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Large-Scale Transfection of Mammalian Cells for the Fast Production of Recombinant Protein
Abstract
Recombinant proteins (r-proteins) are increasingly important in fundamental research and for clinical applications. As many of these r-proteins are of human or animal origin, cultivated mammalian cells are the host of choice to ensure their functional folding and proper posttranslational modifications. Large-scale transfection of human embryonic kidney 293 or Chinese hamster ovary cells is now an established technology that can be used in the production of hundreds of milligram to gram quantities of a r-protein in less than 1 mo from cloning of its cDNA. This chapter aims to provide an overview of large-scale transfection technology with a particular emphasis on calcium phosphate and polyethylenimine-mediated gene transfer.
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When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production.
“When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production (Rosser et al., 2005;Pham et al., 2006;Geisse, 2009;Chahal et al., 2011;Baldi et al., 2012).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Pham et al., 2006
The production rate in transient transfection relies on many factors including efficiency of the transfection phase, cytotoxicity of the transfection reagent, and extensiveness of the feeding strategy applied post-transfection.
“However, the production rate relies on many factors including efficiency of the transfection phase, cytotoxicity of the transfection reagent and extensiveness of the feeding strategy applied to the culture post-transfection (Pham et al., 2006;Daramola et al., 2014).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Pham et al., 2006
Citations
Cites
A rapid alkaline extraction procedure for screening recombinant plasmid DNA
Birnboim, H. C., & Doly, J. (1979) · Nucleic Acids Research · doi:10.1093/nar/7.6.1513 · Cited by 14,686
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
Characteristics of a human cell line transformed by DNA from human adenovirus type 5
Graham, F. L., Russell, W. C., Smiley, J., & Nairn, R. (1977) · Journal of General Virology · doi:10.1099/0022-1317-36-1-59 · Cited by 4,793
Exploring polyethylenimine‐mediated DNA transfection and the proton sponge hypothesis
Akinc, A., Thomas, M., Klibanov, A. M., & Langer, R. (2004) · The Journal of Gene Medicine · doi:10.1002/jgm.696 · Cited by 1,339
Poly(ethylenimine) and its role in gene delivery
Godbey, W. T., Wu, K. K., & Mikos, A. G. (1999) · Journal of Controlled Release · doi:10.1016/s0168-3659(99)00090-5 · Cited by 1,200
A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus
Boshart, M., Weber, F., Jahn, G., DORSCHHLER, K., Fleckenstein, B. W., & Schaffner, W. (1985) · Cell · doi:10.1016/s0092-8674(85)80025-8 · Cited by 1,140
Analysis of Mutation in Human Cells by Using an Epstein-Barr Virus Shuttle System
DuBridge, R. B., Tang, P., Hsia, H. C., Leong-Morgenthaler, P.-M., Miller, J. H., & Calos, M. P. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.1.379 · Cited by 1,134
Durocher, Y. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.2.e9 · Cited by 1,041
Self-citationHigh efficiency transformation by direct microinjection of DNA into cultured mammalian cells
Capecchi, M. R. (1980) · Cell · doi:10.1016/0092-8674(80)90358-x · Cited by 1,000
Polyethylenimine-based non-viral gene delivery systems
Lungwitz, U., Breunig, M., Blunk, T., & Göpferich, A. M. (2005) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2004.11.011 · Cited by 998
Utilization of the beta and gamma chains of the IL‐2 receptor by the novel cytokine IL‐15.
Giri, J. G., Ahdieh, M., Eisenman, J. R., Shanebeck, K. D., Grabstein, K. H., Kumaki, S., Namen, A. E., Park, L. S., Cosman, D. J., & Anderson, D. M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06576.x · Cited by 980
Neu, M., Fischer, D., & Kissel, T. (2005) · The Journal of Gene Medicine · doi:10.1002/jgm.773 · Cited by 880
Jordan, M., Schallhorn, A., & Wurm, F. M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.4.596 · Cited by 862
Tracking the intracellular path of poly(ethylenimine)/DNA complexes for gene delivery
Godbey, W. T., Wu, K. K., & Mikos, A. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.5177 · Cited by 823
Evidence for the role of proteoglycans in cation-mediated gene transfer.
