메뉴 건너뛰기




Volumn 34, Issue 10, 2016, Pages 835-846

N-Glycosylation Design and Control of Therapeutic Monoclonal Antibodies

Author keywords

glycoengineering; mathematical modeling; metabolic characterization; monoclonal antibody; N glycosylation

Indexed keywords

GLYCOSYLATION; MATHEMATICAL MODELS; METABOLISM; MONOCLONAL ANTIBODIES; POLYSACCHARIDES; SURFACE PLASMON RESONANCE;

EID: 84962166067     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2016.02.013     Document Type: Review
Times cited : (118)

References (87)
  • 1
    • 84892170718 scopus 로고    scopus 로고
    • What's fueling the biotech engine – 2012 to 2013
    • 1 Aggarwal, S., What's fueling the biotech engine – 2012 to 2013. Nat. Biotechnol. 32 (2014), 32–39.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 32-39
    • Aggarwal, S.1
  • 2
    • 84861876412 scopus 로고    scopus 로고
    • Can next-generation antibodies offset biosimilar competition?
    • 2 Mullard, A., Can next-generation antibodies offset biosimilar competition?. Nat. Rev. Drug Discov. 11 (2012), 426–428.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 426-428
    • Mullard, A.1
  • 3
    • 77951979046 scopus 로고    scopus 로고
    • Recent advances in large-scale production of monoclonal antibodies and related proteins
    • 3 Shukla, A.A., Thommes, J., Recent advances in large-scale production of monoclonal antibodies and related proteins. Trends Biotechnol. 28 (2010), 253–261.
    • (2010) Trends Biotechnol. , vol.28 , pp. 253-261
    • Shukla, A.A.1    Thommes, J.2
  • 4
    • 84897065464 scopus 로고    scopus 로고
    • Glycosylation analysis of an aggregated antibody produced by Chinese hamster ovary cells in bioreactor culture
    • 4 Onitsuka, M., et al. Glycosylation analysis of an aggregated antibody produced by Chinese hamster ovary cells in bioreactor culture. J. Biosci. Bioeng. 117 (2014), 639–644.
    • (2014) J. Biosci. Bioeng. , vol.117 , pp. 639-644
    • Onitsuka, M.1
  • 5
    • 80052348042 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins – current understanding of structure–function relationships
    • 5 Siemiatkoski, J., et al. Glycosylation of therapeutic proteins – current understanding of structure–function relationships. BioProcess Int. 9 (2011), 48–53.
    • (2011) BioProcess Int. , vol.9 , pp. 48-53
    • Siemiatkoski, J.1
  • 6
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • 6 Beck, A., et al. Strategies and challenges for the next generation of therapeutic antibodies. Nat. Rev. Immunol. 10 (2010), 345–352.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 345-352
    • Beck, A.1
  • 7
    • 34047142084 scopus 로고    scopus 로고
    • Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1
    • 7 Matsumiya, S., et al. Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1. J. Mol. Biol. 368 (2007), 767–779.
    • (2007) J. Mol. Biol. , vol.368 , pp. 767-779
    • Matsumiya, S.1
  • 8
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodelling in vitro
    • 8 Hodoniczky, J., et al. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodelling in vitro. Biotechnol. Prog. 21 (2005), 1644–1652.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1
  • 9
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • 9 Goetze, A.M., et al. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 21 (2011), 949–959.
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1
  • 10
    • 84911946438 scopus 로고    scopus 로고
    • Antibody glycosylation and inflammation
    • 10 Shade, K., Anthony, R.M., Antibody glycosylation and inflammation. Antibodies 2 (2013), 392–414.
    • (2013) Antibodies , vol.2 , pp. 392-414
    • Shade, K.1    Anthony, R.M.2
  • 11
    • 0004338667 scopus 로고    scopus 로고
    • FDA Guidance Concerning Demonstration of Comparability of Human Biological Products, including Therapeutic Biotechnology-derived Products
    • FDA
    • 11 FDA. FDA Guidance Concerning Demonstration of Comparability of Human Biological Products, including Therapeutic Biotechnology-derived Products. 1996, FDA.
