메뉴 건너뛰기




Volumn 10, Issue 10, 2015, Pages 2199-2208

Modifying an Insect Cell N-Glycan Processing Pathway Using CRISPR-Cas Technology

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; GLYCOPROTEIN; NUCLEOTIDE; ACETYLGLUCOSAMINIDASE; DROSOPHILA PROTEIN; FDL PROTEIN, DROSOPHILA; POLYSACCHARIDE; RECOMBINANT PROTEIN;

EID: 84944733586     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00340     Document Type: Article
Times cited : (34)

References (67)
  • 1
    • 80051535219 scopus 로고    scopus 로고
    • Genome engineering with zinc-finger nucleases
    • Carroll, D. (2011) Genome engineering with zinc-finger nucleases Genetics 188, 773-782 10.1534/genetics.111.131433
    • (2011) Genetics , vol.188 , pp. 773-782
    • Carroll, D.1
  • 3
    • 27744530147 scopus 로고    scopus 로고
    • Zinc finger nucleases: Custom-designed molecular scissors for genome engineering of plant and mammalian cells
    • Durai, S., Mani, M., Kandavelou, K., Wu, J., Porteus, M. H., and Chandrasegaran, S. (2005) Zinc finger nucleases: custom-designed molecular scissors for genome engineering of plant and mammalian cells Nucleic Acids Res. 33, 5978-5990 10.1093/nar/gki912
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5978-5990
    • Durai, S.1    Mani, M.2    Kandavelou, K.3    Wu, J.4    Porteus, M.H.5    Chandrasegaran, S.6
  • 4
    • 80053343092 scopus 로고    scopus 로고
    • TAL effectors: Customizable proteins for DNA targeting
    • Bogdanove, A. J. and Voytas, D. F. (2011) TAL effectors: customizable proteins for DNA targeting Science 333, 1843-1846 10.1126/science.1204094
    • (2011) Science , vol.333 , pp. 1843-1846
    • Bogdanove, A.J.1    Voytas, D.F.2
  • 5
    • 84865513069 scopus 로고    scopus 로고
    • TALE nucleases: Tailored genome engineering made easy
    • Mussolino, C. and Cathomen, T. (2012) TALE nucleases: tailored genome engineering made easy Curr. Opin. Biotechnol. 23, 644-650 10.1016/j.copbio.2012.01.013
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 644-650
    • Mussolino, C.1    Cathomen, T.2
  • 6
    • 84871519181 scopus 로고    scopus 로고
    • TALENs: A widely applicable technology for targeted genome editing
    • Joung, J. K. and Sander, J. D. (2013) TALENs: a widely applicable technology for targeted genome editing Nat. Rev. Mol. Cell Biol. 14, 49-55 10.1038/nrm3486
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 49-55
    • Joung, J.K.1    Sander, J.D.2
  • 7
    • 84902096048 scopus 로고    scopus 로고
    • Development and applications of CRISPR-Cas9 for genome engineering
    • Hsu, P. D., Lander, E. S., and Zhang, F. (2014) Development and applications of CRISPR-Cas9 for genome engineering Cell 157, 1262-1278 10.1016/j.cell.2014.05.010
    • (2014) Cell , vol.157 , pp. 1262-1278
    • Hsu, P.D.1    Lander, E.S.2    Zhang, F.3
  • 8
    • 84900314611 scopus 로고    scopus 로고
    • CRISPR-Cas systems for editing, regulating and targeting genomes
    • Sander, J. D. and Joung, J. K. (2014) CRISPR-Cas systems for editing, regulating and targeting genomes Nat. Biotechnol. 32, 347-355 10.1038/nbt.2842
    • (2014) Nat. Biotechnol. , vol.32 , pp. 347-355
    • Sander, J.D.1    Joung, J.K.2
  • 9
    • 84913594397 scopus 로고    scopus 로고
    • Genome editing. The new frontier of genome engineering with CRISPR-Cas9
    • Doudna, J. A. and Charpentier, E. (2014) Genome editing. The new frontier of genome engineering with CRISPR-Cas9 Science 346, 1258096 10.1126/science.1258096
    • (2014) Science , vol.346 , pp. 1258096
    • Doudna, J.A.1    Charpentier, E.2
  • 17
    • 84880020391 scopus 로고    scopus 로고
    • Engineering Chinese hamster ovary (CHO) cells for producing recombinant proteins with simple glycoforms by zinc-finger nuclease (ZFN)-mediated gene knockout of mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (Mgat1)
