메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Using Molecular Markers to Characterize Productivity in Chinese Hamster Ovary Cell Lines

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MESSENGER RNA; MOLECULAR MARKER; MONOCLONAL ANTIBODY; POLYPEPTIDE; RNA;

EID: 84885824826     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075935     Document Type: Article
Times cited : (20)

References (62)
  • 1
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm FM, (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nature Biotechnology 22: 1393-1398.
    • (2004) Nature Biotechnology , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 2
    • 0043208919 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2003
    • Walsh G, (2003) Biopharmaceutical benchmarks 2003. Nat Biotechnol 21: 865-870.
    • (2003) Nat Biotechnol , vol.21 , pp. 865-870
    • Walsh, G.1
  • 3
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh G, (2006) Biopharmaceutical benchmarks 2006. Nat Biotechnol 24: 769-776.
    • (2006) Nat Biotechnol , vol.24 , pp. 769-776
    • Walsh, G.1
  • 5
    • 0344200036 scopus 로고    scopus 로고
    • Cytogenetic analysis of chimeric antibody-producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure
    • Kim S, Lee GM, (1999) Cytogenetic analysis of chimeric antibody-producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure. Biotechnology and Bioengineering 64: 741-749.
    • (1999) Biotechnology and Bioengineering , vol.64 , pp. 741-749
    • Kim, S.1    Lee, G.M.2
  • 6
    • 0035128469 scopus 로고    scopus 로고
    • Key Determinants in the Occurrence of Clonal Variation in Humanized Antibody Expression of CHO Cells during Dihydrofolate Reductase Mediated Gene Amplification
    • Kim NS, Byun TH, Lee GM, (2001) Key Determinants in the Occurrence of Clonal Variation in Humanized Antibody Expression of CHO Cells during Dihydrofolate Reductase Mediated Gene Amplification. Biotechnology Progress 17: 69-75.
    • (2001) Biotechnology Progress , vol.17 , pp. 69-75
    • Kim, N.S.1    Byun, T.H.2    Lee, G.M.3
  • 7
    • 33745045191 scopus 로고    scopus 로고
    • Limitations to the Development of Humanized Antibody Producing Chinese Hamster Ovary Cells Using Glutamine Synthetase-Mediated Gene Amplification
    • Jun SC, Kim MS, Hong HJ, Lee GM, (2006) Limitations to the Development of Humanized Antibody Producing Chinese Hamster Ovary Cells Using Glutamine Synthetase-Mediated Gene Amplification. Biotechnology Progress 22: 770-780.
    • (2006) Biotechnology Progress , vol.22 , pp. 770-780
    • Jun, S.C.1    Kim, M.S.2    Hong, H.J.3    Lee, G.M.4
  • 8
    • 78349303475 scopus 로고    scopus 로고
    • DNA methylation contributes to loss in productivity of monoclonal antibody-producing CHO cell lines
    • Yang Y, Mariati, Chusainow J, Yap MG, (2010) DNA methylation contributes to loss in productivity of monoclonal antibody-producing CHO cell lines. J Biotechnol 147: 180-185.
    • (2010) J Biotechnol , vol.147 , pp. 180-185
    • Yang, Y.1    Mariati2    Chusainow, J.3    Yap, M.G.4
  • 9
    • 60549102844 scopus 로고    scopus 로고
    • A study of monoclonal antibody-producing CHO cell lines: What makes a stable high producer?
    • Chusainow J, Yang YS, Yeo JH, Toh PC, Asvadi P, et al. (2009) A study of monoclonal antibody-producing CHO cell lines: What makes a stable high producer? Biotechnology and Bioengineering 102: 1182-1196.
    • (2009) Biotechnology and Bioengineering , vol.102 , pp. 1182-1196
    • Chusainow, J.1    Yang, Y.S.2    Yeo, J.H.3    Toh, P.C.4    Asvadi, P.5
  • 12
    • 33745221421 scopus 로고    scopus 로고
    • Phenotypic variation during cloning procedures: Analysis of the growth behavior of clonal cell lines
    • Barnes LM, Moy N, Dickson AJ, (2006) Phenotypic variation during cloning procedures: Analysis of the growth behavior of clonal cell lines. Biotechnology and Bioengineering 94: 530-537.