    • (1996)
  • 12
    • 84877015785 scopus 로고    scopus 로고
    • Protein glycosylation control in mammalian cell culture: past precedents and contemporary prospects
    • 12 Hossler, P., Protein glycosylation control in mammalian cell culture: past precedents and contemporary prospects. Adv. Biochem. Eng. Biotechnol. 127 (2012), 187–219.
    • (2012) Adv. Biochem. Eng. Biotechnol. , vol.127 , pp. 187-219
    • Hossler, P.1
  • 13
    • 84889094657 scopus 로고    scopus 로고
    • Integration of models and experimentation to optimise the production of potential biotherapeutics
    • 13 Royle, K.E., et al. Integration of models and experimentation to optimise the production of potential biotherapeutics. Drug Discov. Today 18 (2013), 1250–1255.
    • (2013) Drug Discov. Today , vol.18 , pp. 1250-1255
    • Royle, K.E.1
  • 14
    • 84903852374 scopus 로고    scopus 로고
    • The choice of mammalian cell host and possibilities for glycosylation engineering
    • 14 Butler, M., Spearman, M., The choice of mammalian cell host and possibilities for glycosylation engineering. Curr. Opin. Biotechnol. 30C (2014), 107–112.
    • (2014) Curr. Opin. Biotechnol. , vol.30C , pp. 107-112
    • Butler, M.1    Spearman, M.2
  • 15
    • 34247854443 scopus 로고    scopus 로고
    • Nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients
    • 15 Suzuki, E., et al. Nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients. Clin. Cancer Res. 13 (2007), 1875–1882.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1875-1882
    • Suzuki, E.1
  • 16
    • 38649143213 scopus 로고    scopus 로고
    • Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC
    • 16 Imai-Nishiya, H., et al. Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC. BMC Biotechnol., 7, 2007, 84.
    • (2007) BMC Biotechnol. , vol.7 , pp. 84
    • Imai-Nishiya, H.1
  • 17
    • 77955390706 scopus 로고    scopus 로고
    • Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies
    • 17 Malphettes, L., et al. Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnol. Bioeng. 106 (2010), 774–783.
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 774-783
    • Malphettes, L.1
  • 18
    • 84941187809 scopus 로고    scopus 로고
    • Functional knockout of FUT8 in Chinese hamster ovary cells using CRISPR/Cas9 to produce a defucosylated antibody
    • 18 Sun, T., et al. Functional knockout of FUT8 in Chinese hamster ovary cells using CRISPR/Cas9 to produce a defucosylated antibody. Eng. Life Sci., 15, 2015, 660.
    • (2015) Eng. Life Sci. , vol.15 , pp. 660
    • Sun, T.1
  • 19
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous β1,4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II
    • 19 Ferrara, C., et al. Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous β1,4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II. Biotechnol. Bioeng. 93 (2006), 851–861.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 851-861
    • Ferrara, C.1
  • 20
    • 79961191745 scopus 로고    scopus 로고
    • The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
    • 20 Xu, X., et al. The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line. Nat. Biotechnol. 29 (2011), 735–741.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 735-741
    • Xu, X.1
  • 21
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • 21 Scallon, B.J., et al. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol. Immunol. 44 (2007), 1524–1534.
    • (2007) Mol. Immunol. , vol.44 , pp. 1524-1534
    • Scallon, B.J.1
  • 22
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • 22 Anthony, R.M., et al. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320 (2008), 373–376.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1
  • 23
    • 84940551820 scopus 로고    scopus 로고
    • A common glycan structure on immunoglobulin G for enhancement of effector functions
    • 23 Lin, C.W., et al. A common glycan structure on immunoglobulin G for enhancement of effector functions. Proc. Natl. Acad. Sci. U.S.A. 112 (2015), 10611–10616.
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 10611-10616
    • Lin, C.W.1
  • 24
    • 79960209555 scopus 로고    scopus 로고
    • Enhanced sialylation of recombinant human erythropoietin in Chinese hamster ovary cells by combinatorial engineering of selected genes
    • 24 Son, Y.D., et al. Enhanced sialylation of recombinant human erythropoietin in Chinese hamster ovary cells by combinatorial engineering of selected genes. Glycobiology 21 (2011), 1019–1028.
