메뉴 건너뛰기




Volumn , Issue , 2013, Pages 67-96

Cell Culture-Based Production

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84956586666     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527675272.ch03     Document Type: Chapter
Times cited : (2)

References (155)
  • 1
    • 0030932133 scopus 로고    scopus 로고
    • Immunoadhesins as research tools and therapeutic agents
    • Ashkenazi, A. and Chamow, S.M. (1997) Immunoadhesins as research tools and therapeutic agents. Curr. Opin. Immunol., 9 (2), 195-200.
    • (1997) Curr. Opin. Immunol , vol.9 , Issue.2 , pp. 195-200
    • Ashkenazi, A.1    Chamow, S.M.2
  • 3
    • 0030041799 scopus 로고    scopus 로고
    • Immunoadhesins: Principles and applications
    • Chamow, S.M. and Ashkenazi, A. (1996) Immunoadhesins: principles and applications. Trends Biotechnol., 14 (2), 52-60.
    • (1996) Trends Biotechnol , vol.14 , Issue.2 , pp. 52-60
    • Chamow, S.M.1    Ashkenazi, A.2
  • 4
    • 80052569742 scopus 로고    scopus 로고
    • Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies
    • Beck, A. and Reichert, J.M. (2011) Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies. mAbs, 3 (5), 415-416.
    • (2011) mAbs , vol.3 , Issue.5 , pp. 415-416
    • Beck, A.1    Reichert, J.M.2
  • 5
    • 84867065769 scopus 로고    scopus 로고
    • Fc-fusion proteins: New developments and future perspectives
    • Czajkowsky, D.M., Hu, J., Shao, Z., and Pleass, R.J. (2012) Fc-fusion proteins: new developments and future perspectives. EMBO Mol. Med., 4 (10), 1015-1028.
    • (2012) EMBO Mol. Med , vol.4 , Issue.10 , pp. 1015-1028
    • Czajkowsky, D.M.1    Hu, J.2    Shao, Z.3    Pleass, R.J.4
  • 6
    • 70449706366 scopus 로고    scopus 로고
    • Receptor-Fc fusion therapeutics, traps, and MIMETIBODY technology
    • Huang, C. (2009) Receptor-Fc fusion therapeutics, traps, and MIMETIBODY technology. Curr. Opin. Biotechnol., 20 (6), 692-699.
    • (2009) Curr. Opin. Biotechnol , vol.20 , Issue.6 , pp. 692-699
    • Huang, C.1
  • 7
    • 77949884124 scopus 로고    scopus 로고
    • Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: A comparative study of the affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR
    • Suzuki, T., Ishii-Watabe, A., Tada, M., Kobayashi, T., Kanayasu-Toyoda, T., Kawanishi, T., and Yamaguchi, T. (2010) Importance of neonatal FcR in regulating the serum half-life of therapeutic proteins containing the Fc domain of human IgG1: a comparative study of the affinity of monoclonal antibodies and Fc-fusion proteins to human neonatal FcR. J. Immunol., 184 (4), 1968-1976.
    • (2010) J. Immunol , vol.184 , Issue.4 , pp. 1968-1976
    • Suzuki, T.1    Ishii-Watabe, A.2    Tada, M.3    Kobayashi, T.4    Kanayasu-Toyoda, T.5    Kawanishi, T.6    Yamaguchi, T.7
  • 9
    • 84866565943 scopus 로고    scopus 로고
    • Peptibodies: A flexible alternative format to antibodies
    • Shimamoto, G., Gegg, C., Boone, T., and Queva, C. (2012) Peptibodies: a flexible alternative format to antibodies. mAbs, 4 (5), 586-591.
    • (2012) mAbs , vol.4 , Issue.5 , pp. 586-591
    • Shimamoto, G.1    Gegg, C.2    Boone, T.3    Queva, C.4
  • 11
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class Irelated receptor FcRn
    • Ghetie, V. and Ward, E.S. (2000) Multiple roles for the major histocompatibility complex class Irelated receptor FcRn. Annu. Rev. Immunol., 18, 739-766.
    • (2000) Annu. Rev. Immunol , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 13
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • Roopenian, D.C. and Akilesh, S. (2007) FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol., 7 (9), 715-725.
    • (2007) Nat. Rev. Immunol , vol.7 , Issue.9 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 15
    • 70349798567 scopus 로고    scopus 로고
    • Application of a novel affinity adsorbent for the capture and purification of recombinant Factor VIII compounds
    • McCue, J.T., Selvitelli, K., and Walker, J. (2009) Application of a novel affinity adsorbent for the capture and purification of recombinant Factor VIII compounds. J. Chromatogr. A, 1216 (45), 7824-7830.
    • (2009) J. Chromatogr. A , vol.1216 , Issue.45 , pp. 7824-7830
    • McCue, J.T.1    Selvitelli, K.2    Walker, J.3
  • 17
    • 84878862180 scopus 로고    scopus 로고
    • The impact of glycosylation on the pharmacokinetics of a TNFR2:Fc fusion protein expressed in glycoengineered Pichia pastoris
    • Liu, L., Gomathinayagam, S., Hamuro, L., Prueksaritanont, T., Wang, W., Stadheim, T.A., and Hamilton, S.R. (2013) The impact of glycosylation on the pharmacokinetics of a TNFR2:Fc fusion protein expressed in glycoengineered Pichia pastoris. Pharm. Res., 30 (3), 803-812.
    • (2013) Pharm. Res , vol.30 , Issue.3 , pp. 803-812
    • Liu, L.1    Gomathinayagam, S.2    Hamuro, L.3    Prueksaritanont, T.4    Wang, W.5    Stadheim, T.A.6    Hamilton, S.R.7
  • 18
    • 84882963173 scopus 로고    scopus 로고
    • Glycoengineered Pichiabased expression of monoclonal antibodies
    • Zha, D. (2013) Glycoengineered Pichiabased expression of monoclonal antibodies. Methods Mol. Biol., 988, 31-43.
    • (2013) Methods Mol. Biol , vol.988 , pp. 31-43
    • Zha, D.1
  • 19
    • 0034610095 scopus 로고    scopus 로고
    • Multiple cell culture factors can affect the glycosylation of Asn-in CHO-produced tissue-type plasminogen activator
    • Andersen, D.C., Bridges, T., Gawlitzek, M., and Hoy, C. (2000) Multiple cell culture factors can affect the glycosylation of Asn-in CHO-produced tissue-type plasminogen activator. Biotechnol. Bioeng., 70 (1), 25-31.
    • (2000) Biotechnol. Bioeng , vol.70 , Issue.1 , pp. 25-31
    • Andersen, D.C.1    Bridges, T.2    Gawlitzek, M.3    Hoy, C.4
  • 20
    • 0034691229 scopus 로고    scopus 로고
    • Ammonium alters N-glycan structures of recombinant TNFR-IgG: Degradative versus biosynthetic mechanisms
    • Gawlitzek, M., Ryll, T., Lofgren, J., and Sliwkowski, M.B. (2000) Ammonium alters N-glycan structures of recombinant TNFR-IgG: degradative versus biosynthetic mechanisms. Biotechnol. Bioeng., 68 (6), 637-646.
    • (2000) Biotechnol. Bioeng , vol.68 , Issue.6 , pp. 637-646
    • Gawlitzek, M.1    Ryll, T.2    Lofgren, J.3    Sliwkowski, M.B.4
  • 22
    • 84864306052 scopus 로고    scopus 로고
    • Probing of C-terminal lysine variation in a recombinant monoclonal antibody production using Chinese hamster ovary cells with chemically defined media
    • Luo, J., Zhang, J., Ren, D., Tsai, W.L., Li, F., Amanullah, A., and Hudson, T. (2012) Probing of C-terminal lysine variation in a recombinant monoclonal antibody production using Chinese hamster ovary cells with chemically defined media. Biotechnol. Bioeng., 109 (9), 2306-2315.
    • (2012) Biotechnol. Bioeng , vol.109 , Issue.9 , pp. 2306-2315
    • Luo, J.1    Zhang, J.2    Ren, D.3    Tsai, W.L.4    Li, F.5    Amanullah, A.6    Hudson, T.7
  • 23
    • 37749041309 scopus 로고    scopus 로고
    • A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior
    • Quan, C., Alcala, E., Petkovska, I., Matthews, D., Canova-Davis, E., Taticek, R., and Ma, S. (2008) A study in glycation of a therapeutic recombinant humanized monoclonal antibody: where it is, how it got there, and how it affects charge-based behavior. Anal. Biochem., 373 (2), 179-191.
