The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
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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In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
Citations
Cites
Encyclopedia of bioprocess technology: fermentation, biocatalysis, and bioseparation
(1999) · Choice Reviews Online · doi:10.5860/choice.37-1896 · Cited by 864
Yoon, S. K., Song, J. Y., & Lee, G. M. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10566 · Cited by 244
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
Borth, N., Mattanovich, D., Kunert, R., & Katinger, H. W. D. (2005) · Biotechnology Progress · doi:10.1021/bp0498241 · Cited by 191
Kim, S. H., & Lee, G. M. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0654-5 · Cited by 135
Effect of solution pH on protein transport through ultrafiltration membranes
Burns, D. B., & Zydney, A. L. (1999) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19990705)64:1 · Cited by 122
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
Kim, N. S., & Lee, G. M. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(02)00011-1 · Cited by 106
What's fueling the biotech engine?
Aggarwal, S. (2007) · Nature Biotechnology · doi:10.1038/nbt1007-1097 · Cited by 105
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
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Research works printed but not linked: 2
- 10.1016/S0168-1656(02)00011-1 · DOI
- Chung J. Y. Development of recombinant Chinese hamster ovary cell lines producing human thrombopoietin analogs.PhD thesis Department of Biological Sciences KAIST Daejeon Korea 2002.
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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
Glycosylation of Therapeutic Proteins
Solá, R. J., & Griebenow, K. H. (2010) · BioDrugs · doi:10.2165/11530550-000000000-00000 · Cited by 443
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Chakrabarti, A., Chen, A. W., & Varner, J. D. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23282 · Cited by 428
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
Therapeutic glycoprotein production in mammalian cells
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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
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
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Grillberger, L., Kreil, T. R., Nasr, S., & Reiter, M. (2009) · Biotechnology Journal · doi:10.1002/biot.200800241 · Cited by 144
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Datta, P., Linhardt, R. J., & Sharfstein, S. T. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.24841 · Cited by 136
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 117
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 116
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 97
Hansen, H. G., Pristovšek, N., Kildegaard, H. F., & Lee, G. M. (2016) · Biotechnology Advances · doi:10.1016/j.biotechadv.2016.11.008 · Cited by 73
Cell Line Techniques and Gene Editing Tools for Antibody Production: A Review
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Hussain, H., Maldonado‐Agurto, R., & Dickson, A. J. (2014) · Biotechnology Letters · doi:10.1007/s10529-014-1537-y · Cited by 59
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Sharker, S. M., & Rahman, A. (2020) · Current Drug Discovery Technologies · doi:10.2174/1570163817666200312102137 · Cited by 62
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 62
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Estes, S. D., & Melville, M. W. (2013) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2013_260 · Cited by 65
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
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Matoba, N., Davis, K., & Palmer, K. E. (2010) · Methods in molecular biology · doi:10.1007/978-1-61737-957-4_11 · Cited by 46
Sheikholeslami, Z., Jolicœur, M., & Henry, O. (2014) · Biotechnology Progress · doi:10.1002/btpr.1907 · Cited by 45
Deshpande, R., Yang, T. H., & Heinzle, E. (2009) · Biotechnology Journal · doi:10.1002/biot.200800143 · Cited by 45
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
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
Lee, H. W., Christie, A., Liu, J. J., & Yoon, S. (2012) · Biotechnology Progress · doi:10.1002/btpr.1536 · Cited by 32
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Wei, M., Mi, C., Jing, C., & Wang, T. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.879222 · Cited by 34
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
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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
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Baek, E. H., Lee, J. S., & Lee, G. M. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26777 · Cited by 12
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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
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
Raigani, M., Barkhordari, F., Moazzami, R., Davami, F., & Mahboudi, F. (2022) · Brazilian Journal of Pharmaceutical Sciences · doi:10.1590/s2175-97902022e19692 · Cited by 1
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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
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
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Becker, E. (2008) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1784
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Barata, D. B. (2009) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
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(2008) · Biotechnology Journal · doi:10.1002/biot.200890071
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Metadata
- Authors
- Mohan, C., Kim, Y., Koo, J., & Lee, G. M.
- Affiliations
- Korea Advanced Institute of Science and Technology (KR)
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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