메뉴 건너뛰기




Volumn 23, Issue 5, 2014, Pages 517-525

Over-expression of secreted proteins from mammalian cell lines

Author keywords

Mammalian cell culture; Protein expression; Receptor; Secreted protein

Indexed keywords

ANTIBIOTIC G 418; BLASTICIDIN S; ELEMENT; HYGROMYCIN; PHLEOMYCIN; PUROMYCIN; SIGNAL PEPTIDE; RECOMBINANT PROTEIN;

EID: 84901062733     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2439     Document Type: Review
Times cited : (111)

References (64)
  • 2
    • 84856272158 scopus 로고    scopus 로고
    • Protein secretion in Pichia pastoris and advances in protein production
    • Damasceno LM, Huang CJ, Batt CA (2012) Protein secretion in Pichia pastoris and advances in protein production. Appl Microbiol Biotechnol 93:31-39.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 31-39
    • Damasceno, L.M.1    Huang, C.J.2    Batt, C.A.3
  • 3
    • 33845497166 scopus 로고    scopus 로고
    • Process technology for production and recovery of heterologous proteins with Pichia pastoris
    • Jahic M, Veide A, Charoenrat T, Teeri T, Enfors SO (2006) Process technology for production and recovery of heterologous proteins with Pichia pastoris. Biotechnol Prog 22:1465-1473.
    • (2006) Biotechnol Prog , vol.22 , pp. 1465-1473
    • Jahic, M.1    Veide, A.2    Charoenrat, T.3    Teeri, T.4    Enfors, S.O.5
  • 4
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S, Fazenda ML, McNeil B, Harvey LM (2005) Heterologous protein production using the Pichia pastoris expression system. Yeast 22:249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 5
    • 78651301416 scopus 로고    scopus 로고
    • Recombinant antibodies: Engineering and production in yeast and bacterial hosts
    • Jeong KJ, Jang SH, Velmurugan N (2011) Recombinant antibodies: engineering and production in yeast and bacterial hosts. Biotechnol J 6:16-27.
    • (2011) Biotechnol J , vol.6 , pp. 16-27
    • Jeong, K.J.1    Jang, S.H.2    Velmurugan, N.3
  • 6
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • Wildt S, Gerngross TU (2005) The humanization of N-glycosylation pathways in yeast. Nature Rev Microbiol 3:119-128.
    • (2005) Nature Rev Microbiol , vol.3 , pp. 119-128
    • Wildt, S.1    Gerngross, T.U.2
  • 7
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis DL (2009) Baculovirus-insect cell expression systems. Methods Enzymol 463:191-222.
    • (2009) Methods Enzymol , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 8
    • 80555156119 scopus 로고    scopus 로고
    • Recombinant protein expression in the baculovirus-infected insect cell system
    • Unger T, Peleg Y (2012) Recombinant protein expression in the baculovirus-infected insect cell system. Methods Mol Biol 800:187-199.
    • (2012) Methods Mol Biol , vol.800 , pp. 187-199
    • Unger, T.1    Peleg, Y.2
  • 9
  • 11
    • 0025340630 scopus 로고
    • High-level production of a functional immunoglobulin heterodimer in a baculovirus expression system
    • .Hasemann CA, Capra JD (1990) High-level production of a functional immunoglobulin heterodimer in a baculovirus expression system. Proc Natl Acad Sci USA 87: 3942-3946.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3942-3946
    • Hasemann, C.A.1    Capra, J.D.2
  • 12
    • 0032485869 scopus 로고    scopus 로고
    • Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells
    • Ailor E, Betenbaugh MJ (1998) Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells. Biotechnol Bioengin 58:196-203.
    • (1998) Biotechnol Bioengin , vol.58 , pp. 196-203
    • Ailor, E.1    Betenbaugh, M.J.2
  • 13
    • 0033022809 scopus 로고    scopus 로고
