Cited by 129Viral Infectious Diseases and Gene Expression in InsectsAnimal Genetics and ReproductionTransgenic Plants and Applications

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Advances in animal cell recombinant protein production: GS-NS0 expression system

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Barnes, Louise M., Bentley, Catherine M., Dickson, Alan J.·2000·Cytotechnology

DOI 10.1023/a:1008170710003PMC PMC3449689

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Abstract

The production of recombinant proteins using mammalian cell expression systems is of growing importance within biotechnology, largely due to the ability of specific mammalian cells to carry out post-translational modifications of the correct fidelity. The Glutamine Synthetase-NS0 system is now one such industrially important expression system.Glutamine synthetase catalyses the formation ofglutamine from glutamate and ammonia. NS0 cellscontain extremely low levels of endogenous glutaminesynthetase activity, therefore exogenous glutaminesynthetase can be used efficiently as a selectablemarker to identify successful transfectants in theabsence of glutamine in the media. In addition, theinclusion of methionine sulphoximine, an inhibitor ofglutamine synthetase activity, enables furtherselection of those clones producing relatively highlevels of transfected glutamine synthetase and henceany heterologous gene which is coupled to it. Theglutamine synthetase system technology has been usedfor research and development purposes during thisdecade and its importance is clearly demonstrated nowthat two therapeutic products produced using thissystem have reached the market place.

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Continuous cultures of fused cells secreting antibody of predefined specificity
KÖHLER, G., & MILSTEIN, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,229
Derivation of specific antibody‐producing tissue culture and tumor lines by cell fusion
Köhler, G., & Milstein, C. (1976) · European Journal of Immunology · doi:10.1002/eji.1830060713 · Cited by 1,922
[1] Preparation of monoclonal antibodies: Strategies and procedures
Galfrè, G., & Milstein, C. (1981) · Methods in Enzymology · doi:10.1016/0076-6879(81)73054-4 · Cited by 1,771
Evidence that glutamine, not sugar, is the major energy source for cultured HeLa cells.
Reitzer, L. J., Wice, B. M., & Kennell, D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30124-2 · Cited by 1,240
Efficient Neutralization of Primary Isolates of HIV-1 by a Recombinant Human Monoclonal Antibody
Burton, D. R., Pyati, J., Koduri, R., Sharp, S. J., Thornton, G. B., Parren, P. W. H. I., Sawyer, L. S. W., Hendry, R. M., Dunlop, N., Nara, P. L., et al. (1994) · Science · doi:10.1126/science.7973652 · Cited by 1,100
Biochemical Characterization of Human Collagenase-3
Knäuper, V., López-Otin, C., Smith, B., Knight, G., & Murphy, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1544 · Cited by 881
Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
Urlaub, G., & Chasin, L. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.4216 · Cited by 876
Fusion between immunoglobulin‐secreting and nonsecreting myeloma cell lines
Köhler, G., Howe, S. C., & Milstein, C. (1976) · European Journal of Immunology · doi:10.1002/eji.1830060411 · Cited by 717
Development of a Humanized Monoclonal Antibody (MEDI‐493) with Potent In Vitro and In Vivo Activity against Respiratory Syncytial Virus
Johnson, S., Oliver, C. N., Prince, G. A., Hemming, V. G., Pfarr, D. S., Wang, S., Dormitzer, M., O'Grady, J., Koenig, S., Tamura, J. K., et al. (1997) · The Journal of Infectious Diseases · doi:10.1086/514115 · Cited by 653
GENE AMPLIFICATION
Stark, G. R., & Wahl, G. M. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.002311 · Cited by 583
Mouse myelomas and lymphomas in culture
Horibata, K., & Harris, A. W. (1970) · Experimental Cell Research · doi:10.1016/0014-4827(70)90489-1 · Cited by 532
High-Level Expression of a Recombinant Antibody from Myeloma Cells Using a Glutamine Synthetase Gene as an Amplifiable Selectable Marker
Bebbington, C. R., Renner, G., Thomson, S., King, D., Abrams, D., & Yarranton, G. T. (1992) · Nature Biotechnology · doi:10.1038/nbt0292-169 · Cited by 462
Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP)
Murphy, G., Cockett, M. I., Ward, R. V., & Docherty, A. J. P. (1991) · Biochemical Journal · doi:10.1042/bj2770277 · Cited by 457
Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.
Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.3.761 · Cited by 340
Mechanism of inhibition of glutamine synthetase by methionine sulfoximine
Ronzio, R. A., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00831a038 · Cited by 327
The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
Murphy, G., Houbrechts, A., Cockett, M. I., Williamson, R. A., O'Shea, M., & Docherty, A. J. P. (1991) · Biochemistry · doi:10.1021/bi00247a001 · Cited by 324
Induction of Plasma-Cell Neoplasms in Strain BALB/c Mice with Mineral Oil and Mineral Oil Adjuvants
Potter, M., & BOYCE, C. R. (1962) · Nature · doi:10.1038/1931086a0 · Cited by 309
The role of the C-terminal domain in collagenase and stromelysin specificity.
Murphy, G., Allan, J. A., Willenbrock, F., Cockett, M. I., O'Connell, J. P., & Docherty, A. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50134-x · Cited by 308
Transcriptional interference and termination between duplicated α-globin gene constructs suggests a novel mechanism for gene regulation
Proudfoot, N. J. (1986) · Nature · doi:10.1038/322562a0 · Cited by 301
Coamplification and coexpression of human tissue-type plasminogen activator and murine dihydrofolate reductase sequences in Chinese hamster ovary cells.
