메뉴 건너뛰기




Volumn 28, Issue 5, 2010, Pages 253-261

Recent advances in large-scale production of monoclonal antibodies and related proteins

Author keywords

[No Author keywords available]

Indexed keywords

BIOPROCESS DEVELOPMENT; CHROMATOGRAPHIC SEPARATIONS; DOWNSTREAM PROCESS; INDUSTRIAL PRODUCTION; LARGE-SCALE PRODUCTION; MAMMALIAN CELL CULTURE; MANUFACTURING PROCESS; PLATFORM APPROACH; RAPID DEVELOPMENT; RELATED PRODUCTS;

EID: 77951979046     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2010.02.001     Document Type: Review
Times cited : (465)

References (79)
  • 1
    • 34247876138 scopus 로고    scopus 로고
    • Development trends for monoclonal antibody cancer therapeutics
    • Reichert J., Valge-Archer V. Development trends for monoclonal antibody cancer therapeutics. Nat. Rev. Drug Discov. 2007, 6:349-356.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 349-356
    • Reichert, J.1    Valge-Archer, V.2
  • 2
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter P. Potent antibody therapeutics by design. Nat. Rev. Immunol. 2006, 6:343-357.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 343-357
    • Carter, P.1
  • 3
    • 58749104213 scopus 로고    scopus 로고
    • Novel human antibody therapeutics: the age of the Umabs
    • Ruuls S., et al. Novel human antibody therapeutics: the age of the Umabs. Biotechnol. J. 2008, 3:1157-1171.
    • (2008) Biotechnol. J. , vol.3 , pp. 1157-1171
    • Ruuls, S.1
  • 4
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nature 2009, 8:226-234.
    • (2009) Nature , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 5
    • 33644819090 scopus 로고    scopus 로고
    • Fully human therapeutic monoclonal antibodies J
    • Weiner L. Fully human therapeutic monoclonal antibodies J. Immunotherapy 2006, 29:1-9.
    • (2006) Immunotherapy , vol.29 , pp. 1-9
    • Weiner, L.1
  • 6
    • 33847611596 scopus 로고    scopus 로고
    • Downstream processing of monoclonal antibodies - application of platform approaches
    • Shukla A., et al. Downstream processing of monoclonal antibodies - application of platform approaches. J. Chromatogr. B 2007, 848:28-39.
    • (2007) J. Chromatogr. B , vol.848 , pp. 28-39
    • Shukla, A.1
  • 7
    • 35348866110 scopus 로고    scopus 로고
    • Very large-scale monoclonal antibody purification - the case for conventional unit operations
    • Kelley B. Very large-scale monoclonal antibody purification - the case for conventional unit operations. Biotechnol. Prog. 2007, 23:995-1008.
    • (2007) Biotechnol. Prog. , vol.23 , pp. 995-1008
    • Kelley, B.1
  • 8
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology - the bioprocessing industry at a crossroads
    • Kelley B. Industrialization of mAb production technology - the bioprocessing industry at a crossroads. MAbs 2009, 1:1-10.
    • (2009) MAbs , vol.1 , pp. 1-10
    • Kelley, B.1
  • 10
    • 60549102844 scopus 로고    scopus 로고
    • A study of monoclonal antibody producing CHO cell lines - what makes a stable high producer?
    • Chusainow J., et al. A study of monoclonal antibody producing CHO cell lines - what makes a stable high producer?. Biotechnol. Bioeng. 2009, 102:1182-1196.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1182-1196
    • Chusainow, J.1
  • 11
    • 32344448765 scopus 로고    scopus 로고
    • Regulation of recombinant monoclonal antibody production in CHO cells - a comparative study of gene copy number, mRNA level and protein expression
    • Jiang Z., et al. Regulation of recombinant monoclonal antibody production in CHO cells - a comparative study of gene copy number, mRNA level and protein expression. Biotechnol. Progr. 2006, 22:313-318.