    • (2011) Glycobiology , vol.21 , pp. 1019-1028
    • Son, Y.D.1
  • 25
    • 66149104098 scopus 로고    scopus 로고
    • Enhanced sialylation of recombinant erythropoietin in genetically engineered Chinese-hamster ovary cells
    • 25 Jeong, Y.T., et al. Enhanced sialylation of recombinant erythropoietin in genetically engineered Chinese-hamster ovary cells. Biotechnol. Appl. Biochem. 52 (2009), 283–291.
    • (2009) Biotechnol. Appl. Biochem. , vol.52 , pp. 283-291
    • Jeong, Y.T.1
  • 26
    • 33646029110 scopus 로고    scopus 로고
    • Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells
    • 26 Wong, N.S., et al. Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells. Biotechnol. Bioeng. 93 (2006), 1005–1016.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 1005-1016
    • Wong, N.S.1
  • 27
    • 33748438957 scopus 로고    scopus 로고
    • RNA interference of sialidase improves glycoprotein sialic acid content consistency
    • 27 Ngantung, F.A., et al. RNA interference of sialidase improves glycoprotein sialic acid content consistency. Biotechnol. Bioeng. 95 (2006), 106–119.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 106-119
    • Ngantung, F.A.1
  • 28
    • 84931562808 scopus 로고    scopus 로고
    • Tailoring recombinant protein quality by rational media design
    • 28 Brühlmann, D., et al. Tailoring recombinant protein quality by rational media design. Biotechnol. Prog. 31 (2015), 615–629.
    • (2015) Biotechnol. Prog. , vol.31 , pp. 615-629
    • Brühlmann, D.1
  • 29
    • 78149250500 scopus 로고    scopus 로고
    • An investigation of intracellular glycosylation activities in CHO cells: effects of nucleotide sugar precursor feeding
    • 29 Wong, N.S., et al. An investigation of intracellular glycosylation activities in CHO cells: effects of nucleotide sugar precursor feeding. Biotechnol. Bioeng. 107 (2010), 321–336.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 321-336
    • Wong, N.S.1
  • 30
    • 84890158776 scopus 로고    scopus 로고
    • The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody
    • 30 Liu, B., et al. The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody. J. Biotechnol. 170 (2014), 17–27.
    • (2014) J. Biotechnol. , vol.170 , pp. 17-27
    • Liu, B.1
  • 31
    • 79956155356 scopus 로고    scopus 로고
    • Modulation of antibody galactosylation through feeding of uridine, manganese chloride, and galactose
    • 31 Gramer, M.J., et al. Modulation of antibody galactosylation through feeding of uridine, manganese chloride, and galactose. Biotechnol. Bioeng. 108 (2011), 1591–1602.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1591-1602
    • Gramer, M.J.1
  • 32
    • 84928429962 scopus 로고    scopus 로고
    • A robust method for increasing Fc glycan high mannose level of recombinant antibodies
    • 32 Huang, C.J., et al. A robust method for increasing Fc glycan high mannose level of recombinant antibodies. Biotechnol. Bioeng. 112 (2015), 1200–1209.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1200-1209
    • Huang, C.J.1
  • 33
    • 84958280421 scopus 로고    scopus 로고
    • Mannose metabolism in recombinant CHO cells and its effect on IgG glycosylation
    • Published online January 1, 2016
    • 33 Slade, P.G., et al. Mannose metabolism in recombinant CHO cells and its effect on IgG glycosylation. Biotechnol. Bioeng., 2016, 10.1002/bit.25924 Published online January 1, 2016.
    • (2016) Biotechnol. Bioeng.
    • Slade, P.G.1
  • 34
    • 80054092824 scopus 로고    scopus 로고
    • Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in CHO cells
    • 34 Burleigh, S.C., et al. Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in CHO cells. BMC Biotechnol., 11, 2011, 95.
    • (2011) BMC Biotechnol. , vol.11 , pp. 95
    • Burleigh, S.C.1
  • 35
    • 84904346024 scopus 로고    scopus 로고
    • Role of Chinese hamster ovary central carbon metabolism
    • 35 McAtee, A.G., et al. Role of Chinese hamster ovary central carbon metabolism. Pharm. Bioprocess 2 (2014), 63–74.
