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Volumn 94, Issue 1, 2012, Pages 69-80

Enhancement of sialylation on humanized IgG-like bispecific antibody by overexpression of α2,6-sialyltransferase derived from Chinese hamster ovary cells

Author keywords

Antibody production; Beta galactosyl alpha 2,6 sialyltransferase (ST6Gal I); Bispecific diabody; Chinese hamster ovary (CHO) cell; Glycosylation control; Sialylation

Indexed keywords

ANTIBODY PRODUCTION; BETA-GALACTOSYL ALPHA-2,6 SIALYLTRANSFERASE (ST6GAL I); BISPECIFIC DIABODY; CHINESE HAMSTER OVARY CELLS; SIALYLATION;

EID: 84858441807     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3814-1     Document Type: Article
Times cited : (37)

References (58)
  • 1
    • 0028061380 scopus 로고
    • The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins
    • DOI 10.1016/0958-1669(94)90072-8
    • DC Andersen CF Goochee 1994 The effect of cell-culture conditions on the oligosaccharide structures of secreted glycoproteins Curr Opin Biotechnol 5 546 549 10.1016/0958-1669(94)90072-8 1:CAS:528:DyaK2cXmslyrurY%3D (Pubitemid 24321425)
    • (1994) Current Opinion in Biotechnology , vol.5 , Issue.5 , pp. 546-549
    • Andersen, D.C.1    Goochee, C.F.2
  • 2
    • 0029778345 scopus 로고    scopus 로고
    • Cloning and sequencing of the V(H) and V(κ) genes of an anti-CD3 monoclonal antibody, and construction of a mouse/human chimeric antibody
    • F Arakawa M Kuroki M Kuwahara T Senba H Ozaki Y Matsuoka Y Misumi H Kanda T Watanabe 1996 Cloning and sequencing of the VH and V kappa genes of an anti-CD3 monoclonal antibody, and construction of a mouse/human chimeric antibody J Biochem 120 657 662 1:CAS:528:DyaK28XmvFCnu7k%3D (Pubitemid 26331658)
    • (1996) Journal of Biochemistry , vol.120 , Issue.3 , pp. 657-662
    • Arakawa, F.1    Kuroki, M.2    Kuwahara, M.3    Senba, T.4    Ozaki, H.5    Matsuoka, Y.6    Misumi, Y.7    Kanda, H.8    Watanabe, T.9
  • 3
    • 3142537435 scopus 로고    scopus 로고
    • Elution of antibodies from a Protein-A column by aqueous arginine solutions
    • DOI 10.1016/j.pep.2004.04.009, PII S1046592804001238
    • T Arakawa JS Philo K Tsumoto R Yumioka D Ejima 2004 Elution of antibodies from a Protein-A column by aqueous arginine solutions Protein Expr Purif 36 244 248 10.1016/j.pep.2004.04.009 1:CAS:528:DC%2BD2cXlsFymsrk%3D (Pubitemid 38893161)
    • (2004) Protein Expression and Purification , vol.36 , Issue.2 , pp. 244-248
    • Arakawa, T.1    Philo, J.S.2    Tsumoto, K.3    Yumioka, R.4    Ejima, D.5
  • 4
    • 34948911585 scopus 로고    scopus 로고
    • Highly effective recombinant format of a humanized IgG-like bispecific antibody for cancer immunotherapy with retargeting of lymphocytes to tumor cells
    • DOI 10.1074/jbc.M704719200
    • R Asano Y Watanabe H Kawaguchi H Fukazawa T Nakanishi M Umetsu H Hayashi Y Katayose M Unno T Kudo I Kumagai 2007 Highly effective recombinant format of a humanized IgG-like bispecific antibody for cancer immunotherapy with retargeting of lymphocytes to tumor cells J Biol Chem 282 27659 27665 10.1074/jbc.M704719200 1:CAS:528:DC%2BD2sXhtVeju7rN (Pubitemid 47529493)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.38 , pp. 27659-27665
