconj J. 26:313-324.
    • (2009) Glycoconj J. , vol.26 , pp. 313-324
    • Koles, K.1    Repnikova, E.2    Pavlova, G.3    Korochkin, L.I.4    Panin, V.M.5
  • 45
    • 57849159697 scopus 로고    scopus 로고
    • Identification of a thrombospondin-like immunodominant and phosphorylcholinecontaining glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes
    • Kooyman FN, van Balkom BW, de Vries E, van Putten JP. 2009. Identification of a thrombospondin-like immunodominant and phosphorylcholinecontaining glycoprotein (GP300) in Dictyocaulus viviparus and related nematodes. Mol Biochem Parasitol. 163:85-94.
    • (2009) Mol Biochem Parasitol. , vol.163 , pp. 85-94
    • Kooyman, F.N.1    Van Balkom, B.W.2    De Vries, E.3    Van Putten, J.P.4
  • 48
    • 0031036860 scopus 로고    scopus 로고
    • The role of selectins in Drosophila eye and bristle development
    • Leshko-Lindsay LA, Corces VG. 1997. The role of selectins in Drosophila eye and bristle development. Development. 124:169-180.
    • (1997) Development. , vol.124 , pp. 169-180
    • Leshko-Lindsay, L.A.1    Corces, V.G.2
  • 49
    • 70449732650 scopus 로고    scopus 로고
    • Pharmacological significance of glycosylation in therapeutic proteins
    • Li H, d'Anjou M. 2009. Pharmacological significance of glycosylation in therapeutic proteins. Curr Opin Biotechnol. 20:678-684.
    • (2009) Curr Opin Biotechnol. , vol.20 , pp. 678-684
    • Li, H.1    D'anjou, M.2
  • 50
    • 24044514683 scopus 로고    scopus 로고
    • Anti-pig antibody adsorption efficacy of α-Gal carrying recombinant P-selectin glycoprotein ligand-1/immunoglobulin chimeras increases with core 2 β1, 6-N-acetylglucosaminyltransferase expression
    • Liu J, Gustafsson A, Breimer ME, Kussak A, Holgersson J. 2005. Anti-pig antibody adsorption efficacy of α-Gal carrying recombinant P-selectin glycoprotein ligand-1/immunoglobulin chimeras increases with core 2 β1, 6-N-acetylglucosaminyltransferase expression. Glycobiology. 15:571-583.
    • (2005) Glycobiology. , vol.15 , pp. 571-583
    • Liu, J.1    Gustafsson, A.2    Breimer, M.E.3    Kussak, A.4    Holgersson, J.5
  • 51
    • 0033783188 scopus 로고    scopus 로고
    • Phosphorylcholine substituents in nematodes: Structures, occurrence and biological implications
    • Lochnit G, Dennis RD, Geyer R. 2000. Phosphorylcholine substituents in nematodes: Structures, occurrence and biological implications. Biol Chem. 381:839-847.
    • (2000) Biol Chem. , vol.381 , pp. 839-847
    • Lochnit, G.1    Dennis, R.D.2    Geyer, R.3
  • 53
    • 0141756182 scopus 로고    scopus 로고
    • Glycan-dependent leukocyte adhesion and recruitment in inflammation
    • Lowe JB. 2003. Glycan-dependent leukocyte adhesion and recruitment in inflammation. Curr Opin Cell Biol. 15:531-538.
    • (2003) Curr Opin Cell Biol. , vol.15 , pp. 531-538
    • Lowe, J.B.1
  • 54
    • 0030273241 scopus 로고    scopus 로고
    • Do excretory-secretory products of Onchocerca gibsoni contain phosphorylcholine attached to O-type glycans
    • MacDonald M, Copeman DB, Harnett W. 1996. Do excretory-secretory products of Onchocerca gibsoni contain phosphorylcholine attached to O-type glycans? Int J Parasitol. 26:1075-1080.
