Industry view on the relative importance of “clonality” of biopharmaceutical-producing cell lines
Tài liệu tham khảo
Zhu, 2012, Mammalian cell protein expression for biopharmaceutical production, Biotechnol Adv, 30, 1158, 10.1016/j.biotechadv.2011.08.022
Walsh, 2014, Biopharmceutical benchmarks, Nat Biotechnol, 32, 992, 10.1038/nbt.3040
Barnes, 2003, Stability of protein production from recombinant mammalian cells, Biotechnol Bioeng, 81, 631, 10.1002/bit.10517
Wurm, 2013, CHO Quasispecies – implications for manufacturing processes, Processes, 1, 296, 10.3390/pr1030296
Pilbrough, 2009, PLoS One, 4, 10.1371/journal.pone.0008432
Puck, 1957, The genetics of somatic mammalian cells, Adv Biol Med Phys, 5, 75, 10.1016/B978-1-4832-3111-2.50006-7
Puck, 1985, Development of the chinese hamster ovary (CHO) cell for use in somatic cell genetics, 37
Urlaub, 1980, Isolation of Chinese hamster cell mutants lacking dihydrofolate reductase activity, Proc Natl Acad Sci, 77, 4216, 10.1073/pnas.77.7.4216
Urlaub, 1983, Deletion of the diploid dihydrofolate reductase locus form cultured mammalian cells, Cell, 33, 405, 10.1016/0092-8674(83)90422-1
Wurm, 2011, First CHO genome, Nat Biotechnol, 29, 718, 10.1038/nbt.1943
Fan, 2013, The use of glutamine synthetase as a selection marker: recent advances in Chinese hamster ovary cell line generation processes, Pharm Bioprocess, 1, 487, 10.4155/pbp.13.56
Lefkovits, 1979
Mosser, 1997, Use of a dicistronic expression cassette encoding the green fluorescent protein for the screening and selection of cells expressing inducible gene products, Biotechniques, 22, 150, 10.2144/97221rr02
DeMaria, 2007, Accelerated clone selection for recombinant CHO CELLS using a FACS-based high-throughput screen, Biotechnol Prog, 23, 465, 10.1021/bp060298i
Lee, 2006, High-throughput screening of cell lines expressing monoclonal antibodies, Bioprocess Int, 4, 32
Chusainow, 2009, A study of monoclonal antibody-producing CHO cell lines: what makes a stable high producer?, Biotechnol Bioeng, 102, 1182, 10.1002/bit.22158
Kim, 2011, A mechanistic understanding of production instability in CHO cell lines expressing recombinant monoclonal antibodies, Biotechnol Bioeng, 108, 2434, 10.1002/bit.23189
Yuk, 2015
Zhu-Shimoni, 2014, Host cell protein testing by ELISAs and the use of orthogonal methods, Biotechnol Bioeng, 111, 2367, 10.1002/bit.25327
Venkat, 2015, Expression of difficult-to-remove host cell protein impurities during extended Chinese hamster ovary cell culture and their impact on continuous bioprocessing, Biotechnol Bioeng, 112, 1232, 10.1002/bit.25515
de Zafra, 2015
Yang, 2010, Detecting low level sequence variants in recombinant monoclonal antibodies, Mabs, 2, 285, 10.4161/mabs.2.3.11718
Ren, 2011, Detection and identification of a serine to arginine sequence variant in a therapeutic monoclonal antibody, J Chromatogr B Anal Technol Biomed Life Sci, 879, 2877, 10.1016/j.jchromb.2011.08.015
Guo, 2010, Mechanisms of unintended amino acid sequence changes in recombinant monoclonal antibodies expressed in Chinese hamster ovary (CHO) cells, Biotechnol Bioeng, 107, 163, 10.1002/bit.22780
Zhang, 2013, G/U and certain wobble position mismatches as possible main causes of amino acid misincorporations, Biochemistry, 52, 8165, 10.1021/bi401002c
Wong, 2005, Reproducible doxycycline-inducible transgene expressionat specific loci generated by cre-recombinase mediated cassette exchange, Nucleic Acids Res, 33, e147, 10.1093/nar/gni145
Matasci, 2011, The piggyBac transposon enhances the frequency of CHO cell line generation and yields recombinant cell lines with superior productivity and stability, Biotechnol Bioeng, 108, 2141, 10.1002/bit.23167
Spencer, 2015, Stability of single copy transgene expression in CHOK1 cells is affected by histone modifications but not by DNA methylation, J Biotechnol, 195, 15, 10.1016/j.jbiotec.2014.12.009
Balasubramanian, 2015, Rapid recombinant protein production from piggyBac transposon-mediated stable CHO cell pools, J Biotechnol, 200, 61, 10.1016/j.jbiotec.2015.03.001
