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Volumn 8, Issue 7, 2013, Pages

Multi-Host Expression System for Recombinant Production of Challenging Proteins

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; FLUORESCENT PROTEIN; RECOMBINANT PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

EID: 84880413630     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0068674     Document Type: Article
Times cited : (29)

References (28)
  • 2
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher Y, Perret S, Kamen A, (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic acids research 30: E9.
    • (2002) Nucleic Acids Research , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 3
    • 0029160083 scopus 로고
    • A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine
    • Boussif O, Lezoualc'h F, Zanta MA, Mergny MD, Scherman D, et al. (1995) A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine. Proc Natl Acad Sci U S A 92: 7297-7301.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7297-7301
    • Boussif, O.1    Lezoualc'h, F.2    Zanta, M.A.3    Mergny, M.D.4    Scherman, D.5
  • 4
    • 34250170457 scopus 로고    scopus 로고
    • Optimization of 25 kDa linear polyethylenimine for efficient gene delivery
    • Huh SH, Do HJ, Lim HY, Kim DK, Choi SJ, et al. (2007) Optimization of 25 kDa linear polyethylenimine for efficient gene delivery. Biologicals 35: 165-171.
    • (2007) Biologicals , vol.35 , pp. 165-171
    • Huh, S.H.1    Do, H.J.2    Lim, H.Y.3    Kim, D.K.4    Choi, S.J.5
  • 5
    • 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
    • Backliwal G, Hildinger M, Chenuet S, Wulhfard S, De Jesus M, et al. (2008) 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 research 36: e96.
    • (2008) Nucleic Acids Research , vol.36
    • Backliwal, G.1    Hildinger, M.2    Chenuet, S.3    Wulhfard, S.4    De Jesus, M.5
  • 6
    • 79955597234 scopus 로고    scopus 로고
    • Design of Experiment in CHO and HEK transient transfection condition optimization
    • Bollin F, Dechavanne V, Chevalet L, (2011) Design of Experiment in CHO and HEK transient transfection condition optimization. Protein expression and purification 78: 61-68.
    • (2011) Protein Expression and Purification , vol.78 , pp. 61-68
    • Bollin, F.1    Dechavanne, V.2    Chevalet, L.3
  • 8
    • 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
    • Rajendra Y, Kiseljak D, Manoli S, Baldi L, Hacker DL, et al. (2012) Role of non-specific DNA in reducing coding DNA requirement for transient gene expression with CHO and HEK-293E cells. Biotechnology and Bioengineering 109: 2271-2278.
    • (2012) Biotechnology and Bioengineering , vol.109 , pp. 2271-2278
    • Rajendra, Y.1    Kiseljak, D.2    Manoli, S.3    Baldi, L.4    Hacker, D.L.5
  • 9
    • 0023136672 scopus 로고
    • Differences between rodent and human cell lines in the amount of integrated DNA after transfection
    • Hoeijmakers JH, Odijk H, Westerveld A, (1987) Differences between rodent and human cell lines in the amount of integrated DNA after transfection. Experimental cell research 169: 111-119.
    • (1987) Experimental Cell Research , vol.169 , pp. 111-119
    • Hoeijmakers, J.H.1    Odijk, H.2    Westerveld, A.3
  • 10
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley P, (1989) Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Molecular and cellular biology 9: 377-383.
    • (1989) Molecular and Cellular Biology , vol.9 , pp. 377-383
    • Stanley, P.1
  • 11
    • 0027456631 scopus 로고
    • Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2
    • Davis SJ, Puklavec MJ, Ashford DA, Harlos K, Jones EY, et al. (1993) Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2. Protein engineering 6: 229-232.
    • (1993) Protein Engineering , vol.6 , pp. 229-232
    • Davis, S.J.1    Puklavec, M.J.2    Ashford, D.A.3    Harlos, K.4    Jones, E.Y.5
  • 12
    • 0028109636 scopus 로고
    • Use of mutated FLP recognition target (FRT) sites for the exchange of expression cassettes at defined chromosomal loci
    • Schlake T, Bode J, (1994) Use of mutated FLP recognition target (FRT) sites for the exchange of expression cassettes at defined chromosomal loci. Biochemistry 33: 12746-12751.
    • (1994) Biochemistry , vol.33 , pp. 12746-12751
    • Schlake, T.1    Bode, J.2
  • 13
    • 83055168492 scopus 로고    scopus 로고
    • Streamlining Homogeneous Glycoprotein Production for Biophysical and Structural Applications by Targeted Cell Line Development
    • Wilke S, Groebe L, Maffenbeier V, Jäger V, Gossen M, et al. (2011) Streamlining Homogeneous Glycoprotein Production for Biophysical and Structural Applications by Targeted Cell Line Development. PLoS ONE 6: e27829.
    • (2011) PLoS ONE , vol.6
    • Wilke, S.1    Groebe, L.2    Maffenbeier, V.3    Jäger, V.4    Gossen, M.5
  • 14
    • 0002443557 scopus 로고    scopus 로고
