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Biopharmaceutical benchmarks 2018
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“between 2014 and 2018 the vast majority (84%) of newly approved antibody therapeutics were produced in CHO cells [5].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [5]
In the citing paper
“Coming back to Ig-based biotherapeutics, atezolizumab, an oncolytic anti-PD-L1 mAb, is another clinically approved (2016-US, 2017-EU) glycoengineered product, except the Fc has been engineered to lack glycosylation [5].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [5]
In the citing paper
“CHO cells have become dominant in biotherapeutic production because they produce non-immunogenic and near human-like glycosylation [5].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [5]
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Gerard, C. J. J., Briuglia, M. L., Rajoub, N., Mastropietro, T. F., Chen, W., Heng, J. Y. Y., Profio, G. D., & ter Horst, J. H. (2022) · Crystal Growth & Design · doi:10.1021/acs.cgd.1c01324 · Cited by 15
Gangwar, N., Priyanka, P., & Rathore, A. (2022) · Biochemical engineering journal · doi:10.1016/j.bej.2022.108438 · Cited by 11
Population balance modelling captures host cell protein dynamics in CHO cell cultures
Alhuthali, S., & Kontoravdi, C. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265886 · Cited by 13
“Chinese hamster ovary (CHO) cells are the most commonly used host for industrial mAb production, accounting for 84% of currently approved products [2].”
BackgroundGuo, M., Ye, J.-L., Zheng, C.-Y., & Meng, J. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.462918 · Cited by 11
Kim, D., Yoon, C., & Lee, G. M. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.28013 · Cited by 11
“For decades, Chinese hamster ovary (CHO) cells have routinely been used for the production of therapeutic proteins (Walsh, 2018; Wurm, 2004).”
BackgroundRational design and construction of multi-copy biomanufacturing islands in mammalian cells
Altamura, R., Doshi, J., & Benenson, Y. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1214 · Cited by 10
“Mammalian expression systems are the platform of choice for the production of many high-value biologics, such as recombinant monoclonal antibodies and other recombinant therapeutic proteins, due to their inherent capacity for complex protein folding and post-translational modifications (2).”
Masuda, K., Watanabe, K., Ueno, T., Nakazawa, Y., Tanabe, Y., Ushiki‐Kaku, Y., Ogawa‐Goto, K., Ehara, Y., Saeki, H., Okumura, T., et al. (2021) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2021.11.010 · Cited by 11
Bernau, C. R., Jäpel, R., Hübbers, J. W., Nölting, S., Opdensteinen, P., & Buyel, J. (2021) · Journal of Chromatography A · doi:10.1016/j.chroma.2021.462379 · Cited by 11
Knight, T. J., Turner, S. J., Jaques, C., & Smales, C. (2021) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2021.06.019 · Cited by 11
“correctly fold, assemble and secrete multi-domain/polypeptide chain containing molecules with high yield and quality (Feary, 2017; Kunert, 2016; Mead, 2015; Povey, 2014; Walsh, 2018).”
BackgroundBudge, J. D., Young, R. J., & Smales, C. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.679448 · Cited by 11
“…| Volume 9 | Article 679448 recombinant products in the clinic has consistently increased in recent years largely due to an increase in the number of mAb approvals but also as a result of the emergence of novel format molecules such as Fc-fusion proteins and bispecific antibodies (Walsh, 2018).”
BackgroundStrategies and Applications of Antigen-Binding Fragment (Fab) Production in Escherichia coli
Chen, H., Chen, J.-S., Paerhati, P., Jakoš, T., Bai, S., Zhu, J., & Yuan, Y. (2021) · Pharmaceutical Fronts · doi:10.1055/s-0041-1735145 · Cited by 10
Rameez, S., Gowtham, Y. K., Nayar, G., & Mostafa, S. S. (2021) · Biotechnology Progress · doi:10.1002/btpr.3176 · Cited by 10
“, N-acetylglucosamine [GlcNAc], mannose [Man], fucose, galactose, and sialic acid) are assembled with complex combinations to form a repertoire of glycosylation patterns.(1)”
BackgroundStrobl, F., Duerkop, M., Palmberger, D., & Striedner, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-88813-4 · Cited by 11
“With a two-way valve (3), the cells could either be hoovered from the sample reservoir (1) into the syringe pump (2) or, when the valve was switched, cells were pumped from the syringe pump (2) through an orifice (4), and into the sample collector (5).”