Mislick, K. A., & Baldeschwieler, J. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12349 · Cited by 774
Size-dependent DNA Mobility in Cytoplasm and Nucleus
Lukács, G. L., Haggie, P. M., Seksek, O., Lechardeur, D., Freedman, N. D., & Verkman, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1625 · Cited by 752
Pollard, H., Rémy, J.-S., Loussouarn, G., Demolombe, S., Behr, J., & Escande, D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7507 · Cited by 711
Different behavior of branched and linear polyethylenimine for gene deliveryin vitro andin vivo
Wightman, L., Kircheis, R., R�ssler, V., Carotta, S., Ruzicka, R., Kursa, M., & Wagner, E. (2001) · The Journal of Gene Medicine · doi:10.1002/jgm.187 · Cited by 702
A novel IL‐1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types.
McMahan, C. J., Slack, J. L., Mosley, B., Cosman, D. J., Lupton, S., Brunton, L. L., Grubin, C. E., Wignall, J. M., Jenkins, N. A., & Brannan, C. I. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07831.x · Cited by 668
Metabolic instability of plasmid DNA in the cytosol: a potential barrier to gene transfer
Lechardeur, D., Sohn, K.-J., Haardt, M., Joshi, P. B., Monck, M. A., Graham, R. W., Beatty, B., Squire, J. A., O'Brodovich, H. M., & Lukács, G. L. (1999) · Gene Therapy · doi:10.1038/sj.gt.3300867 · Cited by 632
Characterization of commercially available and synthesized polyethylenimines for gene delivery
von Harpe, A., Petersen, H., Li, Y., & Kissel, T. (2000) · Journal of Controlled Release · doi:10.1016/s0168-3659(00)00317-5 · Cited by 521
Subramanian, S. V., Fitzgerald, M. L., & Bernfield, M. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14713 · Cited by 390
Reisman, D., & Sugden, B. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.11.3838 · Cited by 367
Intracellular route and transcriptional competence of polyethylenimine–DNA complexes
Bieber, T., Meißner, W., Sawa Kostin, D., Niemann, A., & Elsässer, H. (2002) · Journal of Controlled Release · doi:10.1016/s0168-3659(02)00129-3 · Cited by 353
Optimized galenics improve in vitro gene transfer with cationic molecules up to 1000-fold.
Boussif, O., Zanta, M. A., & Behr, J. (1996) · PubMed · Cited by 345
Intervening sequences increase efficiency of RNA 3' processing and accumulation of cytoplasmic RNA
Huang, M. T. F., & Gorman, C. M. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.4.937 · Cited by 303
Use of the human elongation factor 1α promoter as a versatile and efficient expression system
Kim, D. W., Uetsuki, T., Kaziro, Y., Yamaguchi, N., & Sugano, S. (1990) · Gene · doi:10.1016/0378-1119(90)90091-5 · Cited by 277
Powerful and versatile enhancer-promoter unit for mammalian expression vectors
Foecking, M. K., & Hofstetter, H. (1986) · Gene · doi:10.1016/0378-1119(86)90137-x · Cited by 269
Brunner, S., Fuertbauer, E., Sauer, T., Kursa, M., & Wagner, E. (2002) · Molecular Therapy · doi:10.1006/mthe.2001.0509 · Cited by 244
Transfection of adherent and suspended cells by calcium phosphate
Jordan, M. (2004) · Methods · doi:10.1016/j.ymeth.2003.11.011 · Cited by 238
Loyter, A., Scangos, G. A., & Ruddle, F. H. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.2.422 · Cited by 221
Large-scale transient expression in mammalian cells for recombinant protein production