    • Modifying secretion and post-translational processing in insect cells
    • Ailor E, Betenbaugh MJ (1999) Modifying secretion and post-translational processing in insect cells. Curr Opin Biotechnol 10:142-145.
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 142-145
    • Ailor, E.1    Betenbaugh, M.J.2
  • 14
    • 0031055289 scopus 로고    scopus 로고
    • Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from Trichoplusia ni insect cells
    • Hsu TA, Betenbaugh MJ (1997) Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from Trichoplusia ni insect cells. Biotechnol Prog 13:96-104.
    • (1997) Biotechnol Prog , vol.13 , pp. 96-104
    • Hsu, T.A.1    Betenbaugh, M.J.2
  • 15
    • 0030151987 scopus 로고    scopus 로고
    • Rescue of immunoglobulins from insolubility is facilitated by PDI in the baculovirus expression system
    • Hsu TA, Watson S, Eiden JJ, Betenbaugh MJ (1996) Rescue of immunoglobulins from insolubility is facilitated by PDI in the baculovirus expression system. Protein Express Purif 7:281-288.
    • (1996) Protein Express Purif , vol.7 , pp. 281-288
    • Hsu, T.A.1    Watson, S.2    Eiden, J.J.3    Betenbaugh, M.J.4
  • 16
    • 23844433927 scopus 로고    scopus 로고
    • Animal cell cultures: Recent achievements and perspectives in the production of biopharmaceuticals
    • Butler M (2005) Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals. Appl Microbiol Biotechnol 68:283-291.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 283-291
    • Butler, M.1
  • 18
    • 67649664208 scopus 로고    scopus 로고
    • Strategies for analysing and improving the expression and quality of recombinant proteins made in mammalian cells
    • Jenkins N, Meleady P, Tyther R, Murphy L (2009) Strategies for analysing and improving the expression and quality of recombinant proteins made in mammalian cells. Biotechnol Appl Biochem 53:73-83.
    • (2009) Biotechnol Appl Biochem , vol.53 , pp. 73-83
    • Jenkins, N.1    Meleady, P.2    Tyther, R.3    Murphy, L.4
  • 19
    • 84862541940 scopus 로고    scopus 로고
    • Mammalian cell protein expression for biopharmaceutical production
    • Zhu J (2012) Mammalian cell protein expression for biopharmaceutical production. Biotechnol Advan 30: 1158-1170.
    • (2012) Biotechnol Advan , vol.30 , pp. 1158-1170
    • Zhu, J.1
  • 20
    • 77953372273 scopus 로고    scopus 로고
    • Nutrient supplementation strategies for biopharmeceutical production, Part 3: Scaling strategies for rapid nutrient supplement prototyping
    • Fike R (2010) Nutrient supplementation strategies for biopharmeceutical production, Part 3: Scaling strategies for rapid nutrient supplement prototyping. Bioprocess Internatl 8:24-31.
    • (2010) Bioprocess Internatl , vol.8 , pp. 24-31
    • Fike, R.1
  • 22
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher Y, Perret S, Kamen A (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res 30:E9.
    • (2002) Nucleic Acids Res , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 23
    • 0141867826 scopus 로고    scopus 로고
    • Large-scale transient transfection of serum-free suspension-growing HEK293 EBNA1 cells: Peptone additives improve cell growth and transfection efficiency
    • Pham PL, Perret S, Doan HC, Cass B, St-Laurent G, Kamen A, Durocher Y (2003) Large-scale transient transfection of serum-free suspension-growing HEK293 EBNA1 cells: peptone additives improve cell growth and transfection efficiency. Biotechnol Bioengin 84:332-342.
    • (2003) Biotechnol Bioengin , vol.84 , pp. 332-342
    • Pham, P.L.1    Perret, S.2    Doan, H.C.3    Cass, B.4    St-Laurent, G.5    Kamen, A.6    Durocher, Y.7