    • (2008) Anal. Biochem , vol.373 , Issue.2 , pp. 179-191
    • Quan, C.1    Alcala, E.2    Petkovska, I.3    Matthews, D.4    Canova-Davis, E.5    Taticek, R.6    Ma, S.7
  • 24
    • 77957018662 scopus 로고    scopus 로고
    • Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the DHFR-based CHO cell selection system
    • Cacciatore, J.J., Chasin, L.A., and Leonard, E.F. (2010) Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the DHFR-based CHO cell selection system. Biotechnol. Adv., 28 (6), 673-681.
    • (2010) Biotechnol. Adv , vol.28 , Issue.6 , pp. 673-681
    • Cacciatore, J.J.1    Chasin, L.A.2    Leonard, E.F.3
  • 25
    • 84873782420 scopus 로고
    • Genetics of somatic mammalian cells: III. Long-term cultivation of euploid cells from human and animal subjects
    • Puck, T.T., Cieciura, S.J., and Robinson, A. (1958) Genetics of somatic mammalian cells: III. Long-term cultivation of euploid cells from human and animal subjects. J. Exp. Med., 108 (6), 945-956.
    • (1958) J. Exp. Med , vol.108 , Issue.6 , pp. 945-956
    • Puck, T.T.1    Cieciura, S.J.2    Robinson, A.3
  • 26
    • 0035810656 scopus 로고    scopus 로고
    • Metabolic control of recombinant protein N-glycan processing in NS0 and CHO cells
    • Baker, K.N., Rendall, M.H., Hills, A.E., Hoare, M., Freedman, R.B., and James, D.C. (2001) Metabolic control of recombinant protein N-glycan processing in NS0 and CHO cells. Biotechnol. Bioeng., 73 (3), 188-202.
    • (2001) Biotechnol. Bioeng , vol.73 , Issue.3 , pp. 188-202
    • Baker, K.N.1    Rendall, M.H.2    Hills, A.E.3    Hoare, M.4    Freedman, R.B.5    James, D.C.6
  • 27
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of Nglycolylneuraminic acid in recombinant therapeutic glycoproteins
    • Ghaderi, D., Taylor, R.E., Padler-Karavani, V., Diaz, S., and Varki, A. (2010) Implications of the presence of Nglycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat. Biotech., 28 (8), 863-867.
    • (2010) Nat. Biotech , vol.28 , Issue.8 , pp. 863-867
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 28
    • 84934436843 scopus 로고    scopus 로고
    • Comparability and monitoring immunogenic N-linked oligosaccharides from recombinant monoclonal antibodies from two different cell lines using HPLC with fluorescence detection and mass spectrometry
    • Kilgore, B.R., Lucka, A.W., Patel, R., Andrien, B.A., Jr., and Dhume, S.T. (2008) Comparability and monitoring immunogenic N-linked oligosaccharides from recombinant monoclonal antibodies from two different cell lines using HPLC with fluorescence detection and mass spectrometry. Methods Mol. Biol., 446, 333-346.
    • (2008) Methods Mol. Biol , vol.446 , pp. 333-346
    • Kilgore, B.R.1    Lucka, A.W.2    Patel, R.3    Andrien, B.A.4    Dhume, S.T.5
  • 29
    • 33947688082 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupolequadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion
    • Qian, J., Liu, T., Yang, L., Daus, A., Crowley, R., and Zhou, Q. (2007) Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupolequadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion. Anal. Biochem., 364 (1), 8-18.
    • (2007) Anal. Biochem , vol.364 , Issue.1 , pp. 8-18
    • Qian, J.1    Liu, T.2    Yang, L.3    Daus, A.4    Crowley, R.5    Zhou, Q.6
  • 32
    • 0028798520 scopus 로고
    • Immunogenicity of Nglycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells
    • Noguchi, A., Mukuria, C.J., Suzuki, E., and Naiki, M. (1995) Immunogenicity of Nglycolylneuraminic acid-containing carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. J. Biochem., 117 (1), 59-62.
    • (1995) J. Biochem , vol.117 , Issue.1 , pp. 59-62
    • Noguchi, A.1    Mukuria, C.J.2    Suzuki, E.3    Naiki, M.4
  • 33
    • 0032488276 scopus 로고    scopus 로고
    • Chinese hamster ovary cells with constitutively expressed sialidase antisense RNA produce recombinant DNase in batch culture with increased sialic acid
    • Ferrari, J., Gunson, J., Lofgren, J., Krummen, L., and Warner, T.G. (1998) Chinese hamster ovary cells with constitutively expressed sialidase antisense RNA produce recombinant DNase in batch culture with increased sialic acid. Biotechnol. Bioeng., 60 (5), 589-595.
    • (1998) Biotechnol. Bioeng , vol.60 , Issue.5 , pp. 589-595
    • Ferrari, J.1    Gunson, J.2    Lofgren, J.3    Krummen, L.4    Warner, T.G.5
  • 36
    • 79960209555 scopus 로고    scopus 로고
    • Enhanced sialylation of recombinant human erythropoietin in Chinese hamster ovary cells by combinatorial engineering of selected genes
    • Son, Y.D., Jeong, Y.T., Park, S.Y., and Kim, J.H. (2011) Enhanced sialylation of recombinant human erythropoietin in Chinese hamster ovary cells by combinatorial engineering of selected genes. Glycobiology, 21 (8), 1019-1028.
    • (2011) Glycobiology , vol.21 , Issue.8 , pp. 1019-1028
    • Son, Y.D.1    Jeong, Y.T.2    Park, S.Y.3    Kim, J.H.4
  • 38
    • 0034708736 scopus 로고    scopus 로고
    • Loss of Nglycolylneuraminic acid in human evolution: Implications for sialic acid recognition by siglecs
    • Brinkman-Van der Linden, E.C., Sjoberg, E.R., Juneja, L.R., Crocker, P.R., Varki, N., and Varki, A. (2000) Loss of Nglycolylneuraminic acid in human evolution: implications for sialic acid recognition by siglecs. J. Biol. Chem., 275 (12), 8633-8640.
    • (2000) J. Biol. Chem , vol.275 , Issue.12 , pp. 8633-8640
    • Brinkman-Van der Linden, E.C.1    Sjoberg, E.R.2    Juneja, L.R.3    Crocker, P.R.4    Varki, N.5    Varki, A.6
  • 40
    • 0027460941 scopus 로고
    • Expression of recombinant vitamin K-dependent proteins in mammalian cells: Factors IX and VII
    • Berkner, K.L. (1993) Expression of recombinant vitamin K-dependent proteins in mammalian cells: factors IX and VII. Methods Enzymol., 222, 450-477.
    • (1993) Methods Enzymol , vol.222 , pp. 450-477
    • Berkner, K.L.1
  • 42
    • 60549105996 scopus 로고    scopus 로고
    • A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies
    • Lee, C.J., Seth, G., Tsukuda, J., and Hamilton, R.W. (2009) A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies. Biotechnol. Bioeng., 102 (4), 1107-1118.
    • (2009) Biotechnol. Bioeng , vol.102 , Issue.4 , pp. 1107-1118
    • Lee, C.J.1    Seth, G.2    Tsukuda, J.3    Hamilton, R.W.4
  • 43
    • 84859632710 scopus 로고    scopus 로고
    • Highthroughput analysis of intraclonal variability of glycoprotein sialylation
    • Markely, L.R. and Wang, D.I. (2012) Highthroughput analysis of intraclonal variability of glycoprotein sialylation. Biotechnol. Prog., 28 (2), 591-594.
    • (2012) Biotechnol. Prog , vol.28 , Issue.2 , pp. 591-594
    • Markely, L.R.1    Wang, D.I.2
  • 44
    • 84868139133 scopus 로고    scopus 로고
    • Improvement in accuracy and specificity of high-throughput sialic acid assay
    • Markely, L.R.A., Jonnalagadda, K.N., Sinacore, M., Ryll, T., and Prajapati, S. (2012) Improvement in accuracy and specificity of high-throughput sialic acid assay. Anal. Methods, 4 (11), 3565-3569.
    • (2012) Anal. Methods , vol.4 , Issue.11 , pp. 3565-3569
    • Markely, L.R.A.1    Jonnalagadda, K.N.2    Sinacore, M.3    Ryll, T.4    Prajapati, S.5
  • 45
    • 79955591082 scopus 로고    scopus 로고
    • A high-throughput microchip-based glycan screening assay for antibody cell culture samples
    • Primack, J., Flynn, G.C., and Pan, H. (2011) A high-throughput microchip-based glycan screening assay for antibody cell culture samples. Electrophoresis, 32 (10), 1129-1132.