Kaufman, R. J., Wasley, L. C., Spiliotes, A. J., Gossels, S. D., Latt, S. A., Larsen, G. R., & Kay, R. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.7.1750 · Cited by 297
Induction of apoptosis in nutrient‐deprived cultures of hybridoma and myeloma cells
Mercille, S., & Massie, B. (1994) · Biotechnology and Bioengineering · doi:10.1002/bit.260440916 · Cited by 296
The Gene Structure of Tissue Inhibitor of Metalloproteinases (TIMP)-3 and Its Inhibitory Activities Define the Distinct TIMP Gene Family
Apte, S. S., Olsen, B. R., & Murphy, G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14313 · Cited by 295
βig-h3: A Transforming Growth Factor-β-Responsive Gene Encoding a Secreted Protein That Inhibits Cell Attachment In Vitro and Suppresses the Growth of CHO Cells in Nude Mice
SKONIER, J., BENNETT, K., ROTHWELL, V., KOSOWSKI, S., PLOWMAN, G., WALLACE, P., EDELHOFF, S., DISTECHE, C., NEUBAUER, M., MARQUARDT, H., et al. (1994) · DNA and Cell Biology · doi:10.1089/dna.1994.13.571 · Cited by 273
The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
Murphy, G., Willenbrock, F., Ward, R. V., Cockett, M. I., Eaton, D., & Docherty, A. J. P. (1992) · Biochemical Journal · doi:10.1042/bj2830637 · Cited by 265
A model for light distribution and average solar irradiance inside outdoor tubular photobioreactors for the microalgal mass culture
Acién, F. G., García-Camacho, F., Pérez, J. A. S., Fernández-Sevilla, J. M., & Grima, E. M. (1997) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19970905)55:5<773::aid-bit7>3.0.co;2-8 · Cited by 251
High Level Expression of Tissue Inhibitor of Metalloproteinases in Chinese Hamster Ovary Cells Using Glutamine Synthetase Gene Amplification
Cockett, M. I., Bebbington, C. R., & Yarranton, G. T. (1990) · Nature Biotechnology · doi:10.1038/nbt0790-662 · Cited by 250
The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: A kinetic analysis of the inhibition of gelatinase A
Willenbrock, F., Crabbe, T., Slocombe, P. M., Sutton, C. W., Docherty, A. J. P., Cockett, M. I., O'Shea, M., Brocklehurst, K., Phillips, I. R., & Murphy, G. (1993) · Biochemistry · doi:10.1021/bi00067a023 · Cited by 237
Antibody against the Leu-CAM beta-chain (CD18) promotes both LFA-1- and CR3-dependent adhesion events
Robinson, M. K., Andrew, D., Rosen, H., Brown, D., Ortlepp, S., Stephens, P. E., & Butcher, E. C. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.4.1080 · Cited by 212
REVERSIBILITY OF THE ENZYMATIC SYNTHESIS OF GLUTAMINE
Levintow, L., & Meister, A. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65554-1 · Cited by 173
Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions.
Lifely, M. R., Hale, C., Boyce, S., Keen, M., & Phillips, J. (1995) · Glycobiology · doi:10.1093/glycob/5.8.813 · Cited by 173
A stereochemical method for detection of ATP terminal phosphate transfer in enzymatic reactions. Glutamine synthetase.
Midelfort, C. F., & Rose, I. A. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33034-x · Cited by 172
Studies on the enzymic synthesis of glutamine
Elliott, W. H. (1951) · Biochemical Journal · doi:10.1042/bj0490106 · Cited by 167
Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase
Manning, J. M., Moore, S., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00834a066 · Cited by 166
Inhibition of glutamine synthetase by methionine sulfoximine. Studies On Methionine sulfoximine phosphate
Rowe, W. B., Ronzio, R. A., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00834a065 · Cited by 163
Phosphorylation of methionine sulfoximine by glutamine synthetase.
Ronzio, R. A., & Meister, A. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.59.1.164 · Cited by 156
Codon optimization for high-level expression of human erythropoietin (EPO) in mammalian cells
Kim, C. H., Oh, Y., & Lee, T.-H. (1997) · Gene · doi:10.1016/s0378-1119(97)00384-3 · Cited by 154
THE ENZYMATIC SYNTHESIS OF GLUTAMINE, A REACTION UTILIZING ADENOSINE TRIPHOSPHATE
Speck, J. F. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56802-2 · Cited by 152
High Level Expression of the Humanized Monoclonal Antibody CAMPATH-1H in Chinese Hamster Ovary Cells
Pagé, M., & Sydenham, M. A. (1991) · Nature Biotechnology · doi:10.1038/nbt0191-64 · Cited by 143
23. Glutamine Synthetase of Mammals
Meister, A. (1974) · The Enzymes · doi:10.1016/s1874-6047(08)60155-9 · Cited by 143
The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides
Fahnestock, M. L., Johnson, J. L., Feldman, R. M. R., Neveu, J. M., Lane, W. S., & Björkman, P. J. (1995) · Immunity · doi:10.1016/1074-7613(95)90129-9 · Cited by 141
Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses.
Stephens, S., Emtage, S., Vetterlein, O. M., Chaplin, L. C., Bebbington, C. R., Nesbitt, A. M., Sopwith, M., Athwal, D., Novak, C., & Bodmer, M. (1995) · PubMed Central · Cited by 124
Lactate: A major product of glutamine metabolism by human diploid fibroblasts
Zielke, H. R., Sumbilla, C. M., Sevdalian, D. A., Hawkins, R. L., & Ozand, P. T. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041040316 · Cited by 123
Effects of the Position of the Simian Virus 40 Enhancer on Expression of Multiple Transcription Units in a Single Plasmid
Kadesch, T. R., & Berg, P. R. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.7.2593 · Cited by 120
Regulation of glutamine synthetase in cultured 3T3-L1 cells by insulin, hydrocortisone, and dibutyryl cyclic AMP
Miller, R. E., Hackenberg, R., & Gershman, H. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.3.1418 · Cited by 119
Characterization of recombinant gp120 and gp160 from HIV-1
Moore, J. P., McKeating, J. A., Jones, I. M., et al. (1990) · AIDS · doi:10.1097/00002030-199004000-00004 · Cited by 116
High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants.
Davis, S. J., Ward, H. A., Puklavec, M. J., Willis, A. C., Williams, A., & Barclay, A. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)86961-7 · Cited by 115
Intracellular immunoglobulin chain synthesis in non-secreting variants of a mouse myeloma: Detection of inactive light-chain messenger RNA
Cowan, N. J., Secher, D. S., & Milstein, C. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90533-6 · Cited by 115
Recombinant pulmonary surfactant protein D. Post-translational modification and molecular assembly.