    • Asano, R.1    Watanabe, Y.2    Kawaguchi, H.3    Fukazawa, H.4    Nakanishi, T.5    Umetsu, M.6    Hayashi, H.7    Katayose, Y.8    Unno, M.9    Kudo, T.10    Kumagai, I.11
  • 5
    • 59849088809 scopus 로고    scopus 로고
    • Diabody-based recombinant formats of humanized IgG-like bispecific antibody with effective retargeting of lymphocytes to tumor cells
    • 10.1097/CJI.0b013e3181849071 1:CAS:528:DC%2BD1cXhtFCrtLzK
    • R Asano H Kawaguchi Y Watanabe T Nakanishi M Umetsu H Hayashi Y Katayose M Unno T Kudo I Kumagai 2008 Diabody-based recombinant formats of humanized IgG-like bispecific antibody with effective retargeting of lymphocytes to tumor cells J Immunother 31 752 761 10.1097/CJI.0b013e3181849071 1:CAS:528: DC%2BD1cXhtFCrtLzK
    • (2008) J Immunother , vol.31 , pp. 752-761
    • Asano, R.1    Kawaguchi, H.2    Watanabe, Y.3    Nakanishi, T.4    Umetsu, M.5    Hayashi, H.6    Katayose, Y.7    Unno, M.8    Kudo, T.9    Kumagai, I.10
  • 6
    • 74849109669 scopus 로고    scopus 로고
    • L overexpression
    • 10.1002/bit.22534 1:CAS:528:DC%2BD1MXhs1Sru73N
    • L overexpression Biotechnol Bioeng 105 358 367 10.1002/bit.22534 1:CAS:528:DC%2BD1MXhs1Sru73N
    • (2010) Biotechnol Bioeng , vol.105 , pp. 358-367
    • Baik, J.Y.1    Lee, G.M.2
  • 7
    • 33747362656 scopus 로고    scopus 로고
    • Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems
    • 10.1007/s10616-005-4537-x 1:CAS:528:DC%2BD28XotFChs7o%3D
    • M Butler 2006 Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems Cytotechnology 50 57 76 10.1007/s10616-005-4537-x 1:CAS:528:DC%2BD28XotFChs7o%3D
    • (2006) Cytotechnology , vol.50 , pp. 57-76
    • Butler, M.1
  • 8
    • 23844433927 scopus 로고    scopus 로고
    • Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals
    • DOI 10.1007/s00253-005-1980-8
    • M Butler 2005 Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals Appl Microbiol Biotechnol 68 283 291 10.1007/s00253-005-1980-8 1:CAS:528:DC%2BD2MXnsl2gtrk%3D (Pubitemid 41159998)
    • (2005) Applied Microbiology and Biotechnology , vol.68 , Issue.3 , pp. 283-291
    • Butler, M.1
  • 9
    • 1442352043 scopus 로고    scopus 로고
    • Effect of Doxycycline-Regulated Calnexin and Calreticulin Expression on Specific Thrombopoietin Productivity of Recombinant Chinese Hamster Ovary Cells
    • DOI 10.1002/bit.10919
    • JY Chung SW Lim YJ Hong SO Hwang GM Lee 2004 Effect of doxycycline-regulated calnexin and calreticulin expression on specific thrombopoietin productivity of recombinant Chinese hamster ovary cells Biotechnol Bioeng 85 539 546 10.1002/bit.10919 1:CAS:528:DC%2BD2cXhvVCmsLs%3D (Pubitemid 38268670)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.5 , pp. 539-546
    • Chung, J.Y.1    Lim, S.W.2    Hong, Y.J.3    Hwang, S.O.4    Lee, G.M.5
  • 10
    • 0032540299 scopus 로고    scopus 로고
    • Mutation of the sialyltransferase s-sialylmotif alters the kinetics of the donor and acceptor substrates
    • DOI 10.1074/jbc.273.16.9608
    • AK Datta A Sinha JC Paulson 1998 Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates J Biol Chem 273 9608 9614 10.1074/jbc.273.16.9608 1:CAS:528:DyaK1cXivVOrt78%3D (Pubitemid 28183048)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9608-9614
    • Datta, A.K.1    Sinha, A.2    Paulson, J.C.3
  • 11
    • 33846839360 scopus 로고    scopus 로고
