The DOI matches its Crossref record; 218 of the 220 references it cites were found in a registry or an index.
Guidelines to cell engineering for monoclonal antibody production
Open accessAbstract
Monoclonal antibodies (mAbs) are currently used for many diagnostic and therapeutic applications. The high demand for these biopharmaceuticals has led to the development of large-scale manufacturing processes, with productivity improvements being mainly achieved by optimization of bioreactor systems. However, more recently, the early steps of production, previous to bioreactor culture, have been presented as alternative areas where productivity enhancements can be achieved. Thus, this review describes the progress made for the improvement of productivity in mammalian expression systems for the high production of mAbs. Advances in the development of mAb-producing cell lines are being made, particularly regarding expression vector design and methods used for transfection, with the intent to create a reproducible methodology. Selection of the most suitable clones is also a critical step that can be improved, by including variables other than the expression level, which is still the common practice. Furthermore, strategies of cell engineering, although still mostly based on trial-and-error experimentation and not in standard protocols, hold great interest to improve cell growth and productivity, as well as product quality in the future. Improvements of the initial steps of the production process would not only result in cells with higher expression ability, but would also speed-up the process development.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Yet, it is ideal for high throughput screening for hits identification and very helpful for early stage product characterization (Ozturk and Hu, 2005;Rosser et al., 2005;Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010
In the citing paper
“By skipping the lengthy selection process for the cells that have integrated the plasmid within their genome, transient transfection is much faster (Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010
In the citing paper
“For stable expression, a gene marker is usually integrated in the expression plasmid along with the cDNA encoding the gene of interest, conferring a selective advantage to the cells that integrate the plasmid into their genome (Rita Costa et al., 2010).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Rita Costa et al., 2010
Citations
Cites
Continuous cultures of fused cells secreting antibody of predefined specificity
Köhler, G., & Milstein, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,200
A new technique for the assay of infectivity of human adenovirus 5 DNA
Graham, F. L., & van der Eb, A. J. (1973) · Virology · doi:10.1016/0042-6822(73)90341-3 · Cited by 9,302
Boussif, O., Lezoualc’h, F., Zanta, M. A., Djavaheri‐Mergny, M., Scherman, D., DEMENEIX, B. A., & Behr, J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7297 · Cited by 6,256
Kozak, M. (1986) · Cell · doi:10.1016/0092-8674(86)90762-2 · Cited by 4,741
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Freshney, R. I. (2005) · Wiley eBooks · doi:10.1002/9780470649367 · Cited by 3,904
Transcriptional Activation by Tetracyclines in Mammalian Cells
Gossen, M., Freundlieb, S., Bender, G., Müller, G., Hillen, W., & Bujard, H. (1995) · Science · doi:10.1126/science.7792603 · Cited by 2,488 · cited 1×
“[68], the tetracycline (tet) [69,70], the streptogramin [71] and the ecdysone [72] systems.”
