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Volumn 92, Issue 1, 2013, Pages 67-76

Polyethyleneimine-based transient gene expression processes for suspension-adapted HEK-293E and CHO-DG44 cells

Author keywords

CHO DG44; HEK 293; Mammalian cells; Orbital shaking; Polyethylenimine; Recombinant protein; Suspension culture; Transfection; Transient gene expression

Indexed keywords

DRUG CARRIER; POLYETHYLENEIMINE; RECOMBINANT PROTEIN;

EID: 84884736571     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.09.001     Document Type: Review
Times cited : (62)

References (141)
  • 1
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • DOI 10.1038/nbt1026
    • F.M. Wurm Production of recombinant protein therapeutics in cultivated mammalian cells Nat. Biotechnol. 22 2004 1393 1398 (Pubitemid 39482858)
    • (2004) Nature Biotechnology , vol.22 , Issue.11 , pp. 1393-1398
    • Wurm, F.M.1
  • 2
    • 58749101153 scopus 로고    scopus 로고
    • Reflections on more than 10 years of TGE approaches
    • S. Geisse Reflections on more than 10 years of TGE approaches Protein Expr. Purif. 64 2009 99 107
    • (2009) Protein Expr. Purif. , vol.64 , pp. 99-107
    • Geisse, S.1
  • 3
    • 77955947553 scopus 로고    scopus 로고
    • Recent advances in the production of proteins in insect and mammalian cells for structural biology
    • J.E. Nettleship, R. Assenberg, J.M. Diprose, N. Rahman-Huq, and R.J. Owens Recent advances in the production of proteins in insect and mammalian cells for structural biology J. Struct. Biol. 172 2010 55 65
    • (2010) J. Struct. Biol. , vol.172 , pp. 55-65
    • Nettleship, J.E.1    Assenberg, R.2    Diprose, J.M.3    Rahman-Huq, N.4    Owens, R.J.5
  • 5
    • 84877800939 scopus 로고    scopus 로고
    • Overexpression of membrane proteins in mammalian cells for structural studies
    • J. Andrell, and C.G. Tate Overexpression of membrane proteins in mammalian cells for structural studies Mol. Membr. Biol. 30 2013 52 63
    • (2013) Mol. Membr. Biol. , vol.30 , pp. 52-63
    • Andrell, J.1    Tate, C.G.2
  • 6
    • 84856690548 scopus 로고    scopus 로고
    • MultiBac: Expanding the research toolbox for multiprotein complexes
    • C. Bieniossek, T. Imasaki, Y. Takagi, and I. Berger MultiBac: expanding the research toolbox for multiprotein complexes Trends Biochem. Sci. 37 2012 49 57
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 49-57
    • Bieniossek, C.1    Imasaki, T.2    Takagi, Y.3    Berger, I.4
  • 7
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Y. Durocher, S. Perret, and A. Kamen High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells Nucleic Acids Res. 30 2002 E9
    • (2002) Nucleic Acids Res. , vol.30 , pp. 9
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 9
    • 13544265276 scopus 로고    scopus 로고
    • Transient production of recombinant proteins by Chinese hamster ovary cells using polyethyleneimine/DNA complexes in combination with microtubule disrupting anti-mitotic agents
    • DOI 10.1002/bit.20265
    • A.S. Tait, C.J. Brown, D.J. Galbraith, M.J. Hines, M. Hoare, J.R. Birch, and D.C. James Transient production of recombinant proteins by Chinese hamster ovary cells using polyethyleneimine/DNA complexes in combination with microtubule disrupting anti-mitotic agents Biotechnol. Bioeng. 88 2004 707 721 (Pubitemid 40775327)
    • (2004) Biotechnology and Bioengineering , vol.88 , Issue.6 , pp. 707-721
    • Tait, A.S.1    Brown, C.J.2    Galbraith, D.J.3    Hines, M.J.4    Hoare, M.5    Birch, J.R.6    James, D.C.7
  • 10
    • 33845935849 scopus 로고    scopus 로고
    • Large-scale transfection of mammalian cells for the fast production of recombinant protein
    • DOI 10.1385/MB:34:2:225, PII MB342225
    • P.L. Pham, A. Kamen, and Y. Durocher Large-scale transfection of mammalian cells for the fast production of recombinant protein Mol. Biotechnol. 34 2006 225 237 (Pubitemid 46030396)
    • (2006) Molecular Biotechnology , vol.34 , Issue.2 , pp. 225-237
    • Pham, P.L.1    Kamen, A.2    Durocher, Y.3
  • 11
    • 34147125994 scopus 로고    scopus 로고
    • Recombinant protein production by large-scale transient gene expression in mammalian cells: State of the art and future perspectives
    • DOI 10.1007/s10529-006-9297-y
    • L. Baldi, D.L. Hacker, M. Adam, and F.M. Wurm Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives Biotechnol. Lett. 29 2007 677 684 (Pubitemid 46569214)
    • (2007) Biotechnology Letters , vol.29 , Issue.5 , pp. 677-684
    • Baldi, L.1    Hacker, D.L.2    Adam, M.3    Wurm, F.M.4
  • 12
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • DOI 10.1038/nbt1036
    • I. Berger, D.J. Fitzgerald, and T.J. Richmond Baculovirus expression system for heterologous multiprotein complexes Nat. Biotechnol. 22 2004 1583 1587 (Pubitemid 40039463)
    • (2004) Nature Biotechnology , vol.22 , Issue.12 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 13
    • 22844450442 scopus 로고    scopus 로고
    • Baculovirus as versatile vectors for protein expression in insect and mammalian cells
    • DOI 10.1038/nbt1095
    • T.A. Kost, J.P. Condreay, and D.L. Jarvis Baculovirus as versatile vectors for protein expression in insect and mammalian cells Nat. Biotechnol. 23 2005 567 575 (Pubitemid 41724895)
    • (2005) Nature Biotechnology , vol.23 , Issue.5 , pp. 567-575
    • Kost, T.A.1    Condreay, J.P.2    Jarvis, D.L.3
  • 14
    • 50849109798 scopus 로고    scopus 로고
    • Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions
    • G. Backliwal, M. Hildinger, S. Chenuet, S. Wulhfard, M. De Jesus, and F.M. Wurm Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions Nucleic Acids Res. 36 2008 e96
    • (2008) Nucleic Acids Res. , vol.36 , pp. 96
    • Backliwal, G.1    Hildinger, M.2    Chenuet, S.3    Wulhfard, S.4    De Jesus, M.5    Wurm, F.M.6
  • 15
    • 0035086298 scopus 로고    scopus 로고
    • Glycoproteins from insect cells: Sialylated or not?
