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Biopharmaceutical benchmarks 2018

Walsh, Gary·2018·Nature Biotechnology

DOI 10.1038/nbt.4305

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Walsh, G. Biopharmaceutical benchmarks 2014. Nat. Biotechnol. 32, 992–1000 (2014). · DOI · Paper page
Walsh, G. Biopharmaceutical benchmarks 2010. Nat. Biotechnol. 28, 917–924 (2010). · DOI
Walsh, G. Biopharmaceutical benchmarks 2006. Nat. Biotechnol. 24, 769–776 (2006). · DOI
Bertolini, L.R. et al. The transgenic animal platform for biopharmaceutical production. Transgenic Res. 25, 329–343 (2016). · DOI
Park, T.S. et al. Deposition of bioactive human epidermal growth factor in the egg white of transgenic hens using an oviduct-specific minisynthetic promoter. FASEB J. 29, 2386–2396 (2015). · DOI
Miliotou, A.N. & Papadopoulou, L.C. CAR T-cell therapy: a new era in cancer immunotherapy. Curr. Pharm. Biotechnol. 19, 5–18 (2018). · DOI
Kaplon, H. & Reichert, J.M. Antibodies to watch in 2018. MAbs 10, 183–203 (2018). · DOI
Zheng, P.P., Kros, J.M. & Li, J. Approved CAR-T cell therapies: ice bucket challenges on glaring safety risks and long-term impacts. Drug Discov. Today 23 1175–1182 (2018). · DOI
Labanieh, L., Majzner, R.G. & Mackall, C.L. Programming CAR-T cells to kill cancer. Nat. Biomed. Eng. 2, 377–391 (2018). · DOI
Köhl, U., Arsenieva, S., Holzinger, A. & Abken, H. CAR T cells in trials: recent achievements and challenges that remain in the production of modified T cells for clinical applications. Hum. Gene Ther. 29, 559–568 (2018). · DOI
Klinger, M., Benjamin, J., Kischel, R., Stienen, S. & Zugmaier, G. Harnessing T cells to fight cancer with BiTE® antibody constructs—past developments and future directions. Immunol. Rev. 270, 193–208 (2016). · DOI