Crouch, E. C., Chang, D. S., Rust, K. J., Persson, A., & Heuser, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40752-6 · Cited by 112
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein
Nguyen, Q. K., Murphy, G., Hughes, C., Mort, J. S., & Roughley, P. J. (1993) · Biochemical Journal · doi:10.1042/bj2950595 · Cited by 109
Adenosinetriphosphate in Glutamine Synthesis
Elliott, W. H. (1948) · Nature · doi:10.1038/161128a0 · Cited by 104
Effects of Methotrexate on Transfected DNA Stability in Mammalian Cells
Pallavicini, M. G., DeTeresa, P. S., Rosette, C., Gray, J. W., & Wurm, F. M. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.1.401 · Cited by 101
Structural Diversity in Domains of the Immunoglobulin SuperfamilyPreprint
Williams, A., Davis, S. J., He, Q., & Barclay, A. N. (1989) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1989.054.01.075 · Cited by 100
Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules.
Gastinel, L. N., Simister, N. E., & Björkman, P. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.638 · Cited by 98
Histology of Developing Plasma Cell Neoplasia Induced By Mineral Oil in BALB/c Mice
Potter, M. J., & MacCardle, R. C. (1964) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/33.3.497 · Cited by 96
Nutritional aspects of the growth of animal cells in culture
Butler, M., & Jenkins, H. (1989) · Journal of Biotechnology · doi:10.1016/0168-1656(89)90009-6 · Cited by 95
THE ENZYMIC SYNTHESIS OF GLUTAMINE
Speck, J. F. (1947) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35134-7 · Cited by 94
Process development for the production of recombinant antibodies using the glutamine synthetase (GS) system
Brown, M. E., Renner, G., Field, R. P., & Hassell, T. (1992) · Cytotechnology · doi:10.1007/bf02521750 · Cited by 93
Monoclonal Antibody Process Development Using Medium Concentrates
Bibila, T. A., Ranucci, C. S., Glazomitsky, K., Buckland, B. C., & Aunins, J. G. (1994) · Biotechnology Progress · doi:10.1021/bp00025a011 · Cited by 93
Separate Domains of the Human Fas Ligand Dictate Self-association and Receptor Binding
Orlinick, J. R., Elkon, K. B., & Chao, M. V. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32221 · Cited by 91
GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity
Kemble, G. W., Henis, Y. I., & White, J. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.6.1253 · Cited by 91
Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13
O'Shea, M., Willenbrock, F. W., Williamson, R. A., Cockett, M. I., Freedman, R. B., Reynolds, J. J., Docherty, A., & Murphy, G. (1992) · Biochemistry · doi:10.1021/bi00157a002 · Cited by 89
Continuous cultures limited by a gaseous substrate: Development of a simple, unstructured mathematical model and experimental verification with Methanobacterium thermoautotrophicum
Schill, N. A., van Gulik, W. M., Voisard, D., & von Stockar, U. (2000) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19960920)51:6<725::aid-bit12>3.0.co;2-c · Cited by 86
Preparation and preclinical evaluation of humanised A33 immunoconjugates for radioimmunotherapy
King, D., Antoniw, P., Owens, R. J., ADAIR, J., Haines, A., Farnsworth, A., Finney, H. M., Lawson, A., Lyons, A. T., Baker, T., et al. (1995) · British Journal of Cancer · doi:10.1038/bjc.1995.516 · Cited by 86
Synergistic interaction between interleukin-12 and steel factor in support of proliferation of murine lymphohematopoietic progenitors in culture
Hirayama, F., Katayama, N., Neben, S., et al. (1994) · Blood · doi:10.1182/blood.v83.1.92.92 · Cited by 84
Expression of soluble isoforms of rat CD45. Analysis by electron microscopy and use in epitope mapping of anti-CD45R monoclonal antibodies.
McCall, M. N., Shotton, D. M., & Barclay, A. N. (1992) · PubMed · Cited by 84
Engineered anti-CD38 monoclonal antibodies for immunotherapy of multiple myeloma
Ellis, J. H., Barber, K. A., Tutt, A. N. J., Hale, C., Lewis, A., Glennie, M. J., Stevenson, G. T., & Crowe, J. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.2.925 · Cited by 81
Amplified expression constructs for human tissue-type plasminogen activator in Chinese hamster ovary cells: instability in the absence of selective pressure
Weidle, U. H., Buckel, P., & Wienberg, J. (1988) · Gene · doi:10.1016/0378-1119(88)90356-3 · Cited by 80
Variations in the heavy polypeptide chain structure of gamma myeloma immunoglobulins from an inbred strain of mice and a hypothesis as to their origin
Potter, M., Appella, E., & Geisser, S. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80187-5 · Cited by 78
Expression of antibody genes in nonlymphoid mammalian cells
Bebbington, C. R. (1991) · Methods · doi:10.1016/s1046-2023(05)80214-2 · Cited by 76
Catalytic Mechanism of Glutamine Synthetase; Overview of Glutamine Metabolism
Meister, A. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-506040-0.50006-6 · Cited by 73
The synaptic vesicle proteins SV2, synaptotagmin and synaptophysin are sorted to separate cellular compartments in CHO fibroblasts.