BackgroundSV40-transformed simian cells support the replication of early SV40 mutants
Gluzman, Y. (1981) · Cell · doi:10.1016/0092-8674(81)90282-8 · Cited by 2,343
Production of recombinant protein therapeutics in cultivated mammalian cells
Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032
Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413
Flagged first, then by citations
2 of the 220 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Trends in Upstream and Downstream Process Development for Antibody Manufacturing
Gronemeyer, P., Ditz, R., & Strube, J. (2014) · Bioengineering · doi:10.3390/bioengineering1040188 · Cited by 347
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
Perfusion mammalian cell culture for recombinant protein manufacturing – A critical review
Bielser, J., Wolf, M., Souquet, J., Broly, H., & Morbidelli, M. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.04.011 · Cited by 284
Advances in the production and downstream processing of antibodies
Chon, J. H., & Zarbis‐Papastoitsis, G. (2011) · New Biotechnology · doi:10.1016/j.nbt.2011.03.015 · Cited by 230
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
Ho, S. C. L., Bardor, M., Feng, H., Mariati, Tong, Y. W., Song, Z., Yap, M. G. S., & Yang, Y. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.09.023 · Cited by 153
Improving the efficiency of CHO cell line generation using glutamine synthetase gene knockout cells
Fan, L., Kadura, I. A., Krebs, L. E., Hatfield, C. C., Shaw, M., & Frye, C. C. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.24365 · Cited by 151
Yin, G., Garces, E. D., Yang, J., Zhang, J., Tran, C., Steiner, A. R., Roos, C. M., Bajad, S. U., Hudak, S. A., Penta, K., et al. (2012) · mAbs · doi:10.4161/mabs.4.2.19202 · Cited by 145
Host cell protein dynamics in the supernatant of a mAb producing CHO cell line
Tait, A. S., Hogwood, C. E. M., Smales, C. M., & Bracewell, D. G. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.24383 · Cited by 135
Pezzoli, D., Giupponi, E., Mantovani, D., & Candiani, G. (2017) · Scientific Reports · doi:10.1038/srep44134 · Cited by 121
Ho, S. C. L., Koh, E. Y. C., van Beers, M. M. C., Mueller, M., Wan, C., Teo, G., Song, Z., Tong, Y. W., Bardor, M., & Yang, Y. (2013) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.03.019 · Cited by 98
Noh, S. M., Shin, S., & Lee, G. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-23720-9 · Cited by 98
The emerging role of systems biology for engineering protein production in CHO cells
Kuo, C., Chiang, A. W. T., Shamie, I., Samoudi, M., Gutierrez, J. M., & Lewis, N. E. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.11.015 · Cited by 83
Development of generic raman models for a GS‐KO TM CHO platform process
Webster, T. A., Hadley, B. C., Hilliard, W., Jaques, C., & Mason, C. (2018) · Biotechnology Progress · doi:10.1002/btpr.2633 · Cited by 77
Gupta, S. K., & Shukla, P. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00419 · Cited by 81
Ho, S. C. L., Bardor, M., Li, B., Lee, J. J., Song, Z., Tong, Y. W., Goh, L., & Yang, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063247 · Cited by 76
Torkashvand, F., Vaziri, B., Maleknia, S., Heydari, A., Vossoughi, M., Davami, F., & Mahboudi, F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140597 · Cited by 72
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 66
The CAG promoter maintains high‐level transgene expression in HEK293 cells
Dou, Y.-Y., Lin, Y., Wang, T., Wang, X., Jia, Y., & Zhao, C. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.13029 · Cited by 63
Therapeutic proteins: developments, progress, challenges, and future perspectives
