The use of glutamine synthetase as a selection marker: recent advances in Chinese hamster ovary cell line generation processes

Arzneimittelforschung

Miletzki, B., & Gleiter, C. H. (2005) · Bundesgesundheitsblatt - Gesundheitsforschung - Gesundheitsschutz · doi:10.1007/s00103-005-1024-7 · Cited by 9,401 · see citing works

Efficient selection for high-expression transfectants with a novel eukaryotic vector

Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,135 · see citing works

ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering

Gaj, T., Gersbach, C. A., & Barbas, C. F. (2013) · Trends in Biotechnology · doi:10.1016/j.tibtech.2013.04.004 · Cited by 3,820 · see citing works

Production of recombinant protein therapeutics in cultivated mammalian cells

Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032 · see citing works

Targeted genome engineering in human cells with the Cas9 RNA-guided endonuclease

Cho, S. W., Kim, S., Kim, J. M., & Kim, J.-S. (2013) · Nature Biotechnology · doi:10.1038/nbt.2507 · Cited by 1,863 · see citing works

Cetuximab-Induced Anaphylaxis and IgE Specific for Galactose-α-1,3-Galactose

Chung, C. H., Mirakhur, B., Chan, E., Le, Q.-T., Berlin, J., Morse, M., Murphy, B. A., Satinover, S. M., Hosen, J., Mauro, D., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa074943 · Cited by 1,521 · see citing works

Organization of the higher-order chromatin loop: specific DNA attachment sites on nuclear scaffold

Mirkovitch, J., Mirault, M.-É., & Laemmli, U. K. (1984) · Cell · doi:10.1016/0092-8674(84)90208-3 · Cited by 1,088 · see citing works

Interactions between glutamatergic and monoaminergic systems within the basal ganglia-implications for schizophrenia and Parkinson's disease

Carlsson, M. L., & Carlsson, A. (1990) · Trends in Neurosciences · doi:10.1016/0166-2236(90)90108-m · Cited by 1,086 · see citing works

CHO cells in biotechnology for production of recombinant proteins: current state and further potential

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

MANUAL OF INDUSTRIAL MICROBIOLOGY AND BIOTECHNOLOGY

Demain, A. L., & DAVIES, J. E. (1999) · University of Groningen research database (University of Groningen / Centre for Information Technology) · Cited by 793 · see citing works

Chimeric nucleases stimulate gene targeting in human cells

Porteus, M. H., & Baltimore, D. (2003) · Science · doi:10.1126/science.1078395 · Cited by 741 · see citing works

Gene targeting using zinc finger nucleases

Porteus, M. H., & Carroll, D. (2005) · Nature Biotechnology · doi:10.1038/nbt1125 · Cited by 641 · see citing works

A transcription activator-like effector toolbox for genome engineering

Sanjana, N. E., Cong, L., Zhou, Y., Cunniff, M. M., Feng, G., & Zhang, F. (2012) · Nature Protocols · doi:10.1038/nprot.2011.431 · Cited by 628 · see citing works

A nuclear DNA attachment element mediates elevated and position-independent gene activity

Stief, A., Winter, D. M., Strätling, W. H., & Sippel, A. E. (1989) · Nature · doi:10.1038/341343a0 · Cited by 571 · see citing works

Industrial choices for protein production by large-scale cell culture

Chu, L., & Robinson, D. K. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00197-x · Cited by 554 · see citing works

Glycosylation of Recombinant Antibody Therapeutics

Jefferis, R. (2005) · Biotechnology Progress · doi:10.1021/bp040016j · Cited by 526 · see citing works

Zinc finger nucleases: custom-designed molecular scissors for genome engineering of plant and mammalian cells

Durai, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki912 · Cited by 522 · see citing works

Manual of industrial microbiology and biotechnology

Bushell, M. E. (1987) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(87)90013-5 · Cited by 508 · see citing works

Mammalian cell protein expression for biopharmaceutical production

Zhu, J. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.08.022 · Cited by 492 · see citing works

Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA.

Sasaki, H., Bothner, B. B., Dell, A., & Fukuda, M. N. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45317-3 · Cited by 484 · see citing works

Antibody production

Birch, J. R., & Racher, A. J. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.12.006 · Cited by 477 · see citing works

Recombinant protein therapeutics from CHO cells : 20 years and counting

Jayapal, K. P., Wlaschin, K. F., Hu, W., & Yap, M. G. S. (2007) · Chemical engineering progress · Cited by 473 · see citing works

High-Level Expression of a Recombinant Antibody from Myeloma Cells Using a Glutamine Synthetase Gene as an Amplifiable Selectable Marker

Bebbington, C. R., Renner, G., Thomson, S., King, D. J., Abrams, D., & Yarranton, G. T. (1992) · Nature Biotechnology · doi:10.1038/nbt0292-169 · Cited by 464 · see citing works

The role of glutathione in disulphide bond formation and endoplasmic‐reticulum‐generated oxidative stress

Chakravarthi, S., Jessop, C. E., & Bulleid, N. J. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400645 · Cited by 463 · see citing works