    • Comparative transcriptional analysis of mouse hybridoma and recombinant Chinese hamster ovary cells undergoing butyrate treatment
    • DOI 10.1263/jbb.103.82, PII S1389172307700282
    • GM De Leon KF Wlaschin PM Nissom M Yap WS Hu 2007 Comparative transcriptional analysis of mouse hybridoma and recombinant Chinese hamster ovary cells undergoing butyrate treatment J Biosci Bioeng 103 82 91 10.1263/jbb.103.82 (Pubitemid 46216907)
    • (2007) Journal of Bioscience and Bioengineering , vol.103 , Issue.1 , pp. 82-91
    • De Leon Gatti, M.1    Wlaschin, K.F.2    Nissom, P.M.3    Yap, M.4    Hu, W.-S.5
  • 12
    • 49849101676 scopus 로고    scopus 로고
    • Transcriptional profiling of gene expression changes in a PACE-transfected CHO DUKX cell line secreting high levels of rhBMP-2
    • 10.1007/s12033-008-9039-6 1:CAS:528:DC%2BD1cXntVWitr8%3D
    • P Doolan M Melville P Gammell M Sinacore P Meleady K McCarthy L Francullo M Leonard T Charlebois M Clynes 2008 Transcriptional profiling of gene expression changes in a PACE-transfected CHO DUKX cell line secreting high levels of rhBMP-2 Mol Biotechnol 39 187 199 10.1007/s12033-008-9039-6 1:CAS:528:DC%2BD1cXntVWitr8%3D
    • (2008) Mol Biotechnol , vol.39 , pp. 187-199
    • Doolan, P.1    Melville, M.2    Gammell, P.3    Sinacore, M.4    Meleady, P.5    McCarthy, K.6    Francullo, L.7    Leonard, M.8    Charlebois, T.9    Clynes, M.10
  • 13
    • 0027467841 scopus 로고
    • A conserved disulphide bond in sialyltransferases
    • K Drickamer 1993 A conserved disulphide bond in sialyltransferases Glycobiology 3 2 3 10.1093/glycob/3.1.2 1:CAS:528:DyaK3sXitVyntrg%3D (Pubitemid 23123166)
    • (1993) Glycobiology , vol.3 , Issue.1 , pp. 2-3
    • Drickamer, K.1
  • 14
    • 0029154557 scopus 로고
    • Glycobiology: More functions for oligosaccharides
    • 10.1126/science.7652569 1:CAS:528:DyaK2MXnvVeqt7k%3D
    • RA Dwek 1995 Glycobiology: more functions for oligosaccharides Science 269 1234 1235 10.1126/science.7652569 1:CAS:528:DyaK2MXnvVeqt7k%3D
    • (1995) Science , vol.269 , pp. 1234-1235
    • Dwek, R.A.1
  • 15
    • 34250676983 scopus 로고    scopus 로고
    • Fetal calf serum-free culture of Chinese hamster ovary cells employing fish serum
    • DOI 10.1007/s00253-007-0897-9
    • M Fujiwara R Tsukada Y Tsujinaga M Takagi 2007 Fetal calf serum-free culture of Chinese hamster ovary cells employing fish serum Appl Microbiol Biotechnol 75 983 987 10.1007/s00253-007-0897-9 1:CAS:528:DC%2BD2sXmsVKqsbc%3D (Pubitemid 46944525)
    • (2007) Applied Microbiology and Biotechnology , vol.75 , Issue.5 , pp. 983-987
    • Fujiwara, M.1    Tsukada, R.2    Tsujinaga, Y.3    Takagi, M.4
  • 16
    • 34248137611 scopus 로고    scopus 로고
    • Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase
    • DOI 10.1016/j.bbrc.2007.04.054, PII S0006291X07007772
    • K Fujiyama A Furukawa A Katsura R Misaki T Omasa T Seki 2007 Production of mouse monoclonal antibody with galactose-extended sugar chain by suspension cultured tobacco BY2 cells expressing human β(1,4)-galactosyltransferase Biochem Biophys Res Commun 358 85 91 10.1016/j.bbrc.2007.04.054 1:CAS:528:DC%2BD2sXlt1ertLc%3D (Pubitemid 46719084)
    • (2007) Biochemical and Biophysical Research Communications , vol.358 , Issue.1 , pp. 85-91