    • DOI 10.1515/BC.2001.023
    • I. Marchal, D.L. Jarvis, R. Cacan, and A. Verbert Glycoproteins from insect cells: sialylated or not? Biol Chem 382 2001 151 159 (Pubitemid 32243925)
    • (2001) Biological Chemistry , vol.382 , Issue.2 , pp. 151-159
    • Marchal, I.1    Jarvis, D.L.2    Cacan, R.3    Verbert, A.4
  • 17
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • P. Hossler, S.F. Khattak, and Z.J. Li Optimal and consistent protein glycosylation in mammalian cell culture Glycobiology 19 2009 936 949
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 18
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • DOI 10.1073/pnas.212519299
    • P.J. Reeves, N. Callewaert, R. Contreras, and H.G. Khorana Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line Proc. Natl. Acad. Sci. USA 99 2002 13419 13424 (Pubitemid 35215396)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 20
    • 84856866848 scopus 로고    scopus 로고
    • Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells
    • S. Chaudhary, J.E. Pak, F. Gruswitz, V. Sharma, and R.M. Stroud Overexpressing human membrane proteins in stably transfected and clonal human embryonic kidney 293S cells Nat. Protoc. 7 2012 453 466
    • (2012) Nat. Protoc. , vol.7 , pp. 453-466
    • Chaudhary, S.1    Pak, J.E.2    Gruswitz, F.3    Sharma, V.4    Stroud, R.M.5
  • 21
    • 0026657624 scopus 로고
    • Human antibody effector function
    • D.R. Burton, and J.M. Woof Human antibody effector function Adv. Immunol. 51 1992 1 84
    • (1992) Adv. Immunol. , vol.51 , pp. 1-84
    • Burton, D.R.1    Woof, J.M.2
  • 22
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • R. Jefferis Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action Trends Pharmacol. Sci. 30 2009 356 362
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 24
    • 1042264084 scopus 로고    scopus 로고
    • TubeSpin satellites: A fast track approach for process development with animal cells using shaking technology
    • DOI 10.1016/S1369-703X(03)00180-3
    • M.J. De Jesus, P. Girard, M. Bourgeois, G. Baumgartner, B. Jacko, H. Amstutz, and F.M. Wurm TubeSpin satellites: a fast track approach for process development with animal cells using shaking technology Biochem. Eng. J. 17 2004 217 223 (Pubitemid 38201458)
    • (2004) Biochemical Engineering Journal , vol.17 , Issue.3 , pp. 217-223
    • De Jesus, M.J.1    Girard, P.2    Bourgeois, M.3    Baumgartner, G.4    Jacko, B.5    Amstutz, H.6    Wurm, F.M.7
  • 26
    • 14244252530 scopus 로고    scopus 로고
    • Orbital shaker technology for the cultivation of mammalian cells in suspension
    • DOI 10.1002/bit.20358
    • N. Muller, P. Girard, D.L. Hacker, M. Jordan, and F.M. Wurm Orbital shaker technology for the cultivation of mammalian cells in suspension Biotechnol. Bioeng. 89 2005 400 406 (Pubitemid 40288900)
    • (2005) Biotechnology and Bioengineering , vol.89 , Issue.4 , pp. 400-406
    • Muller, N.1    Girard, P.2    Hacker, D.L.3    Jordan, M.4    Wurm, F.M.5
  • 27
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • DOI 10.1107/S0907444906029799
    • A.R. Aricescu, W. Lu, and E.Y. Jones A time- and cost-efficient system for high-level protein production in mammalian cells Acta Crystallogr. D Biol. Crystallogr. 62 2006 1243 1250 (Pubitemid 44526216)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.10 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 28
    • 64949176720 scopus 로고    scopus 로고
    • Production of chimeric heavy-chain antibodies
    • J. Zhang, R. MacKenzie, and Y. Durocher Production of chimeric heavy-chain antibodies Methods Mol. Biol. 525 2009 323 336
    • (2009) Methods Mol. Biol. , vol.525 , pp. 323-336
    • Zhang, J.1    Mackenzie, R.2    Durocher, Y.3
  • 29
    • 80053647240 scopus 로고    scopus 로고
    • A simplified polyethylenimine-mediated transfection process for large-scale and high-throughput applications
    • C. Raymond, R. Tom, S. Perret, P. Moussouami, D. L'Abbe, G. St-Laurent, and Y. Durocher A simplified polyethylenimine-mediated transfection process for large-scale and high-throughput applications Methods 55 2011 44 51
    • (2011) Methods , vol.55 , pp. 44-51
    • Raymond, C.1    Tom, R.2    Perret, S.3    Moussouami, P.4    L'Abbe, D.5    St-Laurent, G.6    Durocher, Y.7
  • 31
    • 24344436812 scopus 로고    scopus 로고
    • Large-scale transient expression of therapeutic proteins in mammalian cells
    • S. Geisse, M. Jordan, and F.M. Wurm Large-scale transient expression of therapeutic proteins in mammalian cells Methods Mol. Biol. 308 2005 87 98
    • (2005) Methods Mol. Biol. , vol.308 , pp. 87-98
    • Geisse, S.1    Jordan, M.2    Wurm, F.M.3
  • 32
    • 84864123068 scopus 로고    scopus 로고
    • Transient expression technologies: Past, present, and future
    • S. Geisse, and B. Voedisch Transient expression technologies: past, present, and future Methods Mol. Biol. 899 2012 203 219
    • (2012) Methods Mol. Biol. , vol.899 , pp. 203-219
    • Geisse, S.1    Voedisch, B.2
  • 33
    • 71549154680 scopus 로고    scopus 로고
    • Recombinant protein production by transient gene transfer into mammalian cells
    • S. Geisse, and C. Fux Recombinant protein production by transient gene transfer into mammalian cells Methods Enzymol. 463 2009 223 238