    • (2006) Biotechnol. Progr. , vol.22 , pp. 313-318
    • Jiang, Z.1
  • 12
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm F. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol. 2004, 22:1393-1398.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1393-1398
    • Wurm, F.1
  • 13
    • 0035313635 scopus 로고    scopus 로고
    • Industrial choices for protein production by large-scale cell culture
    • Chu L., Robinson D. Industrial choices for protein production by large-scale cell culture. Curr. Opin. Biotechnol. 2001, 12:180-187.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 180-187
    • Chu, L.1    Robinson, D.2
  • 14
    • 50049122941 scopus 로고    scopus 로고
    • The way forward, enhanced characterization of therapeutic antibody glycosylation: comparison of three level MS based strategies J
    • Wagner-Rousset E., et al. The way forward, enhanced characterization of therapeutic antibody glycosylation: comparison of three level MS based strategies J. Chromatogr. B 2008, 872:23-37.
    • (2008) Chromatogr. B , vol.872 , pp. 23-37
    • Wagner-Rousset, E.1
  • 15
    • 69149086474 scopus 로고    scopus 로고
    • Mcl-1 overexpression leads to higher viabilities and increased production of humanized monoclonal antibody in CHO cells
    • Majors B., et al. Mcl-1 overexpression leads to higher viabilities and increased production of humanized monoclonal antibody in CHO cells. Biotechnol. Progr. 2009, 25:1161-1168.
    • (2009) Biotechnol. Progr. , vol.25 , pp. 1161-1168
    • Majors, B.1
  • 16
    • 36248985213 scopus 로고    scopus 로고
    • Upstream processes in antibody production - evaluation of critical parameters
    • Jain E., Kumar A. Upstream processes in antibody production - evaluation of critical parameters. Biotechnol. Adv. 2008, 26:46-72.
    • (2008) Biotechnol. Adv. , vol.26 , pp. 46-72
    • Jain, E.1    Kumar, A.2
  • 17
    • 60549105996 scopus 로고    scopus 로고
    • A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies
    • Lee C., et al. A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies. Biotechnol. Bioeng. 2008, 102:1107-1118.
    • (2008) Biotechnol. Bioeng. , vol.102 , pp. 1107-1118
    • Lee, C.1
  • 18
    • 33845936631 scopus 로고    scopus 로고
    • Serum free suspension large-scale transient tranfection of CHO cells in WAVE bioreactors
    • Haldankar R., et al. Serum free suspension large-scale transient tranfection of CHO cells in WAVE bioreactors. Mol. Biotechnol. 2006, 34:191-199.
    • (2006) Mol. Biotechnol. , vol.34 , pp. 191-199
    • Haldankar, R.1
  • 19
    • 65549165087 scopus 로고    scopus 로고
    • High-level protein expression in scaleable CHO transient transfection
    • Ye J., et al. High-level protein expression in scaleable CHO transient transfection. Biotechnol. Bioeng. 2009, 103:542-551.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 542-551
    • Ye, J.1
  • 20
    • 33846927813 scopus 로고    scopus 로고
    • Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system
    • Crowell C., et al. Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system. Biotechnol. Bioeng. 2007, 96:538-549.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 538-549
    • Crowell, C.1
  • 21
    • 12544253860 scopus 로고    scopus 로고
    • Impact of dynamic on-line fed-batch strategies on metabolism, productivity and N-glycosylation in CHO cell cultures
    • Wong D., et al. Impact of dynamic on-line fed-batch strategies on metabolism, productivity and N-glycosylation in CHO cell cultures. Biotechnol. Bioeng. 2004, 89:164-177.
    • (2004) Biotechnol. Bioeng. , vol.89 , pp. 164-177
    • Wong, D.1
  • 22
    • 62949249235 scopus 로고    scopus 로고
    • Estimation of dissolved carbon dioxide stripping in a large bioreactor using model medium
    • Matsunaga N., et al. Estimation of dissolved carbon dioxide stripping in a large bioreactor using model medium. J. Biosci. Bioeng. 2009, 107:49-424.