Feany, M. Β., Yee, A., Delvy, M. L., & Buckley, K. M. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.3.575 · Cited by 71
A Humanized Form of a CD4-Specific Monoclonal Antibody Exhibits Decreased Antigenicity and Prolonged Plasma Half-Life in Rhesus Monkeys While Retaining Its Unique Biological and Antiviral Properties
Reimann, K. A., Lin, W., BIXLER, S., Browning, B., Ehrenfels, B. N., Lucci, J., Miatkowski, K., Olson, D. L., PARISH, T. H., ROSA, M. D., et al. (1997) · AIDS Research and Human Retroviruses · doi:10.1089/aid.1997.13.933 · Cited by 68
The use of engineered E1A genes to transactivate the hCMV-MIE promoter in permanent CHO cell lines
Cockett, M. I., Bebbington, C. R., & Yarranton, G. T. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.2.319 · Cited by 68
The NH2‐terminal domain of rat CD2 binds rat CD48 with a low affinity and binding does not require glycosylation of CD2
van der Merwe, P. A., McPherson, D., Brown, M. H., Barclay, A. N., Cyster, J. G., Williams, A., & Davis, S. J. (1993) · European Journal of Immunology · doi:10.1002/eji.1830230628 · Cited by 66
Characterization of a recombinant antibody produced in the course of a high yield fed‐batch process
Robinson, D. K., Chan, C. P., Lp, C. Y., Tsai, P. K., Tung, J. S., Seamans, T. C., Lenny, A. B., Lee, D. K., Irwin, J., & Silberklang, M. (1994) · Biotechnology and Bioengineering · doi:10.1002/bit.260440609 · Cited by 65
Introduction of Purified Genes Into Mammalian Cell
Kucherlapati, R., Skoultchi, I., & Chasin, L. A. (1984) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238409108719 · Cited by 63
Identification of Functional Domains on gClQ-R, a Cell Surface Protein That Binds to the Globular "Heads" of C1Q, Using Monoclonal Antibodies and Synthetic Peptides
Ghebrehiwet, B., Lu, P. D., Zhang, W., Lim, B. L., Eggleton, P., LEIGH, L. E. A., Reid, K. B. M., & Peerschke, E. I. B. (1996) · Hybridoma · doi:10.1089/hyb.1996.15.333 · Cited by 62
Antibodies that activate β2 integrins can generate different ligand binding states
Ortlepp, S., Stephens, P. E., Hogg, N., Figdor, C. G., & Robinson, M. K. (1995) · European Journal of Immunology · doi:10.1002/eji.1830250302 · Cited by 61
Expression Systems: A User's Guide
Hodgson, J. (1993) · Nature Biotechnology · doi:10.1038/nbt0893-887 · Cited by 61
Characterization of Recombinant Extracellular Domain of Human Interleukin-10 Receptor
Tan, J. C., Braun, S., Rong, H., DiGiacomo, R., Dolphin, E., Baldwin, S., Narula, S. K., Zavodny, P. J., & Chou, C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12906 · Cited by 60
The hinge region of the CD8α chain: structure, antigenicity, and utility in expression of immunoglobulin superfamily domains
Classon, B. J., Brown, M. H., Garnett, D., Somoza, C., Barclay, A. N., Willis, A. C., & Williams, A. (1992) · International Immunology · doi:10.1093/intimm/4.2.215 · Cited by 60
Interaction of the Low-Affinity Receptor CD23/FcεRII Lectin Domain with the Fcε3−4 Fragment of Human Immunoglobulin E
Shi, J., Ghirlando, R., Beavil, R. L., Beavil, A. J., Keown, M. B., Young, R. J., Owens, R. J., Sutton, B. J., & Gould, H. J. (1997) · Biochemistry · doi:10.1021/bi961231e · Cited by 60
Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2
Davis, S. J., Puklavec, M. J., Ashford, D. A., Harlos, K., Jones, E. Y., Stuart, D. I., & Williams, A. (1993) · Protein Engineering Design and Selection · doi:10.1093/protein/6.2.229 · Cited by 58
Site-specific glycosylation of recombinant rat and human soluble CD4 variants expressed in Chinese hamster ovary cells.
Ashford, D. A., Alafi, C. D., Gamble, V., Mackay, D., Rademacher, T. W., Williams, P., Dwek, R. A., Barclay, A. N., Davis, S. J., & Somoza, C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53687-5 · Cited by 57
Monitoring and control of the physiological state of cell cultures
Konstantinov, K. B. (2000) · Biotechnology and Bioengineering · doi:10.1002/bit.260520203 · Cited by 56
Secretion of recombinant human IgE-Fc by mammalian cells and biological activity of glycosylation site mutants
Young, R. J., Owens, R. J., Mackay, G. A., Chan, C. M. W., Shi, J., Hide, M., Francis, D. M., Henry, A. J., Sutton, B. J., & Gould, H. J. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.193 · Cited by 55
Fluorophore‐labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
Flesher, A. R., Marzowski, J., Wang, W., & Raff, H. V. (1995) · Biotechnology and Bioengineering · doi:10.1002/bit.260460502 · Cited by 55
Regulation of glutamine synthetase by dexamethasone in hepatoma tissue culture cells.
Crook, R. B., Louie, M. C., Deuel, T. F., & Tomkins, G. M. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34589-1 · Cited by 54
Expression of immunoglobulin and scavenger receptor superfamily domains as chimeric proteins with domains 3 and 4 of CD4 for ligand analysis
Brown, M. H., & Barclay, A. N. (1994) · Protein Engineering Design and Selection · doi:10.1093/protein/7.4.515 · Cited by 54
Enhanced Transcription of the 78,000-Dalton Glucose-Regulated Protein (GRP78) Gene and Association of GRP78 with Immunoglobulin Light Chains in a Nonsecreting B-Cell Myeloma Line (NS-1)
Nakaki, T., Deans, R. J., & Lee, A. S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.5.2233 · Cited by 53
The I Domain of Integrin LFA-1 Interacts with ICAM-1 Domain 1 at Residue Glu-34 but Not Gln-73
Stanley, P., & Hogg, N. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3358 · Cited by 52
Glutamine regulates glutamine synthetase expression in skeletal muscle cells in culture
Feng, B., Shiber, S. K., & Max, S. R. (1990) · Journal of Cellular Physiology · doi:10.1002/jcp.1041450224 · Cited by 51
Biochemical and immunological properties of rat recombinant interleukin-2 and interleukin-4.