    • (2009) Methods Enzymol. , vol.463 , pp. 223-238
    • Geisse, S.1    Fux, C.2
  • 34
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • F.L. Graham, and A.J. van der Eb A new technique for the assay of infectivity of human adenovirus 5 DNA Virology 52 1973 456 467
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, A.J.2
  • 35
    • 0021988550 scopus 로고
    • Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells
    • DOI 10.1038/313812a0
    • J.L. Yates, N. Warren, and B. Sugden Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells Nature 313 1985 812 815 (Pubitemid 15130835)
    • (1985) Nature , vol.313 , Issue.6005 , pp. 812-815
    • Yates, J.L.1    Warren, N.2    Sugden, B.3
  • 36
    • 0021996888 scopus 로고
    • A mammalian host-vector system that regulates expression and amplification of transfected genes by temperature induction
    • D.C. Rio, S.G. Clark, and R. Tjian A mammalian host-vector system that regulates expression and amplification of transfected genes by temperature induction Science 227 1985 23 28 (Pubitemid 15156215)
    • (1985) Science , vol.227 , Issue.4682 , pp. 23-28
    • Rio, D.C.1    Clark, S.G.2    Tjian, R.3
  • 38
    • 0027237045 scopus 로고
    • Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins
    • G. Cachianes, C. Ho, R.F. Weber, S.R. Williams, D.V. Goeddel, and D.W. Leung Epstein-Barr virus-derived vectors for transient and stable expression of recombinant proteins Biotechniques 15 1993 255 259
    • (1993) Biotechniques , vol.15 , pp. 255-259
    • Cachianes, G.1    Ho, C.2    Weber, R.F.3    Williams, S.R.4    Goeddel, D.V.5    Leung, D.W.6
  • 39
    • 0035689186 scopus 로고    scopus 로고
    • Effects of pCIneo and pCEP4 expression vectors on transient and stable protein production in human and simian cell lines
    • DOI 10.1023/A:1013131415382
    • J.H. Parham, T. Kost, and J.T. Hutchins Effects of pCIneo and pCEP4 expression vectors on transient and stable protein production in human and simian cell lines Cytotechnology 35 2001 181 187 (Pubitemid 34067702)
    • (2001) Cytotechnology , vol.35 , Issue.3 , pp. 181-187
    • Parham, J.H.1    Kost, T.2    Hutchins, J.T.3
  • 40
    • 0141867826 scopus 로고    scopus 로고
    • Large-scale transient transfection of serum-free suspension-growing HEK293 EBNA1 cells: Peptone additives improve cell growth and transfection efficiency
    • DOI 10.1002/bit.10774
    • P.L. Pham, S. Perret, H.C. Doan, B. Cass, G. St-Laurent, A. Kamen, and Y. Durocher Large-scale transient transfection of serum-free suspension-growing HEK293 EBNA1 cells: peptone additives improve cell growth and transfection efficiency Biotechnol. Bioeng. 84 2003 332 342 (Pubitemid 37221535)
    • (2003) Biotechnology and Bioengineering , vol.84 , Issue.3 , pp. 332-342
    • Pham, P.L.1    Perret, S.2    Doan, H.C.3    Cass, B.4    St-Laurent, G.5    Kamen, A.6    Durocher, Y.7
  • 41
    • 33744457017 scopus 로고    scopus 로고
    • 2- adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line
    • DOI 10.1110/ps.062080006
    • P. Chelikani, P.J. Reeves, U.L. Rajbhandary, and H.G. Khorana The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line Protein Sci. 15 2006 1433 1440 (Pubitemid 43800014)
    • (2006) Protein Science , vol.15 , Issue.6 , pp. 1433-1440
    • Chelikani, P.1    Reeves, P.J.2    Rajbhandary, U.L.3    Khorana, H.G.4
  • 42
    • 70149087712 scopus 로고    scopus 로고
    • Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors
    • A. Clayton, C. Siebold, R.J. Gilbert, G.C. Sutton, K. Harlos, R.A. McIlhinney, E.Y. Jones, and A.R. Aricescu Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors J. Mol. Biol. 392 2009 1125 1132
    • (2009) J. Mol. Biol. , vol.392 , pp. 1125-1132
    • Clayton, A.1    Siebold, C.2    Gilbert, R.J.3    Sutton, G.C.4    Harlos, K.5    McIlhinney, R.A.6    Jones, E.Y.7    Aricescu, A.R.8
  • 45
  • 46
    • 84873782420 scopus 로고
    • Genetics of somatic mammalian cells. III. Long-term cultivation of euploid cells from human and animal subjects
    • T.T. Puck, S.J. Cieciura, and A. Robinson Genetics of somatic mammalian cells. III. Long-term cultivation of euploid cells from human and animal subjects J. Exp. Med. 108 1958 945 956
    • (1958) J. Exp. Med. , vol.108 , pp. 945-956
    • Puck, T.T.1    Cieciura, S.J.2    Robinson, A.3
  • 47
    • 0020574233 scopus 로고
    • Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells
    • G. Urlaub, E. Kas, A.M. Carothers, and L.A. Chasin Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells Cell 33 1983 405 412 (Pubitemid 13062492)
    • (1983) Cell , vol.33 , Issue.2 , pp. 405-412
    • Urlaub, G.1    Kas, E.2    Carothers, A.M.3    Chasin, L.A.4
  • 48
    • 0014321756 scopus 로고
    • Genetics of somatic mammalian cells, VII. Induction and isolation of nutritional mutants in Chinese hamster cells
    • F.T. Kao, and T.T. Puck Genetics of somatic mammalian cells, VII. Induction and isolation of nutritional mutants in Chinese hamster cells Proc. Natl. Acad. Sci. USA 60 1968 1275 1281
    • (1968) Proc. Natl. Acad. Sci. USA , vol.60 , pp. 1275-1281
    • Kao, F.T.1    Puck, T.T.2
  • 49
    • 0023614111 scopus 로고
    • Chinese hamster ovary cells
    • M.M. Gottesman Chinese hamster ovary cells Methods Enzymol. 151 1987 3 8
    • (1987) Methods Enzymol. , vol.151 , pp. 3-8