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 49-424
    • Matsunaga, N.1
  • 23
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian D., Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 2007, 7:715-725.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.1    Akilesh, S.2
  • 24
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh G., Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat. Biotechnol. 2006, 24:1241-1252.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 25
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P., et al. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 2009, 19:936-949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1
  • 26
    • 44849102747 scopus 로고    scopus 로고
    • Harvest and recovery of monoclonal antibodies from large-scale mammalian cell culture
    • Shukla A., Kandula J. Harvest and recovery of monoclonal antibodies from large-scale mammalian cell culture. Biopharm. Int. 2008, 7:34-45.
    • (2008) Biopharm. Int. , vol.7 , pp. 34-45
    • Shukla, A.1    Kandula, J.2
  • 27
    • 32344436889 scopus 로고    scopus 로고
    • Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification
    • Yigzaw Y., et al. Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification. Biotechnol. Progr. 2006, 22:288-296.
    • (2006) Biotechnol. Progr. , vol.22 , pp. 288-296
    • Yigzaw, Y.1
  • 28
    • 33747451721 scopus 로고    scopus 로고
    • Current and future issues in the manufacturing and development of monoclonal antibodies
    • Kozlowski S., Swann P. Current and future issues in the manufacturing and development of monoclonal antibodies. Adv. Drug Deliv. Rev. 2006, 58:707-722.
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 707-722
    • Kozlowski, S.1    Swann, P.2
  • 29
    • 33847793307 scopus 로고    scopus 로고
    • Future of antibody purification
    • Low D., et al. Future of antibody purification. J. Chromatogr. B 2007, 848:48-63.
    • (2007) J. Chromatogr. B , vol.848 , pp. 48-63
    • Low, D.1
  • 30
    • 84890614322 scopus 로고    scopus 로고
    • Integrated polishing steps for monoclonal antibody production
    • Wiley, U. Gottschalk (Ed.)
    • Ghose S., et al. Integrated polishing steps for monoclonal antibody production. Process Scale Purification of Antibodies 2009, 145-167. Wiley. 1st edn. U. Gottschalk (Ed.).
    • (2009) Process Scale Purification of Antibodies , pp. 145-167
    • Ghose, S.1
  • 32
    • 84890644914 scopus 로고    scopus 로고
    • Purification of human monoclonal antibodies - non Protein A strategies
    • Wiley, U. Gottschalk (Ed.)
    • Arunakumari A., Wang J. Purification of human monoclonal antibodies - non Protein A strategies. Process Scale Purification of Antibodies 2009, 103-123. Wiley. 1st edn. U. Gottschalk (Ed.).
    • (2009) Process Scale Purification of Antibodies , pp. 103-123
    • Arunakumari, A.1    Wang, J.2
  • 33
    • 16344395381 scopus 로고    scopus 로고
    • Protein interactions in hydrophobic charge induction chromatography (HCIC)
    • Ghose S., et al. Protein interactions in hydrophobic charge induction chromatography (HCIC). Biotechnol. Progr. 2005, 21:498-508.
    • (2005) Biotechnol. Progr. , vol.21 , pp. 498-508
    • Ghose, S.1
  • 34
    • 33745924699 scopus 로고    scopus 로고
    • Evaluation and comparison of alternatives to Protein A chromatography - mimetic and hydrophobic charge induction chromatographic stationary phases
    • Ghose S., et al. Evaluation and comparison of alternatives to Protein A chromatography - mimetic and hydrophobic charge induction chromatographic stationary phases. J. Chromatogr. A 2006, 1122:144-152.
    • (2006) J. Chromatogr. A , vol.1122 , pp. 144-152
    • Ghose, S.1
  • 35
    • 77951975352 scopus 로고    scopus 로고
    • Comparison of camelid antibody ligand to Protein A for monoclonal antibody purification
    • Liu J., et al. Comparison of camelid antibody ligand to Protein A for monoclonal antibody purification. Biopharm. Int. 2009, 22:35-43.
    • (2009) Biopharm. Int. , vol.22 , pp. 35-43
    • Liu, J.1
  • 36
    • 67249105900 scopus 로고    scopus 로고
    • Engineering properties of a camelid antibody affinity sorbent for immunoglobulin G purification
    • Zandian M., Jungbauer A. Engineering properties of a camelid antibody affinity sorbent for immunoglobulin G purification. J. Chromatogr. A 2009, 1216:5548-5556.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5548-5556
    • Zandian, M.1    Jungbauer, A.2
  • 37
    • 28844477910 scopus 로고    scopus 로고
    • Antibody variable region interactions with Protein A - implications for the development of generic purification processes
    • Ghose S., et al. Antibody variable region interactions with Protein A - implications for the development of generic purification processes. Biotechnol. Bioeng. 2005, 92:665-673.