    • (2011) Electrophoresis , vol.32 , Issue.10 , pp. 1129-1132
    • Primack, J.1    Flynn, G.C.2    Pan, H.3
  • 46
    • 27844435168 scopus 로고    scopus 로고
    • The bioreactor: A powerful tool for large-scale culture of animal cells
    • Wang, D., Liu, W., Han, B., and Xu, R. (2005) The bioreactor: a powerful tool for large-scale culture of animal cells. Curr. Pharm. Biotechnol., 6 (5), 397-403.
    • (2005) Curr. Pharm. Biotechnol , vol.6 , Issue.5 , pp. 397-403
    • Wang, D.1    Liu, W.2    Han, B.3    Xu, R.4
  • 47
    • 33745807268 scopus 로고    scopus 로고
    • Bioreactor systems for the production of biopharmaceuticals from animal cells
    • Warnock, J.N. and Al-Rubeai, M. (2006) Bioreactor systems for the production of biopharmaceuticals from animal cells. Biotechnol. Appl. Biochem., 45, 1-12.
    • (2006) Biotechnol. Appl. Biochem , vol.45 , pp. 1-12
    • Warnock, J.N.1    Al-Rubeai, M.2
  • 48
    • 77149175420 scopus 로고    scopus 로고
    • Disposable bioreactors: The current state-of-the-art and recommended applications in biotechnology
    • Eibl, R., Kaiser, S., Lombriser, R., and Eibl, D. (2010) Disposable bioreactors: the current state-of-the-art and recommended applications in biotechnology. Appl. Microbiol. Biotechnol., 86 (1), 41-49.
    • (2010) Appl. Microbiol. Biotechnol , vol.86 , Issue.1 , pp. 41-49
    • Eibl, R.1    Kaiser, S.2    Lombriser, R.3    Eibl, D.4
  • 49
    • 84988826351 scopus 로고    scopus 로고
    • Dynamic single-use bioreactors used in modern liter-and m3-scale biotechnological processes: Engineering characteristics and scaling up
    • Loffelholz, C., Kaiser, S.C., Kraume, M., Eibl, R., and Eibl, D. (2013) Dynamic single-use bioreactors used in modern liter-and m3-scale biotechnological processes: engineering characteristics and scaling up. Adv. Biochem. Eng. Biotechnol. doi: 10.1007/10_2013_187
    • (2013) Adv. Biochem. Eng. Biotechnol
    • Loffelholz, C.1    Kaiser, S.C.2    Kraume, M.3    Eibl, R.4    Eibl, D.5
  • 50
    • 84875253542 scopus 로고    scopus 로고
    • Single-use disposable technologies for biopharmaceutical manufacturing
    • Shukla, A.A. and Gottschalk, U. (2013) Single-use disposable technologies for biopharmaceutical manufacturing. Trends Biotechnol., 31 (3), 147-154.
    • (2013) Trends Biotechnol , vol.31 , Issue.3 , pp. 147-154
    • Shukla, A.A.1    Gottschalk, U.2
  • 52
    • 80053542109 scopus 로고    scopus 로고
    • Performance of high intensity fed-batch mammalian cell cultures in disposable bioreactor systems
    • Smelko, J.P., Wiltberger, K.R., Hickman, E.F., Morris, B.J., Blackburn, T.J., and Ryll, T. (2011) Performance of high intensity fed-batch mammalian cell cultures in disposable bioreactor systems. Biotechnol. Prog., 27 (5), 1358-1364.
    • (2011) Biotechnol. Prog , vol.27 , Issue.5 , pp. 1358-1364
    • Smelko, J.P.1    Wiltberger, K.R.2    Hickman, E.F.3    Morris, B.J.4    Blackburn, T.J.5    Ryll, T.6
  • 53
    • 77955934625 scopus 로고    scopus 로고
    • An improved manufacturing process for Xyntha/ReFacto AF
    • Kelley, B., Jankowski, M., and Booth, J. (2010) An improved manufacturing process for Xyntha/ReFacto AF. Haemophilia, 16 (5), 717-725.
    • (2010) Haemophilia , vol.16 , Issue.5 , pp. 717-725
    • Kelley, B.1    Jankowski, M.2    Booth, J.3
  • 54
    • 1542650080 scopus 로고    scopus 로고
    • The state of biopharmaceutical manufacturing
    • Molowa, D.T. and Mazanet, R. (2003) The state of biopharmaceutical manufacturing. Biotechnol. Annu. Rev., 9, 285-302.
    • (2003) Biotechnol. Annu. Rev , vol.9 , pp. 285-302
    • Molowa, D.T.1    Mazanet, R.2
  • 55
    • 0033758021 scopus 로고    scopus 로고
    • Transgenic plants as factories for biopharmaceuticals
    • Giddings, G., Allison, G., Brooks, D., and Carter, A. (2000) Transgenic plants as factories for biopharmaceuticals. Nat. Biotechnol., 18 (11), 1151-1155.
    • (2000) Nat. Biotechnol , vol.18 , Issue.11 , pp. 1151-1155
    • Giddings, G.1    Allison, G.2    Brooks, D.3    Carter, A.4
  • 56
    • 0028235475 scopus 로고
    • Production of pharmaceutical proteins from transgenic animals
    • Houdebine, L.-M. (1994) Production of pharmaceutical proteins from transgenic animals. J. Biotechnol., 34 (3), 269-287.
    • (1994) J. Biotechnol , vol.34 , Issue.3 , pp. 269-287
    • Houdebine, L.-M.1
  • 57
    • 0031555505 scopus 로고    scopus 로고
    • Production of recombinant proteins in transgenic plants: Practical considerations
    • Kusnadi, A.R., Nikolov, Z.L., and Howard, J.A. (1997) Production of recombinant proteins in transgenic plants: practical considerations. Biotechnol. Bioeng., 56 (5), 473-484.
    • (1997) Biotechnol. Bioeng , vol.56 , Issue.5 , pp. 473-484
    • Kusnadi, A.R.1    Nikolov, Z.L.2    Howard, J.A.3
  • 58
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology: The bioprocessing industry at a crossroads
    • Kelley, B. (2009) Industrialization of mAb production technology: the bioprocessing industry at a crossroads. mAbs, 1 (5), 443-452.
    • (2009) mAbs , vol.1 , Issue.5 , pp. 443-452
    • Kelley, B.1
  • 59
    • 79954613316 scopus 로고    scopus 로고
    • High-end pH-controlled delivery of glucose effectively suppresses lactate accumulation in CHO fed-batch cultures
    • Gagnon, M., Hiller, G., Luan, Y.T., Kittredge, A., DeFelice, J., and Drapeau, D. (2011) High-end pH-controlled delivery of glucose effectively suppresses lactate accumulation in CHO fed-batch cultures. Biotechnol. Bioeng., 108 (6), 1328-1337.
    • (2011) Biotechnol. Bioeng , vol.108 , Issue.6 , pp. 1328-1337
    • Gagnon, M.1    Hiller, G.2    Luan, Y.T.3    Kittredge, A.4    DeFelice, J.5    Drapeau, D.6
  • 60
    • 79952202624 scopus 로고    scopus 로고
    • Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment
    • Huang, Y.M., Hu, W.W., Rustandi, E., Chang, K., Yusuf-Makagiansar, H., and Ryll, T. (2010) Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment. Biotechnol. Prog., 26 (5), 1400-1410.
    • (2010) Biotechnol. Prog , vol.26 , Issue.5 , pp. 1400-1410
    • Huang, Y.M.1    Hu, W.W.2    Rustandi, E.3    Chang, K.4    Yusuf-Makagiansar, H.5    Ryll, T.6
  • 61
    • 84869875529 scopus 로고    scopus 로고
    • Automated dynamic fed-batch process and media optimization for high productivity cell culture process development
    • Lu, F., Toh, P.C., Burnett, I., Li, F., Hudson, T., Amanullah, A., and Li, J. (2013) Automated dynamic fed-batch process and media optimization for high productivity cell culture process development. Biotechnol. Bioeng., 110 (1), 191-205.