    • Gottesman, M.M.1
  • 50
    • 84856563804 scopus 로고    scopus 로고
    • Cell line specific control of polyethylenimine-mediated transient transfection optimized with "design of experiments" methodology
    • B.C. Thompson, C.R. Segarra, O.L. Mozley, O. Daramola, R. Field, P.R. Levison, and D.C. James Cell line specific control of polyethylenimine-mediated transient transfection optimized with "Design of experiments" methodology Biotechnol. Prog. 28 2012 179 187
    • (2012) Biotechnol. Prog. , vol.28 , pp. 179-187
    • Thompson, B.C.1    Segarra, C.R.2    Mozley, O.L.3    Daramola, O.4    Field, R.5    Levison, P.R.6    James, D.C.7
  • 51
    • 24644434888 scopus 로고    scopus 로고
    • Epi-CHO, an episomal expression system for recombinant protein production in CHO cells
    • DOI 10.1002/bit.20534
    • R. Kunaparaju, M. Liao, and N.A. Sunstrom Epi-CHO, an episomal expression system for recombinant protein production in CHO cells Biotechnol. Bioeng. 91 2005 670 677 (Pubitemid 41283859)
    • (2005) Biotechnology and Bioengineering , vol.91 , Issue.6 , pp. 670-677
    • Kunaparaju, R.1    Liao, M.2    Sunstrom, N.-A.3
  • 52
    • 79955919279 scopus 로고    scopus 로고
    • Enhanced CHO cell-based transient gene expression with the epi-CHO expression system
    • J. Codamo, T.P. Munro, B.S. Hughes, M. Song, and P.P. Gray Enhanced CHO cell-based transient gene expression with the epi-CHO expression system Mol. Biotechnol. 48 2011 109 115
    • (2011) Mol. Biotechnol. , vol.48 , pp. 109-115
    • Codamo, J.1    Munro, T.P.2    Hughes, B.S.3    Song, M.4    Gray, P.P.5
  • 53
    • 0021983926 scopus 로고
    • Membrane mutants of animal cells: Rapid identification of those with a primary defect in glycosylation
    • P. Stanley Membrane mutants of animal cells: rapid identification of those with a primary defect in glycosylation Mol. Cell. Biol. 5 1985 923 929 (Pubitemid 15110279)
    • (1985) Molecular and Cellular Biology , vol.5 , Issue.5 , pp. 923-929
    • Stanley, P.1
  • 54
    • 0022073756 scopus 로고
    • Control of carbohydrate processing: The lec1A CHO mutation results in partial loss of N-acetylglucosaminyltransferase i activity
    • P. Stanley, and W. Chaney Control of carbohydrate processing: the lec1A CHO mutation results in partial loss of N-acetylglucosaminyltransferase I activity Mol. Cell. Biol. 5 1985 1204 1211
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1204-1211
    • Stanley, P.1    Chaney, W.2
  • 59
    • 0037279457 scopus 로고    scopus 로고
    • Versatile expression system for rapid and stable production of recombinant proteins
    • DOI 10.1021/bp0255964
    • M.S. Cho, H. Yee, C. Brown, B. Mei, C. Mirenda, and S. Chan Versatile expression system for rapid and stable production of recombinant proteins Biotechnol. Prog. 19 2003 229 232 (Pubitemid 36219327)
    • (2003) Biotechnology Progress , vol.19 , Issue.1 , pp. 229-232
    • Cho, M.-S.1    Yee, H.2    Brown, C.3    Mei, B.4    Mirenda, C.5    Chan, S.6
  • 61
    • 77149175420 scopus 로고    scopus 로고
    • Disposable bioreactors: The current state-of-the-art and recommended applications in biotechnology
    • R. Eibl, S. Kaiser, R. Lombriser, and D. Eibl Disposable bioreactors: the current state-of-the-art and recommended applications in biotechnology Appl. Microbiol. Biotechnol. 86 2010 41 49
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 41-49
    • Eibl, R.1    Kaiser, S.2    Lombriser, R.3    Eibl, D.4
  • 63
    • 0032924570 scopus 로고    scopus 로고
    • Disposable bioreactor for cell culture using wave-induced agitation
    • V. Singh Disposable bioreactor for cell culture using wave-induced agitation Cytotechnology 30 1999 149 158 (Pubitemid 29212114)
    • (1999) Cytotechnology , vol.30 , Issue.1-3 , pp. 149-158
    • Singh, V.1
  • 64
    • 0036417632 scopus 로고    scopus 로고
    • Optimisation of protein expression and establishment of the Wave Bioreactor for Baculovirus/insect cell culture
    • DOI 10.1023/A:1021102015070
    • W. Weber, E. Weber, S. Geisse, and K. Memmert Optimisation of protein expression and establishment of the wave bioreactor for baculovirus/insect cell culture Cytotechnology 38 2002 77 85 (Pubitemid 35307411)
    • (2002) Cytotechnology , vol.38 , Issue.1-3 , pp. 77-85
    • Weber, W.1    Weber, E.2    Geisse, S.3    Memmert, K.4
  • 65
    • 33845936631 scopus 로고    scopus 로고
    • Serum-free suspension large-scale transient transfection of CHO cells in WAVE bioreactors
    • DOI 10.1385/MB:34:2:191, PII MB342191
    • R. Haldankar, D. Li, Z. Saremi, C. Baikalov, and R. Deshpande Serum-free suspension large-scale transient transfection of CHO cells in WAVE bioreactors Mol. Biotechnol. 34 2006 191 199 (Pubitemid 46030392)
    • (2006) Molecular Biotechnology , vol.34 , Issue.2 , pp. 191-199
    • Haldankar, R.1    Li, D.2    Saremi, Z.3    Baikalov, C.4    Deshpande, R.5
  • 67
    • 0035108790 scopus 로고    scopus 로고
    • Development of a shaking bioreactor system for animal cell cultures
    • DOI 10.1016/S1369-703X(00)00111-X, PII S1369703X0000111X
    • C. Liu, and L. Hong Development of a shaking bioreactor system for animal cell cultures Biochem. Eng. J. 7 2001 121 125 (Pubitemid 32162699)
    • (2001) Biochemical Engineering Journal , vol.7 , Issue.2 , pp. 121-125