Induction of Homologous Recombination in Mammalian Chromosomes by Using the I-SceI System of Saccharomyces cerevisiae

Choulika, A., Perrin, A., Dujon, B., & Nicolas, J.-F. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.4.1968 · Cited by 459 · see citing works

NMDA Receptor Losses in Putamen from Patients with Huntington's Disease

Young, A. B., Greenamyre, J. T., Hollingsworth, Z. R., Albin, R. L., D’Amato, C. J., Shoulson, I., & Penney, J. B. (1988) · Science · doi:10.1126/science.2841762 · Cited by 394 · see citing works

Structure–function relationships of glutamine synthetases

Eisenberg, D. S., Gill, H. S., Pfluegl, G. M. U., & Rotstein, S. H. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00270-8 · Cited by 379 · see citing works

Redox proteomics identification of oxidatively modified hippocampal proteins in mild cognitive impairment: Insights into the development of Alzheimer's disease

Butterfield, D. A., Poon, H. F., St. Clair, D., Keller, J. N., Pierce, W. M., Klein, J. B., & Markesbery, W. R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.11.002 · Cited by 377 · see citing works

Recombinant protein expression for therapeutic applications

Andersen, D. C., & KRUMMEN, L. A. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00300-2 · Cited by 365 · see citing works

Amplification and expression of sequences cotransfected with a modular dihydrofolate reductase complementary DNA gene

Kaufman, R. J., & Sharp, P. A. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90103-6 · Cited by 360 · see citing works

Targeted gene knockout in mammalian cells by using engineered zinc-finger nucleases

Santiago, Y., Chan, E. M., Liu, P., Orlando, S., Zhang, L., Urnov, F. D., Holmes, M. C., Guschin, D. Y., Waite, A. J., Miller, J. C., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800940105 · Cited by 358 · see citing works

Maximizing productivity of CHO cell‐based fed‐batch culture using chemically defined media conditions and typical manufacturing equipment

Huang, Y., Hu, W., Rustandi, E., Chang, K., Yusuf‐Makagiansar, H., & Ryll, T. (2010) · Biotechnology Progress · doi:10.1002/btpr.436 · Cited by 353 · see citing works

A study of monoclonal antibody‐producing CHO cell lines: What makes a stable high producer?

Chusainow, J., Yang, Y., Yeo, J. H. M., Toh, P. C., Asvadi, P., Wong, N. S. C., & Yap, M. G. S. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.22158 · Cited by 312 · see citing works

Transcription activator‐like effector nucleases (TALENs): A highly efficient and versatile tool for genome editing

Sun, N., & Zhao, H. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.24890 · Cited by 301 · see citing works

Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops

Tan, S., Evans, R. R., & Singh, B. (2006) · Amino Acids · doi:10.1007/s00726-005-0254-1 · Cited by 256 · see citing works

High Level Expression of Tissue Inhibitor of Metalloproteinases in Chinese Hamster Ovary Cells Using Glutamine Synthetase Gene Amplification

Cockett, M. I., Bebbington, C. R., & Yarranton, G. T. (1990) · Nature Biotechnology · doi:10.1038/nbt0790-662 · Cited by 250 · see citing works

Trends in Glycosylation, Glycoanalysis and Glycoengineering of Therapeutic Antibodies and Fc-Fusion Proteins

Beck, A., Wagner‐Rousset, E., Bussat, M., Lokteff, M., Klinguer, C., Haeuw, J., Goetsch, L., Wurch, T., DORSSELAER, A. V., & Corvaı̈a, N. (2008) · Current Pharmaceutical Biotechnology · doi:10.2174/138920108786786411 · Cited by 246 · see citing works

Glutamine: Metabolism, Enzymology, and Regulation

(1980) · Elsevier eBooks · doi:10.1016/b978-0-125-06040-0.x5001-8 · Cited by 216 · see citing works

A mechanistic understanding of production instability in CHO cell lines expressing recombinant monoclonal antibodies

Kim, M., O’Callaghan, P. M., Droms, K. A., & James, D. C. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.23189 · Cited by 215 · see citing works

Production of pharmaceutical‐grade recombinant aprotinin and a monoclonal antibody product using plant‐based transient expression systems

Pogue, G. P., Vojdani, F., Palmer, K. E., Hiatt, E., Hume, S., Phelps, J., Long, L., Bohorova, N., Kim, D., Pauly, M. H., et al. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2009.00495.x · Cited by 199 · see citing works

Metabolic control of recombinant protein <i>N</i>‐glycan processing in NS0 and CHO cells

Baker, K. N., Rendall, M. H., Hills, A. E., Hoare, M., Freedman, R. B., & James, D. C. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1051 · Cited by 184 · see citing works

25 years of recombinant proteins from reactor-grown cells — Where do we go from here?