    • (2013) Biotechnol. Bioeng , vol.110 , Issue.1 , pp. 191-205
    • Lu, F.1    Toh, P.C.2    Burnett, I.3    Li, F.4    Hudson, T.5    Amanullah, A.6    Li, J.7
  • 62
    • 79953126805 scopus 로고    scopus 로고
    • Understanding the intracellular effect of enhanced nutrient feeding toward high titer antibody production process
    • Yu, M., Hu, Z., Pacis, E., Vijayasankaran, N., Shen, A., and Li, F. (2011) Understanding the intracellular effect of enhanced nutrient feeding toward high titer antibody production process. Biotechnol. Bioeng., 108 (5), 1078-1088.
    • (2011) Biotechnol. Bioeng , vol.108 , Issue.5 , pp. 1078-1088
    • Yu, M.1    Hu, Z.2    Pacis, E.3    Vijayasankaran, N.4    Shen, A.5    Li, F.6
  • 63
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm, F.M. (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol., 22 (11), 1393-1398.
    • (2004) Nat. Biotechnol , vol.22 , Issue.11 , pp. 1393-1398
    • Wurm, F.M.1
  • 64
    • 84890246618 scopus 로고    scopus 로고
    • A generic growth test method for improving quality control of disposables in industrial cell culture
    • Horvath, B., Tsang, V.L., Lin, W., Dai, X., Kunas, K., and Frank, G. (2013) A generic growth test method for improving quality control of disposables in industrial cell culture. Biopharm. Int., 26 (6), 34-41.
    • (2013) Biopharm. Int , vol.26 , Issue.6 , pp. 34-41
    • Horvath, B.1    Tsang, V.L.2    Lin, W.3    Dai, X.4    Kunas, K.5    Frank, G.6
  • 66
    • 0037277056 scopus 로고    scopus 로고
    • Comparison of batch and perfusion culture in combination with pilot-scale expanded bed purification for the production of soluble recombinant beta-secretase
    • Lullau, E., Kanttinen, A., Hassel, J., Berg, M., Haag-Alvarsson, A., Cederbrant, K., Greenberg, B., Fenge, C., and Schweikart, F. (2003) Comparison of batch and perfusion culture in combination with pilot-scale expanded bed purification for the production of soluble recombinant beta-secretase. Biotechnol. Prog., 19 (1), 37-44.
    • (2003) Biotechnol. Prog , vol.19 , Issue.1 , pp. 37-44
    • Lullau, E.1    Kanttinen, A.2    Hassel, J.3    Berg, M.4    Haag-Alvarsson, A.5    Cederbrant, K.6    Greenberg, B.7    Fenge, C.8    Schweikart, F.9
  • 67
    • 84869877665 scopus 로고    scopus 로고
    • Fed-batch and perfusion culture processes: Economic, environmental, and operational feasibility under uncertainty
    • Pollock, J., Ho, S.V., and Farid, S.S. (2013) Fed-batch and perfusion culture processes: economic, environmental, and operational feasibility under uncertainty. Biotechnol. Bioeng., 110 (1), 206-219.
    • (2013) Biotechnol. Bioeng , vol.110 , Issue.1 , pp. 206-219
    • Pollock, J.1    Ho, S.V.2    Farid, S.S.3
  • 68
    • 0034238099 scopus 로고    scopus 로고
    • Performance of small-scale CHO perfusion cultures using an acoustic cell filtration device for cell retention: Characterization of separation ef ficiency and impact of perfusion on product quality
    • Ryll, T., Dutina, G., Reyes, A., Gunson, J., Krummen, L., and Etcheverry, T. (2000) Performance of small-scale CHO perfusion cultures using an acoustic cell filtration device for cell retention: characterization of separation ef ficiency and impact of perfusion on product quality. Biotechnol. Bioeng., 69 (4), 440-449.
    • (2000) Biotechnol. Bioeng , vol.69 , Issue.4 , pp. 440-449
    • Ryll, T.1    Dutina, G.2    Reyes, A.3    Gunson, J.4    Krummen, L.5    Etcheverry, T.6
  • 70
    • 85019788903 scopus 로고    scopus 로고
    • (accessed June 21, 2013)
    • Crucell (2013) http://www.crucell.com/ Technology_-_Cell_Technology_-_Applications_-_Proteins (accessed June 21, 2013).
    • (2013)
    • Crucell1
  • 71
    • 0032949506 scopus 로고    scopus 로고
    • Reactor design for large scale suspension animal cell culture
    • Varley, J. and Birch, J. (1999) Reactor design for large scale suspension animal cell culture. Cytotechnology, 29 (3), 177-205.
    • (1999) Cytotechnology , vol.29 , Issue.3 , pp. 177-205
    • Varley, J.1    Birch, J.2
  • 75
    • 68149137219 scopus 로고    scopus 로고
    • Physiological responses of CHO cells to repetitive hydrodynamic stress
    • Godoy-Silva, R., Chalmers, J.J., Casnocha, S.A., Bass, L.A., and Ma, N. (2009) Physiological responses of CHO cells to repetitive hydrodynamic stress. Biotechnol. Bioeng., 103 (6), 1103-1117.
    • (2009) Biotechnol. Bioeng , vol.103 , Issue.6 , pp. 1103-1117
    • Godoy-Silva, R.1    Chalmers, J.J.2    Casnocha, S.A.3    Bass, L.A.4    Ma, N.5
  • 76
    • 84655167606 scopus 로고    scopus 로고
    • The potential of hydrodynamic damage to animal cells of industrial relevance: Current understanding
    • Hu, W., Berdugo, C., and Chalmers, J.J. (2011) The potential of hydrodynamic damage to animal cells of industrial relevance: current understanding. Cytotechnology, 63 (5), 445-460.
    • (2011) Cytotechnology , vol.63 , Issue.5 , pp. 445-460
    • Hu, W.1    Berdugo, C.2    Chalmers, J.J.3
  • 77
    • 50049088107 scopus 로고    scopus 로고
    • An investigation of small-molecule surfactants to potentially replace pluronic F-68 for reducing bubble-associated cell damage
    • Hu, W., Rathman, J.J., and Chalmers, J.J. (2008) An investigation of small-molecule surfactants to potentially replace pluronic F-68 for reducing bubble-associated cell damage. Biotechnol. Bioeng., 101 (1), 119-127.
    • (2008) Biotechnol. Bioeng , vol.101 , Issue.1 , pp. 119-127
    • Hu, W.1    Rathman, J.J.2    Chalmers, J.J.3
  • 78
    • 33749130483 scopus 로고    scopus 로고
    • The cultivation of animal cells at controlled dissolved oxygen partial pressure
    • Kilburn, D.G. and Webb, F.C. (2000) The cultivation of animal cells at controlled dissolved oxygen partial pressure. Biotechnol. Bioeng., 67 (6), 657-670.
    • (2000) Biotechnol. Bioeng , vol.67 , Issue.6 , pp. 657-670
    • Kilburn, D.G.1    Webb, F.C.2
  • 79
    • 4043130854 scopus 로고    scopus 로고
    • Quantitative studies of cell-bubble interactions and cell damage at different pluronic F-68 and cell concentrations
    • Ma, N., Chalmers, J.J., Aunins, J.G., Zhou, W., and Xie, L. (2004) Quantitative studies of cell-bubble interactions and cell damage at different pluronic F-68 and cell concentrations. Biotechnol. Prog., 20 (4), 1183-1191.
    • (2004) Biotechnol. Prog , vol.20 , Issue.4 , pp. 1183-1191
    • Ma, N.1    Chalmers, J.J.2    Aunins, J.G.3    Zhou, W.4    Xie, L.5
  • 80
    • 55549108737 scopus 로고    scopus 로고
    • NS0 cell damage by high gas velocity sparging in protein-free and cholesterol-free cultures
    • Zhu, Y., Cuenca, J.V., Zhou, W., and Varma, A. (2008) NS0 cell damage by high gas velocity sparging in protein-free and cholesterol-free cultures. Biotechnol. Bioeng., 101 (4), 751-760.
    • (2008) Biotechnol. Bioeng , vol.101 , Issue.4 , pp. 751-760
    • Zhu, Y.1    Cuenca, J.V.2    Zhou, W.3    Varma, A.4
  • 81
    • 84893793023 scopus 로고    scopus 로고
    • Effects of bubble-liquid two-phase turbulent hydrodynamics on cell damage in sparged bioreactor
    • Yang, L., Hu, W., Wiltberger, K., Ryll, T., and Li, F. (2013) Effects of bubble-liquid two-phase turbulent hydrodynamics on cell damage in sparged bioreactor. Biotechnol. Prog. doi: 10.1002/btpr.1790.