    • (2006) Biotechnology and Bioengineering , vol.94 , pp. 530-537
    • Barnes, L.M.1    Moy, N.2    Dickson, A.J.3
  • 13
    • 33344455402 scopus 로고    scopus 로고
    • Correlation of Heavy and Light Chain mRNA Copy Numbers to Antibody Productivity in Mouse Myeloma Production Cell Lines
    • Dorai H, Csirke B, Scallon B, Ganguly S, (2006) Correlation of Heavy and Light Chain mRNA Copy Numbers to Antibody Productivity in Mouse Myeloma Production Cell Lines. Hybridoma 25: 1-9.
    • (2006) Hybridoma , vol.25 , pp. 1-9
    • Dorai, H.1    Csirke, B.2    Scallon, B.3    Ganguly, S.4
  • 14
    • 0033586947 scopus 로고    scopus 로고
    • Relationship between recombinant activated protein C secretion rates and mRNA levels in baby hamster kidney cells
    • Fann CH, Guarna MM, Kilburn DG, Piret JM, (1999) Relationship between recombinant activated protein C secretion rates and mRNA levels in baby hamster kidney cells. Biotechnology and Bioengineering 63: 464-472.
    • (1999) Biotechnology and Bioengineering , vol.63 , pp. 464-472
    • Fann, C.H.1    Guarna, M.M.2    Kilburn, D.G.3    Piret, J.M.4
  • 15
    • 79956064271 scopus 로고    scopus 로고
    • Chemostat-based transcriptional analysis of growth rate change and BCL-2 over-expression in NS0 cells
    • Krampe B, Fagan A, Gaora PÓ, Al-Rubeai M, (2011) Chemostat-based transcriptional analysis of growth rate change and BCL-2 over-expression in NS0 cells. Biotechnology and Bioengineering 108: 1603-1615.
    • (2011) Biotechnology and Bioengineering , vol.108 , pp. 1603-1615
    • Krampe, B.1    Fagan, A.2    Gaora, P.3    Al-Rubeai, M.4
  • 16
    • 58149214617 scopus 로고    scopus 로고
    • Detailed understanding of enhanced specific antibody productivity in NS0 myeloma cells
    • Khoo SH, Al-Rubeai M, (2009) Detailed understanding of enhanced specific antibody productivity in NS0 myeloma cells. Biotechnology and Bioengineering 102: 188-199.
    • (2009) Biotechnology and Bioengineering , vol.102 , pp. 188-199
    • Khoo, S.H.1    Al-Rubeai, M.2
  • 18
    • 20544446100 scopus 로고    scopus 로고
    • A detailed understanding of the enhanced hypothermic productivity of interferon-gamma by Chinese-hamster ovary cells
    • Fox SR, Tan HK, Tan MC, Wong SC, Yap MG, et al. (2005) A detailed understanding of the enhanced hypothermic productivity of interferon-gamma by Chinese-hamster ovary cells. Biotechnol Appl Biochem 41: 255-264.
    • (2005) Biotechnol Appl Biochem , vol.41 , pp. 255-264
    • Fox, S.R.1    Tan, H.K.2    Tan, M.C.3    Wong, S.C.4    Yap, M.G.5
  • 19
    • 0009668445 scopus 로고    scopus 로고
    • Hyperosmotic pressure enhances immunoglobulin transcription rates and secretion rates of KR12H-2 transfectoma
    • Lee MS, Lee GM, (2000) Hyperosmotic pressure enhances immunoglobulin transcription rates and secretion rates of KR12H-2 transfectoma. Biotechnology and Bioengineering 68: 260-268.
    • (2000) Biotechnology and Bioengineering , vol.68 , pp. 260-268
    • Lee, M.S.1    Lee, G.M.2
  • 20
    • 60549105996 scopus 로고    scopus 로고
    • A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies
    • Lee CJ, Seth G, Tsukuda J, Hamilton RW, (2009) A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies. Biotechnology and Bioengineering 102: 1107-1118.