McKnight, A. J., & Classon, B. J. (1992) · PubMed · Cited by 49
Adaptation of cholesterol-requiring NS0 mouse myeloma cells to high density growth in a fully defined protein-free and cholesterol-free culture medium
Keen, M. J., & Steward, T. W. (1995) · Cytotechnology · doi:10.1007/bf00749658 · Cited by 49
Possible role for the Fc receptor on B lymphocytes
Ramasamy, R., MUNRO, A. J., & Milstein, C. (1974) · Nature · doi:10.1038/249573a0 · Cited by 49
Amplification Using CHO Cell Expression Vectors
Kingston, R. E., Kaufman, R. J., Bebbington, C. R., & Rolfe, M. (2002) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb1623s60 · Cited by 48
Temperature control of growth and productivity in mutant Chinese hamster ovary cells synthesizing a recombinant protein
Jenkins, N., & Hovey, A. (1993) · Biotechnology and Bioengineering · doi:10.1002/bit.260420903 · Cited by 48
Construction, Expression, and Activities of L49-sFv-β-Lactamase, a Single-Chain Antibody Fusion Protein for Anticancer Prodrug Activation
Siemers, N. O., Kerr, D. E., Yarnold, S., Stebbins, M. R., Vrudhula, V. M., Hellström, I., Hellström, K. E., & Senter, P. D. (1997) · Bioconjugate Chemistry · doi:10.1021/bc9700751 · Cited by 47
Purification, characterization and immunogenicity of recombinant varicella-zoster virus glycoprotein gE secreted by Chinese hamster ovary cells
Haumont, M., Jacquet, A., Massaer, M., Deleersnyder, V., Mazzu, P., Bollen, A., & Jacobs, P. (1996) · Virus Research · doi:10.1016/0168-1702(95)01270-2 · Cited by 44
Characterization of the extracellular region of the human thyrotrophin receptor expressed as a recombinant protein
Harfst, E., Johnstone, A. P., & Nussey, S. (1992) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0090227 · Cited by 44
Continuous, real‐time monitoring of the oxygen uptake rate (OUR) in animal cell bioreactors
Yoon, S., & Konstantinov, K. B. (1994) · Biotechnology and Bioengineering · doi:10.1002/bit.260440815 · Cited by 43
Effects of exposure to low pH on the lateral mobility of influenza hemagglutinin expressed at the cell surface: correlation between mobility inhibition and inactivation
Gutman, O., Danieli, T., White, J. M., & Henis, Y. I. (1993) · Biochemistry · doi:10.1021/bi00052a014 · Cited by 42
Characterization of O-polysaccharide specific monoclonal antibodies derived from mice infected with the rough Brucella melitensis strain B115
Cloeckaert, A., Zygmunt, M. S., Dubray, G., & Limet, J. N. (1993) · Journal of General Microbiology · doi:10.1099/00221287-139-7-1551 · Cited by 42
Effects of Peptide Length and Composition on Binding to an Empty Class I MHC Heterodimer
Fahnestock, M. L., Johnson, J. L., Feldman, R. M. R., Tsomides, T. J., Mayer, J. P., Narhi, L. O., & Björkman, P. J. (1994) · Biochemistry · doi:10.1021/bi00192a020 · Cited by 41
Selecting and designing cell lines for improved physiological characteristics
Birch, J. R., Boraston, R. C., Metcalfe, H., Brown, M. E., Bebbington, C. R., & Field, R. P. (1994) · Cytotechnology · doi:10.1007/bf00762375 · Cited by 41
The use of the amplifiable high-expression vector pEE14 to study the interactions of autoantibodies with recombinant human thyrotrophin receptor
Harfst, E., Johnstone, A. P., Gout, I. T., Taylor, A. H., Waterfield, M. D., & Nussey, S. (1992) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(92)90152-v · Cited by 41
The effect of dihydrofolate reductase-mediated gene amplification on the expression of transfected immunoglobulin genes.
Dorai, H., & Moore, G. P. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.139.12.4232 · Cited by 40
Purification and Properties of Insulin Receptor Ectodomain from Large-Scale Mammalian Cell Culture
Cosgrove, L. J., Lovrecz, G. O., Verkuylen, A. J., Cavaleri, L., Black, L. A., Bentley, J. D., Howlett, G. J., Gray, P. P., Ward, C. W., & McKern, N. M. (1995) · Protein Expression and Purification · doi:10.1006/prep.1995.0010 · Cited by 40
Prion protein expression in Chinese hamster ovary cells using a glutamine synthetase selection and amplification system
Blochberger, T. C., Cooper, C. L., Peretz, D., Tatzelt, J., Griffith, O. H., Baldwin, M. A., & Prusiner, S. B. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.12.1465 · Cited by 40
O-chain expression in the rough Brucella melitensis strain B115: induction of O-polysaccharide-specific monoclonal antibodies and intracellular localization demonstrated by immunoelectron microscopy
Cloeckaert, A., Zygmunt, M. S., Nicolle, J. C., Dubray, G., & Limet, J. N. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-6-1211 · Cited by 39
Use of the sodium borohydride reduction technique to identify a gamma-glutamyl phosphate intermediary in the Escherichia coli glutamine synthetase reaction.
TODHUNTER, J. A., & Purich, D. L. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41543-3 · Cited by 38
Inhibition of glutamine synthetase by methionine sulfone
Rowe, W. B., & Meister, A. (1973) · Biochemistry · doi:10.1021/bi00732a018 · Cited by 38
Crystal structure of an extracellular fragment of the rat CD4 receptor containing domains 3 and 4
Lange, G., LEWIS, S. J., Murshudov, G. N., Dodson, G. G., Moody, P. C. E., Turkenburg, J. P., Barclay, A. N., & Brady, R. L. (1994) · Structure · doi:10.1016/s0969-2126(00)00048-4 · Cited by 38
Single-chain MHC class II molecules induce T cell activation and apoptosis
Rhode, P. R., Burkhardt, M. R., Jiao, J., Siddiqui, A. H., Huang, G. P., & Wong, H. C. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.11.4885 · Cited by 38
Structural Characterization of the N-Glycans of a Humanized Anti-CD18 Murine Immunoglobulin G
Ip, C. C. Y., Miller, W. J. W., Silberklang, M., Mark, G. E., Ellis, R. W., Huang, L., Glushka, J., Vanhalbeek, H., Zhu, J., & Alhadeff, J. A. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1055 · Cited by 37
Isolation and Characterization of a Stable Chinese Hamster Ovary Cell Line Overexpressing the Plasma Membrane Ca2+-ATPase
Guerini, D., Schröder, S., Foletti, D. L., & Carafoli, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14643 · Cited by 36
Immunoglobulin variable region hypermutation in hybrids derived from a pre-B- and a myeloma cell line.
Green, N., Rabinowitz, J. L., Zhu, M., Kobrin, B. J., & Scharff, M. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6304 · Cited by 36
High-Level Expression of Human Inducible Nitric Oxide Synthase in Chinese Hamster Ovary Cells and Characterization of the Purified Enzyme
Laubach, V. E., Garvey, E. P., & Sherman, P. A. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0143 · Cited by 36
Expression, purification and characterization of B72.3 Fv fragments
King, D. J., Byron, O., Mountain, A., Weir, N., Harvey, A. R., Lawson, A. D. G., Proudfoot, K. A., Baldock, D., Harding, S. E., Yarranton, G. T., et al. (1993) · Biochemical Journal · doi:10.1042/bj2900723 · Cited by 35
Antibodies cross-reactive with E- and P-selectin block both E- and P- selectin functions
Berg, E. L., Fromm, C., Melrose, J. E., et al. (1995) · Blood · doi:10.1182/blood.v85.1.31.bloodjournal85131 · Cited by 35
The structure of the chicken glutamine synthetase-encoding gene
Pu, H., & Young, A. P. (1989) · Gene · doi:10.1016/0378-1119(89)90348-x · Cited by 34
Structural analysis of the CD5 antigen: Expression, disulphide bond analysis and physical characterisation of CD5 scavenger receptor superfamily domain 1
McAlister, M. S. B., Brown, M. H., Willis, A. C., Rudd, P. M., Harvey, D. J., Aplin, R. T., Shotton, D. M., Dwek, R. A., Barclay, A. N., & Driscoll, P. C. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2570131.x · Cited by 33
The cloning and expression of the gene for ovine interleukin-3 (multi-CSF) and a comparison of the in vitro hematopoietic activity of ovine IL-3 with ovine GM-CSF and human M-CSF.
