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Volumn 7, Issue 1, 2012, Pages 61-74

Towards dynamic metabolic flux analysis in CHO cell cultures

Author keywords

Chinese hamster ovary cells; Fed batch culture; Flux dynamics; Mammalian cell culture; Metabolic network model

Indexed keywords

CHINESE HAMSTER OVARY CELLS; FED-BATCH CULTURES; FLUX DYNAMICS; MAMMALIAN CELL CULTURE; METABOLIC NETWORK;

EID: 84855596555     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201100052     Document Type: Review
Times cited : (99)

References (128)
  • 1
    • 77956690413 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks.
    • Walsh, G., Biopharmaceutical benchmarks. Nat. Biotechnol. 2010, 28, 917-924.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 917-924
    • Walsh, G.1
  • 2
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells.
    • Wurm, F. M., Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol. 2004, 22, 1393-1398.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 3
    • 75649140253 scopus 로고    scopus 로고
    • A GFP-based method facilitates clonal selection of transfected CHO cells.
    • Freimark, D., Jèrôme, V., Freitag, R., A GFP-based method facilitates clonal selection of transfected CHO cells. Biotechnol. J. 2010, 5, 24-31.
    • (2010) Biotechnol. J. , vol.5 , pp. 24-31
    • Freimark, D.1    Jèrôme, V.2    Freitag, R.3
  • 5
    • 36148950443 scopus 로고    scopus 로고
    • Protein production by large-scale mammalian cell culture
    • Makrides, S.C., (Ed.), Gene Transfer and Expression in Mammalian Cells, Elsevier
    • Xie, L., Zhou, W., Robinson, D., Protein production by large-scale mammalian cell culture, in: Makrides, S. C. (Ed.), Gene Transfer and Expression in Mammalian Cells, Elsevier 2003, pp. 605-623.
    • (2003) , pp. 605-623
    • Xie, L.1    Zhou, W.2    Robinson, D.3
  • 6
    • 84862312430 scopus 로고    scopus 로고
    • Dynamic mRNA and miRNA profiling of CHO-K1 suspension cell cultures.
    • Bort, J. A. H., Hackl, M., Höflmayer, H., Jadhav, V. et al., Dynamic mRNA and miRNA profiling of CHO-K1 suspension cell cultures. Biotechnol. J. 2011.
    • (2011) Biotechnol. J.
    • Bort, J.A.H.1    Hackl, M.2    Höflmayer, H.3    Jadhav, V.4
  • 7
    • 0030049769 scopus 로고    scopus 로고
    • Comparative analysis of glucose and glutamine metabolism in transformed mammalian cell lines, insect and primary liver cells.
    • Neermann, J., Wagner, R., Comparative analysis of glucose and glutamine metabolism in transformed mammalian cell lines, insect and primary liver cells. J. Cell. Physiol. 1996, 166, 152-169.
    • (1996) J. Cell. Physiol. , vol.166 , pp. 152-169
    • Neermann, J.1    Wagner, R.2
  • 8
    • 0029937194 scopus 로고    scopus 로고
    • The importance of ammonia in mammalian cell culture.
    • Schneider, M., Marison, I. W., vonStockar, U., The importance of ammonia in mammalian cell culture. J. Biotechnol. 1996, 46, 161-185.
    • (1996) J. Biotechnol. , vol.46 , pp. 161-185
    • Schneider, M.1    Marison, I.W.2    vonStockar, U.3
  • 9
    • 0034690723 scopus 로고    scopus 로고
    • Effects of ammonia on CHO cell growth, erythropoietin production, and glycosylation.
    • Yang, M., Butler, M., Effects of ammonia on CHO cell growth, erythropoietin production, and glycosylation. Biotechnol. Bioeng. 2000, 68, 370-380.
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 370-380
    • Yang, M.1    Butler, M.2
  • 10
    • 0031239859 scopus 로고    scopus 로고
    • Effects of ammonium and lactate on growth and metabolism of a recombinant Chinese hamster ovary cell culture.
    • Lao, M. S., Toth, D., Effects of ammonium and lactate on growth and metabolism of a recombinant Chinese hamster ovary cell culture. Biotechnol. Progr. 1997, 13, 688-691.
    • (1997) Biotechnol. Progr. , vol.13 , pp. 688-691
    • Lao, M.S.1    Toth, D.2
  • 11
    • 0026816686 scopus 로고
    • Effects of ammonia and lactate on hybridoma growth, metabolism, and antibody production.
    • Ozturk, S. S., Riley, M. R., Palsson, B. O., Effects of ammonia and lactate on hybridoma growth, metabolism, and antibody production. Biotechnol. Bioeng. 1992, 39, 418-431.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 418-431
    • Ozturk, S.S.1    Riley, M.R.2    Palsson, B.O.3
  • 12
    • 56749142714 scopus 로고    scopus 로고
    • Effect of culture temperature on erythropoietin production and glycosylation in a perfusion culture of recombinant CHO cells.
    • Ahn, W. S., Jeon, J.-J., Jeong, Y.-R., Lee, S. J., Yoon, S. K., Effect of culture temperature on erythropoietin production and glycosylation in a perfusion culture of recombinant CHO cells. Biotechnol. Bioeng. 2008, 101, 1234-1244.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 1234-1244
    • Ahn, W.S.1    Jeon, J.-J.2    Jeong, Y.-R.3    Lee, S.J.4    Yoon, S.K.5
  • 13
    • 0037420754 scopus 로고    scopus 로고
    • Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in chinese hamster ovary cells.
    • Yoon, S. K., Song, J. Y., Lee, G. M., Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in chinese hamster ovary cells. Biotechnol. Bioeng. 2003, 82, 289-298.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 289-298
    • Yoon, S.K.1    Song, J.Y.2    Lee, G.M.3
  • 14
    • 13544269403 scopus 로고    scopus 로고
    • Effects of elevated pCO2 and osmolality on growth of CHO cells and production of antibody-fusion protein B1: a case study.
    • Zhu, M. M., Goyal, A., Rank, D. L., Gupta, S. K. et al., Effects of elevated pCO2 and osmolality on growth of CHO cells and production of antibody-fusion protein B1: a case study. Biotechnol. Progr. 2005, 21, 70-77.
    • (2005) Biotechnol. Progr. , vol.21 , pp. 70-77
    • Zhu, M.M.1    Goyal, A.2    Rank, D.L.3    Gupta, S.K.4
  • 15
    • 12544253860 scopus 로고    scopus 로고
    • Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures.
    • Chee Furng Wong, D., Tin Kam Wong, K., Tang Goh, L., Kiat Heng, C., Gek Sim Yap, M., Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures. Biotechnol. Bioeng. 2005, 89, 164-177.
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 164-177
    • Chee Furng Wong, D.1    Tin Kam Wong, K.2    Tang Goh, L.3    Kiat Heng, C.4    Gek Sim Yap, M.5
  • 16
    • 77954718030 scopus 로고    scopus 로고
    • Feed development for fed-batch CHO production process by semisteady state analysis.
    • Khattak, S. F., Xing, Z., Kenty, B., Koyrakh, I., Li, Z. J., Feed development for fed-batch CHO production process by semisteady state analysis. Biotechnol. Progr. 2010, 26, 797-804.
    • (2010) Biotechnol. Progr. , vol.26 , pp. 797-804
    • Khattak, S.F.1    Xing, Z.2    Kenty, B.3    Koyrakh, I.4    Li, Z.J.5
  • 17
    • 0033952514 scopus 로고    scopus 로고
    • Improvement of CHO cell culture medium formulation: simultaneous substitution of glucose and glutamine.