BackgroundMethodInfluential‘Omics driven discoveries of gene targets for apoptosis attenuation in CHO cells
Orellana, C. A., Martínez, V. S., MacDonald, M. A., Henry, M. N., Gillard, M., Gray, P. P., Nielsen, L. K., Mahler, S. M., & Marcellin, E. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27548 · Cited by 13
“The biopharmaceutical industry is fast growing, with global sales of over USD 188 billion in 2017 (Walsh, 2018).”
BackgroundInfluentialToward Antibody Production in Genome-Minimized Bacillus subtilis Strains
Schilling, T., Biedendieck, R., Morán‐Torres, R., Saaranen, M. J., Ruddock, L. W., Daniel, R., & van Dijl, J. M. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00688 · Cited by 11
Zhu, Y., Chen, X., Zheng, H., Ma, Q., Chen, K., & Li, H. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s493374 · Cited by 9
Duan, M., Dev, I., Lu, A. Y., Ayrapetyan, G., You, M. Y., & Shapiro, M. G. (2024) · Cell Systems · doi:10.1016/j.cels.2024.06.001 · Cited by 15
Zhang, Z., Lang, Z., Chen, G., Zhou, H., & Zhou, W. (2024) · Biotechnology and Bioengineering · doi:10.1002/bit.28717 · Cited by 10
Sachio, S., Likozar, B., Kontoravdi, C., & Papathanasiou, M. M. (2024) · Journal of Chromatography A · doi:10.1016/j.chroma.2024.464890 · Cited by 10
When will we have a clone? An industry perspective on the typical CLD timeline
Clarke, H., Mayer-Bartschmid, A., Zheng, C., Masterjohn, E., Patel, F. N., Moffat, M. A., Wei, Q., Liu, R., Emmins, R., Fischer, S., et al. (2024) · Biotechnology progress (Print) · doi:10.1002/btpr.3449 · Cited by 10
In pursuit of a minimal CHO genome: Establishment of large-scale genome deletions
Jerabek, T., Weiß, L., Fahrion, H., Zeh, N., Raab, N., Lindner, B., Fischer, S., & Otte, K. (2023) · New Biotechnology · doi:10.1016/j.nbt.2023.12.007 · Cited by 10
Kim, D., Kim, S. H., Yoon, C., & Lee, G. (2023) · Biotechnology and Bioengineering · doi:10.1002/bit.28611 · Cited by 10
“Increasing demand for therapeutic proteins necessitates the improvement of the productivity of Chinese hamster ovary (CHO) cells that are widely used for therapeutic protein production (Walsh, 2018; Wurm, 2004).”
BackgroundBoosting Productivity for Advanced Biomanufacturing by Re-Using Viable Cells
Reger, L. N., Saballus, M., Matuszczyk, J., Kampmann, M., Wijffels, R. H., Martens, D. E., & Niemann, J. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1106292 · Cited by 10
“…bed centrifuge, intermediate 9 harvest, monoclonal antibodies 1 Introduction Recombinantly expressed biotherapeutics, such as monoclonal antibodies (mAb), hormones, cytokines, and vaccines, have gained attention in the pharmaceutical industry during recent years (Walsh, 2018).”
BackgroundEffects and mechanisms of animal-free hydrolysates on recombination protein yields in CHO cells
Du, Q.-J., Zhang, X., Wang, T., & Wang, X. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12229-x · Cited by 14
“Walsh’s report indicated that 54 of the 67 monoclonal antibodies (mAb) approved from 2014 to 2018 in the market were made in CHO cells (Walsh 2018).”
BackgroundCurrent Strategies to Improve Yield of Recombinant Protein Production in Rice Suspension Cells
Chi, Y., & Huang, L.-F. (2022) · Processes · doi:10.3390/pr10061120 · Cited by 10
Allard, J. L., Shields, K. A., Munro, T. P., & Lua, L. H. L. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.109996 · Cited by 14
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“Biopharmaceutical products represent an increasing percentage in drug development and new drug applications for market approval [3], but their commercial and academic usage is currently limited by their physical stability.”