    • Sealover, N. R., Davis, A. M., Brooks, J. K., George, H. J., Kayser, K. J., and Lin, N. (2013) Engineering Chinese hamster ovary (CHO) cells for producing recombinant proteins with simple glycoforms by zinc-finger nuclease (ZFN)-mediated gene knockout of mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (Mgat1) J. Biotechnol. 167, 24-32 10.1016/j.jbiotec.2013.06.006
    • (2013) J. Biotechnol. , vol.167 , pp. 24-32
    • Sealover, N.R.1    Davis, A.M.2    Brooks, J.K.3    George, H.J.4    Kayser, K.J.5    Lin, N.6
  • 19
    • 84861376809 scopus 로고    scopus 로고
    • Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant
    • Zhang, P., Haryadi, R., Chan, K. F., Teo, G., Goh, J., Pereira, N. A., Feng, H., and Song, Z. (2012) Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant Glycobiology 22, 897-911 10.1093/glycob/cws064
    • (2012) Glycobiology , vol.22 , pp. 897-911
    • Zhang, P.1    Haryadi, R.2    Chan, K.F.3    Teo, G.4    Goh, J.5    Pereira, N.A.6    Feng, H.7    Song, Z.8
  • 21
    • 84884211354 scopus 로고    scopus 로고
    • Biallelic knockout of the alpha-1,3 galactosyltransferase gene in porcine liver-derived cells using zinc finger nucleases
    • Li, P., Estrada, J. L., Burlak, C., and Tector, A. J. (2013) Biallelic knockout of the alpha-1,3 galactosyltransferase gene in porcine liver-derived cells using zinc finger nucleases J. Surg. Res. 181, e39-45 10.1016/j.jss.2012.06.035
    • (2013) J. Surg. Res. , vol.181 , pp. e39-45
    • Li, P.1    Estrada, J.L.2    Burlak, C.3    Tector, A.J.4
  • 23
    • 84894627942 scopus 로고    scopus 로고
    • Establishment of HeLa cell mutants deficient in sphingolipid-related genes using TALENs
    • Yamaji, T. and Hanada, K. (2014) Establishment of HeLa cell mutants deficient in sphingolipid-related genes using TALENs PLoS One 9, e88124 10.1371/journal.pone.0088124
    • (2014) PLoS One , vol.9 , pp. e88124
    • Yamaji, T.1    Hanada, K.2
  • 24
    • 84924777828 scopus 로고    scopus 로고
    • TALEN mediated targeted editing of GM2/GD2-synthase gene modulates anchorage independent growth by reducing anoikis resistance in mouse tumor cells
    • Mahata, B., Banerjee, A., Kundu, M., Bandyopadhyay, U., and Biswas, K. (2015) TALEN mediated targeted editing of GM2/GD2-synthase gene modulates anchorage independent growth by reducing anoikis resistance in mouse tumor cells Sci. Rep. 5, 9048 10.1038/srep09048
    • (2015) Sci. Rep. , vol.5 , pp. 9048
    • Mahata, B.1    Banerjee, A.2    Kundu, M.3    Bandyopadhyay, U.4    Biswas, K.5
  • 27
    • 84901934624 scopus 로고    scopus 로고
    • The combinational use of CRISPR/Cas9-based gene editing and targeted toxin technology enables efficient biallelic knockout of the alpha-1,3-galactosyltransferase gene in porcine embryonic fibroblasts
    • Sato, M., Miyoshi, K., Nagao, Y., Nishi, Y., Ohtsuka, M., Nakamura, S., Sakurai, T., and Watanabe, S. (2014) The combinational use of CRISPR/Cas9-based gene editing and targeted toxin technology enables efficient biallelic knockout of the alpha-1,3-galactosyltransferase gene in porcine embryonic fibroblasts Xenotransplantation 21, 291-300 10.1111/xen.12089
    • (2014) Xenotransplantation , vol.21 , pp. 291-300
    • Sato, M.1    Miyoshi, K.2    Nagao, Y.3    Nishi, Y.4    Ohtsuka, M.5    Nakamura, S.6    Sakurai, T.7    Watanabe, S.8
  • 28
    • 77956850407 scopus 로고
    • Protein glycosylation in insects
    • (Montreuil, J. Vliegenthart, J. F. G. and Schachter, H. Eds.), Elsevier, Amsterdam
    • Marz, L., Altmann, F., Staudacher, E., and Kubelka, V. (1995) Protein glycosylation in insects. In Glycoproteins (Montreuil, J., Vliegenthart, J. F. G., and Schachter, H., Eds.), pp 543-563, Elsevier, Amsterdam.