    • Fujiyama, K.1    Furukawa, A.2    Katsura, A.3    Misaki, R.4    Omasa, T.5    Seki, T.6
  • 17
    • 0031086055 scopus 로고    scopus 로고
    • Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: Implications for their mechanism of action
    • 10.1093/glycob/7.2.161 1:CAS:528:DyaK2sXis1Ontrk%3D
    • RA Geremia A Harduin-Lepers P Delannoy 1997 Identification of two novel conserved amino acid residues in eukaryotic sialyltransferases: implications for their mechanism of action Glycobiology 7 v vii 10.1093/glycob/7.2.161 1:CAS:528:DyaK2sXis1Ontrk%3D
    • (1997) Glycobiology , vol.7
    • Geremia, R.A.1    Harduin-Lepers, A.2    Delannoy, P.3
  • 18
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • 10.1038/nbt.1651 1:CAS:528:DC%2BC3cXpt1art7c%3D
    • D Ghaderi RE Taylor V Padler-Karavani S Diaz A Varki 2010 Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins Nat Biotechnol 28 863 867 10.1038/nbt.1651 1:CAS:528: DC%2BC3cXpt1art7c%3D
    • (2010) Nat Biotechnol , vol.28 , pp. 863-867
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 19
    • 0026649441 scopus 로고
    • Cloning and expression of the Gal β1, 3GalNAc α2,3- sialyltransferase
    • 1:CAS:528:DyaK3sXktVajtL0%3D
    • W Gillespie S Kelm JC Paulson 1992 Cloning and expression of the Gal β1, 3GalNAc α2,3-sialyltransferase J Biol Chem 267 21004 21010 1:CAS:528:DyaK3sXktVajtL0%3D
    • (1992) J Biol Chem , vol.267 , pp. 21004-21010
    • Gillespie, W.1    Kelm, S.2    Paulson, J.C.3
  • 20
    • 25144501600 scopus 로고    scopus 로고
    • The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach
    • DOI 10.1093/glycob/cwi063
    • A Harduin-Lepers R Mollicone P Delannoy R Oriol 2005 The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach Glycobiology 15 805 817 10.1093/glycob/cwi063 1:CAS:528:DC%2BD2MXlslyrtr4%3D (Pubitemid 41417983)
    • (2005) Glycobiology , vol.15 , Issue.8 , pp. 805-817
    • Harduin-Lepers, A.1    Mollicone, R.2    Delannoy, P.3    Oriol, R.4
  • 21
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • A Helenius M Aebi 2001 Intracellular functions of N-linked glycans Science 291 2364 2369 10.1126/science.291.5512.2364 1:CAS:528: DC%2BD3MXit1KnsLw%3D (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 22
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • DOI 10.1021/bp050228w
    • J Hodoniczky YZ Zheng DC James 2005 Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro Biotechnol Prog 21 1644 1652 10.1021/bp050228w 1:CAS:528:DC%2BD2MXhtVOis7zN (Pubitemid 41778987)
    • (2005) Biotechnology Progress , vol.21 , Issue.6 , pp. 1644-1652
    • Hodoniczky, J.1    Yuan, Z.Z.2    James, D.C.3
  • 23
    • 79952108569 scopus 로고    scopus 로고
    • Substitution of glutamine by glutamate enhances production and galactosylation of recombinant IgG in Chinese hamster ovary cells
    • 10.1007/s00253-010-2790-1 1:CAS:528:DC%2BC3cXhtFyqt7nN
    • JK Hong SM Cho SK Yoon 2010 Substitution of glutamine by glutamate enhances production and galactosylation of recombinant IgG in Chinese hamster ovary cells Appl Microbiol Biotechnol 88 869 876 10.1007/s00253-010-2790-1 1:CAS:528:DC%2BC3cXhtFyqt7nN
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 869-876
    • Hong, J.K.1    Cho, S.M.2    Yoon, S.K.3
  • 25
    • 1842640513 scopus 로고    scopus 로고
