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Volumn 90, Issue 3, 2005, Pages 354-364

Cytochalasin D can improve heterologous protein productivity in adherent Chinese hamster ovary cells

Author keywords

Chinese hamster ovary cells; Cytochalasin D; Gene amplification; Productivity; Proteomics

Indexed keywords

ALKALINITY; CELLS; CLONING; CYTOLOGY; ELECTROPHORESIS; GENES; MASS SPECTROMETRY;

EID: 20344403310     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20438     Document Type: Article
Times cited : (34)

References (52)
  • 1
    • 0030067028 scopus 로고    scopus 로고
    • High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer
    • Albright RA, Mossing MC, Matthews BW. 1996. High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer. Biochemistry 35(3):735-742.
    • (1996) Biochemistry , vol.35 , Issue.3 , pp. 735-742
    • Albright, R.A.1    Mossing, M.C.2    Matthews, B.W.3
  • 2
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bachinger HP. 1987. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J Biol Chem 262(35): 17144-17148.
    • (1987) J Biol Chem , vol.262 , Issue.35 , pp. 17144-17148
    • Bachinger, H.P.1
  • 4
    • 0025952140 scopus 로고
    • Characterization of two cDNAs encoding folate-binding proteins from L1210 murine leukemia cells. Increased expression associated with a genomic rearrangement
    • Brigle KE, Westin EH, Houghton MT, Goldman ID. 1991. Characterization of two cDNAs encoding folate-binding proteins from L1210 murine leukemia cells. Increased expression associated with a genomic rearrangement. J Biol Chem 266(26):17243-17249.
    • (1991) J Biol Chem , vol.266 , Issue.26 , pp. 17243-17249
    • Brigle, K.E.1    Westin, E.H.2    Houghton, M.T.3    Goldman, I.D.4
  • 5
    • 0026499520 scopus 로고
    • Insertion of an intracisternal A particle within the 5′-regulatory region of a gene encoding folate-binding protein in L1210 leukemia cells in response to low folate selection. Association with increased protein expression
    • Brigle KE, Westin EH, Houghton MT, Goldman ID. 1992. Insertion of an intracisternal A particle within the 5′-regulatory region of a gene encoding folate-binding protein in L1210 leukemia cells in response to low folate selection. Association with increased protein expression. J Biol Chem 267(31):22351-22355.
    • (1992) J Biol Chem , vol.267 , Issue.31 , pp. 22351-22355
    • Brigle, K.E.1    Westin, E.H.2    Houghton, M.T.3    Goldman, I.D.4
  • 6
    • 0018611857 scopus 로고
    • Cytochalasin inhibits the rate of elongation of actin filament fragments
    • Brown SS, Spudich JA. 1979. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol 83(3):657-662.
    • (1979) J Cell Biol , vol.83 , Issue.3 , pp. 657-662
    • Brown, S.S.1    Spudich, J.A.2
  • 7
    • 0026082012 scopus 로고
    • Ammonium decreases human polymorphonuclear leukocyte cytoskeletal actin
    • Brunkhorst B, Niederman R. 1991. Ammonium decreases human polymorphonuclear leukocyte cytoskeletal actin. Infect Immunol 59: 1378-1386.
    • (1991) Infect Immunol , vol.59 , pp. 1378-1386
    • Brunkhorst, B.1    Niederman, R.2
  • 8
    • 1642480149 scopus 로고    scopus 로고
    • Metabolic changes during cell growth inhibition by p27 overexpression
    • Carvalhal AV, Marcelino I, Carrondo MJ. 2003a. Metabolic changes during cell growth inhibition by p27 overexpression. Appl Microbiol Biotechnol 63(2):164-173.
    • (2003) Appl Microbiol Biotechnol , vol.63 , Issue.2 , pp. 164-173
    • Carvalhal, A.V.1    Marcelino, I.2    Carrondo, M.J.3
  • 9
    • 0037279250 scopus 로고    scopus 로고
    • Cell growth arrest by nucleotides, nucleosides and bases as a tool for improved production of recombinant proteins
    • Carvalhal AV, Santos SS, Calado J, Haury M, Carrondo MJ. 2003b. Cell growth arrest by nucleotides, nucleosides and bases as a tool for improved production of recombinant proteins. Biotechnol Prog 19(1): 69-83.