    • Liu, C.-M.1    Hong, L.-N.2
  • 68
    • 34147112902 scopus 로고    scopus 로고
    • Scalable transient gene expression in Chinese hamster ovary cells in instrumented and non-instrumented cultivation systems
    • DOI 10.1007/s10529-006-9298-x
    • N. Muller, M. Derouazi, F. Van Tilborgh, S. Wulhfard, D.L. Hacker, M. Jordan, and F.M. Wurm Scalable transient gene expression in Chinese hamster ovary cells in instrumented and non-instrumented cultivation systems Biotechnol. Lett. 29 2007 703 711 (Pubitemid 46569215)
    • (2007) Biotechnology Letters , vol.29 , Issue.5 , pp. 703-711
    • Muller, N.1    Derouazi, M.2    Van Tilborgh, F.3    Wulhfard, S.4    Hacker, D.L.5    Jordan, M.6    Wurm, F.M.7
  • 70
    • 84861343057 scopus 로고    scopus 로고
    • Advances in shaking technologies
    • W. Klockner, and J. Büchs Advances in shaking technologies Trends Biotechnol. 30 2012 307 314
    • (2012) Trends Biotechnol. , vol.30 , pp. 307-314
    • Klockner, W.1    Büchs, J.2
  • 71
    • 79955114139 scopus 로고    scopus 로고
    • TubeSpin bioreactor 50 for the high-density cultivation of Sf-9 insect cells in suspension
    • Q. Xie, P.O. Michel, L. Baldi, D.L. Hacker, X. Zhang, and F.M. Wurm TubeSpin bioreactor 50 for the high-density cultivation of Sf-9 insect cells in suspension Biotechnol. Lett. 33 2011 897 902
    • (2011) Biotechnol. Lett. , vol.33 , pp. 897-902
    • Xie, Q.1    Michel, P.O.2    Baldi, L.3    Hacker, D.L.4    Zhang, X.5    Wurm, F.M.6
  • 72
    • 0035107955 scopus 로고    scopus 로고
    • Small-scale bioreactor system for process development and optimization
    • DOI 10.1016/S1369-703X(00)00110-8, PII S1369703X00001108
    • P. Girard, M. Jordan, M. Tsao, and F.M. Wurm Small-scale bioreactor system for process development and optimization Biochem. Eng. J. 7 2001 117 119 (Pubitemid 32162698)
    • (2001) Biochemical Engineering Journal , vol.7 , Issue.2 , pp. 117-119
    • Girard, P.1    Jordan, M.2    Tsao, M.3    Wurm, F.M.4
  • 73
    • 33846581487 scopus 로고    scopus 로고
    • Multiplexed expression and screening for recombinant protein production in mammalian cells
    • S.D. Chapple, A.M. Crofts, S.P. Shadbolt, J. McCafferty, and M.R. Dyson Multiplexed expression and screening for recombinant protein production in mammalian cells BMC Biotechnol. 6 2006 49
    • (2006) BMC Biotechnol. , vol.6 , pp. 49
    • Chapple, S.D.1    Crofts, A.M.2    Shadbolt, S.P.3    McCafferty, J.4    Dyson, M.R.5
  • 76
    • 0035328221 scopus 로고    scopus 로고
    • Evaluation of maximum to specific power consumption ratio in shaking bioreactors
    • DOI 10.1252/jcej.34.647, Special Issue - Symposium on Mixing
    • J. Büchs, and B. Zoels Evaluation of maximum to specific power consumption ratio in shaking bioreactors J. Chem. Eng. Jpn. 34 2001 647 653 (Pubitemid 32704382)
    • (2001) Journal of Chemical Engineering of Japan , vol.34 , Issue.5 , pp. 647-653
    • Buchs, J.1    Zoels, B.2
  • 78
    • 84856368988 scopus 로고    scopus 로고
    • K(L)a as a predictor for successful probe-independent mammalian cell bioprocesses in orbitally shaken bioreactors
    • S. Tissot, P.O. Michel, D.L. Hacker, L. Baldi, M. De Jesus, and F.M. Wurm K(L)a as a predictor for successful probe-independent mammalian cell bioprocesses in orbitally shaken bioreactors N. Biotechnol. 29 2012 387 394
    • (2012) N. Biotechnol. , vol.29 , pp. 387-394
    • Tissot, S.1    Michel, P.O.2    Hacker, D.L.3    Baldi, L.4    De Jesus, M.5    Wurm, F.M.6
  • 79
    • 42049084801 scopus 로고    scopus 로고
    • Mild hypothermia improves transient gene expression yields several fold in Chinese hamster ovary cells
    • DOI 10.1021/bp070286c
    • S. Wulhfard, S. Tissot, S. Bouchet, J. Cevey, M. De Jesus, D.L. Hacker, and F.M. Wurm Mild hypothermia improves transient gene expression yields several fold in Chinese hamster ovary cells Biotechnol. Prog. 24 2008 458 465 (Pubitemid 351520363)
    • (2008) Biotechnology Progress , vol.24 , Issue.2 , pp. 458-465
    • Wulhfard, S.1    Tissot, S.2    Bouchet, S.3    Cevey, J.4    De Jesus, M.5    Hacker, D.L.6    Wurm, F.M.7
  • 80
    • 13544257263 scopus 로고    scopus 로고
    • Transient gene expression in suspension HEK-293 cells: Application to large-scale protein production
    • DOI 10.1021/bp049830x
    • L. Baldi, N. Muller, S. Picasso, R. Jacquet, P. Girard, H.P. Thanh, E. Derow, and F.M. Wurm Transient gene expression in suspension HEK-293 cells: application to large-scale protein production Biotechnol. Prog. 21 2005 148 153 (Pubitemid 40218483)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 148-153
    • Baldi, L.1    Muller, N.2    Picasso, S.3    Jacquet, R.4    Girard, P.5    Huy, P.T.6    Derow, E.7    Wurm, F.M.8
  • 81
    • 13544259722 scopus 로고    scopus 로고
    • On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells
    • DOI 10.1021/bp049780w
    • S. Schlatter, S.H. Stansfield, D.M. Dinnis, A.J. Racher, J.R. Birch, and D.C. James On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells Biotechnol. Prog. 21 2005 122 133 (Pubitemid 40218480)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 122-133
    • Schlatter, S.1    Stansfield, S.H.2    Dinnis, D.M.3    Racher, A.J.4    Birch, J.R.5    James, D.C.6
  • 82
    • 34247230228 scopus 로고    scopus 로고