Hacker, D. L., de Jesús, M., & Wurm, F. M. (2009) · Biotechnology Advances · doi:10.1016/j.biotechadv.2009.05.008 · Cited by 178 · 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

Recombinase-Mediated Cassette Exchange (RMCE): Traditional Concepts and Current Challenges

Turan, S., Galla, M., Ernst, E., Qiao, J., Voelkel, C., Schiedlmeier, B., Zehe, C., & Bode, J. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.004 · Cited by 177 · see citing works

Glutathione Is Required to Regulate the Formation of Native Disulfide Bonds within Proteins Entering the Secretory Pathway

Chakravarthi, S., & Bulleid, N. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406912200 · Cited by 176 · see citing works

Expression and characterization of the product of a human immune interferon cDNA gene in Chinese hamster ovary cells.

SCAHILL, S. J., Devos, R., der Heyden, J. V., & Fiers, W. C. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.15.4654 · Cited by 165 · see citing works

Highly efficient deletion of <i>FUT8</i> in CHO cell lines using zinc‐finger nucleases yields cells that produce completely nonfucosylated antibodies

Malphettes, L., Freyvert, Y., Chang, J., Liu, P., Chan, E., Miller, J. C., Zhou, Z., Nguyen, T., Tsai, C., Snowden, A. W., et al. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22751 · Cited by 164 · see citing works

Gene targeting approaches to complex genetic diseases: atherosclerosis and essential hypertension.

Smithies, O., & Maeda, N. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5266 · Cited by 162 · see citing works

BAK and BAX deletion using zinc‐finger nucleases yields apoptosis‐resistant CHO cells

Cost, G. J., Freyvert, Y., Vafiadis, A., Santiago, Y., Miller, J. C., Rebar, E. J., Collingwood, T. N., Snowden, A., & Gregory, P. D. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22541 · Cited by 160 · see citing works

Phosphorylation of methionine sulfoximine by glutamine synthetase.

Ronzio, R. A., & Meister, A. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.59.1.164 · Cited by 156 · see citing works

Production technologies for monoclonal antibodies and their fragments

Andersen, D. C., & Reilly, D. E. (2004) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2004.08.002 · Cited by 156 · see citing works

A simple method for enriching populations of transfected CHO cells for cells of higher specific productivity

Brezinsky, S. C. G., Chiang, G. G., Szilvasi, A., Mohan, S. B., Shapiro, R. I., MacLean, A. G., Sisk, W. P., & Thill, G. (2003) · Journal of Immunological Methods · doi:10.1016/s0022-1759(03)00108-x · Cited by 156 · see citing works

IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines

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 148 · see citing works

The Story of Glutamine Synthetase Regulation

Stadtman, E. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100055200 · Cited by 147 · see citing works

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 146 · see citing works

Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: effects of amino acids and selective inhibition of enzymes.

Griffith, O. W., Bridges, R. J., & Meister, A. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5405 · Cited by 141 · see citing works

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 · see citing works

Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design

Krajewski, W. W., Collins, R., Holmberg-Schiavone, L., Jones, T. A., Karlberg, T., & Mowbray, S. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.029 · Cited by 135 · see citing works

Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes

Liaw, S., & Eisenberg, D. S. (1994) · Biochemistry · doi:10.1021/bi00169a007 · Cited by 131 · see citing works

Advances in animal cell recombinant protein production: GS-NS0 expression system

Barnes, L. M., Bentley, C. M., & Dickson, A. J. (2000) · Cytotechnology · doi:10.1023/a:1008170710003 · Cited by 129 · see citing works

Determination of Chinese hamster ovary cell line stability and recombinant antibody expression during long‐term culture

Bailey, L., Hatton, D., Field, R. P., & Dickson, A. J. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24485 · Cited by 127 · see citing works

All four Mycobacterium tuberculosis gln A genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis

Harth, G., Masleša-Galić, S., Tullius, M. V., & Horwitz, M. A. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04899.x · Cited by 118 · see citing works

Recombinant therapeutic protein production in cultivated mammalian cells: current status and future prospects

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

Generation of a triple-gene knockout mammalian cell line using engineered zinc-finger nucleases

Liu, P., Chan, E. M., Cost, G. J., Zhang, L., Wang, J., Miller, J. C., Guschin, D. Y., Reik, A., Holmes, M. C., Mott, J. E., et al. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22654 · Cited by 107 · see citing works

A simple high-yielding process for transient gene expression in CHO cells

Rajendra, Y., Kiseljak, D., Baldi, L., Hacker, D. L., & Wurm, F. M. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.03.001 · Cited by 106 · see citing works

Green fluorescent protein as a second selectable marker for selection of high producing clones from transfected CHO cells

Meng, Y. G., Liang, J., Wong, W. L., & Chisholm, V. (2000) · Gene · doi:10.1016/s0378-1119(99)00524-7 · Cited by 99 · see citing works

The use of UCOE vectors in combination with a preadapted serum free, suspension cell line allows for rapid production of large quantities of protein

Benton, T., Chen, T., McEntee, M., Fox, B., King, D., Crombie, R., Thomas, T. C., & Bebbington, C. (2002) · Cytotechnology · doi:10.1023/a:1021141712344 · Cited by 98 · see citing works

Animal cell technology : developments, processes, and products

Spier, R. E., Griffiths, J. B., & MacDonald, C. (1992) · Cited by 97 · see citing works

5-Methylcytosine DNA glycosylase participates in the genome-wide loss of DNA methylation occurring during mouse myoblast differentiation