    • (2003) Biotechnol Prog , vol.19 , Issue.1 , pp. 69-83
    • Carvalhal, A.V.1    Santos, S.S.2    Calado, J.3    Haury, M.4    Carrondo, M.J.5
  • 10
    • 0032903914 scopus 로고    scopus 로고
    • Proteome analysis of factor for inversion stimulation (Fis) overproduction in Escherichia coli
    • Choe LH, Chen W, Lee KH. 1999. Proteome analysis of factor for inversion stimulation (Fis) overproduction in Escherichia coli. Electrophoresis 20(4-5):798-805.
    • (1999) Electrophoresis , vol.20 , Issue.4-5 , pp. 798-805
    • Choe, L.H.1    Chen, W.2    Lee, K.H.3
  • 11
    • 0346504006 scopus 로고    scopus 로고
    • Quantitative and qualitative measure of intra-laboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis
    • Choe LH, Lee KH. 2003. Quantitative and qualitative measure of intra-laboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis. Electrophoresis 24(19-20):3500-3507.
    • (2003) Electrophoresis , vol.24 , Issue.19-20 , pp. 3500-3507
    • Choe, L.H.1    Lee, K.H.2
  • 12
    • 0037028505 scopus 로고    scopus 로고
    • Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins
    • Clinton JM, Chansky HA, Odell DD, Zielinska-Kwiatkowska A, Hickstein DD, Yang L. 2002. Characterization and expression of the human gene encoding two translocation liposarcoma protein-associated serine-arginine (TASR) proteins. Gene 284(1-2):141-147.
    • (2002) Gene , vol.284 , Issue.1-2 , pp. 141-147
    • Clinton, J.M.1    Chansky, H.A.2    Odell, D.D.3    Zielinska-Kwiatkowska, A.4    Hickstein, D.D.5    Yang, L.6
  • 13
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper JA. 1987. Effects of cytochalasin and phalloidin on actin. J Cell Biol 105(4):1473-1478.
    • (1987) J Cell Biol , vol.105 , Issue.4 , pp. 1473-1478
    • Cooper, J.A.1
  • 14
    • 14744303350 scopus 로고
    • Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion
    • Davis TR, Trotter KM, Granados RR, Wood HA. 1992. Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion. BioTechnology (NY) 10(10): 1148-1150.
    • (1992) BioTechnology (NY) , vol.10 , Issue.10 , pp. 1148-1150
    • Davis, T.R.1    Trotter, K.M.2    Granados, R.R.3    Wood, H.A.4
  • 15
    • 0041659182 scopus 로고    scopus 로고
    • Actin remodeling to facilitate membrane fusion
    • Eitzen G. 2003. Actin remodeling to facilitate membrane fusion. Biochim Biophys Acta 1641(2-3):175-181.
    • (2003) Biochim Biophys Acta , vol.1641 , Issue.2-3 , pp. 175-181
    • Eitzen, G.1
  • 16
    • 0038348755 scopus 로고    scopus 로고
    • Small-molecule inhibitors of actin dynamics and cell motility
    • Fenteany G, Zhu S. 2003. Small-molecule inhibitors of actin dynamics and cell motility. Curr Top Med Chem 3(6):593-616.
    • (2003) Curr Top Med Chem , vol.3 , Issue.6 , pp. 593-616
    • Fenteany, G.1    Zhu, S.2
  • 17
    • 0347764580 scopus 로고    scopus 로고
    • Comparison of automated in-gel digest methods for femtomole level samples
    • Finehout EJ, Lee KH. 2003. Comparison of automated in-gel digest methods for femtomole level samples. Electrophoresis 24(19-20): 3508-3516.
    • (2003) Electrophoresis , vol.24 , Issue.19-20 , pp. 3508-3516
    • Finehout, E.J.1    Lee, K.H.2
  • 18
    • 0019320646 scopus 로고
    • Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin
    • Flanagan MD, Lin S. 1980. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J Biol Chem 255(3):835-838.