    • (2014) Pharm. Bioprocess , vol.2 , pp. 63-74
    • McAtee, A.G.1
  • 36
    • 33846927813 scopus 로고    scopus 로고
    • Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system
    • 36 Crowell, C.K., et al. Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system. Biotechnol. Bioeng. 96 (2007), 538–549.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 538-549
    • Crowell, C.K.1
  • 37
    • 0036008002 scopus 로고    scopus 로고
    • Effects of ammonia and glucosamine on EPO glycoforms
    • 37 Yang, M., Butler, M., Effects of ammonia and glucosamine on EPO glycoforms. Biotechnol. Prog. 18 (2002), 129–138.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 129-138
    • Yang, M.1    Butler, M.2
  • 38
    • 84884530112 scopus 로고    scopus 로고
    • CHO cell line specific prediction and control of recombinant monoclonal antibody N-glycosylation
    • 38 Grainger, R.K., James, D.C., CHO cell line specific prediction and control of recombinant monoclonal antibody N-glycosylation. Biotechnol. Bioeng. 110 (2013), 2970–2982.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2970-2982
    • Grainger, R.K.1    James, D.C.2
  • 39
    • 84922974254 scopus 로고    scopus 로고
    • Control of galactosylated glycoforms distribution in cell culture system
    • 39 McCracken, N.A., et al. Control of galactosylated glycoforms distribution in cell culture system. Biotechnol. Prog. 30 (2014), 547–553.
    • (2014) Biotechnol. Prog. , vol.30 , pp. 547-553
    • McCracken, N.A.1
  • 40
    • 84904490835 scopus 로고    scopus 로고
    • Effects of nutrient levels and average culture pH on the glycosylation pattern of camelid-humanized monoclonal antibody
    • 40 Aghamohseni, H., et al. Effects of nutrient levels and average culture pH on the glycosylation pattern of camelid-humanized monoclonal antibody. J. Biotechnol. 186 (2014), 98–109.
    • (2014) J. Biotechnol. , vol.186 , pp. 98-109
    • Aghamohseni, H.1
  • 41
    • 84873323391 scopus 로고    scopus 로고
    • Fed-batch CHO cell t-PA production and feed glutamine replacement to reduce ammonia production
    • 41 Kim, D.Y., et al. Fed-batch CHO cell t-PA production and feed glutamine replacement to reduce ammonia production. Biotechnol. Prog. 29 (2013), 165–175.
    • (2013) Biotechnol. Prog. , vol.29 , pp. 165-175
    • Kim, D.Y.1
  • 42
    • 78349269949 scopus 로고    scopus 로고
    • CHO-K1 host cells adapted to growth in glutamine-free medium by FACS-assisted evolution
    • 42 Bort, J.A.H., et al. CHO-K1 host cells adapted to growth in glutamine-free medium by FACS-assisted evolution. Biotechnol. J. 5 (2010), 1090–1097.
    • (2010) Biotechnol. J. , vol.5 , pp. 1090-1097
    • Bort, J.A.H.1
  • 43
    • 84855668252 scopus 로고    scopus 로고
    • Growth, productivity and protein glycosylation in a CHO EpoFc producer cell line adapted to glutamine-free growth
    • 43 Taschwer, M., et al. Growth, productivity and protein glycosylation in a CHO EpoFc producer cell line adapted to glutamine-free growth. J. Biotechnol. 157 (2012), 295–303.
    • (2012) J. Biotechnol. , vol.157 , pp. 295-303
    • Taschwer, M.1
  • 44
    • 18144373127 scopus 로고    scopus 로고
    • Effects of amino acid additions on ammonium stressed CHO cells
    • 44 Chen, P., Harcum, S.W., Effects of amino acid additions on ammonium stressed CHO cells. J. Biotechnol. 117 (2005), 277–286.
    • (2005) J. Biotechnol. , vol.117 , pp. 277-286
    • Chen, P.1    Harcum, S.W.2
  • 45
    • 80051798475 scopus 로고    scopus 로고
    • Effects of cell culture conditions on antibody N-linked glycosylation – what affects high mannose 5 glycoform
    • 45 Pacis, E., et al. Effects of cell culture conditions on antibody N-linked glycosylation – what affects high mannose 5 glycoform. Biotechnol. Bioeng. 108 (2011), 2348–2358.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 2348-2358
    • Pacis, E.1
  • 46
    • 84944905703 scopus 로고    scopus 로고
    • Real-time product attribute control to manufacture antibodies with defined N-linked glycan levels
    • 46 Zupke, C., et al. Real-time product attribute control to manufacture antibodies with defined N-linked glycan levels. Biotechnol. Prog. 31 (2015), 1433–1441.
