Publication

[220] “Comprehensive Physicochemical and Biological Characterization of the Proposed Biosimilar Darbepoetin-a, LBDE and Originator Darbepoetin-a, NESP®” Y. R. Jeong, R. U. Jeong, J. H. Son, M. A. Song, J. A. Hwang, and G. M. Lee, BioDrugs. (2018).

[219] “Glutamine Synthetase Gene-Knockout Human Embryonic Kidney 293E Cells for Stable Production of Monoclonal Antibody”,  D. Y. Yu, S. Y. Lee, and G. M. Lee, Biotechnol. Bioeng. (2018).

[218] “Using Titer and Titer Normalized to Confluence Are Complementary Strategies for Obtaining Chinese Hamster Ovary Cell Lines with High Volumetric Productivity of Etanercept”, N. Pristovšek, H. G. Hansen, D. Sergeeva, N. Borth, G. M. Lee, M. R. Andersen, and H. F. Kildegaard, Biotechnol. J. (2018).

[217] “Anti-Apoptosis Engineering for Improved Protein Production from CHO Cells”, E. Baek, S. M. Noh, and G. M. Lee, Method Mol. Biol. (2017).

[216] “Proteomic Analysis of Host Cell Protein Dynamics in the Supernatant of Fc-Fusion Protein-Producing CHO DG44 and DUKX-B11 Cell Lines in Batch and Fed-Batch Cultures”, J. H. Park, J. H. Jin, I. J. Ji, H. J. An, J. W. Kim, and G. M. Lee, Biotechnol. Bioeng. (2017).

[215] “Understanding of Decreased Sialylation of Fc-fusion Protein in Hyperosmotic Recombinant Chinese Hamster Ovary Cell Culture: N-Glycosylation Gene Expression and N-linked Glycan Antennary Profile”, J. H. Lee, Y. R. Jeong, Y. G. Kim, and G. M. Lee, Biotechnol. Bioeng. (2017). 

[214] “Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells”, J. H. Park, J. H. Jin, M. S. Lim, H. J. An, J. W. Kim, and G. M. Lee, Sci. Rep. 7:44246 (2017). 

[213] “Investigation of the Relationship between EBNA-1 Expression Level and Specific Foreign Protein Productivity in Transient Gene Expression of HEK293 Cells”, J. H. Lee, S. M. Lim, E. G. Lee, H. W. Lee, J. K. Jung, G. M. Lee, and Y. G. Kim, Process Biochem. (2017). 

[212] “Ribosome Profiling-Guided Depletion of an mRNA Improves CHO Cell Growth and Recombinant Product Titers”, T. B. Kallehauge, S. Li, L. E. Pedersen, T. K. Ha, D. Ley, M. R. Andersen, H. F. Kildegaard, G. M. Lee, and N. E. Lewis, Sci. Rep., 7:40388 (2017). 

[211] “Improving the Secretory Capacity of Chinese Hamster Ovary Cells by Ectopic Expression of Effector Genes: Lessons Learned and Future Directions”, H. G. Hansen, N. Pristovšek, H. F. Kildegaard, and G. M. Lee, Biotechnol. Adv. 35:64 (2017). 

[210] "Reduction of Ammonia and Lactate through the Coupling of Glutamine Synthetase Selection and Lactate Dehydrogenase-A Down-Regulation in CHO Cells”, S. M. Noh, J. H. Park, M. S. Lim, J. R. Woo, J. W. Kim, and G. M. Lee, Appl. Microbiol. Biotechnol. 101:1035 (2017). 

[209] “Case Study on Human α1-Antitrypsin: Recombinant Protein Titers Obtained by Commercial ELISA Kits Are Inaccurate”, H. G. Hansen, H. F. Kildegaard, G. M. Lee, and S. Kol, Biotechnol. J. 11:1648 (2016). 

[208] “Combinatorial Treatment with Lithium Chloride Enhances Recombinant Antibody Production in Transiently Transfected CHO-NK and HEK293E Cells”,  C. L. Kim, T. K. Ha, and G. M. Lee,  Biotechnol. Bioproc. Eng., 21:667 (2016). 

[207] “Endoplasmic Reticulum-Directed Recombinant mRNA Displays Subcellular Localization Equal to Endogenous mRNA During Transient Expression in CHO cells”, T. B. Kallehauge, S. Kol, M. R. Andersen, C. K. Damgaard, G. M. Lee, and H. F. Kildegaard, Biotechnol. J. 11:1362 (2016).

[206] “Limitations to the Development of Recombinant Human Embryonic Kidney 293 Cells Using Glutamine Synthetase”, D. Y. Yu, S. M. Noh, and G. M. Lee, J. Biotechnol. 231:136 (2016). 

[205] “Alleviation of Proteolytic Degradation of Recombinant Human Bone Morphogenetic Protein-4 by Repeated Batch Culture of Chinese Hamster Ovary Cells”, C. L. Kim, Y. L. Bang, Y. S. Kim, J. W. Jang, and G. M. Lee, Process Biochem. (2016). 

[204] “Accelerated Homology-Directed Targeted Integration of Transgenes in Chinese Hamster Ovary Cells via CRISPR/Cas9 and Fluorescent Enrichment”, J. S. Lee, L. M. Grav, L. E. Pedersen, G. M. Lee, H. F. Kildegaard, Biotechnol. Bioeng, 113:2518 (2016). 

[203] “The Molecular Weight and Concentration of Dextran Sulfate Affect Cell Growth and Antibody Production in CHO Cell Cultures”, J. H. Park, M. S. Lim, J. R. Woo, J. W. Kim, and G. M. Lee, Biotechnol. Prog. (2016).

[202] “Chemical Inhibition of Autophagy: Examining Its Potential to Increase the Specific Productivity of Recombinant CHO Cell Lines”, E. Baek, C. L. Kim, M. G. Kim, J. S. Lee, and G. M. Lee, Biotechnol. Bioeng. 113:1953 (2016). 

[201] “Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)", D. J. Klionsky et al., Autophagy. 12:1 (2016). 

[1]  [2]  [3]  [4]  [5]  [6]  [7]  [8]  [9]  [10]  [11]  [12]  [13] [14]