BackgroundAlsamil, A. M., Giezen, T., Egberts, T., Leufkens, H., & Gardarsdottir, H. (2021) · Pharmaceuticals · doi:10.3390/ph14030189 · Cited by 10
“Biological drugs have become important treatment options for numerous diseases, including cancer and inflammatory diseases [1].”
BackgroundRegulation of pyruvate dehydrogenase complex related to lactate switch in CHO cells
Möller, J., Bhat, K., Guhl, L., Pörtner, R., Jandt, U., & Zeng, A. (2020) · Engineering in Life Sciences · doi:10.1002/elsc.202000037 · Cited by 13
Metzger, K. F. J., Padutsch, W., Pekarsky, A., Kopp, J., Voloshin, A. M., Kühnel, H., & Maurer, M. (2020) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2020.02.014 · Cited by 10
Subphysiological temperature induces pervasive alternative splicing in Chinese hamster ovary cells
Tzani, I., Monger, C., Motheramgari, K., Gallagher, C., Hagan, R., Kelly, P. S., Costello, A., Meiller, J., Floris, P., Zhang, L., et al. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27365 · Cited by 11
Mohammadian, O., Rajabibazl, M., Pourmaleki, E., Bayat, H., Ahani, R., & Rahimpour, A. (2019) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2019.1621893 · Cited by 10
“As the result, mAbs have become the best-selling and most abundant type of recombinant products in the market.([2,3]) The production of mAbs is a multi-billion dollar trade; as by 2016, worldwide sales of these products were around $100 billion and it is estimated that this value will increase further in the coming ye…”
BackgroundTop, O., Geisen, U., Decker, E., & Reski, R. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00261 · Cited by 10
“The global market value of recombinant coagulation factors was approximately $8.5 billion in 2017 (Walsh, 2018).”
BackgroundInfluentialKulkarni, N. A., Das, P. K., Arjun, P., & Veeranki, V. D. (2025) · Protein Expression and Purification · doi:10.1016/j.pep.2025.106764 · Cited by 10
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Pang, K., Hong, Y.-F., Shozui, F., Furomitsu, S., Myint, M., Ho, Y., Silberberg, Y. R., Walsh, I., & Lakshmanan, M. (2024) · Biotechnology Journal · doi:10.1002/biot.202400072 · Cited by 9
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Hamaker, N. K., & Lee, K. H. (2023) · Biotechnology and Bioengineering · doi:10.1002/bit.28393 · Cited by 9
“Furthermore, these methods must provide robust improvements to achieve multilocus targeted integration of RMCE landing pads to support commercial manufacturing of complex therapeutic modalities such as bispecific and trispecific mAbs (Spiess et al., 2015; Walsh, 2018).”
BackgroundMethodEngineering protein glycosylation in CHO cells to be highly similar to murine host cells
Gupta, S., Shah, B., Fung, C., Chan, P. K., Wakefield, D. L., Kuhns, S., Goudar, C., & Piret, J. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1113994 · Cited by 9
“Recombinant therapeutic proteins, also known as biologics, have been successfully used to treat a wide range of diseases, including cancers, inflammatory disorders, and cardiovascular diseases (Walsh, 2018).”
BackgroundKumar, R., Sarin, D., & Rathore, A. S. (2023) · ELECTROPHORESIS · doi:10.1002/elps.202200208 · Cited by 10
“Monoclonal antibodies (mAbs) presently form the bulk of biopharmaceutical pipelines [1].”
BackgroundUdugama, I. A., Badr, S., Hirono, K., Scholz, B. X., Hayashi, Y., Kino‐oka, M., & Sugiyama, H. (2023) · Computers & Chemical Engineering · doi:10.1016/j.compchemeng.2023.108144 · Cited by 9
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“Moreover, in the plant-based expression systems, folding and modification of proteins are more similar to human processes [77, 78].”