Kumar, V., Barwal, A., Sharma, N., Mir, D. S., Kumar, P., & Kumar, V. (2024) · 3 Biotech · doi:10.1007/s13205-024-03958-z · Cited by 62
Ho, S. C. L., Mariati, Yeo, J. H. M., Fang, S. G., & Yang, Y. (2014) · Molecular Biotechnology · doi:10.1007/s12033-014-9809-2 · Cited by 62
Precision genome editing: A small revolution for glycobiology
Steentoft, C., Bennett, E., Schjoldager, K. T.-B. G., Vakhrushev, S. Y., Wandall, H. H., & Clausen, H. (2014) · Glycobiology · doi:10.1093/glycob/cwu046 · Cited by 62
Monoclonal antibodies: A review of therapeutic applications and future prospects
Mahmuda, A., Bande, F., Al-Zihiry, K. J. K., Abdulhaleem, N., Majid, R. A., Hamat, R. A., Abdullah, W. O., & Unyah, N. Z. (2017) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v16i3.29 · Cited by 54
The present state of the art in expression, production and characterization of monoclonal antibodies
Gaughan, C. L. (2015) · Molecular Diversity · doi:10.1007/s11030-015-9625-z · Cited by 57
Multimodal chromatography: debottlenecking the downstream processing of monoclonal antibodies
Pinto, I. F., Aires-Barros, M. R., & Azevedo, A. M. (2015) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.15.7 · Cited by 53
Lanza, A. M., Kim, D. S., & Alper, H. S. (2013) · Biotechnology Journal · doi:10.1002/biot.201200364 · Cited by 53
Development of a highly-efficient CHO cell line generation system with engineered SV40E promoter
Fan, L., Kadura, I. A., Krebs, L. E., Larson, J. L., Bowden, D. M., & Frye, C. C. (2013) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.08.021 · Cited by 46
Optimizing antibody expression: The nuts and bolts
Ayyar, B. V., Arora, S., & Ravi, S. S. (2017) · Methods · doi:10.1016/j.ymeth.2017.01.009 · Cited by 46
Nishimiya, D., Mano, T., Miyadai, K., Yoshida, H., & Takahashi, T. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4365-9 · Cited by 47
Process analytical technology as key‐enabler for digital twins in continuous biomanufacturing
Schmidt, A., Helgers, H., Lohmann, L. J., Vetter, F. L., Juckers, A., Mouellef, M., Zobel‐Roos, S., & Strube, J. (2021) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.7008 · Cited by 45
Site‐specific proteolytic degradation of IgG monoclonal antibodies expressed in tobacco plants
Hehle, V. K., Lombardi, R., van Dolleweerd, C. J., Paul, M. J., Micco, P. D., Morea, V., Benvenuto, E., Donini, M., & K‐C., J. (2014) · Plant Biotechnology Journal · doi:10.1111/pbi.12266 · Cited by 45
Zhao, C., Guo, X. H., Chen, S.-J., Li, C., Yang, Y., Zhang, J., Chen, S.-N., Jia, Y., & Wang, T. (2017) · Scientific Reports · doi:10.1038/srep42805 · Cited by 44
Majumdar, S., Desai, R., Hans, A. K., Dandekar, P. P., & Jain, R. D. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01060-6 · Cited by 44
Generation of monoclonal antibody-producing mammalian cell lines
Ho, S. C., Tong, Y. W., & Yang, Y. (2013) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.13.8 · Cited by 41
Lin, P.-C., Chan, K. F., Kieß, I. A., Tan, J. L., Shahreel, W., Wong, S.-Y., & Song, Z. (2019) · mAbs · doi:10.1080/19420862.2019.1612690 · Cited by 42
Mozziconacci, O., Kerwin, B. A., & Schöneich, C. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100193b · Cited by 41
Noh, S. M., Park, J. H., Lim, J., Kim, J., & Lee, G. M. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7876-y · Cited by 42
Jutras, P. V., D’Aoust, M., Couture, M., Vezina, L. P., Goulet, M., Michaud, D., & Sainsbury, F. (2015) · Biotechnology Journal · doi:10.1002/biot.201500056 · Cited by 39
Gronemeyer, P., Ditz, R., & Strube, J. (2016) · Biochemical Engineering Journal · doi:10.1016/j.bej.2016.06.016 · Cited by 39
Moritz, B., Woltering, L., Becker, P. B., & Göpfert, U. (2016) · Biotechnology Progress · doi:10.1002/btpr.2271 · Cited by 37
