Assessment of cell engineering strategies for improved therapeutic protein production in CHO cells
Abstract
Recombinant glycoprotein therapeutics have proven to be invaluable pharmaceuticals for the treatment of various diseases. Chinese hamster ovary (CHO) cells are widely used in industry for the production of these proteins. Several strategies for engineering CHO cells for improved protein production have been tried with considerable results. The focus has mainly been to increase the specific productivity and to extend the culture longevity by preventing programmed cell death. These CHO cell engineering strategies, particularly those developed in Korea, are reviewed here.
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Chaperones have been employed by many groups as cell engineering tools but have given variable results.
“They have been employed by many groups as cell engineering tools but have given variable results (Mohan et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Mohan et al., 2008
The BiP chaperone gave mixed results, with enhanced or decreased productivity.
“Similarly, the heavy chain-binding protein (BiP) chaperone gave mixed results, with enhanced or decreased productivity (Mohan et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Mohan et al., 2008
Overexpression of ERp57 together with calnexin/calreticulin was able to increase thrombopoietin production in CHO cells.
“Moreover, overexpression of the endoplasmic-reticulum ERp57 protein, an isoform of PDI, together with calnexin/calreticulin was able to increase thrombopoietin production in CHO cells (Mohan et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Mohan et al., 2008
Other studies observed either a negative or no effect on productivity with PDI overexpression.
“However, other studies observed either a negative or no effect on productivity (Mohan et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Mohan et al., 2008
Translational and/or post-translational processes might also be rate-limiting for protein production, because of the lack of correlation between gene copy number and the amount of secreted proteins.
“It has been suggested that translational and/or post-translational processes might also be rate-limiting for protein production, because of the lack of correlation between gene copy number and the amount of secreted proteins (Wilson et al., 1990;Mohan et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Mohan et al., 2008
Cites
Encyclopedia of bioprocess technology: fermentation, biocatalysis, and bioseparation
(1999) · Choice Reviews Online · doi:10.5860/choice.37-1896 · Cited by 864 · see citing works
Yoon, S. K., Song, J. Y., & Lee, G. M. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10566 · Cited by 244 · see citing works
Cell death in bioreactors: A role for apoptosis
Singh, R. P., Al.‐Rubeai, M., Gregory, C. D., & Emery, A. N. (1994) · Biotechnology and Bioengineering · doi:10.1002/bit.260440608 · Cited by 244 · see citing works
Borth, N., Mattanovich, D., Kunert, R., & Katinger, H. W. D. (2005) · Biotechnology Progress · doi:10.1021/bp0498241 · Cited by 191 · see citing works
Kim, S. H., & Lee, G. M. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0654-5 · Cited by 135 · see citing works
Nutrient deprivation induces autophagy as well as apoptosis in Chinese hamster ovary cell culture
Hwang, S. O., & Lee, G. M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21589 · Cited by 112 · see citing works
Kim, N. S., & Lee, G. M. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(02)00011-1 · Cited by 106 · see citing works
What's fueling the biotech engine?