    • Transient gene expression levels from multigene expression vectors
    • DOI 10.1021/bp060225z
    • M.F. Underhill, C.M. Smales, L.H. Naylor, J.R. Birch, and D.C. James Transient gene expression levels from multigene expression vectors Biotechnol. Prog. 23 2007 435 443 (Pubitemid 46626319)
    • (2007) Biotechnology Progress , vol.23 , Issue.2 , pp. 435-443
    • Underhill, M.F.1    Smales, C.M.2    Naylor, L.H.3    Birch, J.R.4    James, D.C.5
  • 83
    • 22744444388 scopus 로고    scopus 로고
    • Stable antibody expression at therapeutic levels using the 2A peptide
    • DOI 10.1038/nbt1087
    • J. Fang, J.J. Qian, S. Yi, T.C. Harding, G.H. Tu, M. VanRoey, and K. Jooss Stable antibody expression at therapeutic levels using the 2A peptide Nat. Biotechnol. 23 2005 584 590 (Pubitemid 41724897)
    • (2005) Nature Biotechnology , vol.23 , Issue.5 , pp. 584-590
    • Fang, J.1    Qian, J.-J.2    Yi, S.3    Harding, T.C.4    Tu, G.H.5    VanRoey, M.6    Jooss, K.7
  • 84
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation
    • DOI 10.1093/nar/24.4.596
    • M. Jordan, A. Schallhorn, and F.M. Wurm Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation Nucleic Acids Res. 24 1996 596 601 (Pubitemid 26085833)
    • (1996) Nucleic Acids Research , vol.24 , Issue.4 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 85
    • 0035922883 scopus 로고    scopus 로고
    • Transient gene expression: Recombinant protein production with suspension-adapted HEK293-EBNA cells
    • DOI 10.1002/bit.1179
    • P. Meissner, H. Pick, A. Kulangara, P. Chatellard, K. Friedrich, and F.M. Wurm Transient gene expression: recombinant protein production with suspension-adapted HEK293-EBNA cells Biotechnol. Bioeng. 75 2001 197 203 (Pubitemid 32937290)
    • (2001) Biotechnology and Bioengineering , vol.75 , Issue.2 , pp. 197-203
    • Meissner, P.1    Pick, H.2    Kulangara, A.3    Chatellard, P.4    Friedrich, K.5    Wurm, F.M.6
  • 87
    • 38449121649 scopus 로고    scopus 로고
    • High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI
    • DOI 10.1002/bit.21596
    • G. Backliwal, M. Hildinger, V. Hasija, and F.M. Wurm High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI Biotechnol. Bioeng. 99 2008 721 727 (Pubitemid 351158270)
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.3 , pp. 721-727
    • Backliwal, G.1    Hildinger, M.2    Hasija, V.3    Wurm, F.M.4
  • 88
    • 84860613890 scopus 로고    scopus 로고
    • Poly(ethyleneimine)-mediated large-scale transient gene expression: Influence of molecular weight, polydispersity and N-propionyl groups
    • Z. Kadlecova, S. Nallet, D.L. Hacker, L. Baldi, H.A. Klok, and F.M. Wurm Poly(ethyleneimine)-mediated large-scale transient gene expression: influence of molecular weight, polydispersity and N-propionyl groups Macromol. Biosci. 12 2012 628 636
    • (2012) Macromol. Biosci. , vol.12 , pp. 628-636
    • Kadlecova, Z.1    Nallet, S.2    Hacker, D.L.3    Baldi, L.4    Klok, H.A.5    Wurm, F.M.6
  • 89
    • 79955536348 scopus 로고    scopus 로고
    • A simple high-yielding process for transient gene expression in CHO cells
    • Y. Rajendra, D. Kiseljak, L. Baldi, D.L. Hacker, and F.M. Wurm A simple high-yielding process for transient gene expression in CHO cells J. Biotechnol. 153 2011 22 26
    • (2011) J. Biotechnol. , vol.153 , pp. 22-26
    • Rajendra, Y.1    Kiseljak, D.2    Baldi, L.3    Hacker, D.L.4    Wurm, F.M.5
  • 90
    • 84864321651 scopus 로고    scopus 로고
    • Role of non-specific DNA in reducing coding DNA requirement for transient gene expression with CHO and HEK-293E cells
    • Y. Rajendra, D. Kiseljak, S. Manoli, L. Baldi, D.L. Hacker, and F.M. Wurm Role of non-specific DNA in reducing coding DNA requirement for transient gene expression with CHO and HEK-293E cells Biotechnol. Bioeng. 109 2012 2271 2278
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 2271-2278
    • Rajendra, Y.1    Kiseljak, D.2    Manoli, S.3    Baldi, L.4    Hacker, D.L.5    Wurm, F.M.6
  • 91
    • 84858008748 scopus 로고    scopus 로고
    • Reduced glutamine concentration improves protein production in growth-arrested CHO-DG44 and HEK-293E cells
    • Y. Rajendra, D. Kiseljak, L. Baldi, D.L. Hacker, and F.M. Wurm Reduced glutamine concentration improves protein production in growth-arrested CHO-DG44 and HEK-293E cells Biotechnol. Lett. 34 2012 619 626
    • (2012) Biotechnol. Lett. , vol.34 , pp. 619-626
    • Rajendra, Y.1    Kiseljak, D.2    Baldi, L.3    Hacker, D.L.4    Wurm, F.M.5
  • 92
    • 50049130165 scopus 로고    scopus 로고
    • Valproic acid: A viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures
    • G. Backliwal, M. Hildinger, I. Kuettel, F. Delegrange, D.L. Hacker, and F.M. Wurm Valproic acid: a viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures Biotechnol. Bioeng. 101 2008 182 189
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 182-189
    • Backliwal, G.1    Hildinger, M.2    Kuettel, I.3    Delegrange, F.4    Hacker, D.L.5    Wurm, F.M.6
  • 94
    • 0037144082 scopus 로고    scopus 로고
    • Balancing GFP reporter plasmid quantity in large-scale transient transfections for recombinant anti-human rhesus-D IgG1 synthesis
    • DOI 10.1002/bit.10309