    • Structure-function analysis of the human sialyltransferase ST3Gal I: Role of N-glycosylation and a novel conserved sialylmotif
    • DOI 10.1074/jbc.M311764200
    • C Jeanneau V Chazalet C Auge DM Soumpasis A Harduin-Lepers P Delannoy A Imberty C Breton 2004 Structure-function analysis of the human sialyltransferase ST3Gal I: role of N-glycosylation and a novel conserved sialylmotif J Biol Chem 279 13461 13468 10.1074/jbc.M311764200 1:CAS:528:DC%2BD2cXis1emurs%3D (Pubitemid 38468870)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13461-13468
    • Jeanneau, C.1    Chazalet, V.2    Auge, C.3    Soumpasis, D.M.4    Harduin-Lepers, A.5    Delannoy, P.6    Imberty, A.7    Breton, C.8
  • 26
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • DOI 10.1021/bp040016j
    • R Jefferis 2005 Glycosylation of recombinant antibody therapeutics Biotechnol Prog 21 11 16 10.1021/bp040016j 1:CAS:528:DC%2BD2cXhtFSlurrP (Pubitemid 40218466)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 11-16
    • Jefferis, R.1
  • 27
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • N Jenkins RB Parekh DC James 1996 Getting the glycosylation right: implications for the biotechnology industry Nat Biotechnol 14 975 981 10.1038/nbt0896-975 1:CAS:528:DyaK28Xks1Gms7k%3D (Pubitemid 26286569)
    • (1996) Nature Biotechnology , vol.14 , Issue.8 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 29
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Y Kaneko F Nimmerjahn JV Ravetch 2006 Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 670 673 10.1126/science.1129594 1:CAS:528:DC%2BD28Xnsl2hsbY%3D (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 30
    • 67349115980 scopus 로고    scopus 로고
    • Development of serum-free medium supplemented with hydrolysates for the production of therapeutic antibodies in CHO cell cultures using design of experiments
    • 10.1007/s00253-009-1903-1 1:CAS:528:DC%2BD1MXmslOks74%3D
    • SH Kim GM Lee 2009 Development of serum-free medium supplemented with hydrolysates for the production of therapeutic antibodies in CHO cell cultures using design of experiments Appl Microbiol Biotechnol 83 639 648 10.1007/s00253-009-1903-1 1:CAS:528:DC%2BD1MXmslOks74%3D
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 639-648
    • Kim, S.H.1    Lee, G.M.2
  • 33
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase
    • EU Lee J Roth JC Paulson 1989 Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α 2,6-sialyltransferase J Biol Chem 264 13848 13855 1:CAS:528:DyaL1MXltFWktb4%3D (Pubitemid 19198479)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.23 , pp. 13848-13855
    • Lee, E.U.1    Roth, J.2    Paulson, J.C.3
  • 34
    • 0027298677 scopus 로고
    • Polymerase chain reaction cloning of a developmentally regulated member of the sialyltransferase gene family
    • BD Livingston JC Paulson 1993 Polymerase chain reaction cloning of a developmentally regulated member of the sialyltransferase gene family J Biol Chem 268 11504 11507 1:CAS:528:DyaK3sXkvVyjurY%3D (Pubitemid 23168090)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11504-11507
    • Livingston, B.D.1    Paulson, J.C.2
  • 35
    • 0027319101 scopus 로고
    • Control of IgG/Fc glycosylation: A comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs
    • 10.1016/0161-5890(93)90145-2 1:CAS:528:DyaK3sXkslSjt7g%3D