Fan, L., Frye, C. C., & Racher, A. J. (2013) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.13.56 · Cited by 35
Tozuka, Y., Higashi, K., Morita, T., Nishikawa, M., Uchiyama, H., Zhang, J., Moribe, K., Nishikawa, K., Takeuchi, H., & Yamamoto, K. (2012) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2012.05.005 · Cited by 35
Webster, T. A., Hadley, B. C., Dickson, M., Busa, J. K., Jaques, C., & Mason, C. (2021) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-020-02429-y · Cited by 33
Olivier, S., Jacoby, M., Brillon, C., Bouletreau, S., Mollet, T., Nerrière, O., Angel, A., Danet, S., Souttou, B., Guéhenneux, F., et al. (2010) · mAbs · doi:10.4161/mabs.12350 · Cited by 34
Monoclonal antibody and its use in the diagnosis of livestock diseases
Deb, R., Chakraborty, S., Veeregowda, B., Verma, A. K., Tiwari, R., & Dhama, K. (2013) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2013.44a008 · Cited by 32
Kornecki, M., Schmidt, A., Lohmann, L. J., Huter, M. J., Mestmäcker, F., Klepzig, L., Mouellef, M., Zobel‐Roos, S., & Strube, J. (2019) · Processes · doi:10.3390/pr7080495 · Cited by 32
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
Jazayeri, S. H., Amiri‐Yekta, A., Bahrami, S., Gourabi, H., Sanati, M. H., & Khorramizadeh, M. R. (2018) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-017-2689-8 · Cited by 33
Cell factory engineering: Challenges and opportunities for synthetic biology applications
Bachhav, B., de Rossi, J., Llanos, C. P., & Segatori, L. (2023) · Biotechnology and Bioengineering · doi:10.1002/bit.28365 · Cited by 33
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
Kontturi, L.-S., Collin, E. C., Murtomäki, L. S., Pandit, A. S., Yliperttula, M. L., & Urtti, A. O. (2014) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2014.10.005 · Cited by 31
Wang, W., Jia, Y., Li, Y.-C., Jing, C., Guo, X. H., Shang, X., Zhao, C., & Wang, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-10966-y · Cited by 28
RetractedGeneration of recombinant hyperimmune globulins from diverse B-cell repertoires
Keating, S. M., Mizrahi, R. A., Adams, M. S., Asensio, M. A., Benzie, E., Carter, K. P., Chiang, Y., Edgar, R. C., Gautam, B. K., Gras, A., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00894-8 · Cited by 32
Marx, N., Dhiman, H., Schmieder, V., Freire, C. M., Ly, N. N., Klanert, G., & Borth, N. (2021) · Metabolic Engineering · doi:10.1016/j.ymben.2021.04.014 · Cited by 26
Mounaouer, B., Nesrine, A., & Hassen, A. (2013) · Desalination and Water Treatment · doi:10.1080/19443994.2013.823565 · Cited by 27
Ebadat, S., Ahmadi, S., Ahmadi, M., Nematpour, F., Barkhordari, F., Mahdian, R., Davami, F., & Mahboudi, F. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185967 · Cited by 27
Scale-Up of Protein Purification: Downstream Processing Issues
Milne, J. J. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-913-0_5 · Cited by 26
Gulis, G., Simi, K. C. R., de Toledo, R. R., Maranhão, A. Q., & Brígido, M. M. (2014) · BMC Biotechnology · doi:10.1186/1472-6750-14-26 · Cited by 26
Abali, F., Stevens, M., Tibbe, A. G. J., Terstappen, L. W. M. M., van der Velde, P. N., & Schasfoort, R. B. M. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.05.021 · Cited by 24
Stamatis, C., & Farid, S. S. (2020) · Biotechnology Journal · doi:10.1002/biot.202000238 · Cited by 24
Recombinant Antibody Production Using a Dual-Promoter Single Plasmid System
Carrara, S. C., Fiebig, D., Bogen, J. P., Grzeschik, J., Hock, B. M., & Kolmar, H. (2021) · Antibodies · doi:10.3390/antib10020018 · Cited by 22
González-Hernández, Y., & Perré, P. (2024) · Metabolic Engineering Communications · doi:10.1016/j.mec.2024.e00232 · Cited by 21