    • (2013) Biotechnol. Prog
    • Yang, L.1    Hu, W.2    Wiltberger, K.3    Ryll, T.4    Li, F.5
  • 82
    • 77950877204 scopus 로고    scopus 로고
    • Application of nearinfrared (NIR) spectroscopy for screening of raw materials used in the cell culture medium for the production of a recombinant therapeutic protein
    • Kirdar, A.O., Chen, G., Weidner, J., and Rathore, A.S. (2010) Application of nearinfrared (NIR) spectroscopy for screening of raw materials used in the cell culture medium for the production of a recombinant therapeutic protein. Biotechnol. Prog., 26 (2), 527-531.
    • (2010) Biotechnol. Prog , vol.26 , Issue.2 , pp. 527-531
    • Kirdar, A.O.1    Chen, G.2    Weidner, J.3    Rathore, A.S.4
  • 83
    • 84878863603 scopus 로고    scopus 로고
    • Screening soy hydrolysates for the production of a recombinant therapeutic protein in commercial cell line by combined approach of near-infrared spectroscopy and chemometrics
    • Li, G. and Wen, Z.-q. (2013) Screening soy hydrolysates for the production of a recombinant therapeutic protein in commercial cell line by combined approach of near-infrared spectroscopy and chemometrics. Appl. Microbiol. Biotechnol., 97 (6), 2653-2660.
    • (2013) Appl. Microbiol. Biotechnol , vol.97 , Issue.6 , pp. 2653-2660
    • Li, G.1    Wen, Z.-q.2
  • 84
    • 34547637286 scopus 로고    scopus 로고
    • Combined approach of NMR and chemometrics for screening peptones used in the cell culture medium for the production of a recombinant therapeutic protein
    • Luo, Y. and Chen, G. (2007) Combined approach of NMR and chemometrics for screening peptones used in the cell culture medium for the production of a recombinant therapeutic protein. Biotechnol. Bioeng., 97 (6), 1654-1659.
    • (2007) Biotechnol. Bioeng , vol.97 , Issue.6 , pp. 1654-1659
    • Luo, Y.1    Chen, G.2
  • 85
    • 0026039271 scopus 로고
    • Nutrient optimization for high density biological production applications
    • Jayme, D.W. (1991) Nutrient optimization for high density biological production applications. Cytotechnology, 5 (1), 15-30.
    • (1991) Cytotechnology , vol.5 , Issue.1 , pp. 15-30
    • Jayme, D.W.1
  • 86
    • 0030583232 scopus 로고    scopus 로고
    • The protein hydrolysate, Primatone RL, is a costeffective multiple growth promoter of mammalian cell culture in serumcontaining and serum-free media and displays anti-apoptosis properties
    • Schlaeger, E.J. (1996) The protein hydrolysate, Primatone RL, is a costeffective multiple growth promoter of mammalian cell culture in serumcontaining and serum-free media and displays anti-apoptosis properties. J. Immunol. Methods, 194 (2), 191-199.
    • (1996) J. Immunol. Methods , vol.194 , Issue.2 , pp. 191-199
    • Schlaeger, E.J.1
  • 87
    • 0031615735 scopus 로고    scopus 로고
    • Raw materials as a source of contamination in large-scale cell culture
    • (eds F. Brown, E. Griffiths, F. Horaud, and J.C. Petriccianipp), S Karger Pub
    • Garnick, R.L. (1998) Raw materials as a source of contamination in large-scale cell culture, in Safety of Biological Products Prepared from Mammalian Cell Culture (eds F. Brown, E. Griffiths, F. Horaud, and J.C. Petriccianipp), vol. 93, S Karger Pub, pp. 21-29.
    • (1998) Safety of Biological Products Prepared from Mammalian Cell Culture , vol.93 , pp. 21-29
    • Garnick, R.L.1
  • 88
    • 18344416903 scopus 로고    scopus 로고
    • The use of peptones as medium additives for the production of a recombinant therapeutic protein in high density perfusion cultures of mammalian cells
    • Heidemann, R., Zhang, C., Qi, H., Larrick Rule, J., Rozales, C., Park, S., Chuppa, S., Ray, M., Michaels, J., Konstantinov, K., and Naveh, D. (2000) The use of peptones as medium additives for the production of a recombinant therapeutic protein in high density perfusion cultures of mammalian cells. Cytotechnology, 32 (2), 157-167.
    • (2000) Cytotechnology , vol.32 , Issue.2 , pp. 157-167
    • Heidemann, R.1    Zhang, C.2    Qi, H.3    Larrick Rule, J.4    Rozales, C.5    Park, S.6    Chuppa, S.7    Ray, M.8    Michaels, J.9    Konstantinov, K.10    Naveh, D.11
  • 91
    • 77956970513 scopus 로고    scopus 로고
    • Quantitative modeling of viable cell density, cell size, intracellular conductivity, and membrane capacitance in batch and fed-batch CHO processes using dielectric spectroscopy
    • Opel, C.F., Li, J., and Amanullah, A. (2010) Quantitative modeling of viable cell density, cell size, intracellular conductivity, and membrane capacitance in batch and fed-batch CHO processes using dielectric spectroscopy. Biotechnol. Prog., 26 (4), 1187-1199.
    • (2010) Biotechnol. Prog , vol.26 , Issue.4 , pp. 1187-1199
    • Opel, C.F.1    Li, J.2    Amanullah, A.3
  • 92
    • 79953152705 scopus 로고    scopus 로고
    • Real time monitoring of multiple parameters in mammalian cell culture bioreactors using an in-line Raman spectroscopy probe
    • Abu-Absi, N.R., Kenty, B.M., Cuellar, M.E., Borys, M.C., Sakhamuri, S., Strachan, D.J., Hausladen, M.C., and Li, Z.J. (2011) Real time monitoring of multiple parameters in mammalian cell culture bioreactors using an in-line Raman spectroscopy probe. Biotechnol. Bioeng., 108 (5), 1215-1221.
    • (2011) Biotechnol. Bioeng , vol.108 , Issue.5 , pp. 1215-1221
    • Abu-Absi, N.R.1    Kenty, B.M.2    Cuellar, M.E.3    Borys, M.C.4    Sakhamuri, S.5    Strachan, D.J.6    Hausladen, M.C.7    Li, Z.J.8
  • 93
    • 77954640700 scopus 로고    scopus 로고
    • Fermentanomics: Monitoring mammalian cell cultures with NMR spectroscopy
    • Bradley, S.A., Ouyang, A., Purdie, J., Smitka, T.A., Wang, T., and Kaerner, A. (2010) Fermentanomics: monitoring mammalian cell cultures with NMR spectroscopy. J. Am. Chem. Soc., 132 (28), 9531-9533.
    • (2010) J. Am. Chem. Soc , vol.132 , Issue.28 , pp. 9531-9533
    • Bradley, S.A.1    Ouyang, A.2    Purdie, J.3    Smitka, T.A.4    Wang, T.5    Kaerner, A.6
  • 94
    • 80053899041 scopus 로고    scopus 로고
    • Predicting Mab product yields from cultivation media components, using nearinfrared and 2D-fluorescence spectroscopies
    • Jose, G.E., Folque, F., Menezes, J.C., Werz, S., Strauss, U., and Hakemeyer, C. (2011) Predicting Mab product yields from cultivation media components, using nearinfrared and 2D-fluorescence spectroscopies. Biotechnol. Prog., 27 (5), 1339-1346.
    • (2011) Biotechnol. Prog , vol.27 , Issue.5 , pp. 1339-1346
    • Jose, G.E.1    Folque, F.2    Menezes, J.C.3    Werz, S.4    Strauss, U.5    Hakemeyer, C.6
  • 95
    • 78149237599 scopus 로고    scopus 로고
    • Rapid characterization and quality control of complex cell culture media solutions using Raman spectroscopy and chemometrics
    • Li, B., Ryan, P.W., Ray, B.H., Leister, K.J., Sirimuthu, N.M.S., and Ryder, A.G. (2010) Rapid characterization and quality control of complex cell culture media solutions using Raman spectroscopy and chemometrics. Biotechnol. Bioeng., 107 (2), 290-301.
    • (2010) Biotechnol. Bioeng , vol.107 , Issue.2 , pp. 290-301
    • Li, B.1    Ryan, P.W.2    Ray, B.H.3    Leister, K.J.4    Sirimuthu, N.M.S.5    Ryder, A.G.6
  • 97
    • 72449187333 scopus 로고    scopus 로고
    • Global antibody development trends
    • Reichert, J.M. (2009) Global antibody development trends. mAbs, 1 (1), 86-87.