  • 25
    • 50549090204 scopus 로고    scopus 로고
    • Advances in high-capacity extrachromosomal vector technology: Episomal maintenance, vector delivery, and transgene expression
    • Lufino MM, Edser PA, Wade-Martins R (2008) Advances in high-capacity extrachromosomal vector technology: episomal maintenance, vector delivery, and transgene expression. Molecular Therapy 16:1525-1538.
    • (2008) Molecular Therapy , vol.16 , pp. 1525-1538
    • Lufino, M.M.1    Edser, P.A.2    Wade-Martins, R.3
  • 27
    • 0034122420 scopus 로고    scopus 로고
    • Advances in animal cell recombinant protein production: GS-NS0 expression system
    • Barnes LM, Bentley CM, Dickson AJ (2000) Advances in animal cell recombinant protein production: GS-NS0 expression system. Cytotechnology 32:109-123.
    • (2000) Cytotechnology , vol.32 , pp. 109-123
    • Barnes, L.M.1    Bentley, C.M.2    Dickson, A.J.3
  • 28
    • 77957018662 scopus 로고    scopus 로고
    • Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the Dhfr-based CHO cell selection system
    • Cacciatore JJ, Chasin LA, Leonard EF (2010) Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the Dhfr-based CHO cell selection system. Biotechnology Advan 28:673-681.
    • (2010) Biotechnology Advan , vol.28 , pp. 673-681
    • Cacciatore, J.J.1    Chasin, L.A.2    Leonard, E.F.3
  • 29
    • 50849109798 scopus 로고    scopus 로고
    • Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions
    • Backliwal G, Hildinger M, Chenuet S, Wulhfard S, De Jesus M, Wurm FM (2008) Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions. Nucleic Acids Res 36:e96.
    • (2008) Nucleic Acids Res , vol.36
    • Backliwal, G.1    Hildinger, M.2    Chenuet, S.3    Wulhfard, S.4    De Jesus, M.5    Wurm, F.M.6
  • 30
    • 0023665902 scopus 로고
    • An analysis of 50-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M (1987) An analysis of 50-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res 15:8125-8148.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 31
    • 0023660877 scopus 로고
    • At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells
    • Kozak M (1987) At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J Mol Biol 196:947-950.
    • (1987) J Mol Biol , vol.196 , pp. 947-950
    • Kozak, M.1
  • 32
    • 0036021444 scopus 로고    scopus 로고
    • Emerging links between initiation of translation and human diseases
    • Kozak M (2002) Emerging links between initiation of translation and human diseases. Mammalian Genome 13:401-410.
    • (2002) Mammalian Genome , vol.13 , pp. 401-410
    • Kozak, M.1
  • 33
    • 0032978712 scopus 로고    scopus 로고
    • Woodchuck hepatitis virus posttranscriptional regulatory element enhances expression of transgenes delivered by retroviral vectors
    • Zufferey R, Donello JE, Trono D, Hope TJ (1999) Woodchuck hepatitis virus posttranscriptional regulatory element enhances expression of transgenes delivered by retroviral vectors. J Virology 73:2886-2892.
    • (1999) J Virology , vol.73 , pp. 2886-2892
    • Zufferey, R.1    Donello, J.E.2    Trono, D.3    Hope, T.J.4
  • 34
    • 33645103149 scopus 로고    scopus 로고
    • Woodchuck hepatitis virus post-transcriptional regulatory element deleted from X protein and promoter sequences enhances retroviral vector titer and expression
    • Schambach A, Bohne J, Baum C, Hermann FG, Egerer L, von Laer D, Giroglou T (2006) Woodchuck hepatitis virus post-transcriptional regulatory element deleted from X protein and promoter sequences enhances retroviral vector titer and expression. Gene Therapy 13: 641-645.