Pape, F. L., Bossard, M., Dutheil, D., Rousselot, M., Polard, V., Férec, C., Leize‐Zal, E., Delépine, P., & Zal, F. (2015) · Artificial Cells Nanomedicine and Biotechnology · doi:10.3109/21691401.2015.1029632 · Cited by 26
Dimasi, N., Fleming, R. L., Wu, H., & Gao, C. (2018) · Methods · doi:10.1016/j.ymeth.2018.08.004 · Cited by 22
Biologic Therapy and Severe Asthma in Children
Russo, D., Filippo, P. D., Attanasi, M., Lizzi, M., Pillo, S. D., & Chiarelli, F. (2021) · Biomedicines · doi:10.3390/biomedicines9070760 · Cited by 23
Ho, S. C. L., & Yang, Y. (2014) · Biotechnology Letters · doi:10.1007/s10529-014-1523-4 · Cited by 21
Okumura, T., Masuda, K., Watanabe, K., Miyadai, K., Nonaka, K., Yabuta, M., & Ōmasa, T. (2015) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2015.01.007 · Cited by 21
New Mammalian Expression Systems
Zhu, J., & Hatton, D. (2017) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2016_55 · Cited by 21
Al‐Taie, A., & Bülbül, E. Ö. (2023) · Journal of drug targeting · doi:10.1080/1061186x.2023.2295803 · Cited by 20
Recent advances in recombinant protein production
Kunert, R., & Casanova, E. (2013) · Bioengineered · doi:10.4161/bioe.24060 · Cited by 21
An arginase-based system for selection of transfected CHO cells without the use of toxic chemicals
Roca, B. C., Lao, N. T., Barron, N., Doolan, P., & CLYNES, M. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011162 · Cited by 25
Al‐Taie, A., & Sheta, N. (2023) · Clinical Therapeutics · doi:10.1016/j.clinthera.2023.10.016 · Cited by 19
Mead, E. J., Masterton, R. J., Feary, M., Obrezanova, O., Zhang, L., Young, R., & Smales, C. M. (2015) · Biochemical Journal · doi:10.1042/bj20150928 · Cited by 18
A doubly auxotrophic CHO‐K1 cell line for the production of recombinant monoclonal antibodies
Zhang, Q., Jiang, B., Du, Z., & Chasin, L. A. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27367 · Cited by 18
Munro, T. P., Mahler, S. M., Huang, E. P., Chin, D. Y., & Gray, P. P. (2011) · mAbs · doi:10.4161/mabs.3.5.16968 · Cited by 19
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
Scale-Up of Protein Purification: Downstream Processing Issues
Milne, J. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6412-3_5 · Cited by 17
Zhao, Y., Xing, J., Xing, J. Z., Ang, W. T., & Chen, J. (2014) · Ultrasonics · doi:10.1016/j.ultras.2014.04.025 · Cited by 17
Gantke, T., Boussouf, S. E., Janzen, J., Morrice, N. A., Howell, S. A., Mühlberger, E., & Ley, S. C. (2013) · Biochemical Journal · doi:10.1042/bj20121873 · Cited by 16
A Stable CHO K1 Cell Line for Producing Recombinant Monoclonal Antibody Against TNF-α
Gupta, K., Modi, D. N., Jain, R. D., & Dandekar, P. P. (2021) · Molecular Biotechnology · doi:10.1007/s12033-021-00329-4 · Cited by 15
Barradas, O. P., Jandt, U., Becker, M., Bahnemann, J., Pörtner, R., & Zeng, A. (2014) · Biotechnology Progress · doi:10.1002/btpr.1944 · Cited by 15
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
Toktay, Y., Dayanc, B., & Şentürk, Ş. (2022) · Scientific Reports · doi:10.1038/s41598-022-09887-2 · Cited by 14
Continuous biomanufacturing in upstream and downstream processing
Schmidt, A., Hengelbrock, A., & Strube, J. (2023) · Physical Sciences Reviews · doi:10.1515/psr-2022-0106 · Cited by 15
An, W., Li, T., Tian, X., Fu, X., Li, C., Wang, Z., Wang, J., & Wang, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910520 · Cited by 16
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
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
Self-citationBioprocess Challenges in Purification of Therapeutic Protein Charge Variants
Gupta, T., Kumar, A., & Seshadri, S. (2023) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-023-0078-4 · Cited by 12