Wurm, F. M., & Bernard, A. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)80027-5 · Cited by 205
Serum‐free large‐scale transient transfection of CHO cells
Derouazi, M., Girard, P., Tilborgh, F. V., Iglesias, K., Müller, N., Bertschinger, M., & Wurm, F. M. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20161 · Cited by 205
Itaka, K., Harada, A., Yamasaki, Y., Nakamura, K., Kawaguchi, H., & Kataoka, K. (2004) · The Journal of Gene Medicine · doi:10.1002/jgm.470 · Cited by 201
Transient gene expression: Recombinant protein production with suspension‐adapted HEK293‐EBNA cells
Meissner, P., Pick, H. M., Kulangara, A., Chatellard, P., Friedrich, K., & Wurm, F. M. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1179 · Cited by 200
Adenovirus tripartite leader sequence enhances translation of mRNAs late after infection
Logan, J., & Shenk, T. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3655 · Cited by 198
Stadler, J., Lemmens, R., & Nyhammar, T. (2004) · The Journal of Gene Medicine · doi:10.1002/jgm.512 · Cited by 193
Gahn, T. A., & Sugden, B. (1995) · Journal of Virology · doi:10.1128/jvi.69.4.2633-2636.1995 · Cited by 191
Transfer and Expression of Foreign Genes in Mammalian Cells
Colosimo, A., Goncz, K. K., Holmes, A. R., Kunzelmann, K., Novelli, G., Malone, R. W., Bennett, M. J., & Gruenert, D. C. (2000) · BioTechniques · doi:10.2144/00292rv01 · Cited by 187
Role of endocytosis in the transfection of L929 fibroblasts by polyethylenimine/DNA complexes
Rémy-Kristensen, A., Clamme, J., Vuilleumier, C., Kuhry, J., & Mély, Y. (2001) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(01)00359-5 · Cited by 163
Chu, G., & Sharp, P. A. (1981) · Gene · doi:10.1016/0378-1119(81)90008-1 · Cited by 159
On the mechanism of DNA transfection: efficient gene transfer without viruses
Coonrod, A., Li, F.-Q., & Horwitz, M. S. (1997) · Gene Therapy · doi:10.1038/sj.gt.3300536 · Cited by 151
Ca2+-sensitive cytosolic nucleases prevent efficient delivery to the nucleus of injected plasmids
Pollard, H., Toumaniantz, G., Amos, J.-L., Avet‐Loiseau, H., Guihard, G., Behr, J., & Escande, D. (2001) · The Journal of Gene Medicine · doi:10.1002/jgm.160 · Cited by 148
(1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80100-7 · Cited by 147
Transient Gene Expression in Suspension HEK-293 Cells: Application to Large-Scale Protein Production
Baldi, L., Müller, N., Picasso, S., Jacquet, R., Girard, P., Thanh, H.-P., Derow, E., & Wurm, F. M. (2005) · Biotechnology Progress · doi:10.1021/bp049830x · Cited by 142
Simian virus 40 replication in adenovirus-transformed human cells antagonizes gene expression
LEBKOWSKI, J. S., Clancy, S., & Calos, M. P. (1985) · Nature · doi:10.1038/317169a0 · Cited by 138
Kaufman, R. J. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.3.689 · Cited by 135
Transfer of high copy number plasmid into mammalian cells by calcium phosphate transfection
Batard, P., Jordan, M., & Wurm, F. M. (2001) · Gene · doi:10.1016/s0378-1119(01)00467-x · Cited by 134
Pham, P. L., Perret, S., Doan, H. C., Cass, B., St‐Laurent, G., Kamen, A., & Durocher, Y. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10774 · Cited by 131
Self-citationLängle-Rouault, F., Patzel, V., Benavente, A., Taillez, M., Silvestre, N., Bompard, A., Sczakiel, G., Jacobs, E. J., & Rittner, K. (1998) · Journal of Virology · doi:10.1128/jvi.72.7.6181-6185.1998 · Cited by 130