    • (2009) Biotechnology and Bioengineering , vol.102 , pp. 1107-1118
    • Lee, C.J.1    Seth, G.2    Tsukuda, J.3    Hamilton, R.W.4
  • 21
    • 8844219682 scopus 로고    scopus 로고
    • Comparative proteomic analysis of GS-NS0 murine myeloma cell lines with varying recombinant monoclonal antibody production rate
    • Smales CM, Dinnis DM, Stansfield SH, Alete D, Sage EA, et al. (2004) Comparative proteomic analysis of GS-NS0 murine myeloma cell lines with varying recombinant monoclonal antibody production rate. Biotechnology and Bioengineering 88: 474-488.
    • (2004) Biotechnology and Bioengineering , vol.88 , pp. 474-488
    • Smales, C.M.1    Dinnis, D.M.2    Stansfield, S.H.3    Alete, D.4    Sage, E.A.5
  • 22
    • 0036353205 scopus 로고    scopus 로고
    • Kinetic model of BiP- and PDI-mediated protein folding and assembly
    • Gonzalez R, Andrews BA, Asenjo JA, (2002) Kinetic model of BiP- and PDI-mediated protein folding and assembly. J Theor Biol 214: 529-537.
    • (2002) J Theor Biol , vol.214 , pp. 529-537
    • Gonzalez, R.1    Andrews, B.A.2    Asenjo, J.A.3
  • 23
    • 0025789619 scopus 로고
    • Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA
    • Lenny N, Green M, (1991) Regulation of endoplasmic reticulum stress proteins in COS cells transfected with immunoglobulin mu heavy chain cDNA. Journal of Biological Chemistry 266: 20532-20537.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 20532-20537
    • Lenny, N.1    Green, M.2
  • 24
    • 44449161504 scopus 로고    scopus 로고
    • Improved production of recombinant human antithrombin III in Chinese hamster ovary cells by ATF4 overexpression
    • Ohya T, Hayashi T, Kiyama E, Nishii H, Miki H, et al. (2008) Improved production of recombinant human antithrombin III in Chinese hamster ovary cells by ATF4 overexpression. Biotechnol Bioeng 100: 317-324.
    • (2008) Biotechnol Bioeng , vol.100 , pp. 317-324
    • Ohya, T.1    Hayashi, T.2    Kiyama, E.3    Nishii, H.4    Miki, H.5
  • 25
    • 3142658576 scopus 로고    scopus 로고
    • XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation
    • Shaffer AL, Shapiro-Shelef M, Iwakoshi NN, Lee AH, Qian SB, et al. (2004) XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21: 81-93.
    • (2004) Immunity , vol.21 , pp. 81-93
    • Shaffer, A.L.1    Shapiro-Shelef, M.2    Iwakoshi, N.N.3    Lee, A.H.4    Qian, S.B.5
  • 26
    • 33646078130 scopus 로고    scopus 로고
    • Xbp1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells
    • Tigges M, Fussenegger M, (2006) Xbp1-based engineering of secretory capacity enhances the productivity of Chinese hamster ovary cells. Metab Eng 8: 264-272.
    • (2006) Metab Eng , vol.8 , pp. 264-272
    • Tigges, M.1    Fussenegger, M.2
  • 27
    • 77950461287 scopus 로고    scopus 로고
    • Evaluation of a combinatorial cell engineering approach to overcome apoptotic effects in XBP-1 (s) expressing cells
    • Becker E, Florin L, Pfizenmaier K, Kaufmann H, (2010) Evaluation of a combinatorial cell engineering approach to overcome apoptotic effects in XBP-1 (s) expressing cells. Journal of Biotechnology 146: 198-206.