McInnes, C. J., Haig, D. M., & Logan, M. (1993) · PubMed · Cited by 31
Feeding of nutrients delays apoptotic death in fed-batch cultures of recombinant NSO myeloma cells
DiSTEFANO, D. J., Mark, G. E., & Robinson, D. K. (1996) · Biotechnology Letters · doi:10.1007/bf00129733 · Cited by 30
Expression and Purification of Recombinant, Glycosylated Human Interferon Alpha 2b in Murine Myeloma NSo Cells
Rossmann, C., Sharp, N. A., Allen, G., & Gewert, D. R. (1996) · Protein Expression and Purification · doi:10.1006/prep.1996.0050 · Cited by 30
The use of serum-free medium for the production of functionally active humanised monoclonal antibody from NS0 mouse myeloma cells engineered using glutamine synthetase as a selectable marker
Keen, M. J., & Hale, C. (1996) · Cytotechnology · doi:10.1007/bf00767768 · Cited by 29
The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family.
Apte, S., Olsen, B. R., & Murphy, G. (1996) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45754-1 · Cited by 27
Optimization of a Fed‐batch Process for Production of a Recombinant Antibody
ROBINSON, D. K., Seamans, T. C., Gould, S. L., DiSTEFANO, D. J., Chan, C. P., Lee, D. K., Bibila, T. A., Glazomitsky, K., Munshi, S., Daugherty, B. L., et al. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44383.x · Cited by 25
Mammalian Cell Culture Systems for Recombinant Protein Production
Birch, J. R., & Froud, S. J. (1994) · Biologicals · doi:10.1006/biol.1994.1019 · Cited by 24
Rapid establishment of high-producing cell lines using dicistronic vectors with glutamine synthetase as the selection marker
Pu, H., Cashion, L. M., Kretschmer, P. J., & Liu, Z. (1998) · Molecular Biotechnology · doi:10.1007/bf02745860 · Cited by 23
Comparison of expression of a humanized monoclonal antibody in mouse NSO myeloma cells and Chinese Hamster Ovary cells
Peakman, T. C., Worden, J., Harris, R. H., Cooper, H. J., Tite, J. P., Pagé, M., Gewert, D. R., Bartholemew, M., Crowe, J. S., & Brett, S. J. (1994) · Human Antibodies · doi:10.3233/hab-1994-51-209 · Cited by 22
Immobilization ofCandida rugosa lipase to nylon fibers using its carbohydrate groups as the chemical link
Braun, B., Klein, E., & López, J. L. (1996) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19960805)51:3<342::aid-bit9>3.0.co;2-d · Cited by 22
A Humanized Antibody against Human Cytomegalovirus (CMV) gpUL75 (gH) for Prophylaxis or Treatment of CMV Infections
Hamilton, A., Manuel, D. M., Grundy, J. E., Turner, A. J., King, S. I., Adair, J. R., White, P., Carr, F. J., & Harris, W. J. (1997) · The Journal of Infectious Diseases · doi:10.1086/514040 · Cited by 22
Large scale production of recombinant mouse and rat growth hormone by fed-batch GS-NSO cell cultures
Zhou, W., Bibila, T. A., Glazomitsky, K., Montalyo, J., Chan, C. P., DiStefano, D. J., Munshi, S., Robinson, D., Buckland, B. C., & Aunins, J. G. (1996) · Cytotechnology · doi:10.1007/bf00353944 · Cited by 20
The LFA‐3 Adhesion Pathway is Differently Utilized by Superantigen‐Activated Human CD4+ T‐Cell Subsets
Gjörloff, A., Hedlund, G., Kalland, T., Sansom, D. M., Fischer, H., Trowsdale, J., Sjögren, H. O., & Dohlsten, M. (1992) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1992.tb03096.x · Cited by 19
Biochemical characterization of murine Fc gamma RI.
Quilliam, A. L., Osman, N., McKenzie, I. F. C., & Hogarth, P. M. (1993) · PubMed · Cited by 18
Mitogenic effects and nuclear localisation of procorticotrophin-releasing hormone expressed within stably transfected fibroblast cells (CHO-K1)
Castrol, M. G., Tomašec, P., Morrison, E. E., Murray, C. A., Hodge, P., Blanning, P., Linton, E. A., Lowry, P. J., & Lowenstein, P. R. (1995) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(94)03416-q · Cited by 18
Interaction of thyrotropin and thyroid-stimulating antibodies with recombinant extracellular region of human TSH receptor
Harfst, E., Johnstone, A. P., & Nussey, S. (1992) · The Lancet · doi:10.1016/0140-6736(92)90273-6 · Cited by 18
The production of equine monoclonal immunoglobulins by horse-mouse heterohybridomas
Richards, C. M., Aucken, H. A., Tucker, E. M., Hannant, D., Mumford, J. A., & Powell, J. R. (1992) · Veterinary Immunology and Immunopathology · doi:10.1016/0165-2427(92)90040-w · Cited by 18
NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments
McAlister, M. S. B., Davis, B. J., Pfuhl, M. A., & Driscoll, P. C. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.10.847 · Cited by 18
Effect of the Corticotrophin Releasing Hormone Precursor on Interleukin-6 Release by Human Mononuclear Cells
Salas, M. A., Brown, O. A., Perone, M. J., Castro, M. G., & Goya, R. G. (1997) · Clinical Immunology and Immunopathology · doi:10.1006/clin.1997.4395 · Cited by 16
Characterization of the glutamine synthetase amplifiable eukaryotic expression system applied to an integral membrane protein—The human thyrotropin receptor
Harfst, E., & Johnstone, A. R. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90504-z · Cited by 16
Production of recombinant proteins in serum-free media
Broad, D., Boraston, R. C., & Rhodes, M. (1991) · Cytotechnology · doi:10.1007/bf00365533 · Cited by 14
Characterization of Five Monoclonal Antibodies Raised against Domain E of the Porcine Estradiol Receptor
Thole, H., & Jakob, F. J. (2009) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/s-0029-1211216 · Cited by 14
Expression of Biologically Active Procorticotrophin‐Releasing Hormone (proCRH) in Stably Transfected CHO‐K1 Cells: Characterization of Nuclear proCRH
Morrison, E. E., Tomašec, P., Linton, E. A., Lowry, P. J., Lowenstein, P. R., & Castro, M. G. (1995) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.1995.tb00756.x · Cited by 14
Investigation of NS0 Cell Metabolic Behavior in Monoclonal Antibody Producing Clones
Bibila, T. A., Ranucci, C. S., Glazomitsky, K., Buckland, B. C., & Aunins, J. G. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44382.x · Cited by 14
Use of vectors based on gene amplification for the expression of cloned genes in mammalian cells
Bebbington, C. R. (1996) · doi:10.1093/oso/9780199634811.003.0003 · Cited by 14
A humanized CD18 antibody can block function without cell destruction.