Transient gene expression in mammalian cells grown in serum-free suspension culture
Schlaeger, E., & Christensen, K. (1999) · Cytotechnology · doi:10.1023/a:1008000327766 · Cited by 129
Eukaryotic Expression Systems: A Comparison
Geisse, S., Gram, H., Kleuser, B., & Kocher, H. P. (1996) · Protein Expression and Purification · doi:10.1006/prep.1996.0101 · Cited by 125
Wu, H., Kapoor, P., & Frappier, L. (2002) · Journal of Virology · doi:10.1128/jvi.76.5.2480-2490.2002 · Cited by 125
Intracellular distribution of DNA internalized through calcium phosphate precipitation
Orrantia, E., & Chang, P. L. (1990) · Experimental Cell Research · doi:10.1016/0014-4827(90)90181-9 · Cited by 118
Gorman, C., Gies, D. R., McCray, G., & Huang, M. T. F. (1989) · Virology · doi:10.1016/0042-6822(89)90605-3 · Cited by 118
Aiyar, A. A., Tyree, C. M., & Sugden, B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6394 · Cited by 117
Production methods for gene transfer vectors based on adeno-associated virus serotypes
Grimm, D. (2002) · Methods · doi:10.1016/s1046-2023(02)00219-0 · Cited by 117
100-liter transient transfection
Girard, P., Derouazi, M., Baumgartner, G., Bourgeois, M., Jordan, M., Jacko, B., & Wurm, F. M. (2002) · Cytotechnology · doi:10.1023/a:1021173124640 · Cited by 115
State-of-the-art of the production of retroviral vectors
Merten, O. W. (2004) · The Journal of Gene Medicine · doi:10.1002/jgm.499 · Cited by 115
Small-scale bioreactor system for process development and optimization
Girard, P., Jordan, M., Tsao, M., & Wurm, F. M. (2001) · Biochemical Engineering Journal · doi:10.1016/s1369-703x(00)00110-8 · Cited by 112
Pham, P. L., Perret, S., Cass, B., Carpentier, E., St‐Laurent, G., Bisson, L., Kamen, A., & Durocher, Y. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20428 · Cited by 112
Self-citationThe Linking Regions of EBNA1 Are Essential for Its Support of Replication and Transcription
Mackey, D. M., & Sugden, B. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3349 · Cited by 102
Current issues in adeno-associated viral vector production
Merten, O.-W., Gény-Fiamma, C., & Douar, A. M. (2005) · Gene Therapy · doi:10.1038/sj.gt.3302615 · Cited by 101
Heffernan, M. J., & Dennis, J. W. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.1.85 · Cited by 101
Geisse, S., & Henke, M. (2005) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-005-2826-4 · Cited by 98
High levels of protein expression using different mammalian CMV promoters in several cell lines
Xia, W., Bringmann, P., McClary, J., Jones, P. P., Manzana, W., Zhu, Y., Wang, S., Liu, Y., Harvey, S., Madlansacay, M. R., et al. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.07.008 · Cited by 88
Tait, A. S., Brown, C. J., Galbraith, D. J., Hines, M. J., Hoare, M., Birch, J. R., & James, D. C. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20265 · Cited by 88
Dolph, P. J., Huang, J. T., & Schneider, R. J. (1990) · Journal of Virology · doi:10.1128/jvi.64.6.2669-2677.1990 · Cited by 87
Berntzen, G., Lunde, E., Flobakk, M., Andersen, J. T., Lauvrak, V., & Sandlie, I. (2005) · Journal of Immunological Methods · doi:10.1016/j.jim.2005.01.002 · Cited by 78
Adenovirus VA RNAI mediates a translational stimulation which is not restricted to the viral mRNAs.
