Improved production of recombinant human antithrombin III in Chinese hamster ovary cells by ATF4 overexpression
Abstract
To improve the production of recombinant human antithrombin III (AT‐III) in Chinese hamster ovary (CHO) cells, the genes encoding transcription factors, ATF4 (activating transcription factor 4) and XBP‐1s (the spliced form of X‐box binding protein 1), which were involved in the mammalian unfolded protein response (UPR), were cloned from CHO‐K1 cells. Overexpression of ATF4 significantly enhanced the production of recombinant AT‐III in CHO 13D‐35D cells. The specific rate of AT‐III production in the ATF4‐overexpressed CHO 13D‐35D cells reached approximately 23 pg/cell/day. After 144 h of incubation, the AT‐III concentration in the culture supernatant was twofold greater compared to that observed with parental CHO 13D‐35D cells. In contrast, ectopic expression of XBP‐1s failed to enhance the production of recombinant AT‐III in CHO 13D‐35D cells. RT‐PCR analysis revealed that high levels of XBP‐1s mRNA were present in the CHO cells, regardless of ectopic expression of XBP‐1s. Our results indicate that overexpression of the UPR transcription factor ATF4 is a promising means for improving the production of secreted protein pharmaceuticals in CHO cells. Biotechnol. Bioeng. 2008;100: 317–324. © 2007 Wiley Periodicals, Inc.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
ATF4 has been overexpressed to restore translation and enhance levels of anti-thrombin III produced in CHO cells.
“ATF4, another critical transcription factor in the UPR system, has been overexpressed to restore translation and enhance levels of anti-thrombin III produced in CHO cells (Ohya et al., 2008).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Ohya et al., 2008
Cites
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054 · see citing works
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310 · see citing works
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,281 · see citing works
Haze, K., Yoshida, H., Yanagi, H., Yura, T., & Mori, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.11.3787 · Cited by 2,073 · see citing works
Lee, A., Iwakoshi, N. N., & Glimcher, L. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7448-7459.2003 · Cited by 2,041 · see citing works
Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H. E., Stevens, J. L., & Ron, D. (1998) · Genes & Development · doi:10.1101/gad.12.7.982 · Cited by 1,996 · see citing works
McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,895 · see citing works
Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α
Novoa, I., Zeng, H., Harding, H. P., & Ron, D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1011 · Cited by 1,392 · see citing works
Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum
Mori, K. (2000) · Cell · doi:10.1016/s0092-8674(00)80855-7 · Cited by 918 · see citing works
Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
Urlaub, G., & Chasin, L. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.4216 · Cited by 876 · see citing works
Translational control in the endoplasmic reticulum stress response
Ron, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci16784 · Cited by 778 · see citing works
Translational control in the endoplasmic reticulum stress response
Ron, D. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216784 · Cited by 728 · see citing works
A Time-Dependent Phase Shift in the Mammalian Unfolded Protein Response
Yoshida, H., Matsui, T., Hosokawa, N., Kaufman, R. J., Nagata, K., & Mori, K. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00022-4 · Cited by 675 · see citing works
Activating transcription factor 4
Ameri, K., & Harris, A. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.01.020 · Cited by 557 · see citing works
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
A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation
Hosokawa, N., Wada, I., Hasegawa, K., Yorihuzi, T., Tremblay, L. O., Herscovics, A. A., & Nagata, K. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve084 · Cited by 467 · see citing works