    • (1980) J Biol Chem , vol.255 , Issue.3 , pp. 835-838
    • Flanagan, M.D.1    Lin, S.2
  • 19
    • 0023007962 scopus 로고
    • Actin polymerization. The mechanism of action of cytochalasin D
    • Goddette DW, Frieden C. 1986. Actin polymerization. The mechanism of action of cytochalasin D. J Biol Chem 261(34):15974-15980.
    • (1986) J Biol Chem , vol.261 , Issue.34 , pp. 15974-15980
    • Goddette, D.W.1    Frieden, C.2
  • 21
    • 0033136939 scopus 로고    scopus 로고
    • Stable production of a human growth hormone antagonist from CHO cells adapted to serum-free suspension culture
    • Haldankar R, Kopchick JJ, Ridgway D. 1999. Stable production of a human growth hormone antagonist from CHO cells adapted to serum-free suspension culture. Biotechnol Prog 15(3):336-346.
    • (1999) Biotechnol Prog , vol.15 , Issue.3 , pp. 336-346
    • Haldankar, R.1    Kopchick, J.J.2    Ridgway, D.3
  • 22
    • 0030967785 scopus 로고    scopus 로고
    • Vertebrates have conserved capping protein alpha isoforms with specific expression patterns
    • Hart MC, Korshunova YO, Cooper JA. 1997. Vertebrates have conserved capping protein alpha isoforms with specific expression patterns. Cell Motil Cytoskeleton 38(2):120-132.
    • (1997) Cell Motil Cytoskeleton , vol.38 , Issue.2 , pp. 120-132
    • Hart, M.C.1    Korshunova, Y.O.2    Cooper, J.A.3
  • 23
    • 4444236379 scopus 로고    scopus 로고
    • A two-dimensional electrophoresis map of Chinese hamster ovary cell proteins based on fluorescence staining
    • Hayduk EJ, Choe LH, Lee KH. 2004. A two-dimensional electrophoresis map of Chinese hamster ovary cell proteins based on fluorescence staining. Electrophoresis 25(15):2545-2556.
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2545-2556
    • Hayduk, E.J.1    Choe, L.H.2    Lee, K.H.3
  • 24
    • 0033526546 scopus 로고    scopus 로고
    • Influence of low temperature on productivity, proteome and protein phosphorylation of CHO cells
    • Kaufmann H, Mazur X, Fussenegger M, Bailey JE. 1999. Influence of low temperature on productivity, proteome and protein phosphorylation of CHO cells. Biotechnol Bioeng 63(5):573-582.
    • (1999) Biotechnol Bioeng , vol.63 , Issue.5 , pp. 573-582
    • Kaufmann, H.1    Mazur, X.2    Fussenegger, M.3    Bailey, J.E.4
  • 25
    • 0002598959 scopus 로고    scopus 로고
    • Characterization of chimeric antibody producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure
    • Kim SJ, Kim NS, Ryu CJ, Hong HJ, Lee GM. 1998. Characterization of chimeric antibody producing CHO cells in the course of dihydrofolate reductase-mediated gene amplification and their stability in the absence of selective pressure. Biotechnol Bioeng 58(1):73-84.
    • (1998) Biotechnol Bioeng , vol.58 , Issue.1 , pp. 73-84
    • Kim, S.J.1    Kim, N.S.2    Ryu, C.J.3    Hong, H.J.4    Lee, G.M.5
  • 26
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen P, Drubin DG. 1997. Cofilin promotes rapid actin filament turnover in vivo. Nature 388(6637):78-82.
    • (1997) Nature , vol.388 , Issue.6637 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 27
    • 0348044478 scopus 로고    scopus 로고
    • Proteome analysis of antibody-expressing CHO cells in response to hyperosmotic pressure
    • Lee MS, Kim KW, Kim YH, Lee GM. 2003. Proteome analysis of antibody-expressing CHO cells in response to hyperosmotic pressure. Biotechnol Prog 19(6):1734-1741.