    • (1995) Glycoproteins , pp. 543-563
    • Marz, L.1    Altmann, F.2    Staudacher, E.3    Kubelka, V.4
  • 29
    • 0035086298 scopus 로고    scopus 로고
    • Glycoproteins from insect cells: Sialylated or not?
    • Marchal, I., Jarvis, D. L., Cacan, R., and Verbert, A. (2001) Glycoproteins from insect cells: sialylated or not? Biol. Chem. 382, 151-159 10.1515/BC.2001.023
    • (2001) Biol. Chem. , vol.382 , pp. 151-159
    • Marchal, I.1    Jarvis, D.L.2    Cacan, R.3    Verbert, A.4
  • 30
    • 33748742271 scopus 로고    scopus 로고
    • Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce 'mammalianized' recombinant glycoproteins
    • Harrison, R. L. and Jarvis, D. L. (2006) Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce 'mammalianized' recombinant glycoproteins Adv. Virus Res. 68, 159-191 10.1016/S0065-3527(06)68005-6
    • (2006) Adv. Virus Res. , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 31
    • 76849103484 scopus 로고    scopus 로고
    • Insect cell glycosylation patterns in the context of biopharmaceuticals
    • (Walsh, B. Ed.), pp, Wiley-Blackwell, Weinheim
    • Geisler, C. and Jarvis, D. L. (2009) Insect cell glycosylation patterns in the context of biopharmaceuticals. In Post-translational Modification of Protein Biopharmaceuticals (Walsh, B., Ed.), pp 165-191, Wiley-Blackwell, Weinheim.
    • (2009) Post-translational Modification of Protein Biopharmaceuticals , pp. 165-191
    • Geisler, C.1    Jarvis, D.L.2
  • 32
    • 84872712215 scopus 로고    scopus 로고
    • The N's and O's of Drosophila glycoprotein glycobiology
    • Katoh, T. and Tiemeyer, M. (2013) The N's and O's of Drosophila glycoprotein glycobiology Glycoconjugate J. 30, 57-66 10.1007/s10719-012-9442-x
    • (2013) Glycoconjugate J. , vol.30 , pp. 57-66
    • Katoh, T.1    Tiemeyer, M.2
  • 33
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis, D. L. (2009) Baculovirus-insect cell expression systems Meth. Enzymol. 463, 191-222 10.1016/S0076-6879(09)63014-7
    • (2009) Meth. Enzymol. , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 34
    • 36049042511 scopus 로고    scopus 로고
    • Transformation of Drosophila cell lines: An alternative approach to exogenous protein expression
    • Cherbas, L. and Cherbas, P. (2007) Transformation of Drosophila cell lines: an alternative approach to exogenous protein expression Methods Mol. Biol. 388, 317-340 10.1007/978-1-59745-457-5-16
    • (2007) Methods Mol. Biol. , vol.388 , pp. 317-340
    • Cherbas, L.1    Cherbas, P.2
  • 35
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides Annu. Rev. Biochem. 54, 631-664 10.1146/annurev.bi.54.070185.003215
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 36
    • 0033980373 scopus 로고    scopus 로고
    • Central brain postembryonic development in Drosophila: Implication of genes expressed at the interhemispheric junction
    • Boquet, I., Hitier, R., Dumas, M., Chaminade, M., and Preat, T. (2000) Central brain postembryonic development in Drosophila: implication of genes expressed at the interhemispheric junction J. Neurobiol. 42, 33-48 10.1002/(SICI)1097-4695(200001)42:1<33::AID-NEU4>3.3.CO;2-K
    • (2000) J. Neurobiol. , vol.42 , pp. 33-48