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 665-673
    • Ghose, S.1
  • 38
    • 33947138076 scopus 로고    scopus 로고
    • Binding capacity differences for antibodies and Fc-fusion proteins on Protein A chromatographic materials
    • Ghose S., et al. Binding capacity differences for antibodies and Fc-fusion proteins on Protein A chromatographic materials. Biotechnol. Bioeng. 2007, 96:768-779.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 768-779
    • Ghose, S.1
  • 39
    • 38449106730 scopus 로고    scopus 로고
    • Maximizing productivity of chromatographic steps for purification of monoclonal antibodies
    • Tugcu N., et al. Maximizing productivity of chromatographic steps for purification of monoclonal antibodies. Biotechnol. Bioeng. 2008, 99:599-613.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 599-613
    • Tugcu, N.1
  • 40
    • 2942726440 scopus 로고    scopus 로고
    • Use and optimization of a dual flow-rate loading strategy for maximizing throughput in Protein A affinity chromatography
    • Ghose S., et al. Use and optimization of a dual flow-rate loading strategy for maximizing throughput in Protein A affinity chromatography. Biotechnol. Progr. 2004, 20:830-840.
    • (2004) Biotechnol. Progr. , vol.20 , pp. 830-840
    • Ghose, S.1
  • 41
    • 67649670454 scopus 로고    scopus 로고
    • A mechanistic study of Protein A chromatography resin lifetime
    • Jiang C., et al. A mechanistic study of Protein A chromatography resin lifetime. J. Chromatogr. A 2009, 1216:5849-5855.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5849-5855
    • Jiang, C.1
  • 42
    • 65249163578 scopus 로고    scopus 로고
    • Development of a rapid sanitization solution for silica-based protein A affinity adsorbents
    • Rogers M., et al. Development of a rapid sanitization solution for silica-based protein A affinity adsorbents. J. Chromatogr. A 2009, 1216:4589-4596.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 4589-4596
    • Rogers, M.1
  • 43
    • 0347928638 scopus 로고    scopus 로고
    • Identification of protein A media performance attributes that can be monitored as surrogates for retrovirus clearance during extended re-use
    • Brorson K., et al. Identification of protein A media performance attributes that can be monitored as surrogates for retrovirus clearance during extended re-use. J. Chromatogr. A 2003, 989:155-163.
    • (2003) J. Chromatogr. A , vol.989 , pp. 155-163
    • Brorson, K.1
  • 44
    • 56249116669 scopus 로고    scopus 로고
    • Host cell protein clearance during Protein A chromatography - development of an improved wash step
    • Shukla A., Hinckley P. Host cell protein clearance during Protein A chromatography - development of an improved wash step. Biotechnol. Progr. 2008, 24:1115-1121.
    • (2008) Biotechnol. Progr. , vol.24 , pp. 1115-1121
    • Shukla, A.1    Hinckley, P.2
  • 45
    • 74849111728 scopus 로고    scopus 로고
    • Profiling of host cell proteins by two dimensional difference gel electrophoresis (2D-DIGE) - implications for downstream process development
    • Jin M., et al. Profiling of host cell proteins by two dimensional difference gel electrophoresis (2D-DIGE) - implications for downstream process development. Biotechnol. Bioeng. 2010, 105:306-316.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 306-316
    • Jin, M.1
  • 46
    • 45149105860 scopus 로고    scopus 로고
    • Demonstration of robust host cell protein clearance in biopharmaceutical downstream processes
    • Shukla A., et al. Demonstration of robust host cell protein clearance in biopharmaceutical downstream processes. Biotechnol. Progr. 2008, 24:615-622.