BackgroundLin, Z., Jing, Y., Huang, Y., Yang, S., Chen, S., Ou, Y.-Y., Pistolozzi, M., & Yang, X. (2022) · Chemical Engineering Science · doi:10.1016/j.ces.2022.118052 · Cited by 11
Church, D. C., Davis, E., Caparco, A. A., Takiguchi, L. P., Chung, Y. H., Steinmetz, N. F., & Pokorski, J. K. (2022) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2022.101067 · Cited by 11
Lu, L., Liu, X., Zuo, C., Zhou, J.-W., Zhu, C., Zhang, Z., Fillet, M., Crommen, J., Jiang, Z.-J., & Wang, Q.-Q. (2022) · Analytica Chimica Acta · doi:10.1016/j.aca.2022.340199 · Cited by 9
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“To establish the utility of the reporter system, we modeled an experimental scheme based on systematic and quantitative comparison of a compendium of existing constitutive promoters in two contexts: (1) transient transfection of different CHO cell variants as well as HEK-293T cells, and (2) stable cultures of CHODG44…”
MethodSchmitz, J., Hertel, O., Yermakov, B., Noll, T., & Grünberger, A. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.716343 · Cited by 10
“Keywords: microfluidics, single-cell cultivation, single-cell analysis, miniaturization, scale comparison, cell culture, GFP production INTRODUCTION The number of biotechnologically manufactured products like biopharmaceuticals has increased rapidly over the last decades (Walsh, 2018).”
BackgroundPriyanka, P., & Rathore, A. (2021) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.6883 · Cited by 9
Barroso, D., Brandão, J. G., Andrade, E. S. N., Correia, A. C. B., Aquino, D., Chen, A. C., Vernal, S., de Araújo, W. D., da Mota, L. M. H., Sampaio, R. N., et al. (2021) · BMC Infectious Diseases · doi:10.1186/s12879-021-06041-7 · Cited by 9
“They represent the most important pharmaceutical products sold in the US, as they are the treatments most frequently prescribed for inflammatory and autoimmune conditions [2].”
BackgroundLin, M., Shen, C., Lin, Y.-J., Chou, M., Pham, N. N., Chang, Y., Chang, C.-W., Hwu, J. R., Nguyen, M. T. T., & Hu, Y. (2021) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2021.03.040 · Cited by 9
Zhang, L., Wang, M., Castan, A., Hjalmarsson, H., & Chotteau, V. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27769 · Cited by 11
“6% of the total biopharmaceutical global sales in 2017 (Walsh, 2018).”
BackgroundInfluentialKaushik, P., Curell, R. V., Henry, M. A., Barron, N., & Meleady, P. (2020) · Biotechnology Letters · doi:10.1007/s10529-020-02953-7 · Cited by 30
“Up to 85% of new monoclonal antibody (Mab) products approved between 2014 and 2018 were produced in Chinese hamster ovary (CHO) cells (Walsh 2018).”
BackgroundNew insights on the interaction mechanism of rhTNFα with its antagonists Adalimumab and Etanercept
Contreras, M. A., Macaya, L., Neira, P., Camacho, F., González, A., Acosta, J., Montesino, R., Toledo, J., & Sánchez, O. (2020) · bioRxiv · doi:10.1101/2020.06.21.163824 · Cited by 9
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“Antibodies have high specificity and efficacy.(1-3) More than 80 antibody drugs are currently approved by FDA,(4) most to treat cancer or autoimmune diseases.”
BackgroundJois, R., Mukherjee, S., Rajeswari, S., Rath, P., Goyal, V., & Gupta, D. (2020) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_43_18 · Cited by 16
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CellShip: An Ambient Temperature Transport and Short-Term Storage Medium for Mammalian Cell Cultures
Buick, E., Mead, A., Al-Hubaysh, A., Assi, P. B., Das, P., Dayus, J., Turner, M. C., Kowalski, L., Murray, J., Renshaw, D., et al. (2023) · Biopreservation and Biobanking · doi:10.1089/bio.2023.0100 · Cited by 8
“20 Despite its widespread use, methods for transporting cells remain largely unchanged, with cryopreservation being the most popular.”
Barnard, G. C., Zhou, M., Shen, A., Yuk, I. H., & Laird, M. W. (2023) · Biotechnology progress (Print) · doi:10.1002/btpr.3399 · Cited by 8
Consistency of Product Quality for SB5, an Adalimumab Biosimilar
Lee, J., Lee, N., Seo, Y. J., & Kim, I.-K. (2023) · BioDrugs · doi:10.1007/s40259-023-00581-x · Cited by 8
Life at the periphery: what makes CHO cells survival talents
Jerabek, T., Klingler, F., Raab, N., Zeh, N., Pfannstiel, J., & Otte, K. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-12123-6 · Cited by 10
“CHO cells continue to be the most frequently used mammalian expression system in the biopharmaceutical industry (Walsh 2018).”