Svensson, C., & Akusjärvi, G. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03724.x · Cited by 77
Functional Analyses of the EBNA1 Origin DNA Binding Protein of Epstein-Barr Virus
Ceccarelli, D. F. J., & Frappier, L. (2000) · Journal of Virology · doi:10.1128/jvi.74.11.4939-4948.2000 · Cited by 77
Jordan, M., Köhne, C., & Wurm, F. M. (1998) · Cytotechnology · doi:10.1023/a:1007917318181 · Cited by 75
Mechanisms of DNA entry into mammalian cells
Loyter, A., Scangos, G. A., Juricek, D. K., Keene, D. R., & Ruddle, F. H. (1982) · Experimental Cell Research · doi:10.1016/0014-4827(82)90336-6 · Cited by 74
Establishment of a Human Somatic Hybrid Cell Line for Recombinant Protein Production
Cho, M. S., Yee, H., & Chan, S. (2002) · Journal of Biomedical Science · doi:10.1007/bf02254991 · Cited by 72
Dioleoylmelittin as a Novel Serum-Insensitive Reagent for Efficient Transfection of Mammalian Cells
Legendre, J., Trzeciak, A. M., Bohrmann, B., Deuschle, U., Kitas, E. A., & Supersaxo, A. (1997) · Bioconjugate Chemistry · doi:10.1021/bc960076d · Cited by 70
Rosser, M. P., Xia, W., Hartsell, S., McCaman, M., Zhu, Y., Wang, S., Harvey, S., Bringmann, P., & Cobb, R. R. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2004.07.015 · Cited by 68
The use of engineered E1A genes to transactivate the hCMV-MIE promoter in permanent CHO cell lines
Cockett, M. I., Bebbington, C. R., & Yarranton, G. T. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.2.319 · Cited by 68
Highly Efficient, Large Volume Flow Electroporation
Li, L., Shivakumar, R., Feller, S., Allen, C., Weiss, J. M., Dzekunov, S. M., Singh, V., Holaday, J. W., Fratantoni, J. C., & Liu, L. N. (2002) · Technology in Cancer Research & Treatment · doi:10.1177/153303460200100504 · Cited by 65
Dee, K. U., Shuler, M. L., & Wood, H. A. (1997) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19970505)54:3 · Cited by 63
Serum-Free Suspension Large-Scale Transient Transfection of CHO Cells in WAVE Bioreactors
Haldankar, R., Li, D., Saremi, Z., Baikalov, C., & Deshpande, R. R. (2006) · Molecular Biotechnology · doi:10.1385/mb:34:2:191 · Cited by 61
Shi, C., Shin, Y., Hanson, J., Cass, B., Loewen, M. C., & Durocher, Y. (2005) · Biochemistry · doi:10.1021/bi051292p · Cited by 59
Self-citationRepression of simian virus 40 early transcription by viral DNA replication in human 293 cells
Lewis, E. D., & Manley, J. L. (1985) · Nature · doi:10.1038/317172a0 · Cited by 58
Epi‐CHO, an episomal expression system for recombinant protein production in CHO cells
Kunaparaju, R., Liao, M. M., & Sunstrom, N.-A. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20534 · Cited by 57
Atkinson, A., & Jack, G. W. (1973) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(73)90120-2 · Cited by 57
Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins.
Cachianes, G., Ho, C., Weber, R. F., Williams, S. R., Goeddel, D. V., & Leung, D. W. (1993) · PubMed · Cited by 56
Huang, W., & Flint, S. J. (1998) · Journal of Virology · doi:10.1128/jvi.72.1.225-235.1998 · Cited by 52
Helper activity for gene expression, a novel function of the SV40 enhancer
Graessmann, M., Menne, J., Liebler, M., Graeber, I., & Graessmann, A. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.16.6603 · Cited by 52
Kim, S., Lee, J. H., Shin, H.-S., Kang, H.-J., & Kim, Y. S. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(01)00388-1 · Cited by 50
Large scale transient expression with COS cells
Blasey, H. D., Aubry, J., Mazzei, G. J., & Bernard, A. R. (1996) · Cytotechnology · doi:10.1007/bf00767766 · Cited by 45
Versatile Expression System for Rapid and Stable Production of Recombinant Proteins
Cho, M. ‐., Yee, H., Brown, C. N., Mei, B., Mirenda, C. A., & Chan, S. (2003) · Biotechnology Progress · doi:10.1021/bp0255964 · Cited by 44
Tomiyasu, K.-I., Satoh, E., Oda, Y., Nishizaki, K., Kondo, M., Imanishi, J., & Mazda, O. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9835 · Cited by 42
Stability without a centromere
Calos, M. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4084 · Cited by 40
Large-Scale Transient Expression of Therapeutic Proteins in Mammalian Cells
Geisse, S., Jordan, M., & Wurm, F. M. (2005) · Humana Press eBooks · doi:10.1385/1-59259-922-2:087 · Cited by 39
McNeall, J., Sánchez, A., Gray, P. P., Chesterman, C. N., & Sleigh, M. J. (1989) · Gene · doi:10.1016/0378-1119(89)90010-3 · Cited by 37
Plasmid origin of replication of Epstein-Barr virus, oriP, does not limit replication in cis.