Jost, J. P. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.21.4452 · Cited by 94 · see citing works

Process development for the production of recombinant antibodies using the glutamine synthetase (GS) system

Brown, M. E., Renner, G., Field, R. P., & Hassell, T. (1992) · Cytotechnology · doi:10.1007/bf02521750 · Cited by 93 · see citing works

The cloning and nucleotide sequence of cDNA for an amplified glutamine synthetase gene from the Chinese hamster

Hayward, B. E., Hussain, A., Wilson, R. H., Lyons, A., Woodcock, V., McIntosh, B., & Harris, T. J. R. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.2.999 · Cited by 92 · see citing works

LC‐MS‐based metabolic characterization of high monoclonal antibody‐producing Chinese hamster ovary cells

Chong, W. P. K., Thng, S. H., Hiu, A. P., Lee, D., Chan, E. C. Y., & Ho, Y. S. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24580 · Cited by 92 · see citing works

Plant Cell Cultures: Bioreactors for Industrial Production

Ruffoni, B., Pistelli, L., Bertoli, A., & Pistelli, L. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7347-4_15 · Cited by 92 · see citing works

Targeting early apoptotic genes in batch and fed‐batch CHO cell cultures

Wong, D. C. F., Wong, K. T. K., Nissom, P. M., Heng, C., & Yap, M. G. S. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20871 · Cited by 92 · see citing works

Cell-Based Screening Using High-Throughput Flow Cytometry

Black, C. B., Duensing, T. D., Trinkle, L. S., & Dunlay, R. T. (2010) · Assay and Drug Development Technologies · doi:10.1089/adt.2010.0308 · Cited by 89 · see citing works

Design of Experiment in CHO and HEK transient transfection condition optimization

Bollin, F., Dechavanne, V., & Chevalet, L. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.02.008 · Cited by 85 · see citing works

Detection of glutamine synthetase in the cerebrospinal fluid of Alzheimer diseased patients: a potential diagnostic biochemical marker.

Gunnersen, D., & Haley, B. E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11949 · Cited by 85 · see citing works

Appropriate mammalian expression systems for biopharmaceuticals.

Werner, R. G., Noé, W., Kopp, K., & Schlüter, M. (1998) · PubMed · Cited by 82 · see citing works

Amplification and cloning of the Chinese hamster glutamine synthetase gene.

Sanders, P. G., & Wilson, R. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01762.x · Cited by 80 · see citing works

Understanding the intracellular effect of enhanced nutrient feeding toward high titer antibody production process

Yu, M., Hu, Z., Pacis, E., Vijayasankaran, N., Shen, A. Y., & Li, F. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.23031 · Cited by 80 · see citing works

Overexpression of 5-methylcytosine DNA glycosylase in human embryonic kidney cells EcR293 demethylates the promoter of a hormone-regulated reporter gene

Zhu, B., Benjamin, D., Zheng, Y., Angliker, H., Thiry, S., Siegmann, M., & Jost, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091097298 · Cited by 78 · see citing works

Plant-derived vaccines and other therapeutics produced in contained systems

Franconi, R., Demurtas, O. C., & Massa, S. (2010) · Expert Review of Vaccines · doi:10.1586/erv.10.91 · Cited by 78 · see citing works

Co-expression and amplification of dihydrofolate reductase cDNA and the Escherichia coli XGPRT gene in Chinese hamster ovary cells.

RINGOLD, G. M., Dieckmann, B. S., & Lee, F. (1981) · PubMed · Cited by 76 · see citing works

An efficient and targeted gene integration system for high-level antibody expression

Huang, Y., Li, Y., Wang, Y. G., Gu, X., Wang, Y., & Shen, B. F. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.01.022 · Cited by 75 · see citing works

Adaptation of Chinese hamster ovary cells to low culture temperature: Cell growth and recombinant protein production

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

Early prediction of instability of chinese hamster ovary cell lines expressing recombinant antibodies and antibody‐fusion proteins

Dorai, H., Corisdeo, S., Ellis, D., Kinney, C., Chomo, M., Hawley‐Nelson, P., Moore, G. P., Betenbaugh, M. J., & Ganguly, S. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.24367 · Cited by 74 · see citing works

Catalytic Mechanism of Glutamine Synthetase; Overview of Glutamine Metabolism

Meister, A. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-506040-0.50006-6 · Cited by 73 · see citing works

Strategies for selecting recombinant CHO cell lines for cGMP manufacturing: Improving the efficiency of cell line generation

Porter, A. J., Racher, A. J., Preziosi, R. F., & Dickson, A. J. (2010) · Biotechnology Progress · doi:10.1002/btpr.443 · Cited by 71 · see citing works

Glutamine synthetase is essential in early mouse embryogenesis

He, Y., Hakvoort, T. B. M., Vermeulen, J. L. M., Lamers, W. H., & van ROON, M. A. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21185 · Cited by 70 · see citing works

Molecular engineering of exocytic vesicle traffic enhances the productivity of Chinese hamster ovary cells

Peng, R., & Fussenegger, M. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.22141 · Cited by 70 · see citing works