    • J Lund N Takahashi H Nakagawa M Goodall T Bentley SA Hindley R Tyler R Jefferis 1993 Control of IgG/Fc glycosylation: a comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs Mol Immunol 30 741 748 10.1016/0161-5890(93)90145-2 1:CAS:528:DyaK3sXkslSjt7g%3D
    • (1993) Mol Immunol , vol.30 , pp. 741-748
    • Lund, J.1    Takahashi, N.2    Nakagawa, H.3    Goodall, M.4    Bentley, T.5    Hindley, S.A.6    Tyler, R.7    Jefferis, R.8
  • 36
    • 0030425381 scopus 로고    scopus 로고
    • Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ
    • L Monaco A Marc A Eon-Duval G Acerbis G Distefano D Lamotte J-M Engasser M Soria N Jenkins 1996 Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ Cytotechnology 22 197 203 10.1007/BF00353939 1:CAS:528:DyaK1cXislels78%3D (Pubitemid 27133788)
    • (1996) Cytotechnology , vol.22 , Issue.1-3 , pp. 197-203
    • Monaco, L.1    Marc, A.2    Eon-Duval, A.3    Acerbis, G.4    Distefano, G.5    Lamotte, D.6    Engasser, J.-M.7    Soria, M.8    Jenkins, N.9
  • 38
    • 0027112176 scopus 로고
    • Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation
    • 10.1002/bit.260390511 1:CAS:528:DyaK38XhsFSis7w%3D
    • T Omasa K Higashiyama S Shioya K Suga 1992 Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation Biotechnol Bioeng 39 556 564 10.1002/bit.260390511 1:CAS:528:DyaK38XhsFSis7w%3D
    • (1992) Biotechnol Bioeng , vol.39 , pp. 556-564
    • Omasa, T.1    Higashiyama, K.2    Shioya, S.3    Suga, K.4
  • 39
    • 77950881484 scopus 로고    scopus 로고
    • Cell engineering and cultivation of Chinese hamster ovary (CHO) cells
    • Omasa T, Onitsuka M, Kim WD (2010a) Cell engineering and cultivation of Chinese hamster ovary (CHO) cells. Curr Pharm Biotechnol 11:233-240
    • (2010) Curr Pharm Biotechnol , vol.11 , pp. 233-240
    • Omasa, T.1    Onitsuka, M.2    Kim, W.D.3
  • 40
    • 76849087459 scopus 로고    scopus 로고
    • Enhanced antibody production following intermediate addition based on flux analysis in mammalian cell continuous culture
    • 865
    • Omasa T, Furuichi K, Iemura T, Katakura Y, Kishimoto M, Suga K (2010b) Enhanced antibody production following intermediate addition based on flux analysis in mammalian cell continuous culture. Bioproc Biosyst Eng 33:117-125 865
    • (2010) Bioproc Biosyst Eng , vol.33 , pp. 117-125
    • Omasa, T.1    Furuichi, K.2    Iemura, T.3    Katakura, Y.4    Kishimoto, M.5    Suga, K.6
  • 41
    • 51549113358 scopus 로고    scopus 로고
    • Decrease in antithrombin III fucosylation by expressing GDP-fucose transporter siRNA in Chinese hamster ovary cells
    • 10.1263/jbb.106.168 1:CAS:528:DC%2BD1cXhtlWnsrzN
    • T Omasa R Tanaka T Doi M Ando Y Kitamoto K Honda M Kishimoto H Ohtake 2008 Decrease in antithrombin III fucosylation by expressing GDP-fucose transporter siRNA in Chinese hamster ovary cells J Biosci Bioeng 106 168 173 10.1263/jbb.106.168 1:CAS:528:DC%2BD1cXhtlWnsrzN
    • (2008) J Biosci Bioeng , vol.106 , pp. 168-173
    • Omasa, T.1    Tanaka, R.2    Doi, T.3    Ando, M.4    Kitamoto, Y.5    Honda, K.6    Kishimoto, M.7    Ohtake, H.8
  • 42
    • 31144466590 scopus 로고    scopus 로고
    • Identification of linkage-specific sequence motifs in sialyltransferases
    • DOI 10.1093/glycob/cwj046