    • (1996) Int J Parasitol. , vol.26 , pp. 1075-1080
    • Macdonald, M.1    Copeman, D.B.2    Harnett, W.3
  • 56
    • 0035086298 scopus 로고    scopus 로고
    • Glycoproteins from insect cells: Sialylated or not
    • Marchal I, Jarvis DL, Cacan R, Verbert A. 2001. Glycoproteins from insect cells: Sialylated or not? Biol Chem. 382:151-159.
    • (2001) Biol Chem. , vol.382 , pp. 151-159
    • Marchal, I.1    Jarvis, D.L.2    Cacan, R.3    Verbert, A.4
  • 58
    • 0028273059 scopus 로고
    • Biochemical characterization of the O-glycans on recombinant glycophorin A expressed in Chinese hamster ovary cells
    • Pahlsson P, Blackall DP, Ugorski M, Czerwinski M, Spitalnik SL. 1994. Biochemical characterization of the O-glycans on recombinant glycophorin A expressed in Chinese hamster ovary cells. Glycoconj J. 11:43-50.
    • (1994) Glycoconj J. , vol.11 , pp. 43-50
    • Pahlsson, P.1    Blackall, D.P.2    Ugorski, M.3    Czerwinski, M.4    Spitalnik, S.L.5
  • 60
    • 0347297507 scopus 로고    scopus 로고
    • Novel insect cell line capable of complex N-glycosylation and sialylation of recombinant proteins
    • Palomares LA, Joosten CE, Hughes PR, Granados RR, Shuler ML. 2003. Novel insect cell line capable of complex N-glycosylation and sialylation of recombinant proteins. Biotechnol Prog. 19:185-192.
    • (2003) Biotechnol Prog. , vol.19 , pp. 185-192
    • Palomares, L.A.1    Joosten, C.E.2    Hughes, P.R.3    Granados, R.R.4    Shuler, M.L.5
  • 61
    • 0033366602 scopus 로고    scopus 로고
    • Monosaccharide compositions of Danaus plexippus (monarch butterfly) and Trichoplusia ni (cabbage looper) egg glycoproteins
    • Park YI, Wood HA, Lee YC. 1999. Monosaccharide compositions of Danaus plexippus (monarch butterfly) and Trichoplusia ni (cabbage looper) egg glycoproteins. Glycoconj J. 16:629-638.
    • (1999) Glycoconj J. , vol.16 , pp. 629-638
    • Park, Y.I.1    Wood, H.A.2    Lee, Y.C.3
  • 62
    • 84858289905 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the immunodominant glycan epitope of Echinococcus granulosus antigen Ag5
    • Paschinger K, Gonzalez-Sapienza GG, Wilson IB. 2012. Mass spectrometric analysis of the immunodominant glycan epitope of Echinococcus granulosus antigen Ag5. Int J Parasitol. 42:279-285.
    • (2012) Int J Parasitol. , vol.42 , pp. 279-285
    • Paschinger, K.1    Gonzalez-Sapienza, G.G.2    Wilson, I.B.3
  • 65
    • 0025367755 scopus 로고
    • Comparison of the carbohydrate-binding specificities of seven N-acetyl-D-galactosamine-recognizing lectins
    • Piller V, Piller F, Cartron JP. 1990. Comparison of the carbohydrate-binding specificities of seven N-acetyl-D-galactosamine-recognizing lectins. Eur J Biochem. 191:461-466.
    • (1990) Eur J Biochem. , vol.191 , pp. 461-466
    • Piller, V.1    Piller, F.2    Cartron, J.P.3
  • 66
    • 33846457358 scopus 로고    scopus 로고
    • N-Glycans of the porcine nematode parasite Ascaris suum are modified with phosphorylcholine and core fucose residues
    • Poltl G, Kerner D, Paschinger K, Wilson IB. 2007. N-Glycans of the porcine nematode parasite Ascaris suum are modified with phosphorylcholine and core fucose residues. FEBS J. 274:714-726.