    • (2010) Journal of Biotechnology , vol.146 , pp. 198-206
    • Becker, E.1    Florin, L.2    Pfizenmaier, K.3    Kaufmann, H.4
  • 28
    • 44149115663 scopus 로고    scopus 로고
    • An XBP-1 dependent bottle-neck in production of IgG subtype antibodies in chemically defined serum-free Chinese hamster ovary (CHO) fed-batch processes
    • Becker E, Florin L, Pfizenmaier K, Kaufmann H, (2008) An XBP-1 dependent bottle-neck in production of IgG subtype antibodies in chemically defined serum-free Chinese hamster ovary (CHO) fed-batch processes. Journal of Biotechnology 135: 217-223.
    • (2008) Journal of Biotechnology , vol.135 , pp. 217-223
    • Becker, E.1    Florin, L.2    Pfizenmaier, K.3    Kaufmann, H.4
  • 30
    • 35048827454 scopus 로고    scopus 로고
    • Effect of doxycycline'Äêregulated protein disulfide isomerase expression on the specific productivity of recombinant CHO cells: Thrombopoietin and antibody
    • Mohan C, Park SH, Chung JY, Lee GM, (2007) Effect of doxycycline'Äêregulated protein disulfide isomerase expression on the specific productivity of recombinant CHO cells: Thrombopoietin and antibody. Biotechnology and Bioengineering 98: 611-615.
    • (2007) Biotechnology and Bioengineering , vol.98 , pp. 611-615
    • Mohan, C.1    Park, S.H.2    Chung, J.Y.3    Lee, G.M.4
  • 31
    • 77950950835 scopus 로고    scopus 로고
    • Regulation of XBP-1 signaling during transient and stable recombinant protein production in CHO cells
    • Ku SC, Toh PC, Lee YY, Chusainow J, Yap MG, et al. (2010) Regulation of XBP-1 signaling during transient and stable recombinant protein production in CHO cells. Biotechnology Progress 26: 517-526.
    • (2010) Biotechnology Progress , vol.26 , pp. 517-526
    • Ku, S.C.1    Toh, P.C.2    Lee, Y.Y.3    Chusainow, J.4    Yap, M.G.5
  • 32
    • 84879256909 scopus 로고    scopus 로고
    • A CHO cell line engineered to express XBP1 and ERO1-Lα has increased levels of transient protein expression
    • Cain K, Peters S, Hailu H, Sweeney B, Stephens P, et al. (2013) A CHO cell line engineered to express XBP1 and ERO1-Lα has increased levels of transient protein expression. Biotechnology Progress.
    • (2013) Biotechnology Progress
    • Cain, K.1    Peters, S.2    Hailu, H.3    Sweeney, B.4    Stephens, P.5
  • 33
    • 13544249755 scopus 로고    scopus 로고
    • Effect of increased expression of protein disulfide isomerase and heavy chain binding protein on antibody secretion in a recombinant CHO cell line
    • Borth N, Mattanovich D, Kunert R, Katinger H, (2005) Effect of increased expression of protein disulfide isomerase and heavy chain binding protein on antibody secretion in a recombinant CHO cell line. Biotechnology Progress 21: 106-111.
    • (2005) Biotechnology Progress , vol.21 , pp. 106-111
    • Borth, N.1    Mattanovich, D.2    Kunert, R.3    Katinger, H.4
  • 34
    • 81455158753 scopus 로고    scopus 로고
    • Culture temperature modulates aggregation of recombinant antibody in CHO cells
    • Gomez N, Subramanian J, Ouyang J, Nguyen MD, Hutchinson M, et al. (2012) Culture temperature modulates aggregation of recombinant antibody in CHO cells. Biotechnol Bioeng 109: 125-136.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 125-136
    • Gomez, N.1    Subramanian, J.2    Ouyang, J.3    Nguyen, M.D.4    Hutchinson, M.5
  • 36
    • 78751507365 scopus 로고    scopus 로고
    • Differential effect of exocytic SNAREs on the production of recombinant proteins in mammalian cells
    • Peng RW, Abellan E, Fussenegger M, (2010) Differential effect of exocytic SNAREs on the production of recombinant proteins in mammalian cells. Biotechnol Bioeng 108: 611-620.