Ma, Y., & Hendershot, L. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301107200 · Cited by 458 · see citing works
DuRose, J. B., Tam, A. B., & Niwa, M. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-01-0055 · Cited by 219 · see citing works
Tigges, M., & Fussenegger, M. (2006) · Metabolic Engineering · doi:10.1016/j.ymben.2006.01.006 · Cited by 178 · see citing works
Effects of lactate concentration on hybridoma culture in lactate‐controlled fed‐batch operation
Ōmasa, T., Higashiyama, K., Shioya, S., & Suga, K. (1992) · Biotechnology and Bioengineering · doi:10.1002/bit.260390511 · Cited by 151 · see citing works
Dinnis, D. M., Stansfield, S. H., Schlatter, S., Smales, C. M., Alete, D. E., Birch, J. R., Racher, A. J., Marshall, C. T., Nielsen, L. K., & James, D. C. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20899 · Cited by 138 · see citing works
Smales, C. M., Dinnis, D. M., Stansfield, S. H., Alete, D., Sage, E. A., Birch, J. R., Racher, A. J., Marshall, C. T., & James, D. C. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20272 · Cited by 119 · see citing works
Kuwae, S., Ohda, T., Tamashima, H., Miki, H., & Kobayashi, K. (2005) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.100.502 · Cited by 50 · see citing works
Self-citationSchröder, M., & Friedl, P. (1997) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19970320)53:6 · Cited by 50 · see citing works
Schwartz, B., Vicart, P., Delouis, C., & Paulin, D. (1991) · Biology of the Cell · doi:10.1016/0248-4900(91)90003-6 · Cited by 45 · see citing works
Quantitative measurement of events in the mammalian unfolded protein response
Shang, J. (2005) · Methods · doi:10.1016/j.ymeth.2004.10.012 · Cited by 45 · see citing works
Gene amplification in mammalian cells: strategies for protein production
Kellems, R. E. (1991) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(91)90042-4 · Cited by 29 · see citing works
Schmelzer, A. E., deZengotita, V. M., & Miller, W. M. (2000) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(20000120)67:2 · Cited by 26 · see citing works
Mochizuki, S., Miyano, K., Kondo, M., Hirose, M., Masaki, A., & Ohi, H. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.03.010 · Cited by 12 · see citing works
Production of Human Antithrombin-III in a Serum-free Culture of CHO Cells
Yamauchi, T., Asakura, E., Amatsuji, Y., Uno, S., Furuta, R., Tujikawa, M., & Tanabe, T. (1992) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.56.600 · Cited by 8 · see citing works
Flagged first, then by citations
1 of the 31 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
The art of CHO cell engineering: A comprehensive retrospect and future perspectives
Fischer, S., Handrick, R., & Otte, K. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.10.015 · Cited by 314 · 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
Recent advances in technology supporting biopharmaceutical production from mammalian cells
Butler, M., & Meneses‐Acosta, A. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4451-z · Cited by 211 · 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
Engineering mammalian cells in bioprocessing – current achievements and future perspectives
Lim, Y., Wong, N. S. C., Lee, Y. Y., Ku, S. C. Y., Wong, D. C. F., & Yap, M. G. S. (2010) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20090363 · Cited by 134 · see citing works
Davy, A. M., Kildegaard, H. F., & Andersen, M. R. (2017) · Cell Systems · doi:10.1016/j.cels.2017.02.010 · Cited by 133 · see citing works
Reflections on more than 10 years of TGE approaches
Geisse (2009) · doi:10.1016/j.pep.2008.10.017 · Cited by 117 · see citing works
Engineering CHO cell growth and recombinant protein productivity by overexpression of miR-7
Barron, N., Kumar, N., Sanchez, N., Doolan, P., Clarke, C., Meleady, P., O'Sullivan, F., & Clynes, M. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.12.005 · Cited by 110 · see citing works
Delic, M., Göngrich, R., Mattanovich, D., & Gasser, B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5844 · Cited by 108 · see citing works