Sims, M., Hassal, D. G., Brett, S. J., Rowan, W. C., Lockyer, M. J., Angel, A., Lewis, A., Hale, G., Waldmann, H., & Crowe, J. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.151.4.2296 · Cited by 13
Variation in IgG1 heavy chain allotype does not contribute to differences in biological activity of two human anti-Rhesus (D) monoclonal antibodies
Paterson, T., Innes, J., McMillan, L., Downing, I., & Carter, M. C. M. (1998) · Immunotechnology · doi:10.1016/s1380-2933(98)00005-0 · Cited by 13
Fluorophore‐labeled carbohydrate analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
Flesher, A. R., Marzowski, J., Wang, W., & Raff, H. V. (1995) · Biotechnology and Bioengineering · doi:10.1002/bit.260470314 · Cited by 12
Expression, Purification, and Characterization of Recombinant Human Interleukin-13 from NS-0 Cells
Cannon‐Carlson, S., Varnerin, J., Tsarbopoulos, A., Jenh, C., Cox, M. A., Chou, C., Connelly, N., Zavodny, P. J., & Tang, J. (1998) · Protein Expression and Purification · doi:10.1006/prep.1997.0835 · Cited by 11
PRODUCTION OF A CHIMERIC ANTIBODY FOR TUMOUR IMAGING AND THERAPY FROM CHINESE HAMSTER OVARY (CHO) AND MYELOMA CELLS
Field, R. P., Brand, H. N., Renner, G. L., Robertson, H. A., & Boraston, R. C. (1991) · Production of Biologicals from Animal Cells in Culture · doi:10.1016/b978-0-7506-1103-9.50134-7 · Cited by 10
The Molecular Biology of Production Cell Lines
Simonsen, C. C., & McGrogan, M. P. (1994) · Biologicals · doi:10.1006/biol.1994.1014 · Cited by 10
Production and secretion in CHO cells of the extracellular domain of AMOGβ2, a type-II membrane protein
Gloor, S. M., Nasse, K., Essen, L., & Appel, F. (1992) · Gene · doi:10.1016/0378-1119(92)90111-2 · Cited by 10
Production and characterization of monoclonal antibodies to cervine herpesvirus-1.
Lyaku, Ja, S., Pf, N., & Marsden, H. S. (1992) · PubMed · Cited by 10
Production of Engineered Antibodies in Myeloma and Hybridoma Cells
Robinson, D. K., DiSTEFANO, D. J., Gould, S. L., Cuca, G. C., Seamans, T. C., Benincasa, D., Munshi, S., Chan, C. P., Stafford-Hollis, J. M., Hollis, G. F., et al. (1995) · ACS symposium series · doi:10.1021/bk-1995-0604.ch001 · Cited by 10
STABILITY OF PRODUCTION OF RECOMBINANT ANTIBODIES FROM GLUTAMINE SYNTHETASE AMPLIFIED CHO AND NS0 CELL LINES
Hassell, T., Brand, H. N., Renner, G., Westlake, A. J., & Field, R. P. (1992) · Elsevier eBooks · doi:10.1016/b978-0-7506-0421-5.50018-0 · Cited by 9
Bispecific humanized anti-IL-2 receptor alpha beta antibodies inhibitory for both IL-2- and IL-15-mediated proliferation
Pilson, R., Levin, W. J., Desai, B. B., Reik, L. M., Lin, P., Korkmaz-Duffy, E., Campbell, E., Tso, J. Y., Kerwin, J. A., & Hakimi, J. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.3.1543 · Cited by 9
Real-time monitoring of recombinant protein concentration in animal cell cultures using an optical biosensor
Baker, K. C., Ison, A. P., Freedman, R. B., Jones, D. W., & James, D. C. (1997) · Kent Academic Repository (University of Kent) · Cited by 7
Structure and Function of CD45: A Leukocyte-Specific Protein Tyrosine Phosphatase
Trowbridge, I. S., Johnson, P., Ostergaard, H. L., & Hole, N. (1992) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-3396-2_5 · Cited by 7
THE DEVELOPMENT OF A PROCESS FOR THE PRODUCTION OF HIV1 GP120 FROM RECOMBINANT CELL LINES
Froud, S. J., Clements, G., Doyle, M. E., Harris, E. L. V., Lloyd, C., Murray, P., Preneta, A., Stephens, P. E., Thompson, S., & Yarranton, G. T. (1991) · Production of Biologicals from Animal Cells in Culture · doi:10.1016/b978-0-7506-1103-9.50032-9 · Cited by 6
Control of growth and recombinant protein synthesis by heat-shock in a mutant mammalian cell line
Hovey, A., Bebbington, C. R., & Jenkins, N. (1994) · Biotechnology Letters · doi:10.1007/bf00134614 · Cited by 6
Expression of Foreign Genes in Mammalian Cells
Pagé, M. (2003) · Humana Press eBooks · doi:10.1385/0-89603-127-6:371 · Cited by 6
Product Consistency During Long-Term Fed-Batch Culture
Robinson, D. K., Chan, C. P., Seamans, T. C., Lee, D. K., Lenny, A. B., Tung, J. S., DiSTEFANO, D. J., Munshi, S., Gould, S. L., Mark, G. E., et al. (1994) · Elsevier eBooks · doi:10.1016/b978-0-7506-1845-8.50168-x · Cited by 5
Use of a murine T-cell hybridoma expressing human T-cell receptor α- and β-gene products as a tool for the production of human T-cell receptor-specific monoclonal antibodies
Zumla, A. I., McCormack, A. M., George, A., Batchelor, R. J., & Lechler, R. I. (1992) · Human Immunology · doi:10.1016/0198-8859(92)90098-8 · Cited by 5
Production of Novel Monoclonal Antibodies Against Rabbit Platelet Factor Four
Cazzola, F., Saggin, L., & Callegaro, L. (1992) · Hybridoma · doi:10.1089/hyb.1992.11.61 · Cited by 5
The Production of Recombinant Antibodies Using the Glutamine Synthetase (GS) System
Birch, J. R., Bebbington, C. R., Field, R., Renner, G., Brand, H. N., & Finney, H. M. (1993) · Springer eBooks · doi:10.1007/978-94-011-2044-9_78 · Cited by 5