    • (2015) Biotechnol. Prog. , vol.31 , pp. 1433-1441
    • Zupke, C.1
  • 47
    • 84894639207 scopus 로고    scopus 로고
    • Controllability analysis of protein glycosylation in CHO cells
    • 47 St Amand, M.M., et al. Controllability analysis of protein glycosylation in CHO cells. PLoS ONE, 9, 2014, e87973.
    • (2014) PLoS ONE , vol.9 , pp. e87973
    • St Amand, M.M.1
  • 48
    • 84904365784 scopus 로고    scopus 로고
    • Identification of manipulated variables for a glycosylation control strategy
    • 48 St Amand, M.M., et al. Identification of manipulated variables for a glycosylation control strategy. Biotechnol. Bioeng. 111 (2014), 1957–1970.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1957-1970
    • St Amand, M.M.1
  • 49
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • 49 Hossler, P., et al. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19 (2009), 936–949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1
  • 50
    • 84863724161 scopus 로고    scopus 로고
    • Fucose content of monoclonal antibodies can be controlled by culture medium osmolality for high antibody-dependent cellular cytotoxicity
    • 50 Konno, Y., et al. Fucose content of monoclonal antibodies can be controlled by culture medium osmolality for high antibody-dependent cellular cytotoxicity. Cytotechnology 64 (2012), 249–265.
    • (2012) Cytotechnology , vol.64 , pp. 249-265
    • Konno, Y.1
  • 51
    • 0037420754 scopus 로고    scopus 로고
    • Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in Chinese hamster ovary cells
    • 51 Yoon, S.K., et al. Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in Chinese hamster ovary cells. Biotechnol. Bioeng. 82 (2003), 289–298.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 289-298
    • Yoon, S.K.1
  • 52
    • 84929160974 scopus 로고    scopus 로고
    • Bioreactor process parameter screening utilizing a Plackett–Burman design for a model monoclonal antibody
    • 52 Agarabi, C.D., et al. Bioreactor process parameter screening utilizing a Plackett–Burman design for a model monoclonal antibody. J. Pharm. Sci. 104 (2015), 1919–1928.
    • (2015) J. Pharm. Sci. , vol.104 , pp. 1919-1928
    • Agarabi, C.D.1
  • 53
    • 77955949391 scopus 로고    scopus 로고
    • Guidance for Industry. Q8(R2) Pharmaceutical Development
    • FDA
    • 53 U.S. Department of Health Human Services; Food and Drug Administration; Center for Drug Evaluation and Research (CDER); Center for Biologics Evaluation and Research (CBER). Guidance for Industry. Q8(R2) Pharmaceutical Development. 2009, FDA.
    • (2009)
  • 54
    • 78049428272 scopus 로고    scopus 로고
    • A functional analysis of N-glycosylation-related genes on sialylation of recombinant erythropoietin in six commonly used mammalian cell lines
    • 54 Zhang, P., et al. A functional analysis of N-glycosylation-related genes on sialylation of recombinant erythropoietin in six commonly used mammalian cell lines. Metab. Eng. 12 (2010), 526–536.
    • (2010) Metab. Eng. , vol.12 , pp. 526-536
    • Zhang, P.1
  • 55
    • 84906070955 scopus 로고    scopus 로고
    • Glycosylation-related genes in NS0 cells are insensitive to moderately elevated ammonium concentrations
    • 55 Brodsky, A.N., et al. Glycosylation-related genes in NS0 cells are insensitive to moderately elevated ammonium concentrations. J. Biotechnol. 187 (2014), 78–86.
    • (2014) J. Biotechnol. , vol.187 , pp. 78-86
    • Brodsky, A.N.1
  • 56
    • 84860448067 scopus 로고    scopus 로고
    • Glycosylation and post-translational modification gene expression analysis by DNA microarrays for cultured mammalian cells
    • 56 Brodsky, A.N., et al. Glycosylation and post-translational modification gene expression analysis by DNA microarrays for cultured mammalian cells. Methods 56 (2012), 408–417.