    • (2007) FEBS J. , vol.274 , pp. 714-726
    • Poltl, G.1    Kerner, D.2    Paschinger, K.3    Wilson, I.B.4
  • 67
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Ricardo J, Solá KG. 2008. Effects of glycosylation on the stability of protein pharmaceuticals. J Pharm Sci. 98:1223-1245.
    • (2008) J Pharm Sci. , vol.98 , pp. 1223-1245
    • Ricardo, J.1    Solá, K.G.2
  • 68
    • 0036894272 scopus 로고    scopus 로고
    • Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis
    • Schulz BL, Packer NH, Karlsson NG. 2002. Small-scale analysis of O-linked oligosaccharides from glycoproteins and mucins separated by gel electrophoresis. Anal Chem. 74:6088-6097.
    • (2002) Anal Chem. , vol.74 , pp. 6088-6097
    • Schulz, B.L.1    Packer, N.H.2    Karlsson, N.G.3
  • 69
    • 0033887691 scopus 로고    scopus 로고
    • Function and structure of Drosophila glycans
    • Seppo A, Tiemeyer M. 2000. Function and structure of Drosophila glycans. Glycobiology. 10:751-760.
    • (2000) Glycobiology. , vol.10 , pp. 751-760
    • Seppo, A.1    Tiemeyer, M.2
  • 70
    • 0026734854 scopus 로고
    • Distinct N-glycan fucosylation potentials of three lepidopteran cell lines
    • Staudacher E, Kubelka V, Marz 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    Marz, L.3
  • 71
    • 0023747362 scopus 로고
    • Elderberry bark lectin-gold techniques for the detection of Neu5Ac (alpha 2,6) Gal/ GalNAc sequences: Applications and limitations
    • Taatjes DJ, Roth J, Peumans W, Goldstein IJ. 1988. Elderberry bark lectin-gold techniques for the detection of Neu5Ac (alpha 2,6) Gal/ GalNAc sequences: Applications and limitations. Histochem J. 20:478-490.
    • (1988) Histochem J. , vol.20 , pp. 478-490
    • Taatjes, D.J.1    Roth, J.2    Peumans, W.3    Goldstein, I.J.4
  • 72
    • 58149343579 scopus 로고    scopus 로고
    • Glycobiology on the fly: Developmental and mechanistic insights from Drosophila
    • Ten Hagen KG, Zhang L, Tian E, Zhang Y. 2009. Glycobiology on the fly: Developmental and mechanistic insights from Drosophila. Glycobiology. 19:102-111.
    • (2009) Glycobiology. , vol.19 , pp. 102-111
    • Ten Hagen, K.G.1    Zhang, L.2    Tian, E.3    Zhang, Y.4
  • 73
    • 0025273687 scopus 로고
    • Structure of O-glycosidically linked oligosaccharides synthesized by the insect cell line Sf9
    • Thomsen DR, Post LE, Elhammer AP. 1990. Structure of O-glycosidically linked oligosaccharides synthesized by the insect cell line Sf9. J Cell Biochem. 43:67-79.
    • (1990) J Cell Biochem. , vol.43 , pp. 67-79
    • Thomsen, D.R.1    Post, L.E.2    Elhammer, A.P.3
  • 74
    • 0037234667 scopus 로고    scopus 로고
    • Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian [beta]-1,4- galactosyltransferase and [beta]-1,2-Nacetylglucosaminyltransferase II
    • Tomiya N, Howe D, Aumiller JJ, Pathak M, Park J, Palter KB, Jarvis DL, Betenbaugh MJ, Lee YC. 2003. Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian [beta]-1,4-galactosyltransferase and [beta]-1,2-Nacetylglucosaminyltransferase 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.B.6    Jarvis, D.L.7    Betenbaugh, M.J.8    Lee, Y.C.9
  • 75
    • 7244254552 scopus 로고    scopus 로고
    • Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines
    • Tomiya N, Narang S, Lee YC, Betenbaugh MJ. 2004. Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines. Glycoconj J. 21:343-360.