    • RY Patel PV Balaji 2006 Identification of linkage-specific sequence motifs in sialyltransferases Glycobiology 16 108 116 10.1093/glycob/cwj046 1:CAS:528:DC%2BD28XksVylsw%3D%3D (Pubitemid 43125967)
    • (2006) Glycobiology , vol.16 , Issue.2 , pp. 108-116
    • Patel, R.Y.1    Balaji, P.V.2
  • 43
    • 0028909145 scopus 로고
    • The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes
    • WRP Rijcken B Overdijk DH Van den Eijnden W Ferwerda 1995 The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes Biochem J 305 Pt 3 865 870
    • (1995) Biochem J , vol.305 , Issue.PART 3 , pp. 865-870
    • Rijcken, W.R.P.1    Overdijk, B.2    Van Den Eijnden, D.H.3    Ferwerda, W.4
  • 44
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcγ receptor in complex with Fc
    • 10.1074/jbc.M100350200 1:CAS:528:DC%2BD3MXjvFarsrw%3D
    • S Radaev S Motyka WH Fridman C Sautes-Fridman PD Sun 2001 The structure of a human type III Fcγ receptor in complex with Fc J Biol Chem 276 16469 16477 10.1074/jbc.M100350200 1:CAS:528:DC%2BD3MXjvFarsrw%3D
    • (2001) J Biol Chem , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 45
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • DOI 10.1016/j.molimm.2006.09.005, PII S0161589006005839
    • BJ Scallon SH Tam SG McCarthy AN Cai TS Raju 2007 Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality Mol Immunol 44 1524 1534 10.1016/j.molimm.2006.09.005 1:CAS:528:DC%2BD28Xht1ems7zJ (Pubitemid 44792756)
    • (2007) Molecular Immunology , vol.44 , Issue.7 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 47
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • DOI 10.1074/jbc.M210665200
    • T Shinkawa K Nakamura N Yamane E Shoji-Hosaka Y Kanda M Sakurada K Uchida H Anazawa M Satoh M Yamasaki N Hanai K Shitara 2003 The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity J Biol Chem 278 3466 3473 10.1074/jbc.M210665200 1:CAS:528:DC%2BD3sXmt1Kiuw%3D%3D (Pubitemid 36801263)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 48
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex
    • DOI 10.1038/35018508
    • P Sondermann R Huber V Oosthuizen U Jacob 2000 The 3.2-Å crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex Nature 406 267 273 10.1038/35018508 1:CAS:528:DC%2BD3cXlsFKisro%3D (Pubitemid 30604397)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthulzen, V.3    Jacob, U.4
  • 49
    • 36849001215 scopus 로고    scopus 로고
    • β-Galactoside α2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins: A novel regulatory mechanism for α2,6-sialylation
    • DOI 10.1074/jbc.M704766200
    • I Sugimoto S Futakawa R Oka K Ogawa JD Marth E Miyoshi N Taniguchi Y Hashimoto S Kitazume 2007 β-Galactoside α2,6-sialyltransferase I cleavage by BACE1 enhances the sialylation of soluble glycoproteins. A novel regulatory mechanism for α2,6-sialylation J Biol Chem 282 34896 34903 10.1074/jbc.M704766200 1:CAS:528:DC%2BD2sXhtlCrt7%2FL (Pubitemid 350232443)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 34896-34903
    • Sugimoto, I.1    Futakawa, S.2    Oka, R.3    Ogawa, K.4    Marth, J.D.5    Miyoshi, E.6    Taniguchi, N.7    Hashimoto, Y.8    Kitazume, S.9
  • 50
    • 0037560884 scopus 로고    scopus 로고
    • Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma
    • DOI 10.1023/A:1023993400608