Aggarwal, S. (2007) · Nature Biotechnology · doi:10.1038/nbt1007-1097 · Cited by 105 · see citing works
Effect of PDI Overexpression on Recombinant Protein Secretion in CHO Cells
Davis, R., Schooley, K., Rasmussen, B., Thomas, J., & Reddy, P. (2000) · Biotechnology Progress · doi:10.1021/bp000107q · Cited by 105 · see citing works
Relationship between cell size, cell cycle and specific recombinant protein productivity
Lloyd, D. R., Holmes, P., Jackson, L. P., Emery, A. N., & Al-Rubeai, M. (2000) · Cytotechnology · doi:10.1023/a:1008103730027 · Cited by 93 · see citing works
Yoon, S., Hwang, S. O., & Lee, G. M. (2004) · Biotechnology Progress · doi:10.1021/bp049847f · Cited by 88 · see citing works
Kim, N. S., & Lee, G. M. (2002) · Biotechnology and Bioengineering · doi:10.1002/bit.10191 · Cited by 86 · see citing works
Possible Role of Caspase-3 Inhibition in Cadmium-Induced Blockage of Apoptosis
Cai, Y., Kadiiska, M. B., Achanzar, W. E., Mason, R. P., & Waalkes, M. P. (2000) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2000.8921 · Cited by 84 · see citing works
Sung, Y. H., Hwang, S., & Lee, G. M. (2005) · Metabolic Engineering · doi:10.1016/j.ymben.2005.08.001 · Cited by 78 · see citing works
Zanghi, J. A., Renner, W. A., Bailey, J. E., & Fussenegger, M. (2000) · Biotechnology Progress · doi:10.1021/bp0000353 · Cited by 76 · see citing works
Yoon, S. K., Hong, J. K., Choo, S. H., Song, J. Y., Park, H. W., & Lee, G. M. (2005) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2005.09.010 · Cited by 74 · see citing works
Mohan, C., Park, S. H., Chung, J. Y., & Lee, G. M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21453 · Cited by 73 · see citing works
Chung, J. Y., Lim, S. W., Hong, Y. J., Hwang, S. O., & Lee, G. M. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.10919 · Cited by 73 · see citing works
Sung, Y. H., Lee, J. S., Park, S. H., Koo, J., & Lee, G. M. (2007) · Metabolic Engineering · doi:10.1016/j.ymben.2007.08.001 · Cited by 70 · see citing works
Choi, S. S., Rhee, W. J., Kim, E. J., & Park, T. H. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.21023 · Cited by 68 · see citing works
Choi, S. S., Rhee, W. J., & Park, T. H. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20550 · Cited by 68 · see citing works
Can, H. J. L. V., Braake, H. A. B. T., Bijman, A., Hellinga, C., Luyben, K. C. A. M., & Heijnen, J. J. (1999) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19990320)62:6 · Cited by 66 · see citing works
Kim, S. H., & Lee, G. M. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1041-6 · Cited by 60 · see citing works
Effect of glutamine limitation on the death of attached Chinese hamster ovary cells
Sanfeliu, A., & Stephanopoulos, G. N. (1999) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19990705)64:1 · Cited by 53 · see citing works
Chang, K. H., Kim, K. S., & Kim, J. H. (1999) · Free Radical Research · doi:10.1080/10715769900300091 · Cited by 52 · see citing works
Oh, H. K., So, M. K., Yang, J., Yoon, H. C., Ahn, J. S., Lee, J. M., Kim, J. T., Yoo, J. U., & Byun, T. H. (2005) · Biotechnology Progress · doi:10.1021/bp050057v · Cited by 48 · see citing works
Lee, M. S., & Lee, G. M. (2000) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(20000505)68:3 · Cited by 48 · see citing works
Quantification of Active Caspase 3 in Apoptotic Cells
Saunders, P. A., Cooper, J. A., Roodell, M. M., Schroeder, D. A., Borchert, C. J., Isaacson, A. L., Schendel, M. J., Godfrey, K. G., Cahill, D. R., Walz, A. M., et al. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4690 · Cited by 47 · see citing works