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Pan, X., Yang, Y. P., Li, L., Li, X., Li, Q., Cui, C., Wang, B., Kuai, H., Jiang, J., & Tan, W. (2020) · Chemical Science · doi:10.1039/d0sc02279a · Cited by 25
The effect of point mutations on the biophysical properties of an anti-microbial peptide: development of a screening protocol for peptide stability screening.
Pohl, C., Zalar, M., Bialy, I. E., Indrakumar, S., Peters, G. H., Friess, W., Golovanov, A., Streicher, W., Noergaard, A., & Harris, P. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00406 · Cited by 13
A Site‐Specific Integration Reporter System That Enables Rapid Evaluation of CRISPR/Cas9‐Mediated Genome Editing Strategies in CHO Cells
Hamaker, N. K., & Lee, K. H. (2020) · Biotechnology Journal · doi:10.1002/biot.202000057 · Cited by 14
THE EFFECT OF TEMPERATURE IN SODIUM DODECYL SULFATE CAPILLARY GEL ELECTROPHORESIS (SDS-CGE) OF PROTEIN THERAPEUTICS.
Filep, C., & Guttman, A. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05566 · Cited by 13
Clonal variations in CHO IGF signaling investigated by SILAC-based phosphoproteomics and LFQ-MS
Schelletter, L., Albaum, S. P., Walter, S., Noll, T., & Hoffrogge, R. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-10020-z · Cited by 19
Microevolutionary dynamics of eccDNA in Chinese hamster ovary cells grown in fed-batch cultures under control and lactate-stressed conditions
Chitwood, D. G., Wang, Q., Klaubert, S. R., Green, K., Wu, C. H., Harcum, S. W., & Saski, C. A. (2023) · Scientific Reports · doi:10.1038/s41598-023-27962-0 · Cited by 12
Highly efficient transgene‐free ErCas12a RNP‐protoplast genome editing and single‐cell regeneration in Nicotiana benthamiana for glyco‐engineering
Blumberg, L. C., Bakker, G. M., van der Kaaij, A., Gariépy, É., van de Geest, H., Slootweg, E. J., Los, F. C. O., Westerhof, L. B., & Wilbers, R. H. P. (2025) · Plant Biotechnology Journal · doi:10.1111/pbi.70141 · Cited by 13
“Most glycosylated biopharmaceuticals are recombinant human glycoproteins, especially antibodies (Walsh, 2018).”
An automated high inoculation density fed‐batch bioreactor, enabled through N‐1 perfusion, accommodates clonal diversity and doubles titers
Olin, M., Wolnick, N., Crittenden, H., Quach, A., Russell, B., Hendrick, S., Armstrong, J., Webster, T. A., Hadley, B. C., Dickson, M., et al. (2023) · Biotechnology Progress · doi:10.1002/btpr.3410 · Cited by 12
Bimolecular transitions and lipid synthesis in marine microalgae for environmental and human health application
Su, Z., Sharma, M., Zhang, P., Zhang, L., Xing, X., Yue, J., Song, Z., Nan, L., Yujun, S., Zheng, Y., et al. (2023) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2023.110398 · Cited by 14
Epithelium dynamics differ in time and space when exposed to the permeation enhancers penetramax and EGTA. A head-to-head mechanistic comparison
Panou, D., Pedersen, S. F., Kristensen, M., & Nielsen, H. M. (2023) · Frontiers in Drug Delivery · doi:10.3389/fddev.2023.1221628 · Cited by 12
“The number of regulatory approvals for biopharmaceuticals are rising (Lau and Dunn, 2018; Walsh, 2018), driven by the increased discovery and application of novel peptide therapeutics for a variety of drug targets.”
LncRNA analysis of mAb producing CHO clones reveals marker and engineering potential
Novak, N., Baumann, M., Friss, A. F., Cairns, V. R., DeMaria, C., & Borth, N. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.05.003 · Cited by 12
Debottlenecking and reformulating feed media for improved CHO cell growth and titer by data‐driven and model‐guided analyses
Park, S., Choi, D., Song, J., Park, U., Cho, H., Hong, B. H., Silberberg, Y. R., & Lee, D. (2023) · Biotechnology Journal · doi:10.1002/biot.202300126 · Cited by 13
“[1] 10] Ofthem,customizablemediadesignrelevanttothe specific cell line and culture process is a crucial step in early process development for achieving high RTP production with consistent and good quality of RTP during cell culture.”
Background
Polybutylene terephthalate-based stationary phase for ion-pair-free reversed-phase liquid chromatography of small interfering RNA. Part 1: Direct coupling with mass spectrometry.
Li, F., Chen, S., Studzińska, S., & Lämmerhofer, M. (2023) · Journal of Chromatography A · doi:10.1016/j.chroma.2023.463898 · Cited by 12
Half-Life Extension and Biodistribution Modulation of Biotherapeutics via Red Blood Cell Hitch-Hiking with Novel Anti-Band 3 Single-Domain Antibodies
Nguyen, T. D., Bordeau, B. M., Zhang, Y., Mattle, A. G., & Balthasar, J. P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010475 · Cited by 17
“Biotherapeutics have gained outstanding success in recent years, with more than 200 approved for clinical use and more than 1000 currently in clinical development [1].”
Background
Seed Train Intensification Using an Ultra-High Cell Density Cell Banking Process
Müller, J., Ott, V., Eibl, D., & Eibl, R. (2022) · Processes · doi:10.3390/pr10050911 · Cited by 12
“The largest and best-selling group, mAbs, is mainly produced in CHO cells [2].”
Background
Glyco-Engineering Plants to Produce Helminth Glycoproteins as Prospective Biopharmaceuticals: Recent Advances, Challenges and Future Prospects
van der Kaaij, A., van Noort, K. V., Nibbering, P., Wilbers, R., & Schots, A. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.882835 · Cited by 12
“The majority of biopharmaceutical proteins are glycosylated (Walsh, 2018), a process where carbohydrate structures (glycans) are covalently attached to a protein backbone.”
Background
The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli
Restrepo-Pineda, S., Sánchez‐Puig, N., Pérez, N. O., García‐Hernández, E., Valdez‐Cruz, N. A., & Trujillo‐Roldán, M. A. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11908-z · Cited by 14