    • (2009) mAbs , vol.1 , Issue.1 , pp. 86-87
    • Reichert, J.M.1
  • 98
    • 67649851892 scopus 로고    scopus 로고
    • mAbs: A business perspective
    • Scolnik, P.A. (2009) mAbs: a business perspective. mAbs, 1 (2), 179-184.
    • (2009) mAbs , vol.1 , Issue.2 , pp. 179-184
    • Scolnik, P.A.1
  • 100
  • 101
    • 84945467389 scopus 로고    scopus 로고
    • Immunex Corporation, assignee. US Patent No. 7,294,481 B1
    • Fung, V.P. (inventor(s) (2007) Method for producing recombinant proteins. Immunex Corporation, assignee. US Patent No. 7,294,481 B1.
    • (2007) Method for producing recombinant proteins
    • Fung, V.P.1
  • 102
    • 34447296997 scopus 로고    scopus 로고
    • Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys
    • Jones, A.J.S., Papac, D.I., Chin, E.H., Keck, R., Baughman, S.A., Lin, Y.S., Kneer, J., and Battersby, J.E. (2007) Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys. Glycobiology, 17 (5), 529-540.
    • (2007) Glycobiology , vol.17 , Issue.5 , pp. 529-540
    • Jones, A.J.S.1    Papac, D.I.2    Chin, E.H.3    Keck, R.4    Baughman, S.A.5    Lin, Y.S.6    Kneer, J.7    Battersby, J.E.8
  • 103
    • 38349175313 scopus 로고    scopus 로고
    • Characterization of a complex glycoprotein whose variable metabolic clearance in humans is dependent on terminal N-acetylglucosamine content
    • Keck, R., Nayak, N., Lerner, L., Raju, S., Ma, S., Schreitmueller, T., Chamow, S., Moorhouse, K., Kotts, C., and Jones, A. (2008) Characterization of a complex glycoprotein whose variable metabolic clearance in humans is dependent on terminal N-acetylglucosamine content. Biologicals, 36 (1), 49-60.
    • (2008) Biologicals , vol.36 , Issue.1 , pp. 49-60
    • Keck, R.1    Nayak, N.2    Lerner, L.3    Raju, S.4    Ma, S.5    Schreitmueller, T.6    Chamow, S.7    Moorhouse, K.8    Kotts, C.9    Jones, A.10
  • 105
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell, G. and Harford, J. (1982) Carbohydrate-specific receptors of the liver. Annu. Rev. Biochem., 51, 531-554.
    • (1982) Annu. Rev. Biochem , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 106
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • Stockert, R.J. (1995) The asialoglycoprotein receptor: relationships between structure, function, and expression. Physiol. Rev., 75 (3), 591-609.
    • (1995) Physiol. Rev , vol.75 , Issue.3 , pp. 591-609
    • Stockert, R.J.1
  • 107
    • 84990438221 scopus 로고
    • Fluorophore-labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
    • Flesher, A.R., Marzowski, J., Wang, W.C., and Raff, H.V. (1995) Fluorophore-labeled carbohydrate analysis of immunoglobulin fusion proteins: correlation of oligosaccharide content with in vivo clearance profile. Biotechnol. Bioeng., 47 (3), 405-405.
    • (1995) Biotechnol. Bioeng , vol.47 , Issue.3 , pp. 405-405
    • Flesher, A.R.1    Marzowski, J.2    Wang, W.C.3    Raff, H.V.4
  • 108
    • 0029548335 scopus 로고
    • Immunomodulation by LFA3TIP, an LFA-3/IgG1 fusion protein: Cell line dependent glycosylation effects on pharmacokinetics and pharmacodynamic markers
    • Meier, W., Gill, A., Rogge, M., Dabora, R., Majeau, G.R., Oleson, F.B., Jones, W.E., Frazier, D., Miatkowski, K., and Hochman, P.S. (1995) Immunomodulation by LFA3TIP, an LFA-3/IgG1 fusion protein: cell line dependent glycosylation effects on pharmacokinetics and pharmacodynamic markers. Ther. Immunol., 2 (3), 159-171.
    • (1995) Ther. Immunol , vol.2 , Issue.3 , pp. 159-171
    • Meier, W.1    Gill, A.2    Rogge, M.3    Dabora, R.4    Majeau, G.R.5    Oleson, F.B.6    Jones, W.E.7    Frazier, D.8    Miatkowski, K.9    Hochman, P.S.10
  • 109
    • 0025974324 scopus 로고
    • Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells
    • Thotakura, N.R., Desai, R.K., Bates, L.G., Cole, E.S., Pratt, B.M., and Weintraub, B. D. (1991) Biological activity and metabolic clearance of a recombinant human thyrotropin produced in Chinese hamster ovary cells. Endocrinology, 128 (1), 341-348.
    • (1991) Endocrinology , vol.128 , Issue.1 , pp. 341-348
    • Thotakura, N.R.1    Desai, R.K.2    Bates, L.G.3    Cole, E.S.4    Pratt, B.M.5    Weintraub, B.D.6
  • 110
    • 0027910071 scopus 로고
    • Temperature control of growth and productivity in mutant Chinese hamster ovary cells synthesizing a recombinant protein
    • Jenkins, N. and Hovey, A. (1993) Temperature control of growth and productivity in mutant Chinese hamster ovary cells synthesizing a recombinant protein. Biotechnol. Bioeng., 42 (9), 1029-1036.
    • (1993) Biotechnol. Bioeng , vol.42 , Issue.9 , pp. 1029-1036
    • Jenkins, N.1    Hovey, A.2
  • 111
    • 0028708951 scopus 로고
    • Low temperature cultivation: A step towards process optimisation
    • Weidemann, R., Ludwig, A., and Kretzmer, G. (1994) Low temperature cultivation: a step towards process optimisation. Cytotechnology, 15 (1-3), 111-116.
    • (1994) Cytotechnology , vol.15 , Issue.1-3 , pp. 111-116
    • Weidemann, R.1    Ludwig, A.2    Kretzmer, G.3
  • 112
    • 0030891616 scopus 로고    scopus 로고
    • Effects of temperature shift on cell cycle, apoptosis and nucleotide pools in CHO cell batch cultures
    • Moore, A., Mercer, J., Dutina, G., Donahue, C.J., Bauer, K.D., Mather, J.P., Etcheverry, T., and Ryll, T. (1997) Effects of temperature shift on cell cycle, apoptosis and nucleotide pools in CHO cell batch cultures. Cytotechnology, 23 (1-3), 47-54.
    • (1997) Cytotechnology , vol.23 , Issue.1-3 , pp. 47-54
    • Moore, A.1    Mercer, J.2    Dutina, G.3    Donahue, C.J.4    Bauer, K.D.5    Mather, J.P.6    Etcheverry, T.7    Ryll, T.8
  • 113
    • 0026147822 scopus 로고
    • Effect of medium osmolarity on hybridoma growth, metabolism, and antibody production
    • Ozturk, S.S. and Palsson, B.O. (1991) Effect of medium osmolarity on hybridoma growth, metabolism, and antibody production. Biotechnol. Bioeng., 37 (10), 989-993.
    • (1991) Biotechnol. Bioeng , vol.37 , Issue.10 , pp. 989-993
    • Ozturk, S.S.1    Palsson, B.O.2
  • 114
    • 0009668445 scopus 로고    scopus 로고
    • Hyperosmotic pressure enhances immunoglobulin transcription rates and secretion rates of KR12H-2 transfectoma
    • Lee, M.S. and Lee, G.M. (2000) Hyperosmotic pressure enhances immunoglobulin transcription rates and secretion rates of KR12H-2 transfectoma. Biotechnol. Bioeng., 68 (3), 260-268.
    • (2000) Biotechnol. Bioeng , vol.68 , Issue.3 , pp. 260-268
    • Lee, M.S.1    Lee, G.M.2
  • 115
    • 0024404910 scopus 로고
    • Increased synthesis of secreted proteins induces expression of glucoseregulated proteins in butyrate-treated Chinese hamster ovary cells
    • Dorner, A.J., Wasley, L.C., and Kaufman, R.J. (1989) Increased synthesis of secreted proteins induces expression of glucoseregulated proteins in butyrate-treated Chinese hamster ovary cells. J. Biol. Chem., 264 (34), 20602-20607.