    • (2003) Biotechnol Prog , vol.19 , Issue.6 , pp. 1734-1741
    • Lee, M.S.1    Kim, K.W.2    Kim, Y.H.3    Lee, G.M.4
  • 29
    • 0033589374 scopus 로고    scopus 로고
    • A novel autoregulated proliferation-controlled production process using recombinant CHO cells
    • Mazur X, Eppenberger HM, Bailey JE, Fussenegger M. 1999. A novel autoregulated proliferation-controlled production process using recombinant CHO cells. Biotechnol Bioeng 65(2):144-150.
    • (1999) Biotechnol Bioeng , vol.65 , Issue.2 , pp. 144-150
    • Mazur, X.1    Eppenberger, H.M.2    Bailey, J.E.3    Fussenegger, M.4
  • 30
    • 0036384371 scopus 로고    scopus 로고
    • NIRF, a novel RING finger protein, is involved in cell-cycle regulation
    • Mon T, Li Y, Hata H, Ono K, Kochi H. 2002. NIRF, a novel RING finger protein, is involved in cell-cycle regulation. Biochem Biophys Res Commun 296(3):530-536.
    • (2002) Biochem Biophys Res Commun , vol.296 , Issue.3 , pp. 530-536
    • Mon, T.1    Li, Y.2    Hata, H.3    Ono, K.4    Kochi, H.5
  • 31
    • 0344464720 scopus 로고    scopus 로고
    • Wnts and Hedgehogs: Lipid-modified proteins and similarities in signaling mechanisms at the cell surface
    • Nusse R. 2003. Wnts and Hedgehogs: lipid-modified proteins and similarities in signaling mechanisms at the cell surface. Development 130(22):5297-5305.
    • (2003) Development , vol.130 , Issue.22 , pp. 5297-5305
    • Nusse, R.1
  • 32
    • 0034527246 scopus 로고    scopus 로고
    • Efficiency of promoter and cell line in high-level expression of erythropoietin
    • Park JH, Kim C, Kim WB, Kim YK, Lee SY, Yang JM. 2000. Efficiency of promoter and cell line in high-level expression of erythropoietin. Biotechnol Appl Biochem 32(Pt 3):167-172.
    • (2000) Biotechnol Appl Biochem , vol.32 , Issue.PART 3 , pp. 167-172
    • Park, J.H.1    Kim, C.2    Kim, W.B.3    Kim, Y.K.4    Lee, S.Y.5    Yang, J.M.6
  • 33
    • 0036182506 scopus 로고    scopus 로고
    • High-level expression of human thyroid-stimulating hormone in Chinese hamster ovary cells by co-transfection of dicistronic expression vectors followed by a dual-marker amplification strategy
    • Peroni CN, Soares CR, Gimbo E, Morganti L, Ribela MT, Bartolini P. 2002. High-level expression of human thyroid-stimulating hormone in Chinese hamster ovary cells by co-transfection of dicistronic expression vectors followed by a dual-marker amplification strategy. Biotechnol Appl Biochem 35(1):19-26.
    • (2002) Biotechnol Appl Biochem , vol.35 , Issue.1 , pp. 19-26
    • Peroni, C.N.1    Soares, C.R.2    Gimbo, E.3    Morganti, L.4    Ribela, M.T.5    Bartolini, P.6
  • 34
    • 0037310350 scopus 로고    scopus 로고
    • The correlation between rDNA copy number and genome size in eukaryotes
    • Prokopowich CD, Gregory TR, Crease TJ. 2003. The correlation between rDNA copy number and genome size in eukaryotes. Genome 46(1): 48-50.
    • (2003) Genome , vol.46 , Issue.1 , pp. 48-50
    • Prokopowich, C.D.1    Gregory, T.R.2    Crease, T.J.3
  • 35
    • 0026530460 scopus 로고
    • Cytochalasins induce actin polymerization in human leukocytes
    • Rao KM, Padmanabhan J, Cohen HJ. 1992. Cytochalasins induce actin polymerization in human leukocytes. Cell Motil Cytoskeleton 21(1): 58-64.