“Additionally, within the biopharmaceuticals approved through 2018, ~ 22% were produced in E. coli (Walsh 2018).”
Background
Development of a novel platform for recombinant protein production in Corynebacterium glutamicum on ethanol
Yu, X., Liu, X., Gao, X., Luo, X., Yang, Y., Li, Y., Liu, C., Zhang, C., & Bai, Z. (2022) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2022.03.004 · Cited by 13
“The expansion of biologics and the biopharmaceutical industry has fuelled the demand for recombinant proteins in recent years [1,2].”
Background
Applying intensified design of experiments to mammalian cell culture processes
Nold, V., Junghans, L., Bisgen, L., Drerup, R., Presser, B., Gorr, I. H., Schwab, T., Knapp, B. L., & Wieschalka, S. (2021) · Engineering in Life Sciences · doi:10.1002/elsc.202100123 · Cited by 14
“Over the last decade, biopharmaceutical industry yielded an increasing number of novel products and faced a strong competition among individual companies to accelerate the development pipeline [4, 5].”
Background
Mapping the molecular basis for growth related phenotypes in industrial producer CHO cell lines using differential proteomic analysis
Bryan, L., Henry, M., Kelly, R. M., Frye, C., Osborne, M., Clynes, M., & Meleady, P. (2021) · BMC Biotechnology · doi:10.1186/s12896-021-00704-8 · Cited by 12
“Background CHO cells are the most frequently used host cell line for the production of therapeutic proteins [1] due to their ability to produce human like post-translational modifications, their high level of approval among regulatory authorities and their stable transgene expression [2, 3].”
Background
The Instability of Dimeric Fc-Fusions Expressed in Plants Can Be Solved by Monomeric Fc Technology
Gattinger, P., Izadi, S., Grünwald-Gruber, C., Kallolimath, S., & Castilho, A. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.671728 · Cited by 12
“Chinese hamster ovary (CHO) cells are the most common host for Fc-fusion protein production, and several therapeutic Fc-fusion proteins on the market are expressed in CHO cells (Walsh, 2018).”
Background
Continuous optical in‐line glucose monitoring and control in CHO cultures contributes to enhanced metabolic efficiency while maintaining darbepoetin alfa product quality
Lederle, M., Tric, M., Roth, T., Schütte, L., Rattenholl, A., Lütkemeyer, D., Wölfl, S., Werner, T., & Wiedemann, P. (2021) · Biotechnology Journal · doi:10.1002/biot.202100088 · Cited by 14
“cesses dominate this field and account for 80% of animal cell derived biopharmaceuticals.[2] Ideally, process parameters are monitored inline without sampling and breaching the sterile barrier of a cultivation vessel.”
Background
Production of butyrate and branched‐chain amino acid catabolic byproducts by CHO cells in fed‐batch culture enhances their specific productivity
Harrington, C., Jacobs, M. R., Bethune, Q., Kalomeris, T. A., Hiller, G. W., & Mulukutla, B. C. (2021) · Biotechnology and Bioengineering · doi:10.1002/bit.27942 · Cited by 13
Finding the Needle in the Haystack: High-Resolution Techniques for Characterization of Mixed Protein Particles Containing Shed Silicone Rubber Particles Generated During Pumping
Deiringer, N., Haase, C., Wieland, K., Zahler, S., Haisch, C., & Frieß, W. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.12.002 · Cited by 12
Questioning coverage values determined by 2D western blots: A critical study on the characterization of anti‐HCP ELISA reagents
Seisenberger, C., Graf, T., Haindl, M., Wegele, H., Wiedmann, M., & Wohlrab, S. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27635 · Cited by 12
N-glycosylation analysis of biopharmaceuticals by multicapillary gel electrophoresis: Generation and application of a new glucose unit database.
Filep, C., Borza, B., Járvás, G., & Guttman, A. (2020) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2019.112892 · Cited by 12
Downstream Processing of Biotechnology Products
Carta, G., & Jungbauer, A. (2010) · Protein Chromatography · doi:10.1002/9783527630158.ch1 · Cited by 12
Unravelling the essential elements for recombinant adeno-associated virus (rAAV) production in animal cell-based platforms
Catalán-Tatjer, D., Tzimou, K., Nielsen, L. K., & Lavado‐García, J. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108370 · Cited by 15
Tuning plasmid DNA amounts for cost-effective transfections of mammalian cells: when less is more
Carreño, A., Guerrero-Yagüe, R., Casal, E., Mendoza, R., & Corchero, J. L. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-024-13003-x · Cited by 12
“Production of biopharmaceuticals in mammalian “cell factories” has been consistently gaining importance in the industry over the last years (Walsh 2018; Walsh and Walsh 2022).”
Effects and mechanism of small molecule additives on recombinant protein in CHO cells
Zhang, Q., Mi, C., & Wang, T. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12486-4 · Cited by 13
“Currently, CHO cells are the most commonly used cells in bio-pharmaceuticals, and 84% of the recently approved monoclonal antibodies (mAbs) are produced in CHO (Walsh 2018).”
Background
Effect of co-overexpression of the cargo receptor ERGIC-53/MCFD2 on antibody production and intracellular IgG secretion in recombinant Chinese hamster ovary cells
Kirimoto, Y., Yamano, N., Koga, Y., & Ōmasa, T. (2022) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2022.07.002 · Cited by 11

Authors: Walsh, G.
Affiliations: University of Limerick (IE)
Corresponding author: Walsh, Gary
ORCID: Walsh, Gary
Venue: Nature Biotechnology
Publisher: Springer Science and Business Media LLC
Published: 2018-12
Volume: 36
Issue: 12
Pages: 1136-1145
ISSN: 0733-222X (ISSN-L)
1087-0156
1546-1696
DOI: 10.1038/nbt.4305
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: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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