BackgroundOliviero, C., Hinz, S. C., Bogen, J. P., Kornmann, H., Hock, B. M., Kolmar, H., & Hagens, G. (2022) · Biotechnology Progress · doi:10.1002/btpr.3254 · Cited by 7
“the current workhorse for recombinant protein expression using mammalian cells.(2,3) In 2017, the majority of the antibodies with the highest market share was produced in CHO cells.”
BackgroundZaghmi, A., Pérez-Mato, M., Dopico-López, A., Candamo-Lourido, M., Campos, F., & Gauthier, M. (2022) · Biomacromolecules · doi:10.1021/acs.biomac.2c00117 · Cited by 8
Kaya, U., Gopireddy, S., Urbanetz, N., Nopens, I., & Verwaeren, J. (2022) · Chemical engineering research & design · doi:10.1016/j.cherd.2022.03.042 · Cited by 8
Energy metabolism in Chinese hamster ovary (CHO) cells: Productivity and beyond
Park, J. U., Han, H., & Baik, J. Y. (2022) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-022-1062-y · Cited by 8
Genetically engineered birds; pre-CRISPR and CRISPR era
Dehdilani, N., Taemeh, S. Y., Goshayeshi, L., & Dehghani, H. (2021) · Biology of Reproduction · doi:10.1093/biolre/ioab196 · Cited by 21
“The last two decades have seen a growing trend towards the production and marketing of more than 150 billion US dollars worth of biopharmaceuticals [3].”
BackgroundElectrostatics Drive Oligomerization and Aggregation of Human Interferon Alpha-2a
Pohl, C., Polimeni, M., Indrakumar, S., Streicher, W., Peters, G. H., Nørgaard, A., Lund, M., & Harris, P. (2021) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c07090 · Cited by 8
“Currently two approaches are used to reduce aggregation: (1) finding a suitable formulation which is labor-intensive and requires large protein quantities or (2) engineering the protein by specific, stabilizing mutations, which requires specific knowledge about the protein aggregation pathway.”
Bryan, L., Henry, M., Barron, N., Gallagher, C., Kelly, R. M., Frye, C., Osborne, M., Clynes, M., & Meleady, P. (2021) · Biotechnology Letters · doi:10.1007/s10529-021-03153-7 · Cited by 8
“The Chinese hamster ovary (CHO) cell is widely accepted as the cell line of choice for the production of large scale commercial therapeutic proteins (Walsh 2018).”
BackgroundGelb, M. B., & Maynard, H. D. (2021) · Macromolecular Materials and Engineering · doi:10.1002/mame.202100197 · Cited by 8
Stantič, M., Gunčar, G., Kuzman, D., Mravljak, R., Cvijić, T., & Podgornik, A. (2021) · Journal of Chromatography B · doi:10.1016/j.jchromb.2021.122731 · Cited by 8
Wolffia arrhiza as a promising producer of recombinant hirudin
Khvatkov, P., Firsov, A., Shvedova, A., Kozlov, O., Chernobrovkina, M., Pushin, A., Shaloiko, L., & Dolgov, S. (2021) · 3 Biotech · doi:10.1007/s13205-021-02762-3 · Cited by 8
“Currently, the biopharming industry has a wide range of expression platforms (cells of bacteria, yeast, mammals and insects) for the production of therapeutic proteins (Walsh 2018; Rader and Langer 2015; Sysuev and Pokrovskaya 2015).”
BackgroundShang, M., Kwon, T., Hamel, J. P., Lim, C. T., Khoo, B. L., & Han, J. (2021) · Scientific Reports · doi:10.1038/s41598-020-80576-8 · Cited by 9
Error propagation in constraint‐based modeling of Chinese hamster ovary cells
Széliová, D., Iurashev, D., Ruckerbauer, D. E., Koellensperger, G., Borth, N., Melcher, M., & Zanghellini, J. (2020) · Biotechnology Journal · doi:10.1002/biot.202000320 · Cited by 6
“Chinese hamster ovary (CHO) cells are the primary host for the production of biopharmaceuticals, particularly monoclonal antibodies and other complex therapeutic proteins 1 .”
BackgroundVerhagen, N., Teleki, A., Heinrich, C., Schilling, M., Unsoeld, A., & Takors, R. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27484 · Cited by 9
“Therapeutic proteins such as monoclonal antibodies (mAB) dominate the global market for biopharmaceuticals and are mostly produced in Chinese hamster ovary (CHO) cells (Walsh, 2018).”