Metabolic burden in recombinant CHO cells: effect ofdhfr gene amplification andlacZ expression
Gu, M. B., Todd, P. W., & Kompala, D. S. (1996) · Cytotechnology · doi:10.1007/bf00767763 · Cited by 46 · see citing works
Park, H.-S., Kim, I. H., Kim, K., Kim, K., & Kim, H.-J. (2000) · Journal of Biotechnology · doi:10.1016/s0168-1656(00)00282-0 · Cited by 45 · see citing works
The role of the cell cycle in determining gene expression and productivity in CHO cells
Lloyd, D., Leelavatcharamas, V., Emery, A. N., & Al‐Rubeai, M. (1999) · Cytotechnology · doi:10.1023/a:1008093404237 · Cited by 44 · see citing works
Hwang, S. O., Chung, J. Y., & Lee, G. M. (2003) · Biotechnology Progress · doi:10.1021/bp025578m · Cited by 39 · see citing works
Development of apoptosis‐resistant dihydrofolate reductase‐deficient Chinese hamster ovary cell line
Lee, S. K., & Lee, G. M. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10633 · Cited by 35 · see citing works
Banik, G. G., Todd, P. W., & Kompala, D. S. (1996) · Cytotechnology · doi:10.1007/bf00353937 · Cited by 23 · see citing works
Hong, J. K., Kim, Y., Yoon, S. K., & Lee, G. M. (2006) · Metabolic Engineering · doi:10.1016/j.ymben.2006.11.003 · Cited by 18 · see citing works
Insect cell line dependent gene expression of recombinant human tumor necrosis factor-β
Chai, H., Al‐Rubeai, M., Chua, K. L., Oh, S., & Yap, M. G. S. (1996) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(95)00081-x · Cited by 16 · see citing works
The cellular response to protein unfolding stress
Schröder, M. (2007) · Cambridge University Press eBooks · doi:10.1017/cbo9780511902451.009 · Cited by 12 · see citing works
Gu, M. B., Todd, P. W., & Kompala, D. S. (1996) · Biotechnology Progress · doi:10.1021/bp950074s · Cited by 10 · see citing works
Chung, J. Y., Kim, T. K., & Lee, G. M. (2000) · BioTechniques · doi:10.2144/00294st02 · Cited by 9 · see citing works
Lloyd, D., & Al‐Rubeai, M. (1999) · Encyclopedia of Bioprocess Technology · doi:10.1002/0471250589.ebt038 · Cited by 1 · see citing works
Kim (2000) · doi:10.1002/1097-0290(2000)71:3
Flagged first, then by citations
Cited by
Sorted by citations
Kim, J. Y., Kim, Y.-G., & Lee, G. M. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3758-5 · Cited by 801 · see citing works
Microbial factories for recombinant pharmaceuticals
Ferrer‐Miralles, N., Domingo‐Espín, J., Corchero, J. L., Vázquez, E., & Villaverde, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-17 · Cited by 465 · see citing works
Glycosylation of Therapeutic Proteins
Solá, R. J., & Griebenow, K. H. (2010) · BioDrugs · doi:10.2165/11530550-000000000-00000 · Cited by 440 · see citing works
A review of the mammalian unfolded protein response
Chakrabarti, A., Chen, A. W., & Varner, J. D. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23282 · Cited by 408 · see citing works
Advances in Mammalian cell line development technologies for recombinant protein production
Lai, T., Yang, Y., & Ng, S. (2013) · Pharmaceuticals · doi:10.3390/ph6050579 · Cited by 322 · see citing works
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296 · see citing works
Guidelines to cell engineering for monoclonal antibody production
Rita Costa, A., Elisa Rodrigues, M., Henriques, M., Azeredo, J., & Oliveira, R. (2010) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2009.10.002 · Cited by 178 · see citing works
Proteomic analysis of Chinese hamster ovary cells