    • Altamirano, C., Paredes, C., Cairó, J. J., Gòdia, F., Improvement of CHO cell culture medium formulation: simultaneous substitution of glucose and glutamine. Biotechnol. Progr. 2000, 16, 69-75.
    • (2000) Biotechnol. Progr. , vol.16 , pp. 69-75
    • Altamirano, C.1    Paredes, C.2    Cairó, J.J.3    Gòdia, F.4
  • 18
    • 34548043957 scopus 로고    scopus 로고
    • Functional expression of human pyruvate carboxylase for reduced lactic acid formation of Chinese hamster ovary cells (DG44).
    • Kim, S. H., Lee, G. M., Functional expression of human pyruvate carboxylase for reduced lactic acid formation of Chinese hamster ovary cells (DG44). Appl. Microbiol. Biotechnol. 2007, 76, 659-665.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 659-665
    • Kim, S.H.1    Lee, G.M.2
  • 19
    • 65549153512 scopus 로고    scopus 로고
    • Expression of anti-apoptosis genes alters lactate metabolism of Chinese Hamster Ovary cells in culture.
    • Dorai, H., Kyung, Y. S., Ellis, D., Kinney, C. et al., Expression of anti-apoptosis genes alters lactate metabolism of Chinese Hamster Ovary cells in culture. Biotechnol. Bioeng. 2009, 103, 592-608.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 592-608
    • Dorai, H.1    Kyung, Y.S.2    Ellis, D.3    Kinney, C.4
  • 20
    • 76749097100 scopus 로고    scopus 로고
    • Metabolic flux analysis and pharmaceutical production.
    • Boghigian, B. A., Seth, G., Kiss, R., Pfeifer, B. A., Metabolic flux analysis and pharmaceutical production. Metab. Eng. 2010, 12, 81-95.
    • (2010) Metab. Eng. , vol.12 , pp. 81-95
    • Boghigian, B.A.1    Seth, G.2    Kiss, R.3    Pfeifer, B.A.4
  • 21
    • 33845679072 scopus 로고    scopus 로고
    • Elementary metabolite units (EMU): A novel framework for modeling isotopic distributions.
    • Antoniewicz, M. R., Kelleher, J. K., Stephanopoulos, G., Elementary metabolite units (EMU): A novel framework for modeling isotopic distributions. Metab. Eng. 2007, 9, 68-86.
    • (2007) Metab. Eng. , vol.9 , pp. 68-86
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 22
    • 33745155105 scopus 로고    scopus 로고
    • Determination of confidence intervals of metabolic fluxes estimated from stable isotope measurements.
    • Antoniewicz, M. R., Kelleher, J. K., Stephanopoulos, G., Determination of confidence intervals of metabolic fluxes estimated from stable isotope measurements. Metab. Eng. 2006, 8, 324-337.
    • (2006) Metab. Eng. , vol.8 , pp. 324-337
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 23
    • 35348941242 scopus 로고    scopus 로고
    • Accurate assessment of amino acid mass isotopomer distributions for metabolic flux analysis.
    • Antoniewicz, M. R., Kelleher, J. K., Stephanopoulos, G., Accurate assessment of amino acid mass isotopomer distributions for metabolic flux analysis. Anal. Chem. 2007, 79, 7554-7559.
    • (2007) Anal. Chem. , vol.79 , pp. 7554-7559
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 24
    • 79954522565 scopus 로고    scopus 로고
    • Measuring deuterium enrichment of glucose hydrogen atoms by gas chromatography/mass spectrometry.
    • Antoniewicz, M. R., Kelleher, J. K., Stephanopoulos, G., Measuring deuterium enrichment of glucose hydrogen atoms by gas chromatography/mass spectrometry. Anal. Chem. 2011, 83, 3211-3216.
    • (2011) Anal. Chem. , vol.83 , pp. 3211-3216
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 25
    • 79952104485 scopus 로고    scopus 로고
    • Tandem mass spectrometry: a novel approach for metabolic flux analysis.
    • Choi, J., Antoniewicz, M. R., Tandem mass spectrometry: a novel approach for metabolic flux analysis. Metab. Eng. 2011, 13, 225-233.
    • (2011) Metab. Eng. , vol.13 , pp. 225-233
    • Choi, J.1    Antoniewicz, M.R.2
  • 26
    • 0030804853 scopus 로고    scopus 로고
    • Flux analysis of underdetermined metabolic networks: the quest for the missing constraints.
    • Bonarius, H. P. J., Schmid, G., Tramper, J., Flux analysis of underdetermined metabolic networks: the quest for the missing constraints. Trends Biotechnol. 1997, 15, 308-314.
    • (1997) Trends Biotechnol. , vol.15 , pp. 308-314
    • Bonarius, H.P.J.1    Schmid, G.2    Tramper, J.3
  • 27
    • 66149122278 scopus 로고    scopus 로고
    • Linking high-resolution metabolic flux phenotypes and transcriptional regulation in yeast modulated by the global regulator Gcn4p.
    • Moxley, J. F., Jewett, M. C., Antoniewicz, M. R., Villas-Boas, S. G. et al., Linking high-resolution metabolic flux phenotypes and transcriptional regulation in yeast modulated by the global regulator Gcn4p. Proc. Natl. Acad. Sci. USA 2009, 106, 6477-6482.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6477-6482
    • Moxley, J.F.1    Jewett, M.C.2    Antoniewicz, M.R.3    Villas-Boas, S.G.4
  • 28
    • 79952145912 scopus 로고    scopus 로고
    • Resolving the TCA cycle and pentose-phosphate pathway of Clostridium acetobutylicum ATCC 824: Isotopomer analysis, in vitro activities and expression analysis.
    • Crown, S. B., Indurthi, D. C., Ahn, W. S., Choi, J. et al., Resolving the TCA cycle and pentose-phosphate pathway of Clostridium acetobutylicum ATCC 824: Isotopomer analysis, in vitro activities and expression analysis. Biotechnol. J. 2011, 6, 300-305.
    • (2011) Biotechnol. J. , vol.6 , pp. 300-305
    • Crown, S.B.1    Indurthi, D.C.2    Ahn, W.S.3    Choi, J.4
  • 29
    • 0034741983 scopus 로고    scopus 로고
    • C-13 metabolic flux analysis.
    • Wiechert, W., C-13 metabolic flux analysis. Metab. Eng. 2001, 3, 195-206.
    • (2001) Metab. Eng. , vol.3 , pp. 195-206
    • Wiechert, W.1
  • 30
  • 31
    • 80555149221 scopus 로고    scopus 로고
    • Dynamic metabolic flux analysis (DMFA): A framework for determining fluxes at metabolic non-steady state.
    • Leighty, R. W., Antoniewicz, M. R., Dynamic metabolic flux analysis (DMFA): A framework for determining fluxes at metabolic non-steady state. Metab. Eng. 2011, 13, 745-755.
    • (2011) Metab. Eng. , vol.13 , pp. 745-755
    • Leighty, R.W.1    Antoniewicz, M.R.2
  • 32
    • 34249297627 scopus 로고    scopus 로고
    • Metabolic flux analysis in a nonstationary system: Fed-batch fermentation of a high yielding strain of E. coli producing 1, 3-propanediol.
    • Antoniewicz, M. R., Kraynie, D. F., Laffend, L. A., Gonzalez-Lergier, J. et al., Metabolic flux analysis in a nonstationary system: Fed-batch fermentation of a high yielding strain of E. coli producing 1, 3-propanediol. Metab. Eng. 2007, 9, 277-292.