Animal-Derived Pharmaceutical Proteins

Redwan, E. M. M. M. (2009) · Journal of Immunoassay and Immunochemistry · doi:10.1080/15321810903084400 · Cited by 69 · see citing works

High‐throughput laser‐mediated in situ cell purification with high purity and yield

Koller, M. R., Hanania, E. G., Stevens, J., Eisfeld, T. M., Sasaki, G. C., Fieck, A., & Palsson, B. Ø. (2004) · Cytometry Part A · doi:10.1002/cyto.a.20079 · Cited by 68 · see citing works

Rapid protein production using CHO stable transfection pools

Ye, J., Alvin, K., Latif, H., Hsu, A. H.-M., Parikh, V., Whitmer, T., Tellers, M., Edmonds, M. C. D. L. C., Ly, J., Salmon, P. M., et al. (2010) · Biotechnology Progress · doi:10.1002/btpr.469 · Cited by 68 · see citing works

Generation of stable cell lines by site-specific integration of transgenes into engineered Chinese hamster ovary strains using an FLP-FRT system

Zhou, H., Liu, Z., Sun, Z., Huang, Y., & Yu, W. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.03.020 · Cited by 65 · see citing works

A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies

Lee, C. J., Seth, G., Tsukuda, J., & Hamilton, R. W. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.22126 · Cited by 65 · see citing works

CHO gene expression profiling in biopharmaceutical process analysis and design

Schaub, J., Clemens, C., Schorn, P., Hildebrandt, T., Rust, W., Mennerich, D., Kaufmann, H., & Schulz, T. W. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22549 · Cited by 63 · see citing works

Methods in mammalian cell line engineering: from random mutagenesis to sequence-specific approaches

Krämer, O., Klausing, S., & Noll, T. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2798-6 · Cited by 61 · see citing works

CHO DUKX cell lineages preadapted to growth in serum-free suspension culture enable rapid development of cell culture processes for the manufacture of recombinant proteins

Sinacore, M. S., Charlebois, T. S., Harrison, S., Brennan, S., Richards, T., Hamilton, M. A., Scott, S., Brodeur, S. R., Oakes, P., Leonard, M., et al. (1996) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19961120)52:4 · Cited by 55 · see citing works

Cellular concentrations of glutamine synthetase in murine organs

van Straaten, H. W. M., He, Y., van Duist, M. M., Labruyère, W. T., Vermeulen, J. L. M., van Dijk, P., Ruijter, J. M., Lamers, W. H., & Hakvoort, T. B. M. (2006) · Biochemistry and Cell Biology · doi:10.1139/o05-170 · Cited by 54 · see citing works

Selection of high-producing CHO cells using NPT selection marker with reduced enzyme activity

Sautter, K., & Enenkel, B. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20374 · Cited by 51 · see citing works

Application of destabilizing sequences on selection marker for improved recombinant protein productivity in CHO-DG44

NG, S., Wang, D. I. C., & YAP, M. (2007) · Metabolic Engineering · doi:10.1016/j.ymben.2007.01.001 · Cited by 51 · see citing works

Regulation of the Spatiotemporal Pattern of Expression of the Glutamine Synthetase Gene

Lie‐Venema, H., Hakvoort, T. B. M., van Hemert, F. J., Moorman, A. F. M., & Lamers, W. H. (1998) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60829-6 · Cited by 49 · see citing works

Flow cytometry: An improved method for the selection of highly productive gene‐amplified CHO cells using flow cytometry

Yoshikawa, T., Nakanishi, F., Ogura, Y., Oi, D., Ōmasa, T., Katakura, Y., Kishimoto, M., & Suga, K. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1134 · Cited by 48 · see citing works

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 · see citing works

Effect of inducible co‐overexpression of protein disulfide isomerase and endoplasmic reticulum oxidoreductase on the specific antibody productivity of recombinant Chinese hamster ovary cells

Mohan, C., & Lee, G. M. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22781 · Cited by 43 · see citing works

Transient expression of an IL-23R extracellular domain Fc fusion protein in CHO vs. HEK cells results in improved plasma exposure

Suen, K. F., Turner, M. S., Gao, F., Liu, B., Althage, A., Slavin, A., Ou, W., Zuo, E. T., Eckart, M. R., Ogawa, T., et al. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2009.12.015 · Cited by 41 · see citing works

Impact of gene vector design on the control of recombinant monoclonal antibody production by chinese hamster ovary cells

Davies, S. L., O’Callaghan, P. M., McLeod, J., Pybus, L. P., Sung, Y. H., Rance, J., Wilkinson, S. J., Racher, A. J., Young, R. J., & James, D. C. (2011) · Biotechnology Progress · doi:10.1002/btpr.692 · Cited by 39 · see citing works

Mammalian Cell Culture for Biopharmaceutical Production

Zhang, J. (2014) · ASM Press eBooks · doi:10.1128/9781555816827.ch12 · Cited by 38 · see citing works

Meganuclease-driven targeted integration in CHO-K1 cells for the fast generation of HTS-compatible cell-based assays