Oxidative stress‐alleviating strategies to improve recombinant protein production in CHO cells
Chevallier, V., Andersen, M. R., & Malphettes, L. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.27247 · Cited by 105 · see citing works
Park, J. H., Noh, S. M., Woo, J. R., Kim, J. W., & Lee, G. M. (2016) · Biotechnology Journal · doi:10.1002/biot.201500327 · Cited by 81 · see citing works
MicroRNAs as targets for engineering of CHO cell factories
Müller, D., Katinger, H. W. D., & Grillari, J. (2008) · Trends in biotechnology · doi:10.1016/j.tibtech.2008.03.010 · Cited by 74 · see citing works
Bright Fluorescent Nanotags from Bottlebrush Polymers with DNA-Tipped Bristles
Fouz, M. F., Mukumoto, K., Averick, S. E., Molinar‐Inglis, O., McCartney, B. M., Matyjaszewski, K. A., Armitage, B. A., & Das, S. R. (2015) · ACS Central Science · doi:10.1021/acscentsci.5b00259 · Cited by 68 · see citing works
Hussain, H., Maldonado‐Agurto, R., & Dickson, A. J. (2014) · Biotechnology Letters · doi:10.1007/s10529-014-1537-y · Cited by 59 · 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
Dynamics of unfolded protein response in recombinant CHO cells
Segar, K. P., & Mehra, S. (2014) · Cytotechnology · doi:10.1007/s10616-013-9678-8 · Cited by 58 · see citing works
Omasa, T., Takami, T., Ohya, T., Kiyama, E., Hayashi, T., Nishii, H., Miki, H., Kobayashi, K., Honda, K., & Ohtake, H. (2008) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.106.568 · Cited by 57 · see citing works
Self-citationMalm, M., Kuo, C., Barzadd, M. M., Mebrahtu, A., Wistbacka, N., Razavi, R., Volk, A.-L., Lundqvist, M., Kotol, D., Tegel, H., et al. (2022) · Metabolic Engineering · doi:10.1016/j.ymben.2022.03.009 · Cited by 52 · see citing works
Nishimiya, D., Mano, T., Miyadai, K., Yoshida, H., & Takahashi, T. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4365-9 · Cited by 46 · see citing works
Burnouf, T. P. R. (2010) · Vox Sanguinis · doi:10.1111/j.1423-0410.2010.01384.x · Cited by 45 · see citing works
Majumdar, S., Desai, R., Hans, A. K., Dandekar, P. P., & Jain, R. D. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01060-6 · Cited by 43 · see citing works
Fomina‐Yadlin, D., Gosink, J. J., McCoy, R. E., Follstad, B. D., Morris, A. E., Russell, C. B., & McGrew, J. T. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.25155 · Cited by 43 · see citing works
Berger, A., Fourn, V. L., Masternak, J., Regamey, A., Bodenmann, I., Girod, P., & Mermod, N. (2020) · Biotechnology and Bioengineering · doi:10.1002/bit.27274 · Cited by 41 · see citing works
Engineering of chaperone systems and of the unfolded protein response
Khan, S. U., & Schröder, M. (2008) · Cytotechnology · doi:10.1007/s10616-008-9157-9 · Cited by 40 · see citing works
Golabgir, A., Gutierrez, J. M., Hefzi, H., Li, S., Palsson, B. Ø., Herwig, C., & Lewis, N. E. (2016) · Biotechnology Advances · doi:10.1016/j.biotechadv.2016.02.011 · Cited by 40 · see citing works
Improved antibody production in Chinese hamster ovary cells by ATF4 overexpression
Haredy, A. M., Nishizawa, A., Honda, K., Ohya, T., Ohtake, H., & Ōmasa, T. (2013) · Cytotechnology · doi:10.1007/s10616-013-9631-x · Cited by 38 · see citing works
Self-citationKaneyoshi, K., Kuroda, K., Uchiyama, K., Onitsuka, M., Yamano, N., Koga, Y., & Ōmasa, T. (2019) · Cytotechnology · doi:10.1007/s10616-018-0286-5 · Cited by 38 · see citing works
Jenkins, N., Meleady, P., Tyther, R., & Murphy, L. (2009) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20080258 · Cited by 36 · see citing works
Non‐invasive UPR monitoring system and its applications in CHO production cultures
Du, Z., Treiber, D., McCoy, R. E., Miller, A. K., Han, M., He, F., Domnitz, S. B., Heath, C. A., & Reddy, P. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.24877 · Cited by 36 · see citing works
Pieper, L. A., Strotbek, M., Wenger, T., Olayioye, M. A., & Haußer, A. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26263 · Cited by 35 · see citing works
Cell line development for biomanufacturing processes: recent advances and an outlook
Le, H., Vishwanathan, N., Jacob, N. M., Gadgil, M., & Hu, W. (2015) · Biotechnology Letters · doi:10.1007/s10529-015-1843-z · Cited by 34 · see citing works