    • Boquet, I.1    Hitier, R.2    Dumas, M.3    Chaminade, M.4    Preat, T.5
  • 37
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound ß-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glossl, J., and Marz, L. (1995) Insect cells contain an unusual, membrane-bound ß-N-acetylglucosaminidase probably involved in the processing of protein N-glycans J. Biol. Chem. 270, 17344-17349 10.1074/jbc.270.29.17344
    • (1995) J. Biol. Chem. , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glossl, J.4    Marz, L.5
  • 38
    • 33646178162 scopus 로고    scopus 로고
    • The Drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing
    • Leonard, R., Rendic, D., Rabouille, C., Wilson, I. B., Preat, 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 10.1074/jbc.M511023200
    • (2006) J. Biol. Chem. , vol.281 , pp. 4867-4875
    • Leonard, R.1    Rendic, D.2    Rabouille, C.3    Wilson, I.B.4    Preat, T.5    Altmann, F.6
  • 39
    • 45549087961 scopus 로고    scopus 로고
    • A fused lobes gene encodes the processing beta-N-acetylglucosaminidase in Sf9 cells
    • Geisler, C., Aumiller, J. J., and Jarvis, D. L. (2008) A fused lobes gene encodes the processing beta-N-acetylglucosaminidase in Sf9 cells J. Biol. Chem. 283, 11330-11339 10.1074/jbc.M710279200
    • (2008) J. Biol. Chem. , vol.283 , pp. 11330-11339
    • Geisler, C.1    Aumiller, J.J.2    Jarvis, D.L.3
  • 40
    • 76849096485 scopus 로고    scopus 로고
    • Identification of genes encoding N-glycan processing beta-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: Implications for glycoengineering of baculovirus expression systems
    • Geisler, C. and Jarvis, D. L. (2010) Identification of genes encoding N-glycan processing beta-N-acetylglucosaminidases in Trichoplusia ni and Bombyx mori: Implications for glycoengineering of baculovirus expression systems Biotechnol. Prog. 26, 34-44 10.1002/btpr.298
    • (2010) Biotechnol. Prog. , vol.26 , pp. 34-44
    • Geisler, C.1    Jarvis, D.L.2
  • 41
    • 84857711440 scopus 로고    scopus 로고
    • Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway
    • Geisler, C. and Jarvis, D. L. (2012) Substrate specificities and intracellular distributions of three N-glycan processing enzymes functioning at a key branch point in the insect N-glycosylation pathway J. Biol. Chem. 287, 7084-7097 10.1074/jbc.M111.296814
    • (2012) J. Biol. Chem. , vol.287 , pp. 7084-7097
    • Geisler, C.1    Jarvis, D.L.2
  • 44
    • 58949100354 scopus 로고    scopus 로고
    • Suppression of beta-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells
    • Kim, Y. K., Kim, K. R., Kang, D. G., Jang, S. Y., Kim, Y. H., and Cha, H. J. (2009) Suppression of beta-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells Glycobiology 19, 301-308 10.1093/glycob/cwn138
    • (2009) Glycobiology , vol.19 , pp. 301-308
    • Kim, Y.K.1    Kim, K.R.2    Kang, D.G.3    Jang, S.Y.4    Kim, Y.H.5    Cha, H.J.6
  • 45
    • 84896929630 scopus 로고    scopus 로고
    • Improving CRISPR-Cas nuclease specificity using truncated guide RNAs
    • Fu, Y., Sander, J. D., Reyon, D., Cascio, V. M., and Joung, J. K. (2014) Improving CRISPR-Cas nuclease specificity using truncated guide RNAs Nat. Biotechnol. 32, 279-284 10.1038/nbt.2808