    • (2008) Biotechnol. Progr. , vol.24 , pp. 615-622
    • Shukla, A.1
  • 47
    • 35348823110 scopus 로고    scopus 로고
    • Protein aggregation kinetics during Protein A chromatography - case study for an Fc fusion protein
    • Shukla A., et al. Protein aggregation kinetics during Protein A chromatography - case study for an Fc fusion protein. J. Chromatogr. A 2007, 1171:22-28.
    • (2007) J. Chromatogr. A , vol.1171 , pp. 22-28
    • Shukla, A.1
  • 48
    • 70350149959 scopus 로고    scopus 로고
    • Design of a filter train for precipitate removal in mAb downstream processing
    • Kandula S., et al. Design of a filter train for precipitate removal in mAb downstream processing. Biotechnol. Appl. Biochem. 2009, 54:149-155.
    • (2009) Biotechnol. Appl. Biochem. , vol.54 , pp. 149-155
    • Kandula, S.1
  • 49
    • 67650874668 scopus 로고    scopus 로고
    • IgG aggregate removal by charged hydrophobic mixed-mode chromatography
    • Gagnon P. IgG aggregate removal by charged hydrophobic mixed-mode chromatography. Curr. Pharm. Biotech. 2009, 10:434-439.
    • (2009) Curr. Pharm. Biotech. , vol.10 , pp. 434-439
    • Gagnon, P.1
  • 50
    • 70350221698 scopus 로고    scopus 로고
    • Ligands for mixed-mode protein chromatography: principles, characteristics and design
    • Zhao G., et al. Ligands for mixed-mode protein chromatography: principles, characteristics and design. J. Biotechnol. 2009, 144:3-11.
    • (2009) J. Biotechnol. , vol.144 , pp. 3-11
    • Zhao, G.1
  • 51
    • 60549100299 scopus 로고    scopus 로고
    • Modeling electrostatic exclusion effects during ion exchange chromatography of monoclonal antibodies
    • Zydney A., et al. Modeling electrostatic exclusion effects during ion exchange chromatography of monoclonal antibodies. Biotechnol. Bioeng. 2009, 102:1131-1140.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1131-1140
    • Zydney, A.1
  • 52
    • 48649097549 scopus 로고    scopus 로고
    • Weak partitioning chromatography for anion-exchange purification of monoclonal antibodies
    • Kelley B., et al. Weak partitioning chromatography for anion-exchange purification of monoclonal antibodies. Biotechnol. Bioeng. 2008, 101:553-566.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 553-566
    • Kelley, B.1
  • 53
    • 44049108746 scopus 로고    scopus 로고
    • Viral clearance using disposable systems in monoclonal antibody commercial downstream processing
    • Zhou J. Viral clearance using disposable systems in monoclonal antibody commercial downstream processing. Biotechnol. Bioeng. 2008, 100:488-496.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 488-496
    • Zhou, J.1
  • 54
    • 33750220103 scopus 로고    scopus 로고
    • Virus removal by filtration - points to consider
    • Kern G., Krishnan M. Virus removal by filtration - points to consider. Biopharm. Int. 2006, 19:32-41.
    • (2006) Biopharm. Int. , vol.19 , pp. 32-41
    • Kern, G.1    Krishnan, M.2
  • 55
    • 18844434391 scopus 로고    scopus 로고
    • Compaction and permeability effects with virus filtration membranes
    • Bohonak D., Zydney A. Compaction and permeability effects with virus filtration membranes. J. Membrane Sci. 2005, 254:71-79.
    • (2005) J. Membrane Sci. , vol.254 , pp. 71-79
    • Bohonak, D.1    Zydney, A.2
  • 56
    • 33750224093 scopus 로고    scopus 로고
    • Optimizing virus filtration performance with prefiltration
    • Ireland T., et al. Optimizing virus filtration performance with prefiltration. Bioprocess Intl. Supplement 2005, 3:44-47.
    • (2005) Bioprocess Intl. Supplement , vol.3 , pp. 44-47
    • Ireland, T.1
  • 57
    • 66149163345 scopus 로고    scopus 로고
    • Virus filtration of high-concentration monoclonal antibody solutions
    • Marques B., et al. Virus filtration of high-concentration monoclonal antibody solutions. Biotechnol. Progr. 2009, 25:483-491.