Bacterial artificial chromosome library for genome‐wide analysis of Chinese hamster ovary cells
Ōmasa, T., Cao, Y., Park, J. Y., Takagi, Y., Kimura, S., Yano, H., Honda, K., Asakawa, S., Shimizu, N., & Ohtake, H. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22463 · Cited by 33 · see citing works
Self-citationKu, S. C. Y., Toh, P. C., Lee, Y. Y., Chusainow, J., Yap, M. G. S., & Chao, S. (2009) · Biotechnology Progress · doi:10.1002/btpr.322 · Cited by 32 · see citing works
Engineering a mammalian super producer
Dietmair, S., Nielsen, L. K., & Timmins, N. E. (2011) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.2576 · Cited by 31 · see citing works
Cell factory engineering: Challenges and opportunities for synthetic biology applications
Bachhav, B., de Rossi, J., Llanos, C. P., & Segatori, L. (2023) · Biotechnology and Bioengineering · doi:10.1002/bit.28365 · Cited by 30 · see citing works
Becker, E., Florin, L., Pfizenmaier, K., & Kaufmann, H. (2009) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2009.11.018 · Cited by 30 · see citing works
Proteins improving recombinant antibody production in mammalian cells
Nishimiya, D. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5427-3 · Cited by 26 · see citing works
Ōmasa, T., Furuichi, K., Iemura, T., Katakura, Y., Kishimoto, M., & Suga, K. (2009) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-009-0351-8 · Cited by 26 · see citing works
Schoellhorn, M., Fischer, S., Wagner, A., Handrick, R., & Otte, K. (2017) · Biotechnology Progress · doi:10.1002/btpr.2475 · Cited by 26 · see citing works
Using Molecular Markers to Characterize Productivity in Chinese Hamster Ovary Cell Lines
Edros, R. Z., McDonnell, S., & Al‐Rubeai, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075935 · Cited by 25 · see citing works
Rajendra, Y., Hougland, M. D., Schmitt, M. G., & Barnard, G. C. (2015) · Biotechnology Letters · doi:10.1007/s10529-015-1938-6 · Cited by 24 · see citing works
Trehalose suppresses antibody aggregation during the culture of Chinese hamster ovary cells
Onitsuka, M., Tatsuzawa, M., Asano, R., Kumagai, I., Shirai, A., Maseda, H., & Ōmasa, T. (2013) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2013.10.022 · Cited by 24 · see citing works
Torres, M., Hussain, H., & Dickson, A. J. (2022) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2022.2047004 · Cited by 23 · see citing works
Transcription factor engineering in CHO cells for recombinant protein production
Gutiérrez-González, M., Latorre, Y., Zúñiga, R., Aguillón, J. C., Molina, M. C., & Altamirano, C. (2019) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2019.1605496 · Cited by 23 · see citing works
Synthetic biology approaches for dynamic CHO cell engineering
Donaldson, J., Kleinjan, D., & Rosser, S. J. (2022) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2022.102806 · Cited by 20 · see citing works
Rapid construction of transgene-amplified CHO cell lines by cell cycle checkpoint engineering
Lee, K. H., Onitsuka, M., Honda, K., Ohtake, H., & Ōmasa, T. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-4923-9 · Cited by 22 · see citing works
Self-citationŌmasa, T., Tanaka, R., Doi, T., Ando, M., Kitamoto, Y., Honda, K., Kishimoto, M., & Ohtake, H. (2008) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.106.168 · Cited by 22 · see citing works
Self-citationShin, S., Kim, S. H., Lee, J. S., & Lee, G. M. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.1c00113 · Cited by 20 · see citing works
The effect of the unfolded protein response on the production of recombinant proteins in plants
Thomas, D. R., & Walmsley, A. M. (2014) · Plant Cell Reports · doi:10.1007/s00299-014-1680-x · Cited by 20 · see citing works
Maldonado‐Agurto, R., & Dickson, A. J. (2018) · Biotechnology Journal · doi:10.1002/biot.201700429 · Cited by 18 · see citing works
Analysis of intracellular IgG secretion in Chinese hamster ovary cells to improve IgG production
Kaneyoshi, K., Uchiyama, K., Onitsuka, M., Yamano, N., Koga, Y., & Ōmasa, T. (2018) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2018.06.018 · Cited by 18 · see citing works