Sugden, B., & Warren, N. (1988) · PubMed · Cited by 35
Production of Lentiviral Vectors
Zufferey, R. (2002) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-56114-6_5 · Cited by 33
Epstein-Barr virus vectors for gene expression and transfer
Sclimenti, C. R., & Calos, M. P. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80032-3 · Cited by 32
SEAP expression in transiently transfected mammalian cells grown in serum-free suspension culture
Schlaeger, E., Kitas, E. A., & Dorn, A. (2003) · Cytotechnology · doi:10.1023/a:1026125016602 · Cited by 32
Long‐term replication of Epstein‐Barr virus‐derived episomal vectors in the rodent cells
Mizuguchi, H., Hosono, T., & Hayakawa, T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01450-2 · Cited by 28
Efficient transfection of DNA by mixing cells in suspension with calcium phosphate
Song, W., & Lahiri, D. K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.17.3609 · Cited by 28
InsectDirectTM System: Rapid, High-level Protein Expression and Purification from Insect Cells
Loomis, K. H., Yaeger, K. W., Batenjany, M. M., Mehler, M., Grabski, A. C., Wong, S. C., & Novy, R. E. (2005) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-005-5241-y · Cited by 28
Calfection: a novel gene transfer method for suspension cells
Lindell, J. S., Girard, P., Müller, N., Jordan, M., & Wurm, F. M. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.11.016 · Cited by 25
Nuclear proteins as gene-transfer vectors
Haberland, A., & Böttger, M. (2005) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20050063 · Cited by 24 · cited 1×
“Nuclear proteins such as histones and high-mobility group proteins can also be used as transfection reagents ( 16 ), but their variable performances and high costs associated with their production are obstacles to largescale applications.”
BackgroundCalcium phosphate transfection optimization for serum-free suspension culture
Girard, P., Porte, L., Berta, T., Jordan, M., & Wurm, F. M. (2001) · Cytotechnology · doi:10.1023/a:1013101927350 · Cited by 22
Biology of cell surface heparan sulfate proteoglycans.
Jalkanen, M. (1987) · PubMed · Cited by 22
Parham, J. H., Kost, T., & Hutchins, J. T. (2001) · Cytotechnology · doi:10.1023/a:1013131415382 · Cited by 21
Farrell, P., & Iatrou, K. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2004.03.010 · Cited by 20
Wright, J. L., Jordan, M., & Wurm, F. M. (2001) · Cytotechnology · doi:10.1023/a:1013106032341 · Cited by 18
A COS-cell-based system for rapid production and quantification of scFv::IgCκ antibody fragments
Ridder, R., Geisse, S., Kleuser, B., Kawalleck, P., & Gram, H. (1995) · Gene · doi:10.1016/0378-1119(95)00638-9 · Cited by 17
[2] Protein expression in mammalian and insect cell systems
Geisse, S., & Kocher, H. P. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)06004-8 · Cited by 17
Liposome-Mediated Transfection of Mammalian Cells
Schenborn, E. T., & Oler, J. (2003) · Humana Press eBooks · doi:10.1385/1-59259-686-x:155 · Cited by 15
A transient expression vector for recombinant protein production in Chinese hamster ovary cells
Liao, M. M., & Sunstrom, N.-A. (2005) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.1361 · Cited by 13
Tonini, T., Claudio, P. P., Giordano, A., & Romano, G. (2004) · Humana Press eBooks · doi:10.1385/1-59259-822-6:141 · Cited by 12
Non-GMP plasmid production for transient transfection in bioreactors
Schmid, G., Schlaeger, E., & Wipf, B. (2001) · Cytotechnology · doi:10.1023/a:1013148203049 · Cited by 9
Energy dependence of DNA-mediated gene transfer and expression
Orrantia, E., Li, Z.-G., & Chang, P. L. (1990) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01232458 · Cited by 9
Blasey, H. D., Hovius, R., Vogel, H., & Bernard, A. R. (1999) · Biochemical Society Transactions · doi:10.1042/bst0270956 · Cited by 5
Recombinant Protein Production by Transient Transfection of Suspension-Growing Cells
Durocher, Y., Perret, S., & Kamen, A. (2001) · Springer eBooks · doi:10.1007/978-94-015-9749-4_24 · Cited by 4
Self-citationTransient expression with COS cells on spinner scale
Blasey, H. D., & Bernard, A. R. (1994) · Elsevier eBooks · doi:10.1016/b978-0-7506-1845-8.50082-x · Cited by 4