    • (1989) J. Biol. Chem , vol.264 , Issue.34 , pp. 20602-20607
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 116
    • 0021101284 scopus 로고
    • Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate
    • Gorman, C.M., Howard, B.H., and Reeves, R. (1983) Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate. Nucleic Acids Res., 11 (21), 7631-7648.
    • (1983) Nucleic Acids Res , vol.11 , Issue.21 , pp. 7631-7648
    • Gorman, C.M.1    Howard, B.H.2    Reeves, R.3
  • 117
    • 0025860171 scopus 로고
    • Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression
    • Palermo, D.P., DeGraaf, M.E., Marotti, K. R., Rehberg, E., and Post, L.E. (1991) Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression. J. Biotechnol., 19 (1), 35-47.
    • (1991) J. Biotechnol , vol.19 , Issue.1 , pp. 35-47
    • Palermo, D.P.1    DeGraaf, M.E.2    Marotti, K.R.3    Rehberg, E.4    Post, L.E.5
  • 118
    • 35948983828 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors decrease Toll-like receptormediated activation of proinflammatory gene expression by impairing transcription factor recruitment
    • Bode, K.A., Schroder, K., Hume, D.A., Ravasi, T., Heeg, K., Sweet, M.J., and Dalpke, A.H. (2007) Histone deacetylase inhibitors decrease Toll-like receptormediated activation of proinflammatory gene expression by impairing transcription factor recruitment. Immunology, 122 (4), 596-606.
    • (2007) Immunology , vol.122 , Issue.4 , pp. 596-606
    • Bode, K.A.1    Schroder, K.2    Hume, D.A.3    Ravasi, T.4    Heeg, K.5    Sweet, M.J.6    Dalpke, A.H.7
  • 120
    • 50049130165 scopus 로고    scopus 로고
    • Valproic acid: A viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures
    • Backliwal, G., Hildinger, M., Kuettel, I., Delegrange, F., Hacker, D.L., and Wurm, F.M. (2008) Valproic acid: a viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures. Biotechnol. Bioeng., 101 (1), 182-189.
    • (2008) Biotechnol. Bioeng , vol.101 , Issue.1 , pp. 182-189
    • Backliwal, G.1    Hildinger, M.2    Kuettel, I.3    Delegrange, F.4    Hacker, D.L.5    Wurm, F.M.6
  • 121
    • 31844440592 scopus 로고    scopus 로고
    • Development of a fed-batch culture process for enhanced production of recombinant human antithrombin by Chinese hamster ovary cells
    • Kuwae, S., Ohda, T., Tamashima, H., Miki, H., and Kobayashi, K. (2005) Development of a fed-batch culture process for enhanced production of recombinant human antithrombin by Chinese hamster ovary cells. J. Biosci. Bioeng., 100 (5), 502-510.
    • (2005) J. Biosci. Bioeng , vol.100 , Issue.5 , pp. 502-510
    • Kuwae, S.1    Ohda, T.2    Tamashima, H.3    Miki, H.4    Kobayashi, K.5
  • 122
    • 84858617893 scopus 로고    scopus 로고
    • Feeding lactate for CHO cell culture processes: Impact on culture metabolism and performance
    • Li, J., Wong, C.L., Vijayasankaran, N., Hudson, T., and Amanullah, A. (2012) Feeding lactate for CHO cell culture processes: impact on culture metabolism and performance. Biotechnol. Bioeng., 109 (5), 1173-1186.
    • (2012) Biotechnol. Bioeng , vol.109 , Issue.5 , pp. 1173-1186
    • Li, J.1    Wong, C.L.2    Vijayasankaran, N.3    Hudson, T.4    Amanullah, A.5
  • 123
    • 33747126481 scopus 로고    scopus 로고
    • Process parameter shifting: Part I. Effect of DOT, pH, and temperature on the performance of Epo-Fc expressing CHO cells cultivated in controlled batch bioreactors
    • Trummer, E., Fauland, K., Seidinger, S., Schriebl, K., Lattenmayer, C., Kunert, R., Vorauer-Uhl, K., Weik, R., Borth, N., Katinger, H., and Muller, D. (2006) Process parameter shifting: Part I. Effect of DOT, pH, and temperature on the performance of Epo-Fc expressing CHO cells cultivated in controlled batch bioreactors. Biotechnol. Bioeng., 94 (6), 1033-1044.
    • (2006) Biotechnol. Bioeng , vol.94 , Issue.6 , pp. 1033-1044
    • Trummer, E.1    Fauland, K.2    Seidinger, S.3    Schriebl, K.4    Lattenmayer, C.5    Kunert, R.6    Vorauer-Uhl, K.7    Weik, R.8    Borth, N.9    Katinger, H.10    Muller, D.11
  • 125
    • 0344222199 scopus 로고    scopus 로고
    • Dissolved oxygen concentration in serum-free continuous culture affects N-linked glycosylation of a monoclonal antibody
    • Kunkel, J.P., Jan, D.C., Jamieson, J.C., and Butler, M. (1998) Dissolved oxygen concentration in serum-free continuous culture affects N-linked glycosylation of a monoclonal antibody. J. Biotechnol., 62 (1), 55-71.
    • (1998) J. Biotechnol , vol.62 , Issue.1 , pp. 55-71
    • Kunkel, J.P.1    Jan, D.C.2    Jamieson, J.C.3    Butler, M.4
  • 126
    • 0027626501 scopus 로고
    • Production of tPA in recombinant CHO cells under oxygen-limited conditions
    • Lin, A.A., Kimura, R., andMiller, W.M. (1993) Production of tPA in recombinant CHO cells under oxygen-limited conditions. Biotechnol. Bioeng., 42 (3), 339-350.
    • (1993) Biotechnol. Bioeng , vol.42 , Issue.3 , pp. 339-350
    • Lin, A.A.1    Kimura, R.2    Miller, W.M.3
  • 127
    • 33745186462 scopus 로고    scopus 로고
    • The effect of dissolved oxygen on the production and the glycosylation profile of recombinant human erythropoietin produced from CHO cells
    • Restelli, V., Wang, M.D., Huzel, N., Ethier, M., Perreault, H., and Butler, M. (2006) The effect of dissolved oxygen on the production and the glycosylation profile of recombinant human erythropoietin produced from CHO cells. Biotechnol. Bioeng., 94 (3), 481-494.
    • (2006) Biotechnol. Bioeng , vol.94 , Issue.3 , pp. 481-494
    • Restelli, V.1    Wang, M.D.2    Huzel, N.3    Ethier, M.4    Perreault, H.5    Butler, M.6
  • 128
    • 0037279448 scopus 로고    scopus 로고
    • 2 removal in large-scale fed-batch cultures
    • 2 removal in large-scale fed-batch cultures. Biotechnol. Prog., 19 (1), 45-51.
    • (2003) Biotechnol. Prog , vol.19 , Issue.1 , pp. 45-51
    • Mostafa, S.S.1    Gu, X.J.2
  • 133
    • 84865394272 scopus 로고    scopus 로고
    • Controlling trisulfide modification in recombinant monoclonal antibody produced in fed-batch cell culture
    • Kshirsagar, R., McElearney, K., Gilbert, A., Sinacore, M., and Ryll, T. (2012) Controlling trisulfide modification in recombinant monoclonal antibody produced in fed-batch cell culture. Biotechnol. Bioeng., 109 (10), 2523-2532.
    • (2012) Biotechnol. Bioeng , vol.109 , Issue.10 , pp. 2523-2532
    • Kshirsagar, R.1    McElearney, K.2    Gilbert, A.3    Sinacore, M.4    Ryll, T.5
  • 135
    • 77951587072 scopus 로고    scopus 로고
    • Effects of culture conditions on Nglycolylneuraminic acid (Neu5Gc) content of a recombinant fusion protein produced in CHO cells
    • Borys, M.C., Dalal, N.G., Abu-Absi, N.R., Khattak, S.F., Jing, Y., Xing, Z., and Li, Z.J. (2010) Effects of culture conditions on Nglycolylneuraminic acid (Neu5Gc) content of a recombinant fusion protein produced in CHO cells. Biotechnol. Bioeng., 105 (6), 1048-1057.
    • (2010) Biotechnol. Bioeng , vol.105 , Issue.6 , pp. 1048-1057
    • Borys, M.C.1    Dalal, N.G.2    Abu-Absi, N.R.3    Khattak, S.F.4    Jing, Y.5    Xing, Z.6    Li, Z.J.7
  • 138
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase
    • Gramer, M.J., Goochee, C.F., Chock, V.Y., Brousseau, D.T., and Sliwkowski, M.B. (1995) Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase. Biotechnology (NY), 13 (7), 692-698.