    • H.M. Pick, P. Meissner, A.K. Preuss, P. Tromba, H. Vogel, and F.M. Wurm Balancing GFP reporter plasmid quantity in large-scale transient transfections for recombinant anti-human Rhesus-D IgG1 synthesis Biotechnol. Bioeng. 79 2002 595 601 (Pubitemid 34966457)
    • (2002) Biotechnology and Bioengineering , vol.79 , Issue.6 , pp. 595-601
    • Pick, H.M.1    Meissner, P.2    Preuss, A.K.3    Tromba, P.4    Vogel, H.5    Wurm, F.M.6
  • 95
    • 33745038944 scopus 로고    scopus 로고
    • Control of culture environment for improved polyethylenimine-mediated transient production of recombinant monoclonal antibodies by CHO cells
    • DOI 10.1021/bp050339v
    • D.J. Galbraith, A.S. Tait, A.J. Racher, J.R. Birch, and D.C. James Control of culture environment for improved polyethylenimine-mediated transient production of recombinant monoclonal antibodies by CHO cells Biotechnol. Prog. 22 2006 753 762 (Pubitemid 43877444)
    • (2006) Biotechnology Progress , vol.22 , Issue.3 , pp. 753-762
    • Galbraith, D.J.1    Tait, A.S.2    Racher, A.J.3    Birch, J.R.4    James, D.C.5
  • 96
    • 70350075814 scopus 로고    scopus 로고
    • Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells
    • S. Nallet, M. Amacker, N. Westerfeld, L. Baldi, I. Konig, D.L. Hacker, C. Zaborosch, R. Zurbriggen, and F.M. Wurm Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells Vaccine 27 2009 6415 6419
    • (2009) Vaccine , vol.27 , pp. 6415-6419
    • Nallet, S.1    Amacker, M.2    Westerfeld, N.3    Baldi, L.4    Konig, I.5    Hacker, D.L.6    Zaborosch, C.7    Zurbriggen, R.8    Wurm, F.M.9
  • 97
    • 33846049519 scopus 로고    scopus 로고
    • Limiting factors governing protein expression following polyethylenimine-mediated gene transfer in HEK293-EBNA1 cells
    • DOI 10.1016/j.jbiotec.2006.10.014, PII S0168165606008984
    • E. Carpentier, S. Paris, A.A. Kamen, and Y. Durocher Limiting factors governing protein expression following polyethylenimine-mediated gene transfer in HEK293-EBNA1 cells J. Biotechnol. 128 2007 268 280 (Pubitemid 46074201)
    • (2007) Journal of Biotechnology , vol.128 , Issue.2 , pp. 268-280
    • Carpentier, E.1    Paris, S.2    Kamen, A.A.3    Durocher, Y.4
  • 98
    • 28544450037 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant G-protein-coupled receptor, Saccharomyces cerevisiae Ste2p, transiently expressed in HEK293 EBNA1 cells
    • DOI 10.1021/bi051292p
    • C. Shi, Y.O. Shin, J. Hanson, B. Cass, M.C. Loewen, and Y. Durocher Purification and characterization of a recombinant G-protein-coupled receptor, Saccharomyces cerevisiae Ste2p, transiently expressed in HEK293 EBNA1 cells Biochemistry (Mosc) 44 2005 15705 15714 (Pubitemid 41746901)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15705-15714
    • Shi, C.1    Shin, Y.-O.2    Hanson, J.3    Cass, B.4    Loewen, M.C.5    Durocher, Y.6
  • 99
    • 2942733360 scopus 로고    scopus 로고
    • Enhancement of the antagonistic potency of transforming growth factor-β receptor extracellular domains by coiled coil-induced homo- and heterodimerization
    • DOI 10.1074/jbc.M400655200
    • G. De Crescenzo, P.L. Pham, Y. Durocher, H. Chao, and M.D. O'Connor-McCourt Enhancement of the antagonistic potency of transforming growth factor-beta receptor extracellular domains by coiled coil-induced homo- and heterodimerization J. Biol. Chem. 279 2004 26013 26018 (Pubitemid 38798743)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26013-26018
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    Chao, H.4    O'Connor-McCourt, M.D.5
  • 101
  • 106
    • 56549095636 scopus 로고    scopus 로고
    • The bioactivity and receptor affinity of recombinant tagged EGF designed for tissue engineering applications is defined by the nature and position of the tags
    • C. Boucher, G. St-Laurent, M. Loignon, M. Jolicoeur, G. De Crescenzo, and Y. Durocher The bioactivity and receptor affinity of recombinant tagged EGF designed for tissue engineering applications is defined by the nature and position of the tags Tissue Eng. Part A 14 2008 2069 2077
    • (2008) Tissue Eng. Part A , vol.14 , pp. 2069-2077
    • Boucher, C.1    St-Laurent, G.2    Loignon, M.3    Jolicoeur, M.4    De Crescenzo, G.5    Durocher, Y.6
  • 107
    • 80053399155 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein 7 exhibits tumor suppressive and vessel stabilization properties in U87MG and T98G glioblastoma cell lines
    • A. Pen, Y. Durocher, J. Slinn, M. Rukhlova, C. Charlebois, D.B. Stanimirovic, and M.J. Moreno Insulin-like growth factor binding protein 7 exhibits tumor suppressive and vessel stabilization properties in U87MG and T98G glioblastoma cell lines Cancer Biol. Ther. 12 2011 634 646
    • (2011) Cancer Biol. Ther. , vol.12 , pp. 634-646
    • Pen, A.1    Durocher, Y.2    Slinn, J.3    Rukhlova, M.4    Charlebois, C.5    Stanimirovic, D.B.6    Moreno, M.J.7
  • 109
    • 77950972617 scopus 로고    scopus 로고
    • Epidermal growth factor and perlecan fragments produced by apoptotic endothelial cells co-ordinately activate ERK1/2-dependent antiapoptotic pathways in mesenchymal stem cells
    • M. Soulez, I. Sirois, N. Brassard, M.A. Raymond, F. Nicodeme, N. Noiseux, Y. Durocher, A.V. Pshezhetsky, and M.J. Hebert Epidermal growth factor and perlecan fragments produced by apoptotic endothelial cells co-ordinately activate ERK1/2-dependent antiapoptotic pathways in mesenchymal stem cells Stem Cells 28 2010 810 820