Baycin-Hizal, D., Tabb, D. L., Chaerkady, R., Chen, L., Lewis, N. E., Nagarajan, H., Sarkaria, V., Kumar, A., Wolozny, D., Colao, J., et al. (2012) · Journal of Proteome Research · doi:10.1021/pr300476w · Cited by 178 · see citing works
Gene Expression in Mammalian Cells and its Applications
Khan, K. H. (2013) · Europe PMC (PubMed Central) · doi:10.5681/apb.2013.042 · Cited by 166 · see citing works
Grillberger, L., Kreil, T. R., Nasr, S., & Reiter, M. (2009) · Biotechnology Journal · doi:10.1002/biot.200800241 · Cited by 144 · see citing works
An 'omics approach towards CHO cell engineering
Datta, P., Linhardt, R. J., & Sharfstein, S. T. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.24841 · Cited by 129 · see citing works
Matasci, M., Hacker, D. L., Baldi, L., & Wurm, F. M. (2008) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2008.12.003 · Cited by 115 · see citing works
Technological progresses in monoclonal antibody production systems
Rodrigues, M. E., Costa, A. R., Henriques, M., Azeredo, J., & Oliveira, R. (2009) · Biotechnology Progress · doi:10.1002/btpr.348 · Cited by 109 · see citing works
Predicting cell-specific productivity from CHO gene expression
Clarke, C., Doolan, P., Barron, N., Meleady, P., O’Sullivan, F., Gammell, P., Melville, M. W., Leonard, M. W., & CLYNES, M. M. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.11.016 · Cited by 94 · see citing works
Hansen, H. G., Pristovšek, N., Kildegaard, H. F., & Lee, G. M. (2016) · Biotechnology Advances · doi:10.1016/j.biotechadv.2016.11.008 · Cited by 72 · see citing works
Cell Line Techniques and Gene Editing Tools for Antibody Production: A Review
Dangi, A. K., Sinha, R., Dwivedi, S., Gupta, S. K., & Shukla, P. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00630 · Cited by 65 · see citing works
Hussain, H., Maldonado‐Agurto, R., & Dickson, A. J. (2014) · Biotechnology Letters · doi:10.1007/s10529-014-1537-y · Cited by 59 · see citing works
Advances in improving mammalian cells metabolism for recombinant protein production
Altamirano, C., Berríos, J., Vergara, M., & Becerra, S. (2013) · Electronic Journal of Biotechnology · doi:10.2225/vol16-issue3-fulltext-2 · Cited by 60 · see citing works
Sharker, S. M., & Rahman, A. (2020) · Current Drug Discovery Technologies · doi:10.2174/1570163817666200312102137 · Cited by 59 · see citing works
Goldrick, S., Lee, K. M. L., Spencer, C., Holmes, W., Kuiper, M., Turner, R., & Farid, S. S. (2017) · Biotechnology Journal · doi:10.1002/biot.201700607 · Cited by 57 · see citing works
Mammalian Cell Line Developments in Speed and Efficiency
Estes, S. D., & Melville, M. W. (2013) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2013_260 · Cited by 56 · see citing works
Identification of a novel temperature sensitive promoter in cho cells
Thaisuchat, H., Baumann, M., Pontiller, J., Hesse, F., & Ernst, W. (2011) · BMC Biotechnology · doi:10.1186/1472-6750-11-51 · Cited by 52 · see citing works
Mammalian cells as biopharmaceutical production hosts in the age of omics
Dietmair, S., Nielsen, L. K., & Timmins, N. E. (2011) · Biotechnology Journal · doi:10.1002/biot.201100369 · Cited by 50 · see citing works
Recombinant Protein Expression in Nicotiana
Matoba, N., Davis, K., & Palmer, K. E. (2010) · Methods in molecular biology · doi:10.1007/978-1-61737-957-4_11 · Cited by 46 · see citing works
Sheikholeslami, Z., Jolicœur, M., & Henry, O. (2014) · Biotechnology Progress · doi:10.1002/btpr.1907 · Cited by 45 · see citing works
Deshpande, R., Yang, T. H., & Heinzle, E. (2009) · Biotechnology Journal · doi:10.1002/biot.200800143 · Cited by 45 · see citing works