    • S Terada T Nishimura M Sasaki H Yamada M Miki 2002 Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma Cytotechnology 40 3 12 10.1023/A:1023993400608 1:CAS:528:DC%2BD3sXktFSmtr0%3D (Pubitemid 36749588)
    • (2003) Cytotechnology , vol.40 , Issue.1-3 , pp. 3-12
    • Terada, S.1    Nishimura, T.2    Sasaki, M.3    Yamada, H.4    Miki, M.5
  • 51
    • 79955870936 scopus 로고    scopus 로고
    • Identification of a novel temperature sensitive promoter in CHO cells
    • 10.1186/1472-6750-11-51 1:CAS:528:DC%2BC3MXmsV2iu7s%3D
    • H Thaisuchat M Baumann J Pontiller F Hesse W Ernst 2011 Identification of a novel temperature sensitive promoter in CHO cells BMC Biotechnol 11 51 10.1186/1472-6750-11-51 1:CAS:528:DC%2BC3MXmsV2iu7s%3D
    • (2011) BMC Biotechnol , vol.11 , pp. 51
    • Thaisuchat, H.1    Baumann, M.2    Pontiller, J.3    Hesse, F.4    Ernst, W.5
  • 52
    • 0033588177 scopus 로고    scopus 로고
    • Incorporation of ammonium into intracellular UDP-activated N- acetylhexosamines and into carbohydrate structures in glycoproteins
    • DOI 10.1002/(SICI)1097-0290(19990820)64:4<401::AID-BIT3>3.0.CO;2-M
    • U Valley M Nimtz HS Conradt R Wagner 1999 Incorporation of ammonium into intracellular UDP-activated N-acetylhexosamines and into carbohydrate structures in glycoproteins Biotechnol Bioeng 64 401 417 10.1002/(SICI)1097-0290(19990820) 64:4<401::AID-BIT3>3.0.CO;2-M 1:CAS:528:DyaK1MXkvVygs7Y%3D (Pubitemid 29334339)
    • (1999) Biotechnology and Bioengineering , vol.64 , Issue.4 , pp. 401-417
    • Valley, U.1    Nimtz, M.2    Conradt, H.S.3    Wagner, R.4
  • 53
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • A Varki 1997 Sialic acids as ligands in recognition phenomena FASEB J 11 248 255 1:CAS:528:DyaK2sXhvVGlsL0%3D (Pubitemid 27118325)
    • (1997) FASEB Journal , vol.11 , Issue.4 , pp. 248-255
    • Varki, A.1
  • 55
    • 33646029110 scopus 로고    scopus 로고
    • Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells
    • 10.1002/bit.20815 1:CAS:528:DC%2BD28Xjt1Grsrg%3D
    • NS Wong MG Yap DI Wang 2006 Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells Biotechnol Bioeng 93 1005 1016 10.1002/bit.20815 1:CAS:528:DC%2BD28Xjt1Grsrg%3D
    • (2006) Biotechnol Bioeng , vol.93 , pp. 1005-1016
    • Wong, N.S.1    Yap, M.G.2    Wang, D.I.3
  • 56
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • DOI 10.1016/S0167-7799(96)10062-7, PII S0167779996100627
    • A Wright SL Morrison 1997 Effect of glycosylation on antibody function: implications for genetic engineering Trends Biotechnol 15 26 32 10.1016/S0167-7799(96)10062-7 1:CAS:528:DyaK2sXhtFCiurc%3D (Pubitemid 27067150)
    • (1997) Trends in Biotechnology , vol.15 , Issue.1 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 58
    • 0036008002 scopus 로고    scopus 로고
    • Effects of ammonia and glucosamine on the heterogeneity of erythropoietin glycoforms
    • DOI 10.1021/bp0101334
    • M Yang M Butler 2002 Effects of ammonia and glucosamine on the heterogeneity of erythropoietin glycoforms Biotechnol Prog 18 129 138 10.1021/bp0101334 1:CAS:528:DC%2BD38XjtF2ruw%3D%3D (Pubitemid 34147387)
    • (2002) Biotechnology Progress , vol.18 , Issue.1 , pp. 129-138
    • Yang, M.1    Butler, M.2


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