    • (2014) Nat. Biotechnol. , vol.32 , pp. 279-284
    • Fu, Y.1    Sander, J.D.2    Reyon, D.3    Cascio, V.M.4    Joung, J.K.5
  • 46
    • 84893695645 scopus 로고    scopus 로고
    • Mutagenesis and homologous recombination in Drosophila cell lines using CRISPR/Cas9
    • Bassett, A. R., Tibbit, C., Ponting, C. P., and Liu, J. L. (2014) Mutagenesis and homologous recombination in Drosophila cell lines using CRISPR/Cas9 Biol. Open 3, 42-49 10.1242/bio.20137120
    • (2014) Biol. Open , vol.3 , pp. 42-49
    • Bassett, A.R.1    Tibbit, C.2    Ponting, C.P.3    Liu, J.L.4
  • 48
    • 0031455984 scopus 로고    scopus 로고
    • Alpha-mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis
    • Chui, D., Oh-Eda, M., Liao, Y. F., Panneerselvam, K., Lal, A., Marek, K. W., Freeze, H. H., Moremen, K. W., Fukuda, M. N., and Marth, J. D. (1997) Alpha-mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis Cell 90, 157-167 10.1016/S0092-8674(00)80322-0
    • (1997) Cell , vol.90 , pp. 157-167
    • Chui, D.1    Oh-Eda, M.2    Liao, Y.F.3    Panneerselvam, K.4    Lal, A.5    Marek, K.W.6    Freeze, H.H.7    Moremen, K.W.8    Fukuda, M.N.9    Marth, J.D.10
  • 49
    • 0035844284 scopus 로고    scopus 로고
    • Insect cells encode a class II alpha-mannosidase with unique properties
    • Kawar, Z., Karaveg, K., Moremen, K. W., and Jarvis, D. L. (2001) Insect cells encode a class II alpha-mannosidase with unique properties J. Biol. Chem. 276, 16335-16340 10.1074/jbc.M100119200
    • (2001) J. Biol. Chem. , vol.276 , pp. 16335-16340
    • Kawar, Z.1    Karaveg, K.2    Moremen, K.W.3    Jarvis, D.L.4
  • 50
    • 33748703846 scopus 로고    scopus 로고
    • Identification and expression analysis of Drosophila melanogaster genes encoding beta-hexosaminidases of the sperm plasma membrane
    • Cattaneo, F., Pasini, M. E., Intra, J., Matsumoto, M., Briani, F., Hoshi, M., and Perotti, M. E. (2006) Identification and expression analysis of Drosophila melanogaster genes encoding beta-hexosaminidases of the sperm plasma membrane Glycobiology 16, 786-800 10.1093/glycob/cwl007
    • (2006) Glycobiology , vol.16 , pp. 786-800
    • Cattaneo, F.1    Pasini, M.E.2    Intra, J.3    Matsumoto, M.4    Briani, F.5    Hoshi, M.6    Perotti, M.E.7
  • 51
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki, K., Perlman, M., Lim, J. M., Cantu, R., Wells, L., and Tiemeyer, M. (2007) Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo J. Biol. Chem. 282, 9127-9142 10.1074/jbc.M606711200
    • (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
  • 52
    • 77956162735 scopus 로고    scopus 로고
    • The glycomics of glycan glucuronylation in Drosophila melanogaster
    • Aoki, K. and Tiemeyer, M. (2010) The glycomics of glycan glucuronylation in Drosophila melanogaster Meth. Enzymol. 480, 297-321 10.1016/S0076-6879(10)80014-X
    • (2010) Meth. Enzymol. , vol.480 , pp. 297-321
    • Aoki, K.1    Tiemeyer, M.2
  • 53
    • 84930936821 scopus 로고    scopus 로고
    • Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects
    • Kurz, S., Aoki, K., Jin, C., Karlsson, N. G., Tiemeyer, M., Wilson, I. B., and Paschinger, K. (2015) Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects J. Proteomics 126, 172-188 10.1016/j.jprot.2015.05.030