Sumitomo, Y., Higashitsuji, H., Higashitsuji, H., Liu, Y., Fujita, T., Sakurai, T., Candeias, M. M., Itoh, K., Chiba, T., & Fujita, J. (2012) · BMC Biotechnology · doi:10.1186/1472-6750-12-72 · Cited by 41 · see citing works
Chin, C. L., Chin, H. K., Chin, C. S. H., Lai, E. T., & Ng, S. K. (2015) · BMC Biotechnology · doi:10.1186/s12896-015-0145-9 · Cited by 37 · see citing works
Lee, H. W., Christie, A., Liu, J. J., & Yoon, S. (2012) · Biotechnology Progress · doi:10.1002/btpr.1536 · Cited by 32 · see citing works
Engineering a mammalian super producer
Dietmair, S., Nielsen, L. K., & Timmins, N. E. (2011) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.2576 · Cited by 31 · see citing works
Wei, M., Mi, C., Jing, C., & Wang, T. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.879222 · Cited by 31 · see citing works
Li, Y., Tian, Z., Xu, D., Wang, X.-Y., & Wang, T. (2018) · Molecular Biology Reports · doi:10.1007/s11033-018-4351-0 · Cited by 30 · see citing works
Hansen, H. G., Nilsson, C. N., Lund, A. M., Kol, S., Grav, L. M., Lundqvist, M., Rockberg, J., Lee, G. M., Andersen, M. R., & Kildegaard, H. F. (2015) · Scientific Reports · doi:10.1038/srep18016 · Cited by 28 · see citing works
Kuang, B., Dhara, V. G., Hoang, D. M., Jenkins, J. P., Ladiwala, P., Tan, Y., Shaffer, S. A., Galbraith, S., Betenbaugh, M. J., & Yoon, S. (2021) · Metabolic Engineering Communications · doi:10.1016/j.mec.2021.e00182 · Cited by 27 · see citing works
Scarcelli, J. J., Hone, M., Beal, K. M., Ortega, A., Figueroa, B., Starkey, J. A., & Anderson, K. (2018) · Biotechnology Progress · doi:10.1002/btpr.2646 · Cited by 27 · see citing works
Proteins improving recombinant antibody production in mammalian cells
Nishimiya, D. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5427-3 · Cited by 26 · see citing works
In search of expression bottlenecks in recombinant CHO cell lines—a case study
Reinhart, D., Sommeregger, W., Debreczeny, M., Gludovacz, E., & Kunert, R. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5584-z · Cited by 25 · see citing works
Zhang, Z., Albanetti, T., Linkous, T., Larkin, C. J., Schoner, R., McGivney, J. B., & Dovichi, N. J. (2017) · ELECTROPHORESIS · doi:10.1002/elps.201600390 · Cited by 23 · see citing works
Exploration of BAC versus plasmid expression vectors in recombinant CHO cells
Mäder, A., Prewein, B., Zboray, K., Casanova, E., & Kunert, R. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4498-x · Cited by 23 · see citing works
Apostolidis, P. A., Tseng, A., Koziol, M.-E., Betenbaugh, M. J., & Chiang, B. (2015) · Biochemical Engineering Journal · doi:10.1016/j.bej.2015.01.013 · Cited by 20 · see citing works
Doolan, P., Barron, N., Kinsella, P., Clarke, C., Meleady, P., O’Sullivan, F., Melville, M. W., Leonard, M. W., & CLYNES, M. M. (2011) · Biotechnology Journal · doi:10.1002/biot.201100255 · Cited by 19 · see citing works
Kim, Y., & Lee, G. M. (2009) · Biotechnology Progress · doi:10.1002/btpr.91 · Cited by 19 · see citing works
Hussain, H., Patel, T., Ozanne, A. M. S., Vito, D., Ellis, M., Hinchliffe, M., Humphreys, D. P., Stephens, P. E., Sweeney, B., White, J., et al. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27944 · Cited by 18 · see citing works
Maldonado‐Agurto, R., & Dickson, A. J. (2018) · Biotechnology Journal · doi:10.1002/biot.201700429 · Cited by 18 · see citing works
Silkworm Storage Protein 1 Inhibits Autophagy-Mediated Apoptosis