    • (2007) Metab. Eng. , vol.9 , pp. 277-292
    • Antoniewicz, M.R.1    Kraynie, D.F.2    Laffend, L.A.3    Gonzalez-Lergier, J.4
  • 33
    • 79956205237 scopus 로고    scopus 로고
    • Quantitative characterization of metabolism and metabolic shifts during growth of the new human cell line AGE1.HN using time resolved metabolic flux analysis.
    • Niklas, J., Schräder, E., Sandig, V., Noll, T., Heinzle, E., Quantitative characterization of metabolism and metabolic shifts during growth of the new human cell line AGE1.HN using time resolved metabolic flux analysis. Bioproc. Biosystems Eng. 2011, 34, 533-545.
    • (2011) Bioproc. Biosystems Eng. , vol.34 , pp. 533-545
    • Niklas, J.1    Schräder, E.2    Sandig, V.3    Noll, T.4    Heinzle, E.5
  • 34
    • 77957828847 scopus 로고    scopus 로고
    • Dynamic metabolic flux analysis demonstrated on cultures where the limiting substrate is changed from carbon to nitrogen and vice versa.
    • Lequeux, G., Beauprez, J., Maertens, J., Van Horen, E. et al., Dynamic metabolic flux analysis demonstrated on cultures where the limiting substrate is changed from carbon to nitrogen and vice versa. J. Biomed. Biotechnol. 2010, 2010.
    • (2010) J. Biomed. Biotechnol. , vol.2010
    • Lequeux, G.1    Beauprez, J.2    Maertens, J.3    Van Horen, E.4
  • 35
    • 38749117205 scopus 로고    scopus 로고
    • A procedure for the estimation over time of metabolic fluxes in scenarios where measurements are uncertain and/or insufficient.
    • Llaneras, F., Picó, J., A procedure for the estimation over time of metabolic fluxes in scenarios where measurements are uncertain and/or insufficient. BMC Bioinformatics 8, 421-421.
    • BMC Bioinformatics , vol.8 , pp. 421-421
    • Llaneras, F.1    Picó, J.2
  • 37
    • 12444279265 scopus 로고
    • On the origin of cancer cells.
    • Warburg, O., On the origin of cancer cells. Science (New York, NY) 1956, 123, 309-314.
    • (1956) Science (New York, NY) , vol.123 , pp. 309-314
    • Warburg, O.1
  • 38
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: the metabolic requirements of cell proliferation.
    • Vander Heiden, M. G., Cantley, L. C., Thompson, C. B., Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science (New York, NY) 2009, 324, 1029-1033.
    • (2009) Science (New York, NY) , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 39
    • 33646549629 scopus 로고    scopus 로고
    • Metabolism of PER.C6 cells cultivated under fed-batch conditions at low glucose and glutamine levels.
    • Maranga, L., Goochee, C. F., Metabolism of PER.C6 cells cultivated under fed-batch conditions at low glucose and glutamine levels. Biotechnol. Bioeng. 2006, 94, 139-150.
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 139-150
    • Maranga, L.1    Goochee, C.F.2
  • 40
    • 0032586148 scopus 로고    scopus 로고
    • Metabolic shifts by nutrient manipulation in continuous cultures of BHK cells.
    • Cruz, H. J., Moreira, J. L., Carrondo, M. J., Metabolic shifts by nutrient manipulation in continuous cultures of BHK cells. Biotechnol. Bioeng. 1999, 66, 104-113.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 104-113
    • Cruz, H.J.1    Moreira, J.L.2    Carrondo, M.J.3
  • 41
    • 0026254351 scopus 로고
    • Growth, metabolic, and antibody production kinetics of hybridoma cell culture: 1. Analysis of data from controlled batch reactors.
    • Ozturk, S. S., Palsson, B. O., Growth, metabolic, and antibody production kinetics of hybridoma cell culture: 1. Analysis of data from controlled batch reactors. Biotechnol. Progr. 1991, 7, 471-480.
    • (1991) Biotechnol. Progr. , vol.7 , pp. 471-480
    • Ozturk, S.S.1    Palsson, B.O.2
  • 42
    • 14244265076 scopus 로고    scopus 로고
    • Effect of culture pH on erythropoietin production by Chinese hamster ovary cells grown in suspension at 32.5 and 37.0 degrees C.
    • Yoon, S. K., Choi, S. L., Song, J. Y., Lee, G. M., Effect of culture pH on erythropoietin production by Chinese hamster ovary cells grown in suspension at 32.5 and 37.0 degrees C. Biotechnol. Bioeng. 2005, 89, 345-356.
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 345-356
    • Yoon, S.K.1    Choi, S.L.2    Song, J.Y.3    Lee, G.M.4
  • 43
    • 0028500473 scopus 로고
    • Catabolic control of hybridoma cells by glucose and glutamine limited fed batch cultures.
    • Ljunggren, J., Häggström, L., Catabolic control of hybridoma cells by glucose and glutamine limited fed batch cultures. Biotechnol. Bioeng. 1994, 44, 808-818.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 808-818
    • Ljunggren, J.1    Häggström, L.2
  • 44
    • 0021894460 scopus 로고
    • The glucose transporter of mammalian cells.
    • Wheeler, T. J., Hinkle, P. C., The glucose transporter of mammalian cells. Annu. Rev. Physiol. 1985, 47, 503-517.
    • (1985) Annu. Rev. Physiol. , vol.47 , pp. 503-517
    • Wheeler, T.J.1    Hinkle, P.C.2
  • 46
    • 0027112176 scopus 로고
    • Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation.
    • Omasa, T., Higashiyama, K. I., Shioya, S., Suga, K. I., Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation. Biotechnol. Bioeng. 1992, 39, 556-564.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 556-564
    • Omasa, T.1    Higashiyama, K.I.2    Shioya, S.3    Suga, K.I.4
  • 47
    • 0034606665 scopus 로고    scopus 로고
    • Multiple steady states with distinct cellular metabolism in continuous culture of mammalian cells.
    • Europa, A. F., Gambhir, A., Fu, P. C., Hu, W. S., Multiple steady states with distinct cellular metabolism in continuous culture of mammalian cells. Biotechnol. Bioeng. 2000, 67, 25-34.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 25-34
    • Europa, A.F.1    Gambhir, A.2    Fu, P.C.3    Hu, W.S.4
  • 48
    • 0028765274 scopus 로고
    • Growth characteristics in fed-batch culture of hybridoma cells with control of glucose and glutamine concentrations.
    • Kurokawa, H., Park, Y. S., Iijima, S., Kobayashi, T., Growth characteristics in fed-batch culture of hybridoma cells with control of glucose and glutamine concentrations. Biotechnol. Bioeng. 1994, 44, 95-103.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 95-103
    • Kurokawa, H.1    Park, Y.S.2    Iijima, S.3    Kobayashi, T.4
  • 49
    • 0029059493 scopus 로고
    • High viable cell concentration fed-batch cultures of hybridoma cells through on-line nutrient feeding.
    • Zhou, W., Rehm, J., Hu, W. S., High viable cell concentration fed-batch cultures of hybridoma cells through on-line nutrient feeding. Biotechnol. Bioeng. 1995, 46, 579-587.
    • (1995) Biotechnol. Bioeng. , vol.46 , pp. 579-587
    • Zhou, W.1    Rehm, J.2    Hu, W.S.3
  • 50
    • 0038367650 scopus 로고    scopus 로고
    • Analysis of cellular metabolism of hybridoma cells at distinct physiological states.
    • Gambhir, A., Korke, R., Lee, J., Fu, P.-C. et al., Analysis of cellular metabolism of hybridoma cells at distinct physiological states. J. Biosci. Bioeng. 2003, 95, 317-327.