    • (2010) Stem Cells , vol.28 , pp. 810-820
    • Soulez, M.1    Sirois, I.2    Brassard, N.3    Raymond, M.A.4    Nicodeme, F.5    Noiseux, N.6    Durocher, Y.7    Pshezhetsky, A.V.8    Hebert, M.J.9
  • 113
    • 84865263603 scopus 로고    scopus 로고
    • The human CST complex is a terminator of telomerase activity
    • L.Y. Chen, S. Redon, and J. Lingner The human CST complex is a terminator of telomerase activity Nature 488 2012 540 544
    • (2012) Nature , vol.488 , pp. 540-544
    • Chen, L.Y.1    Redon, S.2    Lingner, J.3
  • 118
    • 84934438795 scopus 로고    scopus 로고
    • Expressing full-length functional PfEMP1 proteins in the HEK293 expression system
    • A. Srivastava, Y. Durocher, and B. Gamain Expressing full-length functional PfEMP1 proteins in the HEK293 expression system Methods Mol. Biol. 923 2013 307 319
    • (2013) Methods Mol. Biol. , vol.923 , pp. 307-319
    • Srivastava, A.1    Durocher, Y.2    Gamain, B.3
  • 120
    • 37549052183 scopus 로고    scopus 로고
    • High-density transient gene expression in suspension-adapted 293 EBNA1 cells
    • X. Sun, H.C. Hia, P.E. Goh, and M.G. Yap High-density transient gene expression in suspension-adapted 293 EBNA1 cells Biotechnol. Bioeng. 99 2008 108 116
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 108-116
    • Sun, X.1    Hia, H.C.2    Goh, P.E.3    Yap, M.G.4
  • 121
    • 79151472882 scopus 로고    scopus 로고
    • Expression and purification of full-length mouse CARM1 from transiently transfected HEK293T cells using HaloTag technology
    • R.S. Chumanov, P.A. Kuhn, W. Xu, and R.R. Burgess Expression and purification of full-length mouse CARM1 from transiently transfected HEK293T cells using HaloTag technology Protein Expr. Purif. 76 2011 145 153
    • (2011) Protein Expr. Purif. , vol.76 , pp. 145-153
    • Chumanov, R.S.1    Kuhn, P.A.2    Xu, W.3    Burgess, R.R.4
  • 122
    • 84880413630 scopus 로고    scopus 로고
    • Multi-host expression system for recombinant production of challenging proteins
    • S. Meyer, C. Lorenz, B. Baser, M. Wordehoff, V. Jager, and J. van den Heuvel Multi-host expression system for recombinant production of challenging proteins PLoS ONE 8 2013 e68674
    • (2013) PLoS ONE , vol.8 , pp. 68674
    • Meyer, S.1    Lorenz, C.2    Baser, B.3    Wordehoff, M.4    Jager, V.5    Van Den Heuvel, J.6
  • 123
    • 33644545723 scopus 로고    scopus 로고
    • Molecular analysis of receptor protein tyrosine phosphatase μ-mediated cell adhesion
    • DOI 10.1038/sj.emboj.7600974, PII 7600974
    • A.R. Aricescu, W.C. Hon, C. Siebold, W. Lu, P.A. van der Merwe, and E.Y. Jones Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion EMBO J. 25 2006 701 712 (Pubitemid 43292433)
    • (2006) EMBO Journal , vol.25 , Issue.4 , pp. 701-712
    • Aricescu, A.R.1    Hon, W.-C.2    Siebold, C.3    Lu, W.4    Van Der Merwe, P.A.5    Jones, E.Y.6
  • 127
    • 33745899357 scopus 로고    scopus 로고
    • The Crystal Structure of ORF-9b, a Lipid Binding Protein from the SARS Coronavirus
    • DOI 10.1016/j.str.2006.05.012, PII S0969212606002516
    • C. Meier, A.R. Aricescu, R. Assenberg, R.T. Aplin, R.J. Gilbert, J.M. Grimes, and D.I. Stuart The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus Structure 14 2006 1157 1165 (Pubitemid 44041056)
    • (2006) Structure , vol.14 , Issue.7 , pp. 1157-1165
    • Meier, C.1    Aricescu, A.R.2    Assenberg, R.3    Aplin, R.T.4    Gilbert, R.J.C.5    Grimes, J.M.6    Stuart, D.I.7
  • 131
  • 139
    • 72449162211 scopus 로고    scopus 로고
    • Development of a scalable process for high-yield lentiviral vector production by transient transfection of HEK293 suspension cultures
    • S. Ansorge, S. Lanthier, J. Transfiguracion, Y. Durocher, O. Henry, and A. Kamen Development of a scalable process for high-yield lentiviral vector production by transient transfection of HEK293 suspension cultures J. Gene Med. 11 2009 868 876
    • (2009) J. Gene Med. , vol.11 , pp. 868-876
    • Ansorge, S.1    Lanthier, S.2    Transfiguracion, J.3    Durocher, Y.4    Henry, O.5    Kamen, A.6
  • 140
    • 33646543920 scopus 로고    scopus 로고
    • Scalable production of adeno-associated virus type 2 vectors via suspension transfection
    • J.Y. Park, B.P. Lim, K. Lee, Y.G. Kim, and E.C. Jo Scalable production of adeno-associated virus type 2 vectors via suspension transfection Biotechnol. Bioeng. 94 2006 416 430
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 416-430
    • Park, J.Y.1    Lim, B.P.2    Lee, K.3    Kim, Y.G.4    Jo, E.C.5
  • 141
    • 34848876973 scopus 로고    scopus 로고
    • High-titer, serum-free production of adeno-associated virus vectors by polyethyleneimine-mediated plasmid transfection in mammalian suspension cells
    • DOI 10.1007/s10529-007-9441-3
    • M. Hildinger, L. Baldi, M. Stettler, and F.M. Wurm High-titer, serum-free production of adeno-associated virus vectors by polyethyleneimine-mediated plasmid transfection in mammalian suspension cells Biotechnol. Lett. 29 2007 1713 1721 (Pubitemid 47493534)
    • (2007) Biotechnology Letters , vol.29 , Issue.11 , pp. 1713-1721
    • Hildinger, M.1    Baldi, L.2    Stettler, M.3    Wurm, F.M.4


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