Kang, S. J., & Rhee, W. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020318 · Cited by 18 · see citing works
Factors and Mechanisms Affecting the Secretion of Recombinant Protein in CHO Cells
Wang, T., Feng, H., Yang, Y. X., Li, Q., & Li, W. (2022) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201023666220603121316 · Cited by 17 · see citing works
Vector-related stratagems for enhanced monoclonal antibody production in mammalian cells
Gupta, K., Parasnis, M. S., Jain, R. D., & Dandekar, P. P. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107415 · Cited by 17 · see citing works
Advances of Glycometabolism Engineering in Chinese Hamster Ovary Cells
Zhang, H.-Y., Fan, Z., & Wang, T. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.774175 · Cited by 16 · see citing works
Chandrawanshi, V., Kulkarni, R., Prabhu, A., & Mehra, S. (2020) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2020.02.008 · Cited by 15 · see citing works
Plant biofarming: Novel insights for peptide expression in heterologous systems
Viana, A. A. B., Pelegrini, P. B., & Grossi‐de‐Sá, M. F. (2012) · Biopolymers · doi:10.1002/bip.22089 · Cited by 15 · see citing works
Methods for Using Small Non-Coding RNAs to Improve Recombinant Protein Expression in Mammalian Cells
Inwood, S., Betenbaugh, M. J., & Shiloach, J. (2018) · Genes · doi:10.3390/genes9010025 · Cited by 15 · see citing works
Kim, J. Y., Kim, Y., & Lee, G. M. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24442 · Cited by 14 · see citing works
Naik, H. M., Cai, X., Ladiwala, P., Reddy, J. V., Betenbaugh, M. J., & Antoniewicz, M. R. (2024) · Metabolic Engineering · doi:10.1016/j.ymben.2024.03.002 · Cited by 13 · see citing works
Lin, P., Liu, R., Alvin, K., Shahreel, W., Murgolo, N., Ye, J., Du, Z., & Song, Z. (2020) · Biotechnology Journal · doi:10.1002/biot.202000267 · Cited by 13 · see citing works
Evaluation of the OSCAR™ system for the production of monoclonal antibodies by CHO-K1 cells
Costa, A. R., Rodrigues, M. E., Henriques, M., Melton, D., Cunnah, P., Oliveira, R., & Azeredo, J. (2012) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2012.03.028 · Cited by 12 · see citing works
Baek, E. H., Lee, J. S., & Lee, G. M. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26777 · Cited by 12 · see citing works
Ladiwala, P., Cai, X., Naik, H. M., Aliyu, L., Schilling, M., Antoniewicz, M. R., & Betenbaugh, M. J. (2024) · Metabolic Engineering · doi:10.1016/j.ymben.2024.07.008 · Cited by 11 · see citing works
Gonzalez, J. E., Naik, H. M., Oates, E. H., Dhara, V. G., McConnell, B. O., Kumar, S., Betenbaugh, M. J., & Antoniewicz, M. R. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403033121 · Cited by 11 · see citing works
Modifications of a signal sequence for antibody secretion from insect cells
Ohmuro‐Matsuyama, Y., & Yamaji, H. (2017) · Cytotechnology · doi:10.1007/s10616-017-0109-0 · Cited by 11 · see citing works
Ventini, D. C., Damiani, R., de Sousa, A. P. B., Oliveira, J. E., Peroni, C. N., Ribela, M. T. C. P., Bartolini, P., Tonso, A., Soares, C. R. J., & Pereira, C. A. D. B. (2010) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-010-9143-5 · Cited by 10 · see citing works
Rahimi, A., Karimipoor, M., Mahdian, R., Alipour, A., Hosseini, S., Mohammadi, M., Kaghazian, H., Abbasi, A., Shahsavarani, H., & Shokrgozar, M. A. (2023) · PubMed Central · doi:10.30498/ijb.2023.343428.3388 · Cited by 10 · see citing works
Zhu, G., Sun, L., Albanetti, T., Linkous, T., Larkin, C. J., Schoner, R. G., McGivney, J. B., & Dovic̀hi, N. J. (2016) · Biotechnology and Bioengineering · doi:10.1002/bit.25991 · Cited by 10 · see citing works