    • (2003) J. Biosci. Bioeng. , vol.95 , pp. 317-327
    • Gambhir, A.1    Korke, R.2    Lee, J.3    Fu, P.-C.4
  • 51
    • 0346363685 scopus 로고    scopus 로고
    • Large scale gene expression profiling of metabolic shift of mammalian cells in culture.
    • Korke, R., Gatti, M. D., Lau, A. L. Y., Lim, J. W. E. et al., Large scale gene expression profiling of metabolic shift of mammalian cells in culture. J. Biotechnol. 2004, 107, 1-17.
    • (2004) J. Biotechnol. , vol.107 , pp. 1-17
    • Korke, R.1    Gatti, M.D.2    Lau, A.L.Y.3    Lim, J.W.E.4
  • 52
    • 0035515020 scopus 로고    scopus 로고
    • Proteomic investigation of metabolic shift in mammalian cell culture.
    • Seow, T. K., Korke, R., Liang, R. C., Ong, S. E. et al., Proteomic investigation of metabolic shift in mammalian cell culture. Biotechnol. Progr. 2001, 17, 1137-1144.
    • (2001) Biotechnol. Progr. , vol.17 , pp. 1137-1144
    • Seow, T.K.1    Korke, R.2    Liang, R.C.3    Ong, S.E.4
  • 53
    • 0038714272 scopus 로고    scopus 로고
    • Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function.
    • Wilson, J. E., Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J. Exp. Biol. 2003, 206, 2049-2057.
    • (2003) J. Exp. Biol. , vol.206 , pp. 2049-2057
    • Wilson, J.E.1
  • 54
    • 0027692808 scopus 로고
    • Glucose and glutamine metabolism of a murine B-lymphocyte hybridoma grown in batch culture.
    • Fitzpatrick, L., Jenkins, H. A., Butler, M., Glucose and glutamine metabolism of a murine B-lymphocyte hybridoma grown in batch culture. Appl. Biochem. Biotechnol. 1993, 43, 93-116.
    • (1993) Appl. Biochem. Biotechnol. , vol.43 , pp. 93-116
    • Fitzpatrick, L.1    Jenkins, H.A.2    Butler, M.3
  • 55
    • 79951699777 scopus 로고    scopus 로고
    • Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme.
    • Wolf, A., Agnihotri, S., Micallef, J., Mukherjee, J. et al., Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme. J. Exp. Med. 2011, 208, 313-326.
    • (2011) J. Exp. Med. , vol.208 , pp. 313-326
    • Wolf, A.1    Agnihotri, S.2    Micallef, J.3    Mukherjee, J.4
  • 56
    • 40749163248 scopus 로고    scopus 로고
    • The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth.
    • Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A. et al., The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 2008, 452, 230-233.
    • (2008) Nature , vol.452 , pp. 230-233
    • Christofk, H.R.1    Vander Heiden, M.G.2    Harris, M.H.3    Ramanathan, A.4
  • 57
    • 0032486571 scopus 로고    scopus 로고
    • Fluxes and enzyme activities in central metabolism of myeloma cells grown in chemostat culture.
    • Vriezen, N., van Dijken, J. P., Fluxes and enzyme activities in central metabolism of myeloma cells grown in chemostat culture. Biotechnol. Bioeng. 1998, 59, 28-39.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 28-39
    • Vriezen, N.1    van Dijken, J.P.2
  • 58
    • 0028077867 scopus 로고
    • Profile of energy metabolism in a murine hybridoma: glucose and glutamine utilization.
    • Petch, D., Butler, M., Profile of energy metabolism in a murine hybridoma: glucose and glutamine utilization. J. Cell. Physiol. 1994, 161, 71-76.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 71-76
    • Petch, D.1    Butler, M.2
  • 59
    • 23844547597 scopus 로고    scopus 로고
    • Engineering mammalian cell factories for improved recombinant monoclonal antibody production: lessons from nature?
    • Dinnis, D. M., James, D. C., Engineering mammalian cell factories for improved recombinant monoclonal antibody production: lessons from nature? Biotechnol. Bioeng. 2005, 91, 180-189.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 180-189
    • Dinnis, D.M.1    James, D.C.2
  • 60
    • 0033385223 scopus 로고    scopus 로고
    • Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction.
    • Irani, N., Wirth, M., van Den Heuvel, J., Wagner, R., Improvement of the primary metabolism of cell cultures by introducing a new cytoplasmic pyruvate carboxylase reaction. Biotechnol. Bioeng. 1999, 66, 238-246.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 238-246
    • Irani, N.1    Wirth, M.2    van Den Heuvel, J.3    Wagner, R.4
  • 61
    • 0037186256 scopus 로고    scopus 로고
    • Expression of recombinant cytoplasmic yeast pyruvate carboxylase for the improvement of the production of human erythropoietin by recombinant BHK-21 cells.
    • Irani, N., Beccaria, A. J., Wagner, R., Expression of recombinant cytoplasmic yeast pyruvate carboxylase for the improvement of the production of human erythropoietin by recombinant BHK-21 cells. J. Biotechnol. 2002, 93, 269-282.
    • (2002) J. Biotechnol. , vol.93 , pp. 269-282
    • Irani, N.1    Beccaria, A.J.2    Wagner, R.3
  • 62
    • 0037274314 scopus 로고    scopus 로고
    • Improving glucose and glutamine metabolism of human HEK 293 and Trichoplusiani insect cells engineered to express a cytosolic pyruvate carboxylase enzyme.
    • Elias, C. B., Carpentier, E., Durocher, Y., Bisson, L. et al., Improving glucose and glutamine metabolism of human HEK 293 and Trichoplusiani insect cells engineered to express a cytosolic pyruvate carboxylase enzyme. Biotechnol. Progr. 2003, 19, 90-97.
    • (2003) Biotechnol. Progr. , vol.19 , pp. 90-97
    • Elias, C.B.1    Carpentier, E.2    Durocher, Y.3    Bisson, L.4
  • 63
    • 1842425836 scopus 로고    scopus 로고
    • Impact of temperature reduction and expression of yeast pyruvate carboxylase on hGM-CSF-producing CHO cells.
    • Fogolín, M. B., Wagner, R., Etcheverrigaray, M., Kratje, R., Impact of temperature reduction and expression of yeast pyruvate carboxylase on hGM-CSF-producing CHO cells. J. Biotechnol. 2004, 109, 179-191.
    • (2004) J. Biotechnol. , vol.109 , pp. 179-191
    • Fogolín, M.B.1    Wagner, R.2    Etcheverrigaray, M.3    Kratje, R.4
  • 64
    • 0035808169 scopus 로고    scopus 로고
    • Engineering of a mammalian cell line for reduction of lactate formation and high monoclonal antibody production.
    • Chen, K., Liu, Q., Xie, L., Sharp, P. A., Wang, D. I., Engineering of a mammalian cell line for reduction of lactate formation and high monoclonal antibody production. Biotechnol. Bioeng. 2001, 72, 55-61.
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 55-61
    • Chen, K.1    Liu, Q.2    Xie, L.3    Sharp, P.A.4    Wang, D.I.5
  • 65
    • 33745891791 scopus 로고    scopus 로고
    • Effects of lactate dehydrogenase suppression and glycerol-3-phosphate dehydrogenase overexpression on cellular metabolism.
    • Jeong, D. W., Cho, I. T., Kim, T. S., Bae, G. W. et al., Effects of lactate dehydrogenase suppression and glycerol-3-phosphate dehydrogenase overexpression on cellular metabolism. Mol. Cell. Biochem. 2006, 284, 1-8.