    • (2010) Biotechnol Bioeng , vol.108 , pp. 611-620
    • Peng, R.W.1    Abellan, E.2    Fussenegger, M.3
  • 37
    • 70449518020 scopus 로고    scopus 로고
    • The vesicle-trafficking protein munc18b increases the secretory capacity of mammalian cells
    • Peng RW, Guetg C, Tigges M, Fussenegger M, (2010) The vesicle-trafficking protein munc18b increases the secretory capacity of mammalian cells. Metabolic engineering 12: 18-25.
    • (2010) Metabolic Engineering , vol.12 , pp. 18-25
    • Peng, R.W.1    Guetg, C.2    Tigges, M.3    Fussenegger, M.4
  • 38
    • 80053053600 scopus 로고    scopus 로고
    • Promoter methylation and transgene copy numbers predict unstable protein production in recombinant Chinese hamster ovary cell lines
    • Osterlehner A, Simmeth S, Gopfert U, (2011) Promoter methylation and transgene copy numbers predict unstable protein production in recombinant Chinese hamster ovary cell lines. Biotechnol Bioeng 108: 2670-2681.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2670-2681
    • Osterlehner, A.1    Simmeth, S.2    Gopfert, U.3
  • 39
    • 84857443864 scopus 로고    scopus 로고
    • Early prediction of instability of Chinese hamster ovary cell lines expressing recombinant antibodies and antibody-fusion proteins
    • Dorai H, Corisdeo S, Ellis D, Kinney C, Chomo M, et al. (2012) Early prediction of instability of Chinese hamster ovary cell lines expressing recombinant antibodies and antibody-fusion proteins. Biotechnol Bioeng 109: 1016-1030.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 1016-1030
    • Dorai, H.1    Corisdeo, S.2    Ellis, D.3    Kinney, C.4    Chomo, M.5
  • 40
    • 0023055846 scopus 로고
    • The cloning and nucleotide sequence of cDNA for an amplified glutamine synthetase gene from the Chinese hamster
    • Hayward BE, Hussain A, Wilson RH, Lyons A, Woodcock V, et al. (1986) The cloning and nucleotide sequence of cDNA for an amplified glutamine synthetase gene from the Chinese hamster. Nucl Acids Res 14: 999-1008.
    • (1986) Nucl Acids Res , vol.14 , pp. 999-1008
    • Hayward, B.E.1    Hussain, A.2    Wilson, R.H.3    Lyons, A.4    Woodcock, V.5
  • 42
    • 1542410260 scopus 로고    scopus 로고
    • Uncoupling of cell growth and proliferation results in enhancement of productivity in p21CIP1-arrested CHO cells
    • Bi JX, Shuttleworth J, Al-Rubeai M, (2004) Uncoupling of cell growth and proliferation results in enhancement of productivity in p21CIP1-arrested CHO cells. Biotechnology and Bioengineering 85: 741-749.
    • (2004) Biotechnology and Bioengineering , vol.85 , pp. 741-749
    • Bi, J.X.1    Shuttleworth, J.2    Al-Rubeai, M.3
  • 43
    • 28644432158 scopus 로고    scopus 로고
    • Techniques for dual staining of DNA and intracellular immunoglobulins in murine hybridoma cells: applications to cell-cycle analysis of hyperosmotic cultures
    • McNeeley KM, Sun Z, Sharfstein ST, (2005) Techniques for dual staining of DNA and intracellular immunoglobulins in murine hybridoma cells: applications to cell-cycle analysis of hyperosmotic cultures. Cytotechnology 48: 15-26.
    • (2005) Cytotechnology , vol.48 , pp. 15-26
    • McNeeley, K.M.1    Sun, Z.2    Sharfstein, S.T.3
  • 44
    • 0033534485 scopus 로고    scopus 로고
    • Analysis of changes during subclone development and ageing of human antibody-producing heterohybridoma cells by Northern blot and flow cytometry
    • Borth N, Strutzenberger K, Kunert R, Steinfellner W, Katinger H, (1999) Analysis of changes during subclone development and ageing of human antibody-producing heterohybridoma cells by Northern blot and flow cytometry. Journal of Biotechnology 67: 57-66.