    • (2012) Methods , vol.56 , pp. 408-417
    • Brodsky, A.N.1
  • 57
    • 84932199513 scopus 로고    scopus 로고
    • Understanding of altered N-glycosylation-related gene expression in recombinant Chinese hamster ovary cells subjected to elevated ammonium concentration by digital mRNA counting
    • 57 Ha, T.K., et al. Understanding of altered N-glycosylation-related gene expression in recombinant Chinese hamster ovary cells subjected to elevated ammonium concentration by digital mRNA counting. Biotechnol. Bioeng. 112 (2015), 1583–1593.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1583-1593
    • Ha, T.K.1
  • 58
    • 78651471034 scopus 로고    scopus 로고
    • Profiling of N-glycosylation gene expression in CHO cell fed-batch cultures
    • 58 Wong, D.C.F., et al. Profiling of N-glycosylation gene expression in CHO cell fed-batch cultures. Biotechnol. Bioeng. 107 (2010), 516–528.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 516-528
    • Wong, D.C.F.1
  • 59
    • 84894342482 scopus 로고    scopus 로고
    • Dynamics of growth and metabolism controlled by glutamine availability in Chinese hamster ovary cells
    • 59 Wahrheit, J., et al. Dynamics of growth and metabolism controlled by glutamine availability in Chinese hamster ovary cells. Appl. Microbiol. Biotechnol. 98 (2014), 1771–1783.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 1771-1783
    • Wahrheit, J.1
  • 60
    • 84871722305 scopus 로고    scopus 로고
    • Flux balance analysis of CHO cells before and after a metabolic switch from lactate production to consumption
    • 60 Martínez, V.S., et al. Flux balance analysis of CHO cells before and after a metabolic switch from lactate production to consumption. Biotechnol. Bioeng. 110 (2012), 660–666.
    • (2012) Biotechnol. Bioeng. , vol.110 , pp. 660-666
    • Martínez, V.S.1
  • 61
    • 84906352291 scopus 로고    scopus 로고
    • 13C metabolic flux analysis
    • 13C metabolic flux analysis. J. Biotechnol. 187 (2014), 124–134.
    • (2014) J. Biotechnol. , vol.187 , pp. 124-134
    • Nie, Y.1
  • 62
    • 84868010172 scopus 로고    scopus 로고
    • LC-MS-Based metabolic characterization of high monoclonal antibody-producing Chinese hamster ovary cells
    • 62 Chong, W.P.K., et al. LC-MS-Based metabolic characterization of high monoclonal antibody-producing Chinese hamster ovary cells. Biotechnol. Bioeng. 109 (2012), 3103–3111.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 3103-3111
    • Chong, W.P.K.1
  • 63
    • 84940467009 scopus 로고    scopus 로고
    • A multi-pronged investigation into the effect of glucose starvation and culture duration on fed-batch CHO cell culture
    • 63 Fan, Y., et al. A multi-pronged investigation into the effect of glucose starvation and culture duration on fed-batch CHO cell culture. Biotechnol. Bioeng. 112 (2015), 2172–2184.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 2172-2184
    • Fan, Y.1
  • 64
    • 84868324251 scopus 로고    scopus 로고
    • Proteomic analysis of Chinese hamster ovary cells
    • 64 Baycin-Hizal, D., et al. Proteomic analysis of Chinese hamster ovary cells. J. Proteome Res. 11 (2012), 5265–5276.