    • (2006) Mol. Cell. Biochem. , vol.284 , pp. 1-8
    • Jeong, D.W.1    Cho, I.T.2    Kim, T.S.3    Bae, G.W.4
  • 66
    • 33846643485 scopus 로고    scopus 로고
    • Down-regulation of lactate dehydrogenase-A by siRNAs for reduced lactic acid formation of Chinese hamster ovary cells producing thrombopoietin.
    • Kim, S. H., Lee, G. M., Down-regulation of lactate dehydrogenase-A by siRNAs for reduced lactic acid formation of Chinese hamster ovary cells producing thrombopoietin. Appl. Microbiol. Biotechnol. 2007, 74, 152-159.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 152-159
    • Kim, S.H.1    Lee, G.M.2
  • 68
    • 0032562785 scopus 로고    scopus 로고
    • Importance of glucose-6-phosphate dehydrogenase activity for cell growth.
    • Tian, W.-N., Braunstein, L. D., Pang, J., Stuhlmeier, K. M. et al., Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J. Biol. Chem. 1998, 273, 10609-10617.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10609-10617
    • Tian, W.-N.1    Braunstein, L.D.2    Pang, J.3    Stuhlmeier, K.M.4
  • 69
    • 0034045004 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase and the oxidative pentose phosphate cycle protect cells against apoptosis induced by low doses of ionizing radiation.
    • Tuttle, S., Stamato, T., Perez, M. L., Biaglow, J., Glucose-6-phosphate dehydrogenase and the oxidative pentose phosphate cycle protect cells against apoptosis induced by low doses of ionizing radiation. Radiation Res. 2000, 153, 781-787.
    • (2000) Radiation Res. , vol.153 , pp. 781-787
    • Tuttle, S.1    Stamato, T.2    Perez, M.L.3    Biaglow, J.4
  • 70
    • 4344624553 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase plays a crucial role in protection from redox-stress-induced apoptosis.
    • Fico, A., Paglialunga, F., Cigliano, L., Abrescia, P. et al., Glucose-6-phosphate dehydrogenase plays a crucial role in protection from redox-stress-induced apoptosis. Cell Death Differ. 2004, 11, 823-831.
    • (2004) Cell Death Differ. , vol.11 , pp. 823-831
    • Fico, A.1    Paglialunga, F.2    Cigliano, L.3    Abrescia, P.4
  • 71
    • 33745918951 scopus 로고    scopus 로고
    • TIGAR, a p53-inducible regulator of glycolysis and apoptosis.
    • Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C. et al., TIGAR, a p53-inducible regulator of glycolysis and apoptosis. Cell 2006, 126, 107-120.
    • (2006) Cell , vol.126 , pp. 107-120
    • Bensaad, K.1    Tsuruta, A.2    Selak, M.A.3    Vidal, M.N.C.4
  • 72
    • 0033056271 scopus 로고    scopus 로고
    • Importance of glucose-6-phosphate dehydrogenase activity in cell death.
    • Tian, W. N., Braunstein, L. D., Apse, K., Pang, J. et al., Importance of glucose-6-phosphate dehydrogenase activity in cell death. Am. J. Physiol. 1999, 276, C1121-1131.
    • (1999) Am. J. Physiol. , vol.276
    • Tian, W.N.1    Braunstein, L.D.2    Apse, K.3    Pang, J.4
  • 73
    • 0007943192 scopus 로고
    • Effects of thiamine deficiency and of oxythiamine on rat tissue transketolase.
    • Brin, M., Effects of thiamine deficiency and of oxythiamine on rat tissue transketolase. J. Nutr. 1962, 78, 179-183.
    • (1962) J. Nutr. , vol.78 , pp. 179-183
    • Brin, M.1
  • 74
    • 0031804597 scopus 로고    scopus 로고
    • Mass isotopomer study of the nonoxidative pathways of the pentose cycle with [1,2-13C2]glucose.
    • Lee, W. N., Boros, L. G., Puigjaner, J., Bassilian, S. et al., Mass isotopomer study of the nonoxidative pathways of the pentose cycle with [1, 2-13C2]glucose. Am. J. Physiol. 1998, 274, E843-851.
    • (1998) Am. J. Physiol. , vol.274
    • Lee, W.N.1    Boros, L.G.2    Puigjaner, J.3    Bassilian, S.4
  • 75
    • 0030758923 scopus 로고    scopus 로고
    • Oxythiamine and dehydroepiandrosterone inhibit the nonoxidative synthesis of ribose and tumor cell proliferation.
    • Boros, L. G., Puigjaner, J., Cascante, M., Lee, W. N. P. et al., Oxythiamine and dehydroepiandrosterone inhibit the nonoxidative synthesis of ribose and tumor cell proliferation. Cancer Res. 1997, 57, 4242-4248.
    • (1997) Cancer Res. , vol.57 , pp. 4242-4248
    • Boros, L.G.1    Puigjaner, J.2    Cascante, M.3    Lee, W.N.P.4
  • 76
    • 64649105051 scopus 로고    scopus 로고
    • Overexpression of transketolase-like gene 1 is associated with cell proliferation in uterine cervix cancer.
    • Chen, H., Yue, J.-X., Yang, S.-H., Ding, H. et al., Overexpression of transketolase-like gene 1 is associated with cell proliferation in uterine cervix cancer. J. Exp. Clin. Cancer Res. CR 2009, 28, 43-43.
    • (2009) J. Exp. Clin. Cancer Res. CR , vol.28 , pp. 43-43
    • Chen, H.1    Yue, J.-X.2    Yang, S.-H.3    Ding, H.4
  • 77
    • 0029099953 scopus 로고
    • Regulation of glutaminase activity and glutamine metabolism.
    • Curthoys, N. P., Watford, M., Regulation of glutaminase activity and glutamine metabolism. Annu. Rev. Nutr. 1995, 15, 133-159.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 133-159
    • Curthoys, N.P.1    Watford, M.2
  • 78
    • 0027190598 scopus 로고
    • A 1H/15N n.m.r. study of nitrogen metabolism in cultured mammalian cells.
    • Street, J. C., Delort, A. M., Braddock, P. S., Brindle, K. M., A 1H/15N n.m.r. study of nitrogen metabolism in cultured mammalian cells. Biochem. J. 1993, 291, 485-492.
    • (1993) Biochem. J. , vol.291 , pp. 485-492
    • Street, J.C.1    Delort, A.M.2    Braddock, P.S.3    Brindle, K.M.4
  • 79
    • 0032553386 scopus 로고    scopus 로고
    • Elevated glutamate dehydrogenase flux in glucose-deprived hybridoma and myeloma cells: evidence from 1H/15N NMR.
    • Martinelle, K., Doverskog, M., Jacobsson, U., Chapman, B. E. et al., Elevated glutamate dehydrogenase flux in glucose-deprived hybridoma and myeloma cells: evidence from 1H/15N NMR. Biotechnol. Bioeng. 1998, 60, 508-517.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 508-517
    • Martinelle, K.1    Doverskog, M.2    Jacobsson, U.3    Chapman, B.E.4
  • 80
    • 0000409606 scopus 로고
    • Spontaneous decomposition of glutamine in cell culture media.
    • Tritsch, G. L., Moore, G. E., Spontaneous decomposition of glutamine in cell culture media. Exp. Cell Res. 1962, 28, 360-364.
    • (1962) Exp. Cell Res. , vol.28 , pp. 360-364
    • Tritsch, G.L.1    Moore, G.E.2
  • 81
    • 0025397850 scopus 로고
    • Chemical decomposition of glutamine in cell culture media: effect of media type, pH, and serum concentration.