    • (2009) Biotechnol. Progr. , vol.25 , pp. 483-491
    • Marques, B.1
  • 58
    • 3843058933 scopus 로고    scopus 로고
    • Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
    • Harris R., et al. Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies. Drug Dev. Res. 2004, 61:137-154.
    • (2004) Drug Dev. Res. , vol.61 , pp. 137-154
    • Harris, R.1
  • 59
    • 67650812831 scopus 로고    scopus 로고
    • Response of a concentrated monoclonal antibody formulation to high shear
    • Bee J., et al. Response of a concentrated monoclonal antibody formulation to high shear. Biotechnol. Bioeng. 2009, 103:936-943.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 936-943
    • Bee, J.1
  • 60
    • 73949093277 scopus 로고    scopus 로고
    • Aggregation of a monoclonal antibody induced by adsorption to stainless steel
    • Bee J., et al. Aggregation of a monoclonal antibody induced by adsorption to stainless steel. Biotechnol. Bioeng. 2010, 105:121-129.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 121-129
    • Bee, J.1
  • 61
    • 77951977681 scopus 로고    scopus 로고
    • Large-scale freezing of biologics
    • Singh S., et al. Large-scale freezing of biologics. Bioprocess Intl. 2009, 7:32-44.
    • (2009) Bioprocess Intl. , vol.7 , pp. 32-44
    • Singh, S.1
  • 62
    • 4744342353 scopus 로고    scopus 로고
    • Alternative bioseparation operations - life beyond packed-bed chromatography
    • Przybycien T., et al. Alternative bioseparation operations - life beyond packed-bed chromatography. Curr. Opin. Biotech. 2004, 15:469-478.
    • (2004) Curr. Opin. Biotech. , vol.15 , pp. 469-478
    • Przybycien, T.1
  • 63
    • 33847102715 scopus 로고    scopus 로고
    • Alternatives to chromatographic separations
    • Thommes J., Etzel M. Alternatives to chromatographic separations. Biotechnol. Progr. 2007, 23:42-45.
    • (2007) Biotechnol. Progr. , vol.23 , pp. 42-45
    • Thommes, J.1    Etzel, M.2
  • 64
    • 44449151539 scopus 로고    scopus 로고
    • Follow-on biologics - data exclusivity and the balance between innovation and competition
    • Grabowski H. Follow-on biologics - data exclusivity and the balance between innovation and competition. Nat. Rev. Drug. Discov. 2008, 7:478-488.
    • (2008) Nat. Rev. Drug. Discov. , vol.7 , pp. 478-488
    • Grabowski, H.1
  • 65
    • 62549139648 scopus 로고    scopus 로고
    • Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing
    • Azevedo A., et al. Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing. Trends Biotechnol. 2009, 27:240-247.
    • (2009) Trends Biotechnol. , vol.27 , pp. 240-247
    • Azevedo, A.1
  • 66
    • 34047181475 scopus 로고    scopus 로고
    • Chromatography: industrial processing and biotherapeutics Filtration and Separation 44, 26-28
    • Noel, R. (2007) Chromatography: industrial processing and biotherapeutics Filtration and Separation 44, 26-28.
    • (2007)
    • Noel, R.1
  • 67
    • 77951977137 scopus 로고    scopus 로고
    • Precipitation of process-derived impurities in non-Protein A purification schemes for antibodies
    • Biopharm Intl. Special Issue on Downstream Processing 2010 - embracing innovation Oct, 4-10
    • Wang, J. et al. (2009) Precipitation of process-derived impurities in non-Protein A purification schemes for antibodies. Biopharm Intl. Special Issue on Downstream Processing 2010 - embracing innovation Oct, 4-10.
    • (2009)
    • Wang, J.1
  • 68
    • 60549099544 scopus 로고    scopus 로고
    • Selective antibody precipitation using polyelectrolytes - a novel approach to the purification of monoclonal antibodies
    • McDonald P., et al. Selective antibody precipitation using polyelectrolytes - a novel approach to the purification of monoclonal antibodies. Biotechnol. Bioeng. 2009, 102:1141-1151.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1141-1151
    • McDonald, P.1
  • 69
    • 58149299631 scopus 로고    scopus 로고
    • Affinity enhanced purification of human monoclonal antibodies by aqueous two-phase separation
    • Azevedo A., et al. Affinity enhanced purification of human monoclonal antibodies by aqueous two-phase separation. Sepn. Purific. Technol. 2009, 65:31-39.