    • (2012) J. Proteome Res. , vol.11 , pp. 5265-5276
    • Baycin-Hizal, D.1
  • 65
    • 84898861924 scopus 로고    scopus 로고
    • Effect of glucose feeding on the glycosylation quality of antibody produced by a human cell line, F2N78, in fed-batch culture
    • 65 Seo, J.S., et al. Effect of glucose feeding on the glycosylation quality of antibody produced by a human cell line, F2N78, in fed-batch culture. Appl. Microbiol. Biotechnol. 98 (2014), 3509–3515.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 3509-3515
    • Seo, J.S.1
  • 66
    • 84928428105 scopus 로고    scopus 로고
    • How does mild hypothermia affect monoclonal antibody glycosylation
    • 66 Sou, S.N., et al. How does mild hypothermia affect monoclonal antibody glycosylation. Biotechnol. Bioeng. 112 (2015), 1165–1176.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1165-1176
    • Sou, S.N.1
  • 67
    • 84862784156 scopus 로고    scopus 로고
    • Combined in silico modeling and metabolomics analysis to characterize fed-batch CHO cell culture
    • 67 Selvarasu, S., et al. Combined in silico modeling and metabolomics analysis to characterize fed-batch CHO cell culture. Biotechnol. Bioeng. 109 (2012), 1415–1429.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1415-1429
    • Selvarasu, S.1
  • 68
    • 46249121065 scopus 로고    scopus 로고
    • Influence of intracellular nucleotide and nucleotide sugar contents on recombinant interferon-gamma glycosylation during batch and fed-batch cultures of CHO cells
    • 68 Kochanowski, N., et al. Influence of intracellular nucleotide and nucleotide sugar contents on recombinant interferon-gamma glycosylation during batch and fed-batch cultures of CHO cells. Biotechnol. Bioeng. 100 (2008), 721–733.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 721-733
    • Kochanowski, N.1
  • 69
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NSO cells
    • 69 Hills, A.E., et al. Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NSO cells. Biotechnol. Bioeng. 75 (2001), 239–251.
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 239-251
    • Hills, A.E.1
  • 70
    • 84922787460 scopus 로고    scopus 로고
    • Amino acid and glucose metabolism in fed-batch CHO cell culture affects antibody production and glycosylation
    • 70 Fan, Y., et al. Amino acid and glucose metabolism in fed-batch CHO cell culture affects antibody production and glycosylation. Biotechnol. Bioeng. 112 (2015), 521–535.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 521-535
    • Fan, Y.1
  • 71
    • 19544383966 scopus 로고    scopus 로고
    • Gene-expression profiles for five key glycosylation genes for galactose-fed CHO cells expressing recombinant IL-4/13 cytokine trap
    • 71 Clark, K.J., et al. Gene-expression profiles for five key glycosylation genes for galactose-fed CHO cells expressing recombinant IL-4/13 cytokine trap. Biotechnol. Bioeng. 90 (2005), 568–577.
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 568-577
    • Clark, K.J.1
  • 72
    • 33644825884 scopus 로고    scopus 로고
    • Effects of elevated ammonium on glycosylation gene expression in CHO cells
    • 72 Chen, P., Harcum, S.W., Effects of elevated ammonium on glycosylation gene expression in CHO cells. Metab. Eng. 8 (2006), 123–132.
    • (2006) Metab. Eng. , vol.8 , pp. 123-132
    • Chen, P.1    Harcum, S.W.2
  • 73
    • 82955237386 scopus 로고    scopus 로고
    • A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus
    • 73 del Val, I.J., et al. A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus. Biotechnol. Prog. 27 (2011), 1730–1743.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 1730-1743
    • del Val, I.J.1
  • 74
    • 0343581263 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycoform biosynthesis
    • 74 Umana, P., Bailey, J.E., A mathematical model of N-linked glycoform biosynthesis. Biotechnol. Bioeng. 55 (1997), 891–908.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 891-908
    • Umana, P.1    Bailey, J.E.2
  • 75
    • 28844473175 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycosylation
    • 75 Krambeck, F.J., Betenbaugh, M.J., A mathematical model of N-linked glycosylation. Biotechnol. Bioeng. 92 (2005), 711–728.
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 711-728
    • Krambeck, F.J.1    Betenbaugh, M.J.2
  • 76
    • 84914142511 scopus 로고    scopus 로고
    • Galactosyltransferase 4 is a major control point for glycan branching in N-linked glycosylation
    • 76 McDonald, A.G., et al. Galactosyltransferase 4 is a major control point for glycan branching in N-linked glycosylation. J. Cell Sci. 127 (2014), 5014–5026.
    • (2014) J. Cell Sci. , vol.127 , pp. 5014-5026
    • McDonald, A.G.1
  • 77
    • 84896474989 scopus 로고    scopus 로고
    • Towards controlling the glycoform: a model framework linking extracellular metabolites to antibody glycosylation
    • 77 Jedrzejewski, P.M., et al. Towards controlling the glycoform: a model framework linking extracellular metabolites to antibody glycosylation. Int. J. Mol. Sci. 15 (2014), 4492–4522.