    • Ozturk, S. S., Palsson, B. O., Chemical decomposition of glutamine in cell culture media: effect of media type, pH, and serum concentration. Biotechnol. Progr. 1990, 6, 121-128.
    • (1990) Biotechnol. Progr. , vol.6 , pp. 121-128
    • Ozturk, S.S.1    Palsson, B.O.2
  • 82
    • 0023698966 scopus 로고
    • Glutamine decomposition in DMEM: Effect of pH and serum concentration.
    • Lin, A., Agrawal, P., Glutamine decomposition in DMEM: Effect of pH and serum concentration. Biotechnol. Lett. 1988, 10, 695-698.
    • (1988) Biotechnol. Lett. , vol.10 , pp. 695-698
    • Lin, A.1    Agrawal, P.2
  • 83
    • 0343007769 scopus 로고
    • The enzymic hydrolysis of glutamine and its spontaneous decomposition in buffer solutions.
    • Bray, H. G., James, S. P., Raffan, I. M., Thorpe, W. V., The enzymic hydrolysis of glutamine and its spontaneous decomposition in buffer solutions. Biochem. J. 1949, 44, 625-627.
    • (1949) Biochem. J. , vol.44 , pp. 625-627
    • Bray, H.G.1    James, S.P.2    Raffan, I.M.3    Thorpe, W.V.4
  • 84
    • 78349269949 scopus 로고    scopus 로고
    • CHO-K1 host cells adapted to growth in glutamine-free medium by FACS-assisted evolution.
    • Bort, J. A. H., Stern, B., Borth, N., CHO-K1 host cells adapted to growth in glutamine-free medium by FACS-assisted evolution. Biotechnol. J. 2010, 5, 1090-1097.
    • (2010) Biotechnol. J. , vol.5 , pp. 1090-1097
    • Bort, J.A.H.1    Stern, B.2    Borth, N.3
  • 86
    • 0034281427 scopus 로고    scopus 로고
    • Effect of ammonia on the glycosylation of human recombinant erythropoietin in culture.
    • Yang, M., Butler, M., Effect of ammonia on the glycosylation of human recombinant erythropoietin in culture. Biotechnol. Progr. 2000, 16, 751-759.
    • (2000) Biotechnol. Progr. , vol.16 , pp. 751-759
    • Yang, M.1    Butler, M.2
  • 87
    • 0026196692 scopus 로고
    • Growth inhibition in animal cell culture. The effect of lactate and ammonia.
    • Hassell, T., Gleave, S., Butler, M., Growth inhibition in animal cell culture. The effect of lactate and ammonia. Appl. Biochem. Biotechnol. 1991, 30, 29-41.
    • (1991) Appl. Biochem. Biotechnol. , vol.30 , pp. 29-41
    • Hassell, T.1    Gleave, S.2    Butler, M.3
  • 88
    • 0026018555 scopus 로고
    • Growth inhibition of hybridoma cells by ammonium ion: correlation with effects on intracellular pH.
    • McQueen, A., Bailey, J. E., Growth inhibition of hybridoma cells by ammonium ion: correlation with effects on intracellular pH. Bioproc. Eng. 1990, 6, 49-61.
    • (1990) Bioproc. Eng. , vol.6 , pp. 49-61
    • McQueen, A.1    Bailey, J.E.2
  • 89
    • 0027952407 scopus 로고
    • Influence of ammonium on growth, metabolism, and productivity of a continuous suspension Chinese hamster ovary cell culture.
    • Hansen, H. A., Emborg, C., Influence of ammonium on growth, metabolism, and productivity of a continuous suspension Chinese hamster ovary cell culture. Biotechnol. Progr. 1994, 10, 121-124.
    • (1994) Biotechnol. Progr. , vol.10 , pp. 121-124
    • Hansen, H.A.1    Emborg, C.2
  • 90
    • 0029636676 scopus 로고
    • The effect of ammonia on the O-linked glycosylation of granulocyte colony-stimulating factor produced by Chinese hamster ovary cells.
    • Andersen, D. C., Goochee, C. F., The effect of ammonia on the O-linked glycosylation of granulocyte colony-stimulating factor produced by Chinese hamster ovary cells. Biotechnol. Bioeng. 1995, 47, 96-105.
    • (1995) Biotechnol. Bioeng. , vol.47 , pp. 96-105
    • Andersen, D.C.1    Goochee, C.F.2
  • 91
    • 0028393399 scopus 로고
    • Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-I by Chinese hamster ovary cells in a pH-dependent manner.
    • Borys, M. C., Linzer, D. I., Papoutsakis, E. T., Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-I by Chinese hamster ovary cells in a pH-dependent manner. Biotechnol. Bioeng. 1994, 43, 505-514.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 505-514
    • Borys, M.C.1    Linzer, D.I.2    Papoutsakis, E.T.3
  • 92
    • 0022530474 scopus 로고
    • Chloroquine and ammonium chloride prevent terminal glycosylation of immunoglobulins in plasma cells without affecting secretion.
    • Thorens, B., Vassalli, P., Chloroquine and ammonium chloride prevent terminal glycosylation of immunoglobulins in plasma cells without affecting secretion. Nature 1986, 321, 618-620.
    • (1986) Nature , vol.321 , pp. 618-620
    • Thorens, B.1    Vassalli, P.2
  • 93
    • 0036008002 scopus 로고    scopus 로고
    • Effects of ammonia and glucosamine on the heterogeneity of erythropoietin glycoforms.
    • Yang, M., Butler, M., Effects of ammonia and glucosamine on the heterogeneity of erythropoietin glycoforms. Biotechnol. Progr. 2002, 18, 129-138.
    • (2002) Biotechnol. Progr. , vol.18 , pp. 129-138
    • Yang, M.1    Butler, M.2
  • 95
    • 11944265249 scopus 로고
    • 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., High level expression of tissue inhibitor of metalloproteinases in Chinese hamster ovary cells using glutamine synthetase gene amplification. Bio/Technology (Nature Publishing Company) 1990, 8, 662-667.
    • (1990) Bio/Technology (Nature Publishing Company) , vol.8 , pp. 662-667
    • Cockett, M.I.1    Bebbington, C.R.2    Yarranton, G.T.3
  • 96
    • 14744283551 scopus 로고
    • 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. et al., High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Bio/Technology (Nature Publishing Company) 1992, 10, 169-175.
    • (1992) Bio/Technology (Nature Publishing Company) , vol.10 , pp. 169-175
    • Bebbington, C.R.1    Renner, G.2    Thomson, S.3    King, D.4
  • 97
    • 0026560877 scopus 로고
    • Characterization of glutamine metabolism in two related murine hybridomas.
    • Jenkins, H. A., Butler, M., Dickson, A. J., Characterization of glutamine metabolism in two related murine hybridomas. J. Biotechnol. 1992, 23, 167-182.
    • (1992) J. Biotechnol. , vol.23 , pp. 167-182
    • Jenkins, H.A.1    Butler, M.2    Dickson, A.J.3
  • 98
    • 1642460583 scopus 로고    scopus 로고
    • Characterisation of G418-induced metabolic load in recombinant CHO and BHK cells: effect on the activity and expression of central metabolic enzymes.
    • Yallop, C. A., Norby, P. L., Jensen, R., Reinbach, H., Svendsen, I., Characterisation of G418-induced metabolic load in recombinant CHO and BHK cells: effect on the activity and expression of central metabolic enzymes. Cytotechnology 2003, 42, 87-99.