Production and Characterization of Monoclonal Antibodies Against the Ribosome Inactivating Proteins Dianthin32 and Momochin
Porro, G., Bonardi, M. A., Giovanetti, E., Lento, P. A., & Modena, D. (1994) · Hybridoma · doi:10.1089/hyb.1994.13.99 · Cited by 5
Generation of CHO Cell Mutants for Growth Control
Jenkins, N., & Hovey, A. (1993) · Springer eBooks · doi:10.1007/978-94-011-2044-9_37 · Cited by 2
Selecting and designing cell lines for improved physiological characteristics
Birch, J. R., Boraston, R. C., Metcalfe, H., Brown, M. E., Bebbington, C. R., & Field, R. P. (1994) · Current applications of cell culture engineering · doi:10.1007/978-94-011-0257-5_3 · Cited by 2
Simultaneous Control of Growth and Productivity Using a Mutant CHO Cell Line
Hovey, A., Bebbington, C. R., & Jenkins, N. (1994) · Elsevier eBooks · doi:10.1016/b978-0-7506-1845-8.50104-6 · Cited by 1
THE RAPID PRODUCTION OF RECOMBINANT RABBIT METALLOPROTEINASES IN MYELOMA CELLS
Gofton, C., Roberts, G. W., BERGIN, S., & Owens, R. J. (1992) · Elsevier eBooks · doi:10.1016/b978-0-7506-0421-5.50019-2 · Cited by 1

Research works printed but not linked: 11

Anon (1997) FDA advisory committee recommends Roche laboratories' Zenapax for the prevention of renal transplant rejection. Dialysis and Transplantation 26: 816.
Downham MR, Farrell WE & Jenkins HA (1996) Endoplasmic reticulum protein expression in recombinant NS0 myelomas grown in batch culture. Biotechnol Bioeng 51: 691–696. · DOI
Duncan PJ, Jenkins HA & Hobbs G (1997) The effect of hyperosmotic conditions on growth and recombinant protein expression by NS0 myeloma cells in culture. Genetic Engineer Biotechnologist 17: 75–78.
Field R, Cockett M & Froud SJ (1989) Glutamine synthetase amplification of TIMP expression in CHO cells. In: Spier RE, Griffiths JB, Stephenne J & Crooy PJ (eds.) Advances in Animal Cell Biology and Technology for Bioprocesses (pp. 195–197) Butterworth-Heinemann.
Gould S, DiStefano D, Cuca G, Robinson D & Silberklang M (1992) Major metabloic changes accompany transfection and selection for high level expression of recombinant genes. In Vitro Cell Dev Biol 28: 162A.
Lonza Press Release (1998) http://www.lonza.com/framer5.2.html
Murray K, Ang C-E, Gull K, Hickman JA & Dickson AJ (1996) NS0 myeloma cell death: influence of bcl-2 overexpression. Biotechnol Bioeng 51: 298–304. · DOI
Owens RJ, King DJ, Howat D, Lisle H, Mountain A, Harvey A, Bergin S, Turner A, Pedley B, Boden J, Begent R & Yarranton GT (1991) Tumor binding properties of B72.3 Fv fragments. Antibody, Immunoconjugates and Radiopharmaceuticals 4: 459–467.
Pearce A, Downham MR, Farrell WE & Jenkins HA (1995) Characterisation of the isoforms of GRP78 in a recombinant myeloma cell line. Genetic Engineer Biotechnologist 15: 285–287.
Ray NG, Rivera R, Gupta R & Mueller D (1997) Large-scale production of humanized monoclonal antibody expressed in a GS-NS0 cell line. In: Carrondo MJT, Griffiths B & Moreira JLP (eds.) Animal Cell Technology (pp 235–241) Kluwer Academic Publishers, Dordrecht.
Zhou W, Chen C-C, Buckland B & Aunins J (1997) Fed-batch culture of recombinant NS0 myeloma cells with high monoclonal antibody production. Biotechnol Bioeng 55: 783–792. · DOI

Production of recombinant protein therapeutics in cultivated mammalian cells
Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032
Human cell lines for biopharmaceutical manufacturing: history, status, and future perspectives
Dumont, J., Euwart, D., Mei, B., Estes, S., & Kshirsagar, R. (2016) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2015.1084266 · Cited by 483
Therapeutic glycoprotein production in mammalian cells
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See all 129

Authors: Barnes, L. M., Bentley, C. M., & Dickson, A. J.
Affiliations: University of Manchester (GB)
ORCID: Dickson, Alan J.
Venue: Cytotechnology
Publisher: Springer Science and Business Media LLC
Published: 2000-02
Volume: 32
Issue: 2
Pages: 109-123
ISSN: 0920-9069 (ISSN-L)
1573-0778
DOI: 10.1023/a:1008170710003
PMC: PMC3449689
OpenAlex: W1498699116
Cited by: 129
References: 172
Citations by year: 2026: 5 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 7 · 2017: 6 · 2016: 7 · 2015: 6 · 2014: 6 · 2013: 9 · 2012: 6
FWCI: 1.09
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Cytotechnology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Directorate for Biological Sciences
Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Animal Genetics and Reproduction
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
Keywords: recombinant protein expression, mammalian cell expression systems, NS0 cells, glutamine synthetase, methionine sulfoximine, post-translational modification, therapeutic proteins

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Advances in animal cell recombinant protein production: GS-NS0 expression system

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