    • (2014) Int. J. Mol. Sci. , vol.15 , pp. 4492-4522
    • Jedrzejewski, P.M.1
  • 79
    • 85027210803 scopus 로고    scopus 로고
    • A quantitative and mechanistic model for monoclonal antibody glycosylation as a function of nutrient availability during cell culture
    • 79 del Val, J.I., et al. A quantitative and mechanistic model for monoclonal antibody glycosylation as a function of nutrient availability during cell culture. BMC Proc., 7, 2013, O10.
    • (2013) BMC Proc. , vol.7 , pp. O10
    • del Val, J.I.1
  • 80
    • 84969369434 scopus 로고    scopus 로고
    • Dynamics of immature mAb glycoform secretion during CHO cell culture: an integrated modelling framework
    • Published online February 12, 2016
    • 80 del Val, I.J., et al. Dynamics of immature mAb glycoform secretion during CHO cell culture: an integrated modelling framework. Biotechnol. J., 2016, 10.1002/biot.201400663 Published online February 12, 2016.
    • (2016) Biotechnol. J.
    • del Val, I.J.1
  • 81
    • 40249093192 scopus 로고    scopus 로고
    • Systems analysis of N-glycan processing in mammalian cells
    • 81 Hossler, P., et al. Systems analysis of N-glycan processing in mammalian cells. PLoS ONE, 2, 2007, e713.
    • (2007) PLoS ONE , vol.2 , pp. e713
    • Hossler, P.1
  • 82
    • 70350114562 scopus 로고    scopus 로고
    • Centralized modularity of N-linked glycosylation pathways in mammalian cells
    • 82 Kim, P.J., et al. Centralized modularity of N-linked glycosylation pathways in mammalian cells. PLoS ONE, 4, 2009, e7317.
    • (2009) PLoS ONE , vol.4 , pp. e7317
    • Kim, P.J.1
  • 83
    • 84947982943 scopus 로고    scopus 로고
    • A Markov chain model for N-linked protein glycosylation – towards a low-parameter tool for model-driven glycoengineering
    • 83 Spahn, P.N., et al. A Markov chain model for N-linked protein glycosylation – towards a low-parameter tool for model-driven glycoengineering. Metab. Eng. 33 (2016), 52–66.
    • (2016) Metab. Eng. , vol.33 , pp. 52-66
    • Spahn, P.N.1
  • 84
    • 33845247062 scopus 로고    scopus 로고
    • GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells
    • 84 Hossler, P., et al. GlycoVis: visualizing glycan distribution in the protein N-glycosylation pathway in mammalian cells. Biotechnol. Bioeng. 95 (2006), 947–960.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 947-960
    • Hossler, P.1
  • 85
    • 84873283704 scopus 로고    scopus 로고
    • Glycosylation network analysis toolbox: a MATLAB-based environment for systems glycobiology
    • 85 Liu, G., et al. Glycosylation network analysis toolbox: a MATLAB-based environment for systems glycobiology. Bioinformatics 29 (2013), 404–406.
    • (2013) Bioinformatics , vol.29 , pp. 404-406
    • Liu, G.1
  • 86
    • 41949134459 scopus 로고    scopus 로고
    • In silico Biochemical Reaction Network Analysis (IBRENA): a package for simulation and analysis of reaction networks
    • 86 Liu, G., Neelamegham, S., In silico Biochemical Reaction Network Analysis (IBRENA): a package for simulation and analysis of reaction networks. Bioinformatics 24 (2008), 1109–1111.
    • (2008) Bioinformatics , vol.24 , pp. 1109-1111
    • Liu, G.1    Neelamegham, S.2
  • 87
    • 84952802704 scopus 로고    scopus 로고
    • Kinetic modeling of cell metabolism for microbial production
    • 87 Costa, R.S., et al. Kinetic modeling of cell metabolism for microbial production. J. Biotechnol. 219 (2016), 126–141.
    • (2016) J. Biotechnol. , vol.219 , pp. 126-141
    • Costa, R.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.