BackgroundStrategies to improve the expression and solubility of recombinant proteins in E. coli
Nag, N., Khan, H., & Tripathi, T. (2022) · Advances in Protein Molecular and Structural Biology Methods · doi:10.1016/b978-0-323-90264-9.00001-5 · Cited by 8
Bryan, L., Henry, M., Kelly, R. M., Lloyd, M. E., Frye, C., Osborne, M., Clynes, M., & Meleady, P. (2021) · Current Research in Biotechnology · doi:10.1016/j.crbiot.2021.02.002 · Cited by 8
Process analytics 4.0: A paradigm shift in rapid analytics for biologics development
Wasalathanthri, D. P., Shah, R., Ding, J., Leone, A., & Li, Z. J. (2021) · Biotechnology Progress · doi:10.1002/btpr.3177 · Cited by 17
“Biotherapeutic modalities evolve rapidly to deliver unmet patient needs, which require the development and amendment of typical analytical assays for CQAs and CPPs.(80) Unlike manual assays, it would be challenging to simply amend or re-develop automated or PAT type real time analytical assays for specialized biologic…”
MethodNTxPred2: A large language model for predicting neurotoxic peptides and neurotoxins
Rathore, A., Jain, S., Choudhury, S., & Raghava, G. (2025) · bioRxiv · doi:10.1101/2025.03.01.640936 · Cited by 7
“In addition to sequencing, GM organisms, GM crops, and technology have played a key role in the large-scale production of therapeutic proteins like monoclonal antibodies and hormones (Plotkin, 2010; Walsh, 2018).”
Wu, Y., Gardner, R. A., & Schöneich, C. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.4c00445 · Cited by 7
Jarusintanakorn, S., Mastrobattista, E., & Yamabhai, M. (2024) · New Biotechnology · doi:10.1016/j.nbt.2024.06.006 · Cited by 8
Hisada, T., Imai, Y., Takemoto, Y., Kanie, K., & Kato, R. (2024) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2024.01.011 · Cited by 7
Webster, T. A., Hadley, B. C., Dickson, M. R., Hodgkins, J., Olin, M., Wolnick, N., Armstrong, J., Mason, C., & Downey, B. J. (2023) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-023-02912-2 · Cited by 14
“Monoclonal antibodies (mAbs) in particular are expected to continue to be in high demand as different modalities and targets are identified [1].”
BackgroundOptimisation of recombinant TNFα production in Escherichia coli using GFP fusions and flow cytometry
Zulkifly, N. A. H., Castiñeiras, T. S., & Overton, T. W. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1171823 · Cited by 7
“E. coli is an advantageous host for relatively simple proteins that do not require post-translational modi fi cations such as glycosylation (Overton, 2014; Sanchez-Garcia et al., 2016); example products include insulin, granulocyte-colony stimulating factor and antibody fragments (Walsh, 2018).”
Dhenin, J., Lafont, V., Dupré, M., Krick, A., Mauriac, C., & Chamot‐Rooke, J. (2023) · PROTEOMICS · doi:10.1002/pmic.202300069 · Cited by 7
Wu, Z., Xu, G.-L., He, W., Yu, C., Huang, W., Zheng, S.-R., Kang, D., Xie, M. H., Cao, X.-J., Wang, L., et al. (2023) · Antibody Therapeutics · doi:10.1093/abt/tbad017 · Cited by 7
Dai, J., & Ji, C. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.341360 · Cited by 7
Strategies for controlling afucosylation in monoclonal antibodies during upstream manufacturing
Rish, A. J., Siddiquee, K., Huang, Z., Xu, J., Anderson, C. A., Borys, M., & Khetan, A. (2023) · Biotechnology Journal · doi:10.1002/biot.202200604 · Cited by 8
“[3] Due to this, mammalian cells are the preferred host vector for themanufacturing ofmAbs as the glycosylation patterns observed from these cells are similar to those in humans.[1] In contrast, mAbs produced in other types of cells such as”
BackgroundImmortal orexin cell transplants restore motor-arousal synchrony during cataplexy
Pintwala, S. K., Fraigne, J. J., Belsham, D. D., & Peever, J. H. (2023) · Current Biology · doi:10.1016/j.cub.2023.03.077 · Cited by 9
Application of a Novel Aptamer Beacon for Rapid Detection of IgG1 Antibody Drugs
Yang, K., Zheng, W.-W., Huang, X.-S., Chen, K., & Duan, C. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04471-4 · Cited by 7
“Monoclonal antibodies are increasingly advantageous in the biopharmaceutical field, and many monoclonal antibodies are expressed in mammalian systems [25].”