Cabaniols, J.-P., Ouvry, C., Lamamy, V., Fery, I., Craplet, M.-L., Moulharat, N., Guenin, S.-P., Bedut, S., Nosjean, O., Ferry, G., et al. (2010) · SLAS Discovery · doi:10.1177/1087057110375115 · Cited by 36 · see citing works

In vitro changes in plasma membrane heparan sulfate proteoglycans and in perlecan expression participate in the regulation of fibroblast growth factor 2 mitogenic activity

Guillonneau, X., Tassin, J., Berrou, E., Bryckaert, M., Courtois, Y., & Mascarelli, F. (1996) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199601)166:1 · Cited by 33 · see citing works

Regulating apoptosis in mammalian cell cultures

Arden, N., & Betenbaugh, M. J. (2006) · Cytotechnology · doi:10.1007/s10616-006-9008-5 · Cited by 28 · see citing works

Rapid establishment of high-producing cell lines using dicistronic vectors with glutamine synthetase as the selection marker

Pu, H., Cashion, L. M., Kretschmer, P. J., & Liu, Z. (1998) · Molecular Biotechnology · doi:10.1007/bf02745860 · Cited by 23 · see citing works

Comparison of Humanized IgG and FvFc Anti-CD3 Monoclonal Antibodies Expressed in CHO Cells

Serpieri, F., Inocencio, A. L., de Oliveira, J. M., Pimenta, A. A., Garbuio, A., Kalil, J. E., Brígido, M. M., & Moro, A. M. (2010) · Molecular Biotechnology · doi:10.1007/s12033-010-9269-2 · Cited by 21 · see citing works

Use of the Glutamine Synthetase (GS) Expression System for the Rapid Development of Highly Productive Mammalian Cell Processes

Birch, J. R., Mainwaring, D. O., & Racher, A. J. (2005) · doi:10.1002/9783527620982.ch34 · Cited by 19 · see citing works

Optimization of short‐term transgene expression by sodium butyrate and ubiquitous chromatin opening elements (UCOEs)

de Poorter, J. J., Lipinski, K. S., Nelissen, R. G. H. H., Huizinga, T. W. J., & Hoeben, R. C. (2007) · The Journal of Gene Medicine · doi:10.1002/jgm.1057 · Cited by 15 · see citing works

Use of vectors based on gene amplification for the expression of cloned genes in mammalian cells

Bebbington, C. R. (1996) · doi:10.1093/oso/9780199634811.003.0003 · Cited by 14 · see citing works

Regulation of Glutamine Synthetase by Enzyme Catalyzed Structural Modification

Shapiro, B. M. (1970) · Angewandte Chemie International Edition in English · doi:10.1002/anie.197006701 · Cited by 11 · see citing works

Biallelic Gene Knockouts in Chinese Hamster Ovary Cells

Yamane‐Ohnuki, N., Yamano, K., & Satoh, M. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-232-8_1 · Cited by 9 · see citing works

STABILITY OF PRODUCTION OF RECOMBINANT ANTIBODIES FROM GLUTAMINE SYNTHETASE AMPLIFIED CHO AND NS0 CELL LINES

Hassell, T., Brand, H. N., Renner, G., Westlake, A. J., & Field, R. P. (1992) · Elsevier eBooks · doi:10.1016/b978-0-7506-0421-5.50018-0 · Cited by 9 · see citing works

Heterologous Protein Expression in Yeasts and Filamentous Fungi

Zhang, N., & An, Z. (2014) · ASM Press eBooks · doi:10.1128/9781555816827.ch11 · Cited by 7 · see citing works

Bacterial Cultivation for Production of Proteins and Other Biological Products

Shiloach, J., & Rinas, U. (2014) · ASM Press eBooks · doi:10.1128/9781555816827.ch10 · Cited by 4 · see citing works

Cell Xpress™ Technology Facilitates High-Producing Chinese Hamster Ovary Cell Line Generation Using Glutamine Synthetase Gene Expression System

Richardson, G. A., Lin, N., Lacy, K. A., Davis, L. A., Gray, M. I., Cresswell, J. R., Gerber, M. A., Caple, M. V., & Kayser, K. J. (2010) · Springer eBooks · doi:10.1007/978-90-481-3419-9_9 · Cited by 4 · see citing works

Impact on product quality of high productive GS-CHO cell lines

Perani, A., Gloria, B., Wang, D., Murphy, R., Singh, H. K., Smyth, F. E., & Scott, A. M. (2011) · BMC Proceedings · doi:10.1186/1753-6561-5-s8-p17 · Cited by 1 · 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

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 264 · see citing works

Impact of CHO Metabolism on Cell Growth and Protein Production: An Overview of Toxic and Inhibiting Metabolites and Nutrients

Pereira, S., Kildegaard, H. F., & Andersen, M. R. (2018) · Biotechnology Journal · doi:10.1002/biot.201700499 · Cited by 214 · see citing works

Industry view on the relative importance of “clonality” of biopharmaceutical-producing cell lines

Frye, C. C., Deshpande, R. R., Estes, S. D., Francissen, K., Joly, J. C., Lubiniecki, A. S., Munro, T. P., Russell, R. J., Wang, T., & Anderson, K. (2016) · Biologicals · doi:10.1016/j.biologicals.2016.01.001 · Cited by 98 · see citing works