Alves, C. S., Gilbert, A., Dalvi, S., Germain, B. S., Xie, W., Estes, S. D., Kshirsagar, R., & Ryll, T. (2015) · Biotechnology Progress · doi:10.1002/btpr.2091 · Cited by 17 · 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
Samy, A., Kaneyoshi, K., & Ōmasa, T. (2020) · Biotechnology Journal · doi:10.1002/biot.201900352 · Cited by 17 · see citing works
Ashe, M., & Bill, R. M. (2011) · Biotechnology Journal · doi:10.1002/biot.201000333 · Cited by 15 · see citing works
Chandrawanshi, V., Kulkarni, R., Prabhu, A., & Mehra, S. (2020) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2020.02.008 · Cited by 15 · see citing works
Onitsuka, M., Kinoshita, Y., Nishizawa, A., Tsutsui, T., & Ōmasa, T. (2017) · Cytotechnology · doi:10.1007/s10616-017-0170-8 · Cited by 13 · see citing works
Alves, C. S., & Dobrowsky, T. M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6972-2_1 · Cited by 13 · see citing works
Deciphering molecular drivers of lactate metabolic shift in mammalian cell cultures
Torres, M., Hawke, E., Hoare, R., Scholey, R., Pybus, L. P., Young, A., Hayes, A., & Dickson, A. J. (2024) · Metabolic Engineering · doi:10.1016/j.ymben.2024.12.001 · Cited by 13 · see citing works
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 · see citing works
Mallu, M. R., Vemula, S. R., & Ronda, S. R. (2016) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2016.06.002 · Cited by 11 · see citing works
Kaneyoshi, K., Yamano, N., Koga, Y., Uchiyama, K., & Ōmasa, T. (2019) · Cytotechnology · doi:10.1007/s10616-018-0276-7 · Cited by 11 · see citing works
Gerlach, J. Q., Sharma, S., Leister, K. J., & Joshi, L. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_2 · Cited by 10 · see citing works
Engineering Mammalian Cells for Recombinant Monoclonal Antibody Production
Davies, S. L., & James, D. C. (2009) · Cell engineering · doi:10.1007/978-90-481-2245-5_8 · Cited by 9 · see citing works
CHO Cell Engineering for Improved Process Performance and Product Quality
Fischer, S., & Otte, K. (2019) · doi:10.1002/9783527811410.ch9 · Cited by 9 · see citing works
Tsunoda, Y., Yamano, N., Koga, Y., & Ōmasa, T. (2024) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2024.05.003 · Cited by 8 · see citing works
Badsha, M. B., Kurata, H., Onitsuka, M., Oga, T., & Ōmasa, T. (2016) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2015.12.013 · Cited by 8 · see citing works
Cell Engineering for Increasing Production of Recombinant Proteins in Mammalian Cells
Zhang, X., Shen, Y. C., Guo, Z., Wang, Y., Wang, X., & Wang, T. (2025) · BioDrugs · doi:10.1007/s40259-025-00753-x · Cited by 7 · see citing works
Overexpression of Serpinb1 in Chinese hamster ovary cells increases recombinant IgG productivity
Lin, N., Brooks, J. K., Sealover, N. R., George, H. J., & Kayser, K. J. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.10.040 · Cited by 7 · see citing works
Application of Genetic Engineering in Biotherapeutics Development
Schweickert, P. G., & Cheng, Z. (2019) · Journal of Pharmaceutical Innovation · doi:10.1007/s12247-019-09411-6 · Cited by 7 · see citing works
Rives, D., Richbourg, T., Gurtler, S., Martone, J., & Blenner, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157189 · Cited by 6 · see citing works
Kato, T., Yoshizuka, K., & Park, E. Y. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.03.011 · Cited by 6 · see citing works
Analysis of an artificially selected GS‐NS0 variant with increased resistance to apoptosis
Browne, S. M., & Al‐Rubeai, M. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22994 · Cited by 6 · see citing works
Wu, M. Y. M., Rocamora, F., Robinson, C. M., Shin, S., Maurya, S. R., Toth, E. A., Fuerst, T. R., & Lewis, N. E. (2025) · Biotechnology Journal · doi:10.1002/biot.70112 · Cited by 5 · see citing works
Cell Engineering for Therapeutic Protein Production
Baek, E. H., Kim, C. L., Park, J. H., & Lee, G. M. (2014) · Cell engineering · doi:10.1007/978-3-319-10320-4_18 · Cited by 5 · see citing works
Secretory leakage of IgG1 aggregates from recombinant Chinese hamster ovary cells