BackgroundGao, K., Lian, H.-X., Xue, C.-F., Zhou, J., & Yan, X.-M. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c04382 · Cited by 7
A Novel Tandem-Tag Purification Strategy for Challenging Disordered Proteins
Mészáros, A., Muwonge, K., Janvier, S., Ahmed, J., & Tompa, P. (2022) · Biomolecules · doi:10.3390/biom12111566 · Cited by 10
“In the last few years, close to 100 new biopharmaceuticals, the majority being recombinant proteins, have entered the market [2].”
BackgroundKe, H., Guay, K. P., Flotte, T. R., Gierasch, L. M., Gershenson, A., & Hebert, D. N. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2206103119 · Cited by 9
“of biologics that traverse the secretory pathway (49, 50).”
BackgroundThe Impact of Glycoengineering on the Endoplasmic Reticulum Quality Control System in Yeasts
Piirainen, M. A., & Frey, A. D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.910709 · Cited by 7
“The yeast-based biopharmaceuticals currently in market include various insulin products and vaccines, but also other peptide hormones, a blood clotting factor subunit and a recombinant urate oxidase (Walsh, 2018).”
BackgroundWijaya, A. W., Verhagen, N., Teleki, A., & Takors, R. (2021) · Engineering in Life Sciences · doi:10.1002/elsc.202100057 · Cited by 8
“Engineering in Life Sciences published by Wiley-VCH GmbH share [1].”
MethodVerscheure, L., Oosterlynck, M., Cerdobbel, A., Sandra, P., Lynen, F., & Sandra, K. (2020) · Journal of Chromatography A · doi:10.1016/j.chroma.2020.461808 · Cited by 7
A microfluidic chip for screening high-producing hybridomas at single cell level
Zhang, W., Li, R., Jia, F., Hu, Z., Li, Q., & Wei, Z. (2020) · Lab on a Chip · doi:10.1039/d0lc00847h · Cited by 17
Nelson, J. A., Barnett, R. J., Hunt, J. P., Foutz, I., Welton, M., & Bundy, B. C. (2020) · Biotechnology Progress · doi:10.1002/btpr.3079 · Cited by 10
“In 2018, recombinant proteins accounted for 87% of all newly approved biopharmaceuticals and topped small molecules for the first time when considering the top 100 pharmaceuticals by worldwide sales.(3) Due to its fast growth, simple culturing procedure and cost-effectiveness, Escherichia.”
BackgroundCRISPR-Cas9 Genome Editing Tool for the Production of Industrial Biopharmaceuticals
Khan, A. H., Tye, G. J., & Noordin, R. (2020) · Molecular Biotechnology · doi:10.1007/s12033-020-00265-9 · Cited by 11
Metadata
- Authors
- Walsh, G.
- Affiliations
- University of Limerick (IE)
- Corresponding author
- Walsh, Gary
- ORCID
- Walsh, Gary
- Venue
- Nature Biotechnology
- Published
- 2018-12
- Volume
- 36
- Issue
- 12
- Pages
- 1136-1145
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2917928050
- Cited by
- 978
- References
- 15
- Citations by year
- 2026: 68 · 2025: 68 · 2024: 88 · 2023: 141 · 2022: 173 · 2021: 197 · 2020: 173 · 2019: 65
- FWCI
- 165.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Social Sciences › Economics, Econometrics and Finance › Economics and Econometrics › Pharmaceutical Economics and Policy
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- biopharmaceutical market, monoclonal antibodies, cell therapy, gene therapy, biosimilars, biologics, market growth
- MeSH terms
- Animals, Antibodies, Monoclonal, Biological Products, Biotechnology, Drug Industry, European Union, Humans, Nucleic Acids, Recombinant Proteins, United States, United States Food and Drug Administration, Drug Approval, Benchmarking, Biosimilar Pharmaceuticals
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