Perfusion cell culture for the production of conjugated recombinant fusion proteins reduces clipping and quality heterogeneity compared to batch-mode processes

Bielser, J., Chappuis, L., Xiao, Y., Souquet, J., Broly, H., & Morbidelli, M. (2019) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2019.06.006 · Cited by 48 · see citing works

Comparative study of therapeutic antibody candidates derived from mini‐pool and clonal cell lines

Fan, L., Rizzi, G., Bierilo, K. K., Tian, J., Yee, J. C., Russell, R. J., & Das, T. K. (2017) · Biotechnology Progress · doi:10.1002/btpr.2477 · Cited by 38 · see citing works

Methionine sulfoximine supplementation enhances productivity in GS–CHOK1SV cell lines through glutathione biosynthesis

Feary, M., Racher, A. J., Young, R. J., & Smales, C. M. (2016) · Biotechnology Progress · doi:10.1002/btpr.2372 · Cited by 22 · see citing works

Large‐scale functionalLIPAvariant characterization to improve birth prevalence estimates of lysosomal acid lipase deficiency

del Angel, G., Hutchinson, A. T., Jain, N. K., Forbes, C. D., & Reynders, J. (2019) · Human Mutation · doi:10.1002/humu.23837 · Cited by 22 · see citing works

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 · 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

Attenuation of glutamine synthetase selection marker improves product titer and reduces glutamine overflow in Chinese hamster ovary cells

Sacco, S. A., Tuckowski, A. M., Trenary, I. A., Kraft, L., Betenbaugh, M. J., Young, J. D., & Smith, K. D. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28084 · Cited by 15 · see citing works

Bigdata analytics identifies metabolic inhibitors and promoters for productivity improvement and optimization of monoclonal antibody (mAb) production process

Morris, C. S., Polanco, A., Yongky, A., Xu, J., Huang, Z., Zhao, J. C., McFarland, K. S., Park, S., Warrack, B. M., Reily, M. D., et al. (2020) · Bioresources and Bioprocessing · doi:10.1186/s40643-020-00318-6 · Cited by 16 · see citing works

Biological therapeutic modalities

Chhabra, M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821972-0.00015-0 · Cited by 16 · see citing works

Wheels turning: CHO cell modeling moves into a digital biomanufacturing era

Ranpura, S. A., Maralingannavar, V., Gheorghe, A.-G., Ma, E., Morrissey, J., Betenbaugh, M. J., & Demirhan, D. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.06.035 · Cited by 13 · see citing works

Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product

Zacchi, L. F., Recinos, D. R., Pegg, C. L., Phung, T. K., Napoli, M., Aitken, C., Sandford, V., Mahler, S. M., Lee, Y. Y., Schulz, B. L., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01903-x · Cited by 13 · see citing works

Increased MSX level improves biological productivity and production stability in multiple recombinant GS CHO cell lines

Tian, J., He, Q., Oliveira, C. L., Qian, Y., Egan, S., Xu, J., Qian, N., Langsdorf, E. F., Warrack, B. M., Aranı́bar, N., et al. (2020) · Engineering in Life Sciences · doi:10.1002/elsc.201900124 · Cited by 13 · see citing works

S-Trap Eliminates Cell Culture Media Polymeric Surfactants for Effective Proteomic Analysis of Mammalian Cell Bioreactor Supernatants

Zacchi, L. F., Recinos, D. R., Otte, E. A., Aitken, C., Hunt, T., Sandford, V., Lee, Y. Y., Schulz, B. L., & Howard, C. B. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00106 · Cited by 13 · see citing works

Reduction of medium consumption in perfusion mammalian cell cultures using a perfusion rate equivalent concentrated nutrient feed

Bielser, J., Kraus, L., Morales, O. B., Broly, H., & Souquet, J. (2020) · Biotechnology Progress · doi:10.1002/btpr.3026 · Cited by 13 · see citing works

Continuous bleed recycling significantly increases recombinant protein production yield in perfusion cell cultures

Bielser, J., Aeby, M., Caso, S., Roulet, A., Broly, H., & Souquet, J. (2021) · Biochemical Engineering Journal · doi:10.1016/j.bej.2021.107966 · Cited by 13 · see citing works

Transfer of continuous manufacturing process principles for mAb production in a GMP environment: A step in the transition from batch to continuous

Ferreira, K. B., Benlegrimet, A., Diane, G., Pasquier, V., Guillot, R., Poli, M. D., Chappuis, L., Vishwanathan, N., Souquet, J., Broly, H., et al. (2022) · Biotechnology Progress · doi:10.1002/btpr.3259 · Cited by 12 · see citing works

Directed evolution of biomass intensive CHO cells by adaptation to sub-physiological temperature

Syddall, K. L., Fernandez‐Martell, A., Cartwright, J. F., Alexandru-Crivac, C. N., Hodgson, A., Racher, A. J., Young, R. J., & James, D. C. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.11.005 · Cited by 12 · see citing works

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 · see citing works

Effects of pyruvate on primary metabolism and product quality for a high‐density perfusion process