    • (2006) Gene Therapy , vol.13 , pp. 641-645
    • Schambach, A.1    Bohne, J.2    Baum, C.3    Hermann, F.G.4    Egerer, L.5    Von Laer, D.6    Giroglou, T.7
  • 35
    • 0036121419 scopus 로고    scopus 로고
    • CRM1- dependent function of a cis-Acting RNA export element
    • Popa I, Harris ME, Donello JE, Hope TJ (2002) CRM1- dependent function of a cis-Acting RNA export element. Mol Cell Biol 22:2057-2067.
    • (2002) Mol Cell Biol , vol.22 , pp. 2057-2067
    • Popa, I.1    Harris, M.E.2    Donello, J.E.3    Hope, T.J.4
  • 36
    • 0023790358 scopus 로고
    • Comparison of introndependent and intron-independent gene expression
    • Buchman AR, Berg P (1988) Comparison of introndependent and intron-independent gene expression. Mol Cell Biol 8:4395-4405.
    • (1988) Mol Cell Biol , vol.8 , pp. 4395-4405
    • Buchman, A.R.1    Berg, P.2
  • 37
    • 0037398519 scopus 로고    scopus 로고
    • How introns influence and enhance eukaryotic gene expression
    • Le Hir H, Nott A, Moore MJ (2003) How introns influence and enhance eukaryotic gene expression. Trends Biochem Sci 28:215-220.
    • (2003) Trends Biochem Sci , vol.28 , pp. 215-220
    • Le Hir, H.1    Nott, A.2    Moore, M.J.3
  • 38
    • 80052456858 scopus 로고    scopus 로고
    • Improving mammalian cell factories: The selection of signal peptide has a major impact on recombinant protein synthesis and secretion in mammalian cells
    • Stern B, Olsen LC, Trobe C, Ravneberg H, Pryme IF (2007) Improving mammalian cell factories: the selection of signal peptide has a major impact on recombinant protein synthesis and secretion in mammalian cells. Trends Cell Mol Biol 2:1-17.
    • (2007) Trends Cell Mol Biol , vol.2 , pp. 1-17
    • Stern, B.1    Olsen, L.C.2    Trobe, C.3    Ravneberg, H.4    Pryme, I.F.5
  • 39
    • 84874195223 scopus 로고    scopus 로고
    • Optimized signal peptides for the development of high expressing CHO cell lines
    • Kober L, Zehe C, Bode J (2013) Optimized signal peptides for the development of high expressing CHO cell lines. Biotechnol Bioengin 110:1164-1173.
    • (2013) Biotechnol Bioengin , vol.110 , pp. 1164-1173
    • Kober, L.1    Zehe, C.2    Bode, J.3
  • 42
    • 84872533264 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics in the 21st century
    • Becker B, Cooper MA (2013) Aminoglycoside antibiotics in the 21st century. ACS Chem Biol 8:105-115.
    • (2013) ACS Chem Biol , vol.8 , pp. 105-115
    • Becker, B.1    Cooper, M.A.2
  • 43
    • 0024403778 scopus 로고
    • Molecular analysis of the pac gene encoding a puromycin N-Acetyl transferase from Streptomyces alboniger
    • Lacalle RA, Pulido D, Vara J, Zalacain M, Jimenez A (1989) Molecular analysis of the pac gene encoding a puromycin N-Acetyl transferase from Streptomyces alboniger. Gene 79:375-380.
    • (1989) Gene , vol.79 , pp. 375-380
    • Lacalle, R.A.1    Pulido, D.2    Vara, J.3    Zalacain, M.4    Jimenez, A.5
  • 45
    • 41149112510 scopus 로고    scopus 로고
    • Improvement of reporter activity by IRES-mediated polycistronic reporter system
    • Bouabe H, Fassler R, Heesemann J (2008) Improvement of reporter activity by IRES-mediated polycistronic reporter system. Nucleic Acids Res 36:e28.
    • (2008) Nucleic Acids Res , vol.36
    • Bouabe, H.1    Fassler, R.2    Heesemann, J.3
  • 46
    • 84858439862 scopus 로고    scopus 로고
    • Insights into the regulation of protein abundance from proteomic and transcriptomic analyses
    • Vogel C, Marcotte EM (2012) Insights into the regulation of protein abundance from proteomic and transcriptomic analyses. Nature Rev