    • (1999) Journal of Biotechnology , vol.67 , pp. 57-66
    • Borth, N.1    Strutzenberger, K.2    Kunert, R.3    Steinfellner, W.4    Katinger, H.5
  • 45
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-[Delta][Delta]CT Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-[Delta][Delta]CT Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 46
  • 47
    • 0030066488 scopus 로고
    • Metabolic burden in recombinant CHO cells: effect ofdhfr gene amplification andlacZ expression
    • Gu MB, Todd P, Kompala DS, (1995) Metabolic burden in recombinant CHO cells: effect ofdhfr gene amplification andlacZ expression. Cytotechnology 18: 159-166.
    • (1995) Cytotechnology , vol.18 , pp. 159-166
    • Gu, M.B.1    Todd, P.2    Kompala, D.S.3
  • 48
    • 0027112480 scopus 로고
    • Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells
    • Pendse GJ, Karkare S, Bailey JE, (1992) Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells. Biotechnology and Bioengineering 40: 119-129.
    • (1992) Biotechnology and Bioengineering , vol.40 , pp. 119-129
    • Pendse, G.J.1    Karkare, S.2    Bailey, J.E.3
  • 49
    • 0025500378 scopus 로고
    • Mechanisms and kinetics of monoclonal antibody synthesis and secretion in synchronous and asynchronous hybridoma cell cultures
    • Al-Rubeai M, Emery AN, (1990) Mechanisms and kinetics of monoclonal antibody synthesis and secretion in synchronous and asynchronous hybridoma cell cultures. Journal of Biotechnology 16: 67-85.
    • (1990) Journal of Biotechnology , vol.16 , pp. 67-85
    • Al-Rubeai, M.1    Emery, A.N.2
  • 50
    • 0025499794 scopus 로고
    • Cell cycle- and growth phase-dependent variations in size distribution, antibody productivity, and oxygen demand in hybridoma cultures
    • Ramirez OT, Mutharasan R, (1990) Cell cycle- and growth phase-dependent variations in size distribution, antibody productivity, and oxygen demand in hybridoma cultures. Biotechnology and Bioengineering 36: 839-848.
    • (1990) Biotechnology and Bioengineering , vol.36 , pp. 839-848
    • Ramirez, O.T.1    Mutharasan, R.2
  • 51
    • 0025291580 scopus 로고
    • Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately
    • Wiest DL, Burkhardt JK, Hester S, Hortsch M, Meyer DI, et al. (1990) Membrane biogenesis during B cell differentiation: most endoplasmic reticulum proteins are expressed coordinately. J Cell Biol 110: 1501-1511.
    • (1990) J Cell Biol , vol.110 , pp. 1501-1511
    • Wiest, D.L.1    Burkhardt, J.K.2    Hester, S.3    Hortsch, M.4    Meyer, D.I.5
  • 52
    • 0032899430 scopus 로고    scopus 로고
    • The role of the cell cycle in determining gene expression and productivity in CHO cells
    • Lloyd DR, Leelavatcharamas V, Emery AN, Al-Rubeai M, (1999) The role of the cell cycle in determining gene expression and productivity in CHO cells. Cytotechnology 30: 49-57.
    • (1999) Cytotechnology , vol.30 , pp. 49-57
    • Lloyd, D.R.1    Leelavatcharamas, V.2    Emery, A.N.3    Al-Rubeai, M.4
  • 53
    • 0033735339 scopus 로고    scopus 로고
    • Relationship between cell size, cell cycle and specific recombinant protein productivity
    • Lloyd DR, Holmes P, Jackson LP, Emery AN, Al-Rubeai M, (2000) Relationship between cell size, cell cycle and specific recombinant protein productivity. Cytotechnology 34: 59-70.