Caso, S., Aeby, M., Jordan, M., Guillot, R., & Bielser, J. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28033 · Cited by 9 · see citing works

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 · see citing works

Building a Cell Culture Process with Stable Foundations: Searching for Certainty in an Uncertain World

O’Callaghan, P. M., & Racher, A. J. (2014) · Cell engineering · doi:10.1007/978-3-319-10320-4_12 · Cited by 9 · see citing works

Investigating the metabolic load of monoclonal antibody production conveyed to an inducible CHO cell line using a transfer-rate online monitoring system

Reyes, S., Lemire, L., Durocher, Y., Voyer, R., Henry, O., & Pham, P. L. (2025) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2025.01.008 · Cited by 7 · see citing works

CHO stable pool fed‐batch process development of SARS ‐ CoV ‐2 spike protein production: Impact of aeration conditions and feeding strategies

Reyes, S., Pham, P. L., Durocher, Y., & Henry, O. (2024) · Biotechnology Progress · doi:10.1002/btpr.3507 · Cited by 7 · see citing works

Effects of the COVID-19 pandemic: new approaches for accelerated delivery of gene to first-in-human CMC data for recombinant proteins

Broly, H., Souquet, J., & Beck, A. (2023) · mAbs · doi:10.1080/19420862.2023.2220150 · Cited by 5 · see citing works

Bacterial Glutamine Synthetases as a Novel Metabolic Selection Marker to Improve CHO Cell Culture Performance Through Selection Stringency Modulation

Heinzelmann, D., Michelarakis, N., Reuss, F., Lindner, B., Karow‐Zwick, A. R., Bauer, J., Renner, B., Fischer, S., Schulz, P., & Schmidt, M. J. (2025) · Biotechnology Journal · doi:10.1002/biot.70119 · Cited by 4 · see citing works

Development of an efficient method for selection of stable cell pools for protein expression and surface display with Expi293F cells

Chen, C., Wang, Z., Sun, Z., Li, W., & Dimitrov, D. S. (2023) · Cell Biochemistry and Function · doi:10.1002/cbf.3787 · Cited by 4 · see citing works

Effect of adenosine and cordycepin on recombinant antibody production yields in two different Chinease hamster ovary cell lines

Jarusintanakorn, S., Rangnoi, K., Yamabhai, M., & Mastrobattista, E. (2023) · Biotechnology Progress · doi:10.1002/btpr.3403 · Cited by 3 · see citing works

Streamlined rAAV HeLaS3 producer cell line generation via GS selection

Antunes, M., Moura, F., Sebastian, I. R., Alves, P., Gomes‐Alves, P., & Escandell, J. M. (2026) · Scientific Reports · doi:10.1038/s41598-025-34826-2 · Cited by 1 · see citing works

Expression Systems for Recombinant Biopharmaceutical Production by Mammalian Cells in Culture

Brown, A. J., Kalsi, D., Fernandez‐Martell, A., Cartwright, J., Barber, N., Patel, Y. D., Turner, R., Bryant, C. L., Johari, Y. B., & James, D. C. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527699124.ch13 · Cited by 1 · see citing works

Additional file 1 of Bigdata analytics identifies metabolic inhibitors and promoters for productivity improvement and optimization of monoclonal antibody (mAb) production process

Morris, C. S., Polanco, A., Yongky, A., Xu, J., Huang, Z., Zhao, J., McFarland, K. S., Park, S., Warrack, B. M., Reily, M., et al. (2020) · Figshare · doi:10.6084/m9.figshare.12414194

Next‐Generation Glutamine Synthetase Expression Vector for Therapeutic Protein Manufacturing Using CHO Cells

Johari, Y. B., Wensley, S. J., Ammar, M. A., Srivastava, A., Ragurajan, C., Patel, J., Elliott, N. C., Hodgson-Casson, A. C., Fedi, M. O., Anbar, M., et al. (2026) · Biotechnology and Bioengineering · doi:10.1002/bit.70405

Attenuated glutamine synthetase as a selection marker in CHO cells to efficiently isolate highly productive stable cells for the production of antibodies and other biologics

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 · see citing works

Recombinant Protein Production Advances in Mammalian Cell

Jessi, A. (2021) · Biochemistry : an Indian journal

SiMPl‐GS: Advancing Cell Line Development via Synthetic Selection Marker for Next‐Generation Biopharmaceutical Production

Yoon, C., Lee, E., Kim, D., Joung, S., Kim, Y., Jung, H.-C., Kim, Y., & Lee, G. M. (2024) · Advanced Science · doi:10.1002/advs.202405593 · Cited by 6 · see citing works

Proteostasis engineering of glutamine synthetase for stringent, drug-free selection in Chinese hamster ovary cells

Kim, H., Park, J. U., Ha, J., & Baik, J. Y. (2026) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-026-14015-5

Cell Line Isolation and Design

Munro, T. P., Pilbrough, W., Hughes, B. S., & Gray, P. P. (2011) · Elsevier eBooks · doi:10.1016/b978-0-444-64046-8.00013-6 · Cited by 1 · see citing works