    • pTriEx-1 Multisystem Vector for protein expression in E. Coli, mammalian, and insect cells
    • Novy R, Yeager K, Monsma S, (1999) pTriEx-1 Multisystem Vector for protein expression in E. Coli, mammalian, and insect cells. Innovations 10: 5.
    • (1999) Innovations , vol.10 , pp. 5
    • Novy, R.1    Yeager, K.2    Monsma, S.3
  • 15
    • 34247846396 scopus 로고    scopus 로고
    • A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
    • Berrow NS, Alderton D, Sainsbury S, Nettleship J, Assenberg R, et al. (2007) A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Research 35: e45-e45.
    • (2007) Nucleic Acids Research , vol.35
    • Berrow, N.S.1    Alderton, D.2    Sainsbury, S.3    Nettleship, J.4    Assenberg, R.5
  • 16
    • 0027209690 scopus 로고
    • Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli
    • Luckow VA, Lee SC, Barry GF, Olins PO, (1993) Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J Virol 67: 4566-4579.
    • (1993) J Virol , vol.67 , pp. 4566-4579
    • Luckow, V.A.1    Lee, S.C.2    Barry, G.F.3    Olins, P.O.4
  • 17
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger I, Fitzgerald DJ, Richmond TJ, (2004) Baculovirus expression system for heterologous multiprotein complexes. Nature biotechnology 22: 1583-1587.
    • (2004) Nature Biotechnology , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 19
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, et al. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nature biotechnology 22: 1567-1572.
    • (2004) Nature Biotechnology , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5
  • 20
    • 43549115973 scopus 로고    scopus 로고
    • Human antibody RNase fusion protein targeting CD30+ lymphomas
    • Menzel C, Schirrmann T, Konthur Z, Jostock T, Dubel S, (2008) Human antibody RNase fusion protein targeting CD30+ lymphomas. Blood 111: 3830-3837.
    • (2008) Blood , vol.111 , pp. 3830-3837
    • Menzel, C.1    Schirrmann, T.2    Konthur, Z.3    Jostock, T.4    Dubel, S.5
  • 21
    • 44849110490 scopus 로고    scopus 로고
    • Application of hybrid LRR technique to protein crystallization
    • Jin MS, Lee JO, (2008) Application of hybrid LRR technique to protein crystallization. BMB reports 41: 353-357.
    • (2008) BMB Reports , vol.41 , pp. 353-357
    • Jin, M.S.1    Lee, J.O.2
  • 22
    • 0007443728 scopus 로고
    • Strategies to increase the efficiency of membrane aerated and perfused animal cell bioreactors by an improved medium perfusion
    • In: Sasaki R, Ikura R, editors, Dordrecht: Kluwer Academic Publishers
    • Blasey HD, Jäger V (1991) Strategies to increase the efficiency of membrane aerated and perfused animal cell bioreactors by an improved medium perfusion. In: Sasaki R, Ikura R, editors. Animal cell culture and production of biologicals. Dordrecht: Kluwer Academic Publishers. 61-73.
    • (1991) Animal cell culture and production of biologicals , pp. 61-73
    • Blasey, H.D.1    Jäger, V.2
  • 24
    • 34249072595 scopus 로고    scopus 로고
    • TIPS: Titerless Infected-Cells Preservation and Scale-Up
    • Wasilko DJ, Lee SE, (2006) TIPS: Titerless Infected-Cells Preservation and Scale-Up. BioProcessing Journal 5: 29-32.
    • (2006) BioProcessing Journal , vol.5 , pp. 29-32
    • Wasilko, D.J.1    Lee, S.E.2
  • 25
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, et al. (2007) Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 130: 1071-1082.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5
  • 26
    • 71749118913 scopus 로고    scopus 로고
    • Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer
    • Kang JY, Nan X, Jin MS, Youn SJ, Ryu YH, et al. (2009) Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity 31: 873-884.
    • (2009) Immunity , vol.31 , pp. 873-884
    • Kang, J.Y.1    Nan, X.2    Jin, M.S.3    Youn, S.J.4    Ryu, Y.H.5
  • 27
    • 0035166478 scopus 로고    scopus 로고
    • Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments
    • Liang M, Dubel S, Li D, Queitsch I, Li W, et al. (2001) Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments. Journal of immunological methods 247: 119-130.
    • (2001) Journal of Immunological Methods , vol.247 , pp. 119-130
    • Liang, M.1    Dubel, S.2    Li, D.3    Queitsch, I.4    Li, W.5
  • 28
    • 84880439898 scopus 로고    scopus 로고
    • Production of Recombinant Human IgG Antibodies in the Baculovirus Expression System
    • In: Kontermann R, Dübel S, editors, Berlin, Heidelberg: Springer Berlin Heidelberg
    • Liang M, Dübel S (2010) Production of Recombinant Human IgG Antibodies in the Baculovirus Expression System. In: Kontermann R, Dübel S, editors. Antibody Engineering. Berlin, Heidelberg: Springer Berlin Heidelberg. 453-470.
    • (2010) Antibody Engineering , pp. 453-470
    • Liang, M.1    Dübel, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.