Keating, S. M., & Higgins, B. (2024) · Antiviral Research · doi:10.1016/j.antiviral.2024.105902 · Cited by 10
Sensors for surveillance of RNA viruses: a One Health perspective
Chen, Y., Wang, P., Zhang, F., Dai, H., Jiao, X.-Y., Wang, X., Yu, Q., Kang, M., Su, S., & Wang, D. (2024) · The Lancet Microbe · doi:10.1016/j.lanmic.2024.101029 · Cited by 11
The impact of the timing of induction on the metabolism and productivity of CHO cells in culture
Sheikholeslami, Z., Jolicoeur, M., & Henry, O. (2013) · Biochemical Engineering Journal · doi:10.1016/j.bej.2013.07.015 · Cited by 11
Integration of Upstream and Downstream in Continuous Biomanufacturing
Gronemeyer, P., Thiess, H., Zobel‐Roos, S., Ditz, R., & Strube, J. (2017) · doi:10.1002/9783527699902.ch17 · Cited by 11
Improvement of the efficiency and quality in developing a new CHO host cell line
Huhn, S. C., Ou, Y., Tang, X., Jiang, B., Liu, R., Lin, H., & Du, Z. (2021) · Biotechnology Progress · doi:10.1002/btpr.3185 · Cited by 10
Sassi, A. B., Nagarkar, R. P., & Hamblin, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-416603-5.00009-2 · Cited by 10
Recombinant antibodies aggregation and overcoming strategies in CHO cells
Xu, T., Zhang, J., Wang, T., & Wang, X. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11977-0 · Cited by 10
Blaas, L., Musteanu, M., Grabner, B., Eferl, R., Bauer, A., & Casanova, E. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-433-9_31 · Cited by 10
Improved Titer in Late-Stage Mammalian Cell Culture Manufacturing by Re-Cloning
He, Q., Rehmann, M. S., Tian, J., Xu, J., Sabino, L., Vandermark, E., Basson, Z., Po, I., Bierilo, K. K., Tremml, G., et al. (2022) · Bioengineering · doi:10.3390/bioengineering9040173 · Cited by 9
Chastagnier, L., Marquette, C. A., & Petiot, E. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108211 · Cited by 10
Douillard, P., Freissmuth, M., Antoine, G., Thiele, M., Fleischanderl, D., Matthiessen, P., Voelkel, D., Kerschbaumer, R. J., Scheiflinger, F., & Sabarth, N. (2019) · Antibodies · doi:10.3390/antib8030046 · Cited by 9
Liu, Y., Yi, X., Zhuang, Y., & Zhang, S. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.12.005 · Cited by 9
Metadata
- Authors
- Rita Costa, A., Elisa Rodrigues, M., Henriques, M., Azeredo, J., & Oliveira, R.
- Affiliations
- Institute for Biotechnology and Bioengineering (PT)
- Corresponding author
- Henriques, Mariana
- Venue
- European Journal of Pharmaceutics and Biopharmaceutics
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 74
- Issue
- 2
- Pages
- 127-138
- ISSN
- 0939-6411 (ISSN-L)
- OpenAlex
- W2108422551
- Cited by
- 178
- References
- 220
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 10 · 2023: 12 · 2022: 8 · 2021: 14 · 2020: 11 · 2019: 9 · 2018: 13 · 2017: 17 · 2016: 8 · 2015: 10 · 2014: 15 · 2013: 20 · 2012: 10
- FWCI
- 2.80
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- European Journal of Pharmaceutics and Biopharmaceutics (publishedVersion)
- PubMed (publishedVersion)
- RepositóriUM (Universidade do Minho) (submittedVersion, other-oa)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, cc-by-nc-nd)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- monoclonal antibodies, cell engineering, mammalian cell expression systems, expression vector design, transfection, clone selection, antibody productivity, biopharmaceutical manufacturing, cell growth
- MeSH terms
- Animals, Antibodies, Monoclonal, Biotechnology, Humans, Technology, Pharmaceutical, Transfection, Protein Engineering, Cell Culture Techniques
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 ›
Are you an author, or do you see a problem with this page? Request a review