    • (1992) Cell Motil Cytoskeleton , vol.21 , Issue.1 , pp. 58-64
    • Rao, K.M.1    Padmanabhan, J.2    Cohen, H.J.3
  • 36
    • 0022650568 scopus 로고
    • Methotrexate resistance and gene amplification. Mechanisms and implications
    • Schimke RT. 1986. Methotrexate resistance and gene amplification. Mechanisms and implications. Cancer 57(10):1912-1917.
    • (1986) Cancer , vol.57 , Issue.10 , pp. 1912-1917
    • Schimke, R.T.1
  • 37
    • 0020044056 scopus 로고
    • Action of cytochalasin D on cytoskeletal networks
    • Schliwa M. 1982. Action of cytochalasin D on cytoskeletal networks. J Cell Biol 92(1):79-91.
    • (1982) J Cell Biol , vol.92 , Issue.1 , pp. 79-91
    • Schliwa, M.1
  • 38
    • 0026510141 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding
    • Schonbrunner ER, Schmid FX. 1992. Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc Natl Acad Sci USA 89(10):4510-4513.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.10 , pp. 4510-4513
    • Schonbrunner, E.R.1    Schmid, F.X.2
  • 39
    • 0019335278 scopus 로고
    • A proposed mechanism of action of cytochalasin D on muscle actin
    • Selden LA, Gershman LC, Estes JE. 1980. A proposed mechanism of action of cytochalasin D on muscle actin. Biochem Biophys Res Commun 95(4):1854-1860.
    • (1980) Biochem Biophys Res Commun , vol.95 , Issue.4 , pp. 1854-1860
    • Selden, L.A.1    Gershman, L.C.2    Estes, J.E.3
  • 40
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: Lamins and actin are major players in essential nuclear functions
    • Shumaker DK, Kuczmarski ER, Goldman RD. 2003. The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr Opin Cell Biol 15(3):358-366.
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.3 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 41
    • 0028485666 scopus 로고
    • Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: Comparison with native human PAI-1
    • Stromqvist M, Andersson JO, Bostrom S, Deinum J, Ehnebom J, Enquist K, Johansson T, Hansson L. 1994. Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: comparison with native human PAI-1. Protein Expr Purif 5(4): 309-316.
    • (1994) Protein Expr Purif , vol.5 , Issue.4 , pp. 309-316
    • Stromqvist, M.1    Andersson, J.O.2    Bostrom, S.3    Deinum, J.4    Ehnebom, J.5    Enquist, K.6    Johansson, T.7    Hansson, L.8
  • 42
    • 0004155427 scopus 로고
    • New York: WH Freeman and Co.
    • Stryer L. 1995. Biochemistry. New York: WH Freeman and Co.
    • (1995) Biochemistry
    • Stryer, L.1
  • 43
  • 44
    • 0025074908 scopus 로고
    • Targeted disruption of the murine int-1 proto-oncogene resulting in severe abnormalities in midbrain and cerebellar development
    • Thomas KR, Capecchi MR. 1990. Targeted disruption of the murine int-1 proto-oncogene resulting in severe abnormalities in midbrain and cerebellar development. Nature 346(6287):847-850.
    • (1990) Nature , vol.346 , Issue.6287 , pp. 847-850
    • Thomas, K.R.1    Capecchi, M.R.2
  • 45
    • 0043092191 scopus 로고    scopus 로고
    • Wnt pathway activation in mesothelioma: Evidence of Dishevelled overexpression and transcriptional activity of beta-catenin
    • Uematsu K, Kanazawa S, You L, He B, Xu Z, Li K, Peterlin BM, McCormick F, Jablons DM. 2003. Wnt pathway activation in mesothelioma: evidence of Dishevelled overexpression and transcriptional activity of beta-catenin. Cancer Res 63(15):4547-4551.