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Intracellular Delivery by Membrane Disruption: Mechanisms, Strategies, and Concepts
Stewart, M. P., Langer, R., & Jensen, K. F. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00678 · Cited by 762
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Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296
Self-citationProduction of lentiviral vectors
Merten, O.-W., Hebben, M., & Bovolenta, C. (2016) · Molecular Therapy - Methods & Clinical Development · doi:10.1038/mtm.2016.17 · Cited by 294
O’Flaherty, R., Bergin, A., Flampouri, E., Mota, L. M., Obaidi, I., Quigley, A., Xie, Y., & Butler, M. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107552 · Cited by 277
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Tan, E., Chin, C. S. H., Lim, Z. F. S., & Ng, S. K. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.796991 · Cited by 255
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Butler, M., & Meneses‐Acosta, A. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4451-z · Cited by 216
Jäger, V., Büssow, K., Wagner, A., Weber, S., Hust, M., Frenzel, A., & Schirrmann, T. (2013) · BMC Biotechnology · doi:10.1186/1472-6750-13-52 · Cited by 209
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Hacker, D. L., de Jesús, M., & Wurm, F. M. (2009) · Biotechnology Advances · doi:10.1016/j.biotechadv.2009.05.008 · Cited by 186
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Swiech, K., Picanço-Castro, V., & Covas, D. T. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2012.04.023 · Cited by 178
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Butler, M., & Spearman, M. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.06.010 · Cited by 175
Backliwal, G., Hildinger, M., Kuettel, I., Delegrange, F., Hacker, D. L., & Wurm, F. M. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21882 · Cited by 176
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de Jesús, M., & Wurm, F. M. (2011) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2011.01.005 · Cited by 171
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Bono, N., Ponti, F., Mantovani, D., & Candiani, G. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12020183 · Cited by 162
Backliwal, G., Hildinger, M., Hasija, V., & Wurm, F. M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21596 · Cited by 156
Ansorge, S., Lanthier, S., Transfiguracion, J. C., Durocher, Y., Henry, O., & Kamen, A. (2009) · The Journal of Gene Medicine · doi:10.1002/jgm.1370 · Cited by 144
Self-citationDaramola, O., Stevenson, J., Dean, G., Hatton, D., Pettman, G., Holmes, W., & Field, R. (2014) · Biotechnology Progress · doi:10.1002/btpr.1809 · Cited by 134
Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., et al. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.09.001 · Cited by 133
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Link, N., Brunner, T. J., Dreesen, I. A. J., Stark, W. J., & Fussenegger, M. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21525 · Cited by 38
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Metadata
- Authors
- Pham, P. L., Kamen, A., & Durocher, Y.
- Affiliations
- Université de Montréal (CA)
- Biotechnology Research Institute (CA)
- Corresponding author
- Durocher, Yves
- Venue
- Molecular Biotechnology
- Published
- 2006
- Volume
- 34
- Issue
- 2
- Pages
- 225-238
- ISSN
- 1073-6085 (ISSN-L)
- OpenAlex
- W2012250005
- Cited by
- 236
- References
- 119
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 10 · 2023: 6 · 2022: 9 · 2021: 7 · 2020: 21 · 2019: 7 · 2018: 11 · 2017: 8 · 2016: 12 · 2015: 11 · 2014: 22 · 2013: 20 · 2012: 23
- FWCI
- 3.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- NPARC (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- recombinant protein expression, mammalian cell expression systems, HEK293 cells, CHO cells, calcium phosphate transfection, post-translational modification, cDNA cloning
- MeSH terms
- Animals, Biotechnology, Calcium Phosphates, Cell Line, Culture Media, Genetic Vectors, Cricetinae, Humans, Polyethyleneimine, Recombinant Proteins, Transfection
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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