    • (2009) Sepn. Purific. Technol. , vol.65 , pp. 31-39
    • Azevedo, A.1
  • 70
    • 34447303560 scopus 로고    scopus 로고
    • Phase behavior of an intact monoclonal antibody
    • Ahamed T., et al. Phase behavior of an intact monoclonal antibody. Biophys. J. 2007, 93:610-619.
    • (2007) Biophys. J. , vol.93 , pp. 610-619
    • Ahamed, T.1
  • 71
    • 34248591731 scopus 로고    scopus 로고
    • Bioprocess membrane technology
    • van Reis R., Zydney A. Bioprocess membrane technology. J. Membrane Sci. 2007, 302:16-50.
    • (2007) J. Membrane Sci. , vol.302 , pp. 16-50
    • van Reis, R.1    Zydney, A.2
  • 72
    • 33745714054 scopus 로고    scopus 로고
    • High resolution protein separations using affinity ultrafiltration with small charged ligands
    • Rao S., Zydney A. High resolution protein separations using affinity ultrafiltration with small charged ligands. J. Membrane Sci. 2006, 280:781-789.
    • (2006) J. Membrane Sci. , vol.280 , pp. 781-789
    • Rao, S.1    Zydney, A.2
  • 73
    • 33646041909 scopus 로고    scopus 로고
    • Basic concepts in Q membrane chromatography for large-scale antibody production
    • Zhou J., Tressel T. Basic concepts in Q membrane chromatography for large-scale antibody production. Biotechnol. Progr. 2006, 22:341-349.
    • (2006) Biotechnol. Progr. , vol.22 , pp. 341-349
    • Zhou, J.1    Tressel, T.2
  • 74
    • 67649203468 scopus 로고    scopus 로고
    • Advances and challenges in developing cytokine fusion proteins as improved therapeutics
    • Chang C., et al. Advances and challenges in developing cytokine fusion proteins as improved therapeutics. Expert Opin. Drug. Discov. 2009, 4:181-194.
    • (2009) Expert Opin. Drug. Discov. , vol.4 , pp. 181-194
    • Chang, C.1
  • 75
    • 47949132979 scopus 로고    scopus 로고
    • Recombinant antibodies for cancer therapy
    • Deonarain M. Recombinant antibodies for cancer therapy. Expert Opin. Biol. Ther. 2008, 8:1123-1141.
    • (2008) Expert Opin. Biol. Ther. , vol.8 , pp. 1123-1141
    • Deonarain, M.1
  • 76
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P., Hudson P. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 2005, 23:1126-1136.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.2
  • 77
    • 33751347582 scopus 로고    scopus 로고
    • Biopharmaceutical drug discovery using novel protein scaffolds
    • Gill D., Damle N. Biopharmaceutical drug discovery using novel protein scaffolds. Curr. Opin. Biotechnol. 2006, 17:653-658.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 653-658
    • Gill, D.1    Damle, N.2
  • 78
    • 60549096767 scopus 로고    scopus 로고
    • The adnectin CT-322 is a novel VEGF receptor inhibitor that decreases tumor burden in an orthotopic mouse model of pancreatic cancer
    • Dineen S., et al. The adnectin CT-322 is a novel VEGF receptor inhibitor that decreases tumor burden in an orthotopic mouse model of pancreatic cancer. BMC Cancer 2008, 8(352):1-10.
    • (2008) BMC Cancer , vol.8 , Issue.352 , pp. 1-10
    • Dineen, S.1
  • 79
    • 4644309963 scopus 로고    scopus 로고
    • Production technologies for monoclonal antibodies and their fragments
    • Andersen D., Reilly D. Production technologies for monoclonal antibodies and their fragments. Curr. Opin. Biotechnol. 2004, 15:456-462.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 456-462
    • Andersen, D.1    Reilly, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.