Florin, L., Lipske, C., Becker, E., & Kaufmann, H. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.02.002 · Cited by 8 · see citing works
Efficient production of FAM19A4, a novel potential cytokine, in a stable optimized CHO-S cell system
Liu, H., Wang, X., Shi, S. J., Chen, Y., & Han, W. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.05.004 · Cited by 7 · see citing works
Kim, J. Y., Kim, Y., Baik, J. Y., Joo, E. J., Kim, Y. H., & Lee, G. M. (2009) · Biotechnology Progress · doi:10.1002/btpr.323 · Cited by 7 · see citing works
Towards Enhancing Therapeutic Glycoprotein Bioproduction: Interventions in the PI3K/AKT/mTOR Pathway
Mahameed, M., Sulieman, A., Alkam, D., & Tirosh, B. (2019) · Cell Structure and Function · doi:10.1247/csf.19013 · Cited by 6 · see citing works
Rahimi, A., Karimipoor, M., Mahdian, R., Alipour, A., Hosseini, S., Kaghazian, H., Abbasi, A., Shahsavarani, H., & Shokrgozar, M. A. (2023) · Iranian journal of pharmaceutical research · doi:10.5812/ijpr-130236 · Cited by 6 · see citing works
Simultaneous environmental manipulations in semi-perfusion cultures of CHO cells producing rh-tPA
Altamirano, C., Vergara, M., Becerra, S., Díaz‐Barrera, A., & Berríos, J. (2012) · Electronic Journal of Biotechnology · doi:10.2225/vol15-issue6-fulltext-2 · Cited by 6 · see citing works
Ohmuro‐Matsuyama, Y., Mori, K., Hamada, H., Ueda, H., & Yamaji, H. (2016) · Cytotechnology · doi:10.1007/s10616-016-9955-4 · Cited by 6 · see citing works
Cell Engineering for Therapeutic Protein Production
Baek, E. H., Kim, C. L., Park, J. H., & Lee, G. M. (2014) · Cell engineering · doi:10.1007/978-3-319-10320-4_18 · Cited by 5 · see citing works
Sorourian, S., Behzad‐Behbahani, A., Forouzanfar, M., Jafarinia, M., & Safari, F. (2024) · PubMed Central · doi:10.30498/ijb.2024.398567.3714 · Cited by 4 · see citing works
Hysteretic Genetic Circuit for Detection of Proteasomal Degradation in Mammalian Cells
Zeng, Y., Bachhav, B., Zhao, W., Nguyen, T. T. N., & Segatori, L. (2019) · ACS Synthetic Biology · doi:10.1021/acssynbio.9b00074 · Cited by 4 · see citing works
Exploring the Multifaceted Role of Microbes in Pharmacology
Mishra, M., Vishwakarma, K., Singh, J., Jain, S., Kumar, V., Tripathi, D. K., & Sharma, S. (2018) · Springer eBooks · doi:10.1007/978-981-10-7140-9_15 · Cited by 4 · see citing works
Kim, Y., Han, Y. K., Kim, J. Y., Lee, E. G., Lee, H. W., & Lee, G. M. (2011) · Biotechnology Progress · doi:10.1002/btpr.567 · Cited by 4 · see citing works
Bawn, A., Lee, H. W., Downey, A., Xu, J., Starkey, J. A., & Yoon, S. (2013) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.13.31 · Cited by 3 · see citing works
Development of Magoh protein‐overexpressing HEK cells for optimized therapeutic protein production
Mufarrege, E. F., Benizio, E., Prieto, C. C., Chiappini, F. A., Rodríguez, M. C., Etcheverrigaray, M., & Kratje, R. B. (2020) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1915 · Cited by 3 · see citing works
Effects of lithium on the secretory production of recombinant antibody from insect cells
Ohmuro‐Matsuyama, Y., Katsuda, T., & Yamaji, H. (2018) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-018-0303-1 · Cited by 3 · see citing works
Mechanistic Modeling and Analysis of the Mammalian Unfolded Protein ResponsePreprint
Chakrabarti, A., Aboulmouna, L., & Varner, J. D. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/060020 · Cited by 3 · see citing works