    • (2015) J. Proteomics , vol.126 , pp. 172-188
    • Kurz, S.1    Aoki, K.2    Jin, C.3    Karlsson, N.G.4    Tiemeyer, M.5    Wilson, I.B.6    Paschinger, K.7
  • 54
    • 0037085295 scopus 로고    scopus 로고
    • Sialylation of N-glycans on the recombinant proteins expressed by a baculovirus-insect cell system under ß-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 ß-N-acetylglucosaminidase inhibition J. Biol. Chem. 277, 5090-5093 10.1074/jbc.M110548200
    • (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
  • 55
    • 0033526537 scopus 로고    scopus 로고
    • Constraints on the transport and glycosylation of recombinant IFN-gamma 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-gamma in Chinese hamster ovary and insect cells Biotechnol. Bioeng. 63, 559-572 10.1002/(SICI)1097-0290(19990605)63:5<559::AID-BIT6>3.0.CO;2-L
    • (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
  • 56
    • 0035369256 scopus 로고    scopus 로고
    • Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: Sugar nucleotide contents in cultured insect cells and mammalian cells
    • Tomiya, N., Ailor, E., Lawrence, S. M., Betenbaugh, M. J., and Lee, Y. C. (2001) Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: sugar nucleotide contents in cultured insect cells and mammalian cells Anal. Biochem. 293, 129-137 10.1006/abio.2001.5091
    • (2001) Anal. Biochem. , vol.293 , pp. 129-137
    • Tomiya, N.1    Ailor, E.2    Lawrence, S.M.3    Betenbaugh, M.J.4    Lee, Y.C.5
  • 57
    • 0019470313 scopus 로고
    • Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin
    • Butters, T. D., Hughes, R. C., and Vischer, P. (1981) Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin Biochim. Biophys. Acta, Biomembr. 640, 672-686 10.1016/0005-2736(81)90097-3
    • (1981) Biochim. Biophys. Acta, Biomembr. , vol.640 , pp. 672-686
    • Butters, T.D.1    Hughes, R.C.2    Vischer, P.3
  • 58
    • 0035093068 scopus 로고    scopus 로고
    • Engineering lepidopteran insect cells for sialoglycoprotein production by genetic transformation with mammalian ß1,4-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 ß1,4-galactosyltransferase and alpha 2,6-sialyltransferase genes Glycobiology 11, 1-9 10.1093/glycob/11.1.1
    • (2001) Glycobiology , vol.11 , pp. 1-9
    • Hollister, J.R.1    Jarvis, D.L.2
  • 59
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells
    • Altmann, F., Kornfeld, G., Dalik, T., Staudacher, E., and Glossl, J. (1993) Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells Glycobiology 3, 619-625 10.1093/glycob/3.6.619
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glossl, J.5
  • 60
    • 0035086301 scopus 로고    scopus 로고
    • Cloning and expression of Drosophila melanogaster UDP-GlcNAc:alpha-3-D-mannoside beta 1,2-N-acetylglucosaminyltransferase I
    • Sarkar, M. and Schachter, H. (2001) Cloning and expression of Drosophila melanogaster UDP-GlcNAc:alpha-3-D-mannoside beta 1,2-N-acetylglucosaminyltransferase I Biol. Chem. 382, 209-217 10.1515/BC.2001.028
    • (2001) Biol. Chem. , vol.382 , pp. 209-217
    • Sarkar, M.1    Schachter, H.2
  • 61
  • 62
    • 0030250433 scopus 로고    scopus 로고