    • (2003) Cytotechnology , vol.42 , pp. 87-99
    • Yallop, C.A.1    Norby, P.L.2    Jensen, R.3    Reinbach, H.4    Svendsen, I.5
  • 99
    • 84555201597 scopus 로고    scopus 로고
    • Metabolic flux analysis of mammalian cells
    • Al-Rubeai, M., Fussenegger, M. (Eds.), Systems Biology, Springer Netherlands, Dordrecht
    • Martens, D. E., Metabolic flux analysis of mammalian cells, in: Al-Rubeai, M., Fussenegger, M. (Eds.), Systems Biology, Springer Netherlands, Dordrecht 2007, pp. 275-299.
    • (2007) , pp. 275-299
    • Martens, D.E.1
  • 100
    • 79957858590 scopus 로고    scopus 로고
    • Optimizing amino acid composition of CHO cell culture media for a fusion protein production.
    • Xing, Z., Kenty, B., Koyrakh, I., Borys, M. et al., Optimizing amino acid composition of CHO cell culture media for a fusion protein production. Proc. Biochem. 2011, 46, 1423-1429.
    • (2011) Proc. Biochem. , vol.46 , pp. 1423-1429
    • Xing, Z.1    Kenty, B.2    Koyrakh, I.3    Borys, M.4
  • 102
    • 0033524678 scopus 로고    scopus 로고
    • Metabolic effects on recombinant interferon-gamma glycosylation in continuous culture of Chinese hamster ovary cells.
    • Nyberg, G. B., Balcarcel, R. R., Follstad, B. D., Stephanopoulos, G., Wang, D. I., Metabolic effects on recombinant interferon-gamma glycosylation in continuous culture of Chinese hamster ovary cells. Biotechnol. Bioeng. 1999, 62, 336-347.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 336-347
    • Nyberg, G.B.1    Balcarcel, R.R.2    Follstad, B.D.3    Stephanopoulos, G.4    Wang, D.I.5
  • 103
    • 0035543345 scopus 로고    scopus 로고
    • Analysis of CHO cells metabolic redistribution in a glutamate-based defined medium in continuous culture.
    • Altamirano, C., Illanes, A., Casablancas, A., Gamez, X. et al., Analysis of CHO cells metabolic redistribution in a glutamate-based defined medium in continuous culture. Biotechnol. Progr. 2001, 17, 1032-1041.
    • (2001) Biotechnol. Progr. , vol.17 , pp. 1032-1041
    • Altamirano, C.1    Illanes, A.2    Casablancas, A.3    Gamez, X.4
  • 104
    • 33748300981 scopus 로고    scopus 로고
    • Considerations on the lactate consumption by CHO cells in the presence of galactose.
    • Altamirano, C., Illanes, A., Becerra, S., Cairó, J. J., Gòdia, F., Considerations on the lactate consumption by CHO cells in the presence of galactose. J. Biotechnol. 2006, 125, 547-556.
    • (2006) J. Biotechnol. , vol.125 , pp. 547-556
    • Altamirano, C.1    Illanes, A.2    Becerra, S.3    Cairó, J.J.4    Gòdia, F.5
  • 105
    • 80052032471 scopus 로고    scopus 로고
    • Metabolic flux analysis of CHO cells at growth and non-growth phases using isotopic tracers and mass spectrometry.
    • Ahn, W. S., Antoniewicz, M. R., Metabolic flux analysis of CHO cells at growth and non-growth phases using isotopic tracers and mass spectrometry. Metab. Eng. 2011, 13, 598-609.
    • (2011) Metab. Eng. , vol.13 , pp. 598-609
    • Ahn, W.S.1    Antoniewicz, M.R.2
  • 106
    • 69149093375 scopus 로고    scopus 로고
    • Error propagation from prime variables into specific rates and metabolic fluxes for mammalian cells in perfusion culture.
    • Goudar, C. T., Biener, R., Konstantinov, K. B., Piret, J. M., Error propagation from prime variables into specific rates and metabolic fluxes for mammalian cells in perfusion culture. Biotechnol. Progr. 2009, 25, 986-998.
    • (2009) Biotechnol. Progr. , vol.25 , pp. 986-998
    • Goudar, C.T.1    Biener, R.2    Konstantinov, K.B.3    Piret, J.M.4
  • 107
    • 33749237095 scopus 로고    scopus 로고
    • Towards industrial application of quasi real-time metabolic flux analysis for mammalian cell culture.
    • Cell culture engineering, Advances in Biochemical Engineering/Biotechnology Springer, New York
    • Goudar, C., Biener, R., Zhang, C., Michaels, J. et al., Towards industrial application of quasi real-time metabolic flux analysis for mammalian cell culture. in Cell culture engineering, Vol. 101, Advances in Biochemical Engineering/Biotechnology Springer, New York 2006, pp. 99-118.
    • (2006) , vol.101 , pp. 99-118
    • Goudar, C.1    Biener, R.2    Zhang, C.3    Michaels, J.4
  • 108
    • 78649447462 scopus 로고    scopus 로고
    • A detailed metabolic flux analysis of an underdetermined network of CHO cells.
    • Zamorano, F., Wouwer, A. V., Bastin, G., A detailed metabolic flux analysis of an underdetermined network of CHO cells. J. Biotechnol. 2010, 150, 497-508.
    • (2010) J. Biotechnol. , vol.150 , pp. 497-508
    • Zamorano, F.1    Wouwer, A.V.2    Bastin, G.3
  • 109
    • 76749123832 scopus 로고    scopus 로고
    • Metabolic flux analysis in mammalian cell culture.
    • Quek, L. E., Dietmair, S., Kromer, J. O., Nielsen, L. K., Metabolic flux analysis in mammalian cell culture. Metab. Eng. 2010, 12, 161-171.
    • (2010) Metab. Eng. , vol.12 , pp. 161-171
    • Quek, L.E.1    Dietmair, S.2    Kromer, J.O.3    Nielsen, L.K.4
  • 110
    • 2342452470 scopus 로고    scopus 로고
    • Dynamic metabolic modelling under the balanced growth condition.
    • Provost, A., Bastin, G., Dynamic metabolic modelling under the balanced growth condition. Journal of Process Control 2004, 14, 717-728.
    • (2004) Journal of Process Control , vol.14 , pp. 717-728
    • Provost, A.1    Bastin, G.2
  • 111
    • 78650525718 scopus 로고    scopus 로고
    • Dynamic model of CHO cell metabolism.
    • Nolan, R. P., Lee, K., Dynamic model of CHO cell metabolism. Metab. Eng. 2011, 13, 108-124.
    • (2011) Metab. Eng. , vol.13 , pp. 108-124
    • Nolan, R.P.1    Lee, K.2
  • 112
    • 33751303229 scopus 로고    scopus 로고
    • Metabolic design of macroscopic bioreaction models: application to Chinese hamster ovary cells.
    • Provost, A., Bastin, G., Agathos, S. N., Schneider, Y. J., Metabolic design of macroscopic bioreaction models: application to Chinese hamster ovary cells. Bioproc. Biosystems Eng. 2006, 29, 349-366.
    • (2006) Bioproc. Biosystems Eng. , vol.29 , pp. 349-366
    • Provost, A.1    Bastin, G.2    Agathos, S.N.3    Schneider, Y.J.4
  • 113
    • 80053927286 scopus 로고    scopus 로고
    • Development of a mathematical model for evaluating the dynamics of normal and apoptotic Chinese hamster ovary cells.
    • Naderi, S., Meshram, M., Wei, C., McConkey, B. et al., Development of a mathematical model for evaluating the dynamics of normal and apoptotic Chinese hamster ovary cells. Biotechnol. Prog. 2011, 27, 1197-1205.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 1197-1205
    • Naderi, S.1    Meshram, M.2    Wei, C.3    McConkey, B.4
  • 114
    • 77049120710 scopus 로고    scopus 로고
    • Metabolic flux analysis of CHO cells in perfusion culture by metabolite balancing and 2D C-13, H-1 COSY NMR spectroscopy.