    • (2004) Glycoconj J. , vol.21 , pp. 343-360
    • Tomiya, N.1    Narang, S.2    Lee, Y.C.3    Betenbaugh, M.J.4
  • 76
    • 0034723308 scopus 로고    scopus 로고
    • Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo
    • Toyoda H, Kinoshita-Toyoda A, Selleck SB. 2000. Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo. J Biol Chem. 275:2269-2275.
    • (2000) J Biol Chem. , vol.275 , pp. 2269-2275
    • Toyoda, H.1    Kinoshita-Toyoda, A.2    Selleck, S.B.3
  • 77
    • 0025923253 scopus 로고
    • Peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1-3 to the asparagine-linked N-acetylglucosamine residue
    • Tretter V, Altmann F, Marz L. 1991. Peptide-N4-(N-acetyl-beta- glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1-3 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
  • 78
    • 33144469842 scopus 로고    scopus 로고
    • Glycans modulate immune responses in helminth infections and allergy
    • van Die I, Cummings RD. 2006. Glycans modulate immune responses in helminth infections and allergy. Chem Immunol Allergy. 90:91-112.
    • (2006) Chem Immunol Allergy. , vol.90 , pp. 91-112
    • Van Die, I.1    Cummings, R.D.2
  • 79
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acidrecognizing proteins
    • Varki A. 2007. Glycan-based interactions involving vertebrate sialic-acidrecognizing proteins. Nature. 446:1023-1029.
    • (2007) Nature. , vol.446 , pp. 1023-1029
    • Varki, A.1
  • 80
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
    • Vaughn JL, Goodwin RH, Tompkins GJ, McCawley P. 1977. The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae). In Vitro. 13:213-217.
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 82
    • 0026918457 scopus 로고
    • Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system
    • Wickham TJ, Davis T, Granados RR, Shuler ML, Wood HA. 1992. Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system. Biotechnol Prog. 8:391-396.
    • (1992) Biotechnol Prog. , vol.8 , pp. 391-396
    • Wickham, T.J.1    Davis, T.2    Granados, R.R.3    Shuler, M.L.4    Wood, H.A.5
  • 83
    • 0019890808 scopus 로고
    • Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin
    • Yamamoto K, Tsuji T, Matsumoto I, Osawa T. 1981. Structural requirements for the binding of oligosaccharides and glycopeptides to immobilized wheat germ agglutinin. Biochemistry. 20:5894-5899.
    • (1981) Biochemistry. , vol.20 , pp. 5894-5899
    • Yamamoto, K.1    Tsuji, T.2    Matsumoto, I.3    Osawa, T.4
  • 84
    • 0026439093 scopus 로고
    • Purification and characterization of a Neu5Ac alpha 2->6Gal beta 1->4GlcNAc and HSO3(-)- >6Gal beta 1->GlcNAc specific lectin in tuberous roots of Trichosanthes japonica
    • Yamashita K, Umetsu K, Suzuki T, Ohkura T. 1992. Purification and characterization of a Neu5Ac alpha 2->6Gal beta 1->4GlcNAc and HSO3(-)- >6Gal beta 1->GlcNAc specific lectin in tuberous roots of Trichosanthes japonica. Biochemistry. 31:11647-11650.
    • (1992) Biochemistry. , vol.31 , pp. 11647-11650
    • Yamashita, K.1    Umetsu, K.2    Suzuki, T.3    Ohkura, T.4
  • 86
    • 33744484016 scopus 로고    scopus 로고
    • Sialic acid concentrations in plants are in the range of inadvertent contamination
    • Zeleny R, Kolarich D, Strasser R, Altmann F. 2006. Sialic acid concentrations in plants are in the range of inadvertent contamination. Planta. 224:222-227.
    • (2006) Planta. , vol.224 , pp. 222-227
    • Zeleny, R.1    Kolarich, D.2    Strasser, R.3    Altmann, F.4


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