    • (2003) Cancer Res , vol.63 , Issue.15 , pp. 4547-4551
    • Uematsu, K.1    Kanazawa, S.2    You, L.3    He, B.4    Xu, Z.5    Li, K.6    Peterlin, B.M.7    McCormick, F.8    Jablons, D.M.9
  • 46
    • 0043208919 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks - 2003
    • Walsh G. 2003. Biopharmaceutical benchmarks - 2003. Nat Biotechnol 21(8):865-870.
    • (2003) Nat Biotechnol , vol.21 , Issue.8 , pp. 865-870
    • Walsh, G.1
  • 47
    • 0025940658 scopus 로고
    • Actin polymerization in murine B lymphocytes is stimulated by cytochalasin D but not by anti-immunoglobulin
    • Wilder JA, Ashman RF. 1991. Actin polymerization in murine B lymphocytes is stimulated by cytochalasin D but not by anti-immunoglobulin. Cell Immunol 137(2):514-528.
    • (1991) Cell Immunol , vol.137 , Issue.2 , pp. 514-528
    • Wilder, J.A.1    Ashman, R.F.2
  • 48
    • 0029885877 scopus 로고    scopus 로고
    • Gene transfer and amplification in CHO cells. Efficient methods for maximizing specific productivity and assessment of genetic consequences
    • Wurm FM, Johnson A, Ryll T, Kohne C, Scherthan H, Glaab F, Lie YS, Petropoulos CJ, Arathoon WR. 1996. Gene transfer and amplification in CHO cells. Efficient methods for maximizing specific productivity and assessment of genetic consequences. Ann NY Acad Sci 782: 70-78.
    • (1996) Ann NY Acad Sci , vol.782 , pp. 70-78
    • Wurm, F.M.1    Johnson, A.2    Ryll, T.3    Kohne, C.4    Scherthan, H.5    Glaab, F.6    Lie, Y.S.7    Petropoulos, C.J.8    Arathoon, W.R.9
  • 49
    • 0020029505 scopus 로고
    • Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro
    • Yahara I, Harada F, Sekita S, Yoshihira K, Natori S. 1982. Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J Cell Biol 92(1): 69-78.
    • (1982) J Cell Biol , vol.92 , Issue.1 , pp. 69-78
    • Yahara, I.1    Harada, F.2    Sekita, S.3    Yoshihira, K.4    Natori, S.5
  • 50
    • 0041476091 scopus 로고    scopus 로고
    • Effect of low culture temperature on specific productivity and transcription level of anti-4-IBB antibody in recombinant Chinese hamster ovary cells
    • Yoon SK, Kim SH, Lee GM. 2003a. Effect of low culture temperature on specific productivity and transcription level of anti-4-IBB antibody in recombinant Chinese hamster ovary cells. Biotechnol Prog 19(4): 1383-1386.
    • (2003) Biotechnol Prog , vol.19 , Issue.4 , pp. 1383-1386
    • Yoon, S.K.1    Kim, S.H.2    Lee, G.M.3
  • 51
    • 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 SK, Song JY, Lee GM. 2003b. Effect of low culture temperature on specific productivity, transcription level, and heterogeneity of erythropoietin in Chinese hamster ovary cells. Biotechnol Bioeng 82(3): 289-298.
    • (2003) Biotechnol Bioeng , vol.82 , Issue.3 , pp. 289-298
    • Yoon, S.K.1    Song, J.Y.2    Lee, G.M.3
  • 52
    • 0035043839 scopus 로고    scopus 로고
    • The rate of folate receptor alpha (FR alpha) synthesis in folate depleted CHL cells is regulated by a translational mechanism sensitive to media folate levels, while stable overexpression of its mRNA is mediated by gene amplification and an increase in transcript half-life
    • Zhu WY, Alliegro MA, Melera PW. 2001. The rate of folate receptor alpha (FR alpha) synthesis in folate depleted CHL cells is regulated by a translational mechanism sensitive to media folate levels, while stable overexpression of its mRNA is mediated by gene amplification and an increase in transcript half-life. J Cell Biochem 81(2): 205-219.
    • (2001) J Cell Biochem , vol.81 , Issue.2 , pp. 205-219
    • Zhu, W.Y.1    Alliegro, M.A.2    Melera, P.W.3


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