    • Immediate-early baculovirus vectors for foreign gene expression in transformed or infected insect cells
    • Jarvis, D. L., Weinkauf, C., and Guarino, L. A. (1996) Immediate-early baculovirus vectors for foreign gene expression in transformed or infected insect cells Protein Expression Purif. 8, 191-203 10.1006/prep.1996.0092
    • (1996) Protein Expression Purif. , vol.8 , pp. 191-203
    • Jarvis, D.L.1    Weinkauf, C.2    Guarino, L.A.3
  • 63
    • 0033610897 scopus 로고    scopus 로고
    • Identification and characterization of a novel line of Drosophila Schneider S2 cells that respond to wingless signaling
    • Yanagawa, S., Lee, J. S., and Ishimoto, A. (1998) Identification and characterization of a novel line of Drosophila Schneider S2 cells that respond to wingless signaling J. Biol. Chem. 273, 32353-32359 10.1074/jbc.273.48.32353
    • (1998) J. Biol. Chem. , vol.273 , pp. 32353-32359
    • Yanagawa, S.1    Lee, J.S.2    Ishimoto, A.3
  • 64
    • 80054064897 scopus 로고    scopus 로고
    • Factors affecting recombinant Western equine encephalitis virus glycoprotein production in the baculovirus system
    • Toth, A. M., Geisler, C., Aumiller, J. J., and Jarvis, D. L. (2011) Factors affecting recombinant Western equine encephalitis virus glycoprotein production in the baculovirus system Protein Expression Purif. 80, 274-282 10.1016/j.pep.2011.08.002
    • (2011) Protein Expression Purif. , vol.80 , pp. 274-282
    • Toth, A.M.1    Geisler, C.2    Aumiller, J.J.3    Jarvis, D.L.4
  • 65
    • 84871959756 scopus 로고    scopus 로고
    • Impact of a human CMP-sialic acid transporter on recombinant glycoprotein sialylation in glycoengineered insect cells
    • Mabashi-Asazuma, H., Shi, X., Geisler, C., Kuo, C. W., Khoo, K. H., and Jarvis, D. L. (2013) Impact of a human CMP-sialic acid transporter on recombinant glycoprotein sialylation in glycoengineered insect cells Glycobiology 23, 199-210 10.1093/glycob/cws143
    • (2013) Glycobiology , vol.23 , pp. 199-210
    • Mabashi-Asazuma, H.1    Shi, X.2    Geisler, C.3    Kuo, C.W.4    Khoo, K.H.5    Jarvis, D.L.6
  • 66
    • 84894282237 scopus 로고    scopus 로고
    • A novel baculovirus vector for the production of nonfucosylated recombinant glycoproteins in insect cells
    • Mabashi-Asazuma, H., Kuo, C. W., Khoo, K. H., and Jarvis, D. L. (2014) A novel baculovirus vector for the production of nonfucosylated recombinant glycoproteins in insect cells Glycobiology 24, 325-340 10.1093/glycob/cwt161
    • (2014) Glycobiology , vol.24 , pp. 325-340
    • Mabashi-Asazuma, H.1    Kuo, C.W.2    Khoo, K.H.3    Jarvis, D.L.4
  • 67
    • 84913569197 scopus 로고    scopus 로고
    • Engineering beta1,4-galactosyltransferase I to reduce secretion and enhance N-glycan elongation in insect cells
    • Geisler, C., Mabashi-Asazuma, H., Kuo, C. W., Khoo, K. H., and Jarvis, D. L. (2014) Engineering beta1,4-galactosyltransferase I to reduce secretion and enhance N-glycan elongation in insect cells J. Biotechnol. 193, 52-65 10.1016/j.jbiotec.2014.11.013
    • (2014) J. Biotechnol. , vol.193 , pp. 52-65
    • Geisler, C.1    Mabashi-Asazuma, H.2    Kuo, C.W.3    Khoo, K.H.4    Jarvis, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.