Onitsuka, M., Kadoya, Y., & Ōmasa, T. (2018) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2018.11.015 · Cited by 5 · see citing works
Ryan, D., Sideri, C., Henry, M. A., Selvaprakash, K., Efeoğlu, E., & Meleady, P. (2025) · Biotechnology and Bioengineering · doi:10.1002/bit.70081 · Cited by 4 · see citing works
Insights on biomarkers from Chinese hamster ovary ‘omics’ studies
Kyriakopoulos, S., & Kontoravdi, C. (2014) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.14.45 · Cited by 3 · see citing works
Jin, F., Kretschmer, P. J., Harkins, R. N., & Hermiston, T. W. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22536 · Cited by 3 · see citing works
Advanced Bioprocess Engineering: Fed‐Batch and Perfusion Processes
Mehra, S., Chandrawanshi, V., & Segar, K. P. (2017) · doi:10.1002/9783527800599.ch14 · Cited by 3 · see citing works
Geng, S., Mi, C., Wang, C., Li, J., Sun, Q., Li, W., & Wang, T. (2025) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2025160 · Cited by 2 · see citing works
Zhao, Q., Zhang, H., Han, M., Abiti, J., Dong, Y. J., Wang, J., Lu, J., Wang, W., Zhang, X., Geng, S., et al. (2025) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2025.12.001 · Cited by 1 · see citing works
Tsunoda, Y., Somatani, A., Yoshiike, C., Mitoma, S., Yamano, N., & Ōmasa, T. (2026) · New Biotechnology · doi:10.1016/j.nbt.2026.05.010 · Cited by 1 · see citing works
Engineering Protein Folding and Secretion in Eukaryotic Cell Factories
McLeod, J., & James, D. C. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-088504-9.00047-7 · Cited by 1 · see citing works
ATF4 over-expression increased IgG1productivity in Chinese hamster ovary cells
Haredy, A. M., Nishizawa, A., Honda, K., Ohya, T., Ohtake, H., & Ōmasa, T. (2011) · BMC Proceedings · doi:10.1186/1753-6561-5-s8-o11 · Cited by 1 · see citing works
Self-citationMicroRNAs as Engineering Targets: Pathway Manipulation to Impact Bioprocess Phenotypes
Shiloach, J., Druz, A., & Betenbaugh, M. J. (2012) · Springer eBooks · doi:10.1007/978-94-007-5128-6_5 · 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
Cell line development for and characterization of mono- and bivalent antibody derivatives
Berger, V. (2013) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-2171
Becker, E. (2008) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1784
Application of Unfolded Protein Response for Production of Biologics
Ōmasa, T. (2016) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.15-00292-6
New Expression Systems for GPCRs
Gialama, D., Kolisis, F. N., & Σκρέτας, Γ. (2018) · doi:10.1002/9781119378341.ch2
Engineering Protein Folding and Secretion in Eukaryotic Cell Factories
McLeod, J., & James, D. C. (2011) · Elsevier eBooks · doi:10.1016/b978-0-444-64046-8.00026-4
- Authors
- Ohya, T., Hayashi, T., Kiyama, E., Nishii, H., Miki, H., Kobayashi, K., Honda, K., Omasa, T., & Ohtake, H.
- Affiliations
- Tanabe Pharma Corporation (Japan) (JP)
- The University of Osaka (JP)
- Corresponding author
- Ohya, Tomoshi
- Venue
- Biotechnology and Bioengineering
- Publisher
- Wiley
- Published
- 2007-12-13
- Volume
- 100
- Issue
- 2
- Pages
- 317-324
- ISSN
- 0006-3592 (ISSN-L)
- 1097-0290
- OpenAlex
- W2102232272
- Cited by
- 96
- References
- 31
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 7 · 2018: 4 · 2017: 8 · 2016: 4 · 2015: 6 · 2014: 7 · 2013: 9 · 2012: 5
- FWCI
- 2.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biotechnology and Bioengineering (publishedVersion)
- PubMed (publishedVersion)
- 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 › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- ATF4, XBP1, unfolded protein response, CHO cells, transcription factor overexpression, therapeutic proteins
- MeSH terms
- Regulatory Factor X Transcription Factors, X-Box Binding Protein 1, Animals, Antithrombin III, Cricetulus, DNA-Binding Proteins, Cricetinae, Humans, Nuclear Proteins, Recombinant Proteins, Transcription Factors, Protein Engineering, CHO Cells, Genetic Enhancement, Activating Transcription Factor 4
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review