    • (1995) Biotechnology (NY) , vol.13 , Issue.7 , pp. 692-698
    • Gramer, M.J.1    Goochee, C.F.2    Chock, V.Y.3    Brousseau, D.T.4    Sliwkowski, M.B.5
  • 139
    • 84979155767 scopus 로고    scopus 로고
    • Genentech (pending), assignee. US Patent No. 2003/ 0211573 A1
    • Ryll, T. (inventor(s) (2004) Galactosylation of recombinant glycoproteins. Genentech (pending), assignee. US Patent No. 2003/ 0211573 A1.
    • (2004) Galactosylation of recombinant glycoproteins
    • Ryll, T.1
  • 141
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic control of recombinant monoclonal antibody Nglycosylation in GS-NS0 cells
    • Hills, A.E., Patel, A., Boyd, P., and James, D.C. (2001) Metabolic control of recombinant monoclonal antibody Nglycosylation in GS-NS0 cells. Biotechnol. Bioeng., 75 (2), 239-251.
    • (2001) Biotechnol. Bioeng , vol.75 , Issue.2 , pp. 239-251
    • Hills, A.E.1    Patel, A.2    Boyd, P.3    James, D.C.4
  • 142
    • 13544255561 scopus 로고    scopus 로고
    • Enhanced production of monomeric interferon-b by CHO cells through the control of culture conditions
    • Rodriguez, J., Spearman, M., Huzel, N., and Butler, M. (2005) Enhanced production of monomeric interferon-b by CHO cells through the control of culture conditions. Biotechnol. Prog., 21 (1), 22-30.
    • (2005) Biotechnol. Prog , vol.21 , Issue.1 , pp. 22-30
    • Rodriguez, J.1    Spearman, M.2    Huzel, N.3    Butler, M.4
  • 143
    • 78651509902 scopus 로고    scopus 로고
    • Sialylation enhancement of CTLA4-Ig fusion protein in Chinese hamster ovary cells by dexamethasone
    • Jing, Y., Qian, Y., and Li, Z.J. (2010) Sialylation enhancement of CTLA4-Ig fusion protein in Chinese hamster ovary cells by dexamethasone. Biotechnol. Bioeng., 107 (3), 488-496.
    • (2010) Biotechnol. Bioeng , vol.107 , Issue.3 , pp. 488-496
    • Jing, Y.1    Qian, Y.2    Li, Z.J.3
  • 144
    • 84862204695 scopus 로고    scopus 로고
    • Effect of hydrocortisone on the production and glycosylation of an Fcfusion protein in CHO cell cultures
    • Rouiller, Y., Perilleux, A., Marsaut, M., Stettler, M., Vesin, M.N., and Broly, H. (2012) Effect of hydrocortisone on the production and glycosylation of an Fcfusion protein in CHO cell cultures. Biotechnol. Prog., 28 (3), 803-813.
    • (2012) Biotechnol. Prog , vol.28 , Issue.3 , pp. 803-813
    • Rouiller, Y.1    Perilleux, A.2    Marsaut, M.3    Stettler, M.4    Vesin, M.N.5    Broly, H.6
  • 145
    • 0027628305 scopus 로고
    • Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant
    • Gramer, M.J. and Goochee, C.F. (1993) Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant. Biotechnol. Prog., 9 (4), 366-373.
    • (1993) Biotechnol. Prog , vol.9 , Issue.4 , pp. 366-373
    • Gramer, M.J.1    Goochee, C.F.2
  • 146
    • 0028166666 scopus 로고
    • Glycosidase activities of the 293 and NSO cell lines, and of an antibody-producing hybridoma cell line
    • Gramer, M.J. and Goochee, C.F. (1994) Glycosidase activities of the 293 and NSO cell lines, and of an antibody-producing hybridoma cell line. Biotechnol. Bioeng., 43 (5), 423-428.
    • (1994) Biotechnol. Bioeng , vol.43 , Issue.5 , pp. 423-428
    • Gramer, M.J.1    Goochee, C.F.2
  • 147
    • 17944387597 scopus 로고    scopus 로고
    • Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24
    • Muthing, J., Kemminer, S.E., Conradt, H. S., Sagi, D., Nimtz, M., Karst, U., and Peter-Katalinic, J. (2003) Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24. Biotechnol. Bioeng., 83 (3), 321-334.
    • (2003) Biotechnol. Bioeng , vol.83 , Issue.3 , pp. 321-334
    • Muthing, J.1    Kemminer, S.E.2    Conradt, H.S.3    Sagi, D.4    Nimtz, M.5    Karst, U.6    Peter-Katalinic, J.7
  • 148
    • 14244265076 scopus 로고    scopus 로고
    • Effect of culture pH on erythropoietin production by Chinese hamster ovary cells grown in suspension at 32.5 and 37.0 degrees C
    • Yoon, S.K., Choi, S.L., Song, J.Y., and Lee, G.M. (2005) Effect of culture pH on erythropoietin production by Chinese hamster ovary cells grown in suspension at 32.5 and 37.0 degrees C. Biotechnol. Bioeng., 89 (3), 345-356.
    • (2005) Biotechnol. Bioeng , vol.89 , Issue.3 , pp. 345-356
    • Yoon, S.K.1    Choi, S.L.2    Song, J.Y.3    Lee, G.M.4
  • 149
    • 65549131351 scopus 로고    scopus 로고
    • Elevated Golgi pH impairs terminal Nglycosylation by inducing mislocalization of Golgi glycosyltransferases
    • Rivinoja, A., Hassinen, A., Kokkonen, N., Kauppila, A., and Kellokumpu, S. (2009) Elevated Golgi pH impairs terminal Nglycosylation by inducing mislocalization of Golgi glycosyltransferases. J. Cell Physiol., 220 (1), 144-154.
    • (2009) J. Cell Physiol , vol.220 , Issue.1 , pp. 144-154
    • Rivinoja, A.1    Hassinen, A.2    Kokkonen, N.3    Kauppila, A.4    Kellokumpu, S.5
  • 150
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • Hodoniczky, J., Zheng, Y.Z., and James, D.C. (2005) Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol. Prog., 21 (6), 1644-1652.
    • (2005) Biotechnol. Prog , vol.21 , Issue.6 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.C.3
  • 151
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • Raju, T.S., Briggs, J.B., Chamow, S.M., Winkler, M.E., and Jones, A.J. (2001) Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Biochemistry, 40 (30), 8868-8876.
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8868-8876
    • Raju, T.S.1    Briggs, J.B.2    Chamow, S.M.3    Winkler, M.E.4    Jones, A.J.5
  • 152
    • 61849115693 scopus 로고    scopus 로고
    • Blockade of lymphotoxin-beta receptor signaling reduces aspects of Sjogren's syndrome in salivary glands of non-obese diabetic mice
    • Gatumu, M.K., Skarstein, K., Papandile, A., Browning, J.L., Fava, R.A., and Bolstad, A.I. (2009) Blockade of lymphotoxin-beta receptor signaling reduces aspects of Sjogren's syndrome in salivary glands of non-obese diabetic mice. Arthritis Res. Ther., 11 (1), R24.
    • (2009) Arthritis Res. Ther , vol.11 , Issue.1 , pp. R24
    • Gatumu, M.K.1    Skarstein, K.2    Papandile, A.3    Browning, J.L.4    Fava, R.A.5    Bolstad, A.I.6
  • 153
    • 25144476279 scopus 로고    scopus 로고
    • Bcl-x(L) mediates increased production of humanized monoclonal antibodies in chinese hamster ovary cells
    • Chiang, G.G. and Sisk, W.P. (2005) Bcl-x(L) mediates increased production of humanized monoclonal antibodies in chinese hamster ovary cells. Biotechnol. Bioeng., 91 (7), 779-792.
    • (2005) Biotechnol. Bioeng , vol.91 , Issue.7 , pp. 779-792
    • Chiang, G.G.1    Sisk, W.P.2
  • 154
    • 84861642572 scopus 로고    scopus 로고
    • Human cells: New platform for recombinant therapeutic protein production
    • Swiech, K., Picanco-Castro, V., and Covas, D.T. (2012) Human cells: new platform for recombinant therapeutic protein production. Protein Expr. Purif., 84 (1), 147-153.
    • (2012) Protein Expr. Purif , vol.84 , Issue.1 , pp. 147-153
    • Swiech, K.1    Picanco-Castro, V.2    Covas, D.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.