    • (2000) Cytotechnology , vol.34 , pp. 59-70
    • Lloyd, D.R.1    Holmes, P.2    Jackson, L.P.3    Emery, A.N.4    Al-Rubeai, M.5
  • 54
    • 33847374097 scopus 로고    scopus 로고
    • Characterisation of recombinant CHO cell lines by investigation of protein productivities and genetic parameters
    • Lattenmayer C, Trummer E, Schriebl K, Vorauer-Uhl K, Mueller D, et al. (2007) Characterisation of recombinant CHO cell lines by investigation of protein productivities and genetic parameters. Journal of Biotechnology 128: 716-725.
    • (2007) Journal of Biotechnology , vol.128 , pp. 716-725
    • Lattenmayer, C.1    Trummer, E.2    Schriebl, K.3    Vorauer-Uhl, K.4    Mueller, D.5
  • 56
    • 0942265267 scopus 로고    scopus 로고
    • Molecular definition of predictive indicators of stable protein expression in recombinant NS0 myeloma cells
    • Barnes LM, Bentley CM, Dickson AJ, (2003) Molecular definition of predictive indicators of stable protein expression in recombinant NS0 myeloma cells. Biotechnology and Bioengineering 85: 115-121.
    • (2003) Biotechnology and Bioengineering , vol.85 , pp. 115-121
    • Barnes, L.M.1    Bentley, C.M.2    Dickson, A.J.3
  • 57
    • 0019427239 scopus 로고
    • Glycosylation causes an apparent block in translation of immunoglobulin heavy chain
    • Bergman LW, Harris E, Kuehl WM, (1981) Glycosylation causes an apparent block in translation of immunoglobulin heavy chain. J Biol Chem 256: 701-706.
    • (1981) J Biol Chem , vol.256 , pp. 701-706
    • Bergman, L.W.1    Harris, E.2    Kuehl, W.M.3
  • 58
    • 0018647555 scopus 로고
    • Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides
    • Bergman LW, Kuehl WM, (1979) Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides. J Biol Chem 254: 5690-5694.
    • (1979) J Biol Chem , vol.254 , pp. 5690-5694
    • Bergman, L.W.1    Kuehl, W.M.2
  • 59
    • 0015222704 scopus 로고
    • Synthesis, assembly and secretion of gamma globulin by mouse myeloma cells: II. Assembly of IgG2b immunoglobulin by MPC 11 tumor and culture cells
    • Laskov R, Lanzerotti R, Scharff MD, (1971) Synthesis, assembly and secretion of gamma globulin by mouse myeloma cells: II. Assembly of IgG2b immunoglobulin by MPC 11 tumor and culture cells. Journal of Molecular Biology 56: 327-339.
    • (1971) Journal of Molecular Biology , vol.56 , pp. 327-339
    • Laskov, R.1    Lanzerotti, R.2    Scharff, M.D.3
  • 60
    • 13544259722 scopus 로고    scopus 로고
    • On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells
    • Schlatter S, Stansfield SH, Dinnis DM, Racher AJ, Birch JR, et al. (2005) On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells. Biotechnol Prog 21: 122-133.
    • (2005) Biotechnol Prog , vol.21 , pp. 122-133
    • Schlatter, S.1    Stansfield, S.H.2    Dinnis, D.M.3    Racher, A.J.4    Birch, J.R.5
  • 61
    • 0034517368 scopus 로고    scopus 로고
    • Selective Export of MHC Class I Molecules from the ER after Their Dissociation from TAP
    • Spiliotis ET, Osorio M, ̇Òiga MC, Edidin M, (2000) Selective Export of MHC Class I Molecules from the ER after Their Dissociation from TAP. Immunity 13: 841-851.
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Osorio, M.2    Òiga, M.C.3    Edidin, M.4
  • 62
    • 79956064271 scopus 로고    scopus 로고
    • Chemostat-based transcriptional analysis of growth rate change and BCL-2 over-expression in NS0 cells
    • Krampe B, Fagan A, Gaora PO, Al-Rubeai M, (2011) Chemostat-based transcriptional analysis of growth rate change and BCL-2 over-expression in NS0 cells. Biotechnol Bioeng 108: 1603-1615.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1603-1615
    • Krampe, B.1    Fagan, A.2    Gaora, P.O.3    Al-Rubeai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.