Advanced Bioprocess Engineering: Fed‐Batch and Perfusion Processes
Mehra, S., Chandrawanshi, V., & Segar, K. P. (2017) · doi:10.1002/9783527800599.ch14 · Cited by 3 · see citing works
Mammalian cell lines used in bioprocessing
ERGEN, N., & TÜFEKÇİ, H. (2022) · Journal of Experimental and Clinical Medicine · doi:10.52142/omujecm.39.3.55 · Cited by 2 · see citing works
Aihara, Y., Fujiwara, N., Yamazaki, T., Kambe, T., Nagao, M., Hirose, Y., & Masuda, S. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.03.024 · Cited by 2 · see citing works
Kutsuzawa, K., Suzuki, T., Kishimoto, H., Murakami, A., Azuma, T., Abe, R., & Otsuka, H. (2013) · Colloid & Polymer Science · doi:10.1007/s00396-013-3093-8 · Cited by 1 · see citing works
Raigani, M., Barkhordari, F., Moazzami, R., Davami, F., & Mahboudi, F. (2022) · Brazilian Journal of Pharmaceutical Sciences · doi:10.1590/s2175-97902022e19692 · Cited by 1 · see citing works
Recombinant protein expression in mammalian cells
Joshi, M., Verma, P., Mago, P., Agrawal, Y., Gunwal, I., Khurana, S., Tanwar, J., Yadav, U., & Yadav, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-98388-4.00008-3 · Cited by 1 · see citing works
Chin, C. L., Chin, H. K., Chin, C. S. H., Lai, E. T., & KongNg, S. (2015) · BMC Proceedings · doi:10.1186/1753-6561-9-s9-p10 · Cited by 1 · see citing works
Membrane Protein Expression in Mammalian Cells
Hızal, D. B., Ohsfeldt, E., Mai, S., & Betenbaugh, M. J. (2011) · doi:10.1002/9783527634521.ch5
HIGH-ACTIVITY MUTANTS OF HUMAN BUTYRYLCHOLINESTERASE FOR COCAINE ABUSE TREATMENT
Liu, X. (2013) · UKnowledge (University of Kentucky)
Becker, E. (2008) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1784
Current advances in applications of cell culture
Kuystermans, D., & Al‐Rubeai, M. (2012) · Methods · doi:10.1016/j.ymeth.2012.04.008
Production of recombinant protein hLIF in static and dynamic systems of animal cell culture
Barata, D. B. (2009) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Hadbi, P.-M. (2020) · Journal of Bioprocessing & Biotechniques
Recombinant expression systems
(2015) · CRC Press eBooks · doi:10.1201/b19077-7
(2008) · Biotechnology Journal · doi:10.1002/biot.200890071
Research Progress on Prokaryotic and Eukaryotic Expression Systems in Fish
宋, 嘉. (2025) · Hans Journal of Agricultural Sciences · doi:10.12677/hjas.2025.155075
Rahimi, A., Karimipoor, M., Mahdian, R., Alipour, A., Hosseini, S., Mohammadi, M., Kaghazian, H., Shahsavarani, H., & Shokrgozar, M. A. (2025) · Iranian Biomedical Journal · doi:10.61882/ibj.4934
Biological Treatments (Antibodies)
Paradise, W. A., & Radosevich, J. A. (2013) · Springer eBooks · doi:10.1007/978-94-007-5827-8_29
- Authors
- Mohan
- Venue
- Biotechnology Journal
- Publisher
- Wiley
- Published
- 2008-05
- Volume
- 3
- Issue
- 5
- Pages
- 624-630
- ISSN
- 1860-6768 (ISSN-L)
- 1860-7314
- OpenAlex
- W2077304355
- Cited by
- 102
- References
- 41
- Citations by year
- 2025: 2 · 2024: 5 · 2023: 3 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 5 · 2016: 5 · 2015: 6 · 2014: 4 · 2013: 12 · 2012: 9
- FWCI
- 0.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biotechnology Journal (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- CHO cell engineering, therapeutic proteins, specific productivity, culture longevity, programmed cell death, CHO cells, bioprocess optimization
- MeSH terms
- Animals, Cricetulus, Cricetinae, Recombinant Proteins, Technology Assessment, Biomedical, Protein Engineering, CHO Cells, Genetic Enhancement
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