    • Goudar, C., Biener, R., Boisart, C., Heidemann, R. et al., Metabolic flux analysis of CHO cells in perfusion culture by metabolite balancing and 2D C-13, H-1 COSY NMR spectroscopy. Metab. Eng. 2010, 12, 138-149.
    • (2010) Metab. Eng. , vol.12 , pp. 138-149
    • Goudar, C.1    Biener, R.2    Boisart, C.3    Heidemann, R.4
  • 115
    • 78649410664 scopus 로고    scopus 로고
    • Metabolic flux analysis of CHO cell metabolism in the late non-growth phase.
    • Sengupta, N., Rose, S. T., Morgan, J. A., Metabolic flux analysis of CHO cell metabolism in the late non-growth phase. Biotechnol. Bioeng. 2011, 108, 82-92.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 82-92
    • Sengupta, N.1    Rose, S.T.2    Morgan, J.A.3
  • 116
    • 38449111120 scopus 로고    scopus 로고
    • An elementary metabolite unit (EMU) based method of isotopically nonstationary flux analysis.
    • Young, J. D., Walther, J. L., Antoniewicz, M. R., Yoo, H., Stephanopoulos, G., An elementary metabolite unit (EMU) based method of isotopically nonstationary flux analysis. Biotechnol. Bioeng. 2008, 99, 686-699.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 686-699
    • Young, J.D.1    Walther, J.L.2    Antoniewicz, M.R.3    Yoo, H.4    Stephanopoulos, G.5
  • 117
    • 41249094136 scopus 로고    scopus 로고
    • Metabolic flux analysis in Escherichia coli by integrating isotopic dynamic and isotopic stationary 13C labeling data.
    • Schaub, J., Mauch, K., Reuss, M., Metabolic flux analysis in Escherichia coli by integrating isotopic dynamic and isotopic stationary 13C labeling data. Biotechnol. Bioeng. 2008, 99, 1170-1185.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 1170-1185
    • Schaub, J.1    Mauch, K.2    Reuss, M.3
  • 118
    • 79958703818 scopus 로고    scopus 로고
    • Stationary versus non-stationary (13)C-MFA: A comparison using a consistent dataset.
    • Noack, S., Nöh, K., Moch, M., Oldiges, M., Wiechert, W., Stationary versus non-stationary (13)C-MFA: A comparison using a consistent dataset. J. Biotechnol. 2011, 154, 179-190.
    • (2011) J. Biotechnol. , vol.154 , pp. 179-190
    • Noack, S.1    Nöh, K.2    Moch, M.3    Oldiges, M.4    Wiechert, W.5
  • 119
    • 64349111693 scopus 로고    scopus 로고
    • Towards a metabolic and isotopic steady state in CHO batch cultures for reliable isotope-based metabolic profiling.
    • Deshpande, R., Yang, T. H., Heinzle, E., Towards a metabolic and isotopic steady state in CHO batch cultures for reliable isotope-based metabolic profiling. Biotechnol. J. 2009, 4, 247-263.
    • (2009) Biotechnol. J. , vol.4 , pp. 247-263
    • Deshpande, R.1    Yang, T.H.2    Heinzle, E.3
  • 120
    • 70449519259 scopus 로고    scopus 로고
    • Evaluation of 13C isotopic tracers for metabolic flux analysis in mammalian cells.
    • Metallo, C. M., Walther, J. L., Stephanopoulos, G., Evaluation of 13C isotopic tracers for metabolic flux analysis in mammalian cells. J. Biotechnol. 2009, 144, 167-174.
    • (2009) J. Biotechnol. , vol.144 , pp. 167-174
    • Metallo, C.M.1    Walther, J.L.2    Stephanopoulos, G.3
  • 121
    • 51049091904 scopus 로고    scopus 로고
    • Quantifying reductive carboxylation flux of glutamine to lipid in a brown adipocyte cell line.
    • Yoo, H., Antoniewicz, M. R., Stephanopoulos, G., Kelleher, J. K., Quantifying reductive carboxylation flux of glutamine to lipid in a brown adipocyte cell line. J. Biol. Chem. 2008, 283, 20621-20627.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20621-20627
    • Yoo, H.1    Antoniewicz, M.R.2    Stephanopoulos, G.3    Kelleher, J.K.4
  • 122
    • 64349114245 scopus 로고    scopus 로고
    • Emerging trends in plasma-free manufacturing of recombinant protein therapeutics expressed in mammalian cells.
    • Grillberger, L., Kreil, T. R., Nasr, S., Reiter, M., Emerging trends in plasma-free manufacturing of recombinant protein therapeutics expressed in mammalian cells. Biotechnol. J. 2009, 4, 186-201.
    • (2009) Biotechnol. J. , vol.4 , pp. 186-201
    • Grillberger, L.1    Kreil, T.R.2    Nasr, S.3    Reiter, M.4
  • 123
    • 58749110914 scopus 로고    scopus 로고
    • Implementation of advanced technologies in commercial monoclonal antibody production.
    • Zhou, J. X., Tressel, T., Yang, X., Seewoester, T., Implementation of advanced technologies in commercial monoclonal antibody production. Biotechnol. J. 2008, 3, 1185-1200.
    • (2008) Biotechnol. J. , vol.3 , pp. 1185-1200
    • Zhou, J.X.1    Tressel, T.2    Yang, X.3    Seewoester, T.4
  • 124
    • 80052644208 scopus 로고    scopus 로고
    • Metabolite channeling and compartmentation in the human cell line AGE1.HN determined by (13)C labeling experiments and (13)C metabolic flux analysis. J. Biosci. Bioeng.
    • Niklas, J., Sandig, V., Heinzle, E., Metabolite channeling and compartmentation in the human cell line AGE1.HN determined by (13)C labeling experiments and (13)C metabolic flux analysis. J. Biosci. Bioeng. 2011.
    • (2011)
    • Niklas, J.1    Sandig, V.2    Heinzle, E.3
  • 126
    • 53649110425 scopus 로고    scopus 로고
    • Systems-level metabolic flux profiling identifies fatty acid synthesis as a target for antiviral therapy.
    • Munger, J., Bennett, B. D., Parikh, A., Feng, X. J. et al., Systems-level metabolic flux profiling identifies fatty acid synthesis as a target for antiviral therapy. Nat. Biotechnol. 2008, 26, 1179-1186.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1179-1186
    • Munger, J.1    Bennett, B.D.2    Parikh, A.3    Feng, X.J.4
  • 127
    • 0037022527 scopus 로고    scopus 로고
    • 13C NMR isotopomer analysis reveals a connection between pyruvate cycling and glucose-stimulated insulin secretion (GSIS).
    • Lu, D., Mulder, H., Zhao, P., Burgess, S. C. et al., 13C NMR isotopomer analysis reveals a connection between pyruvate cycling and glucose-stimulated insulin secretion (GSIS). Proc. Natl. Acad. Sci. USA 2002, 99, 2708-2713.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2708-2713
    • Lu, D.1    Mulder, H.2    Zhao, P.3    Burgess, S.C.4
  • 128
    • 79551508527 scopus 로고    scopus 로고
    • 13C metabolic flux analysis in complex systems.
    • Zamboni, N., 13C metabolic flux analysis in complex systems. Curr. Opin. Biotechnol. 2011, 22, 103-108.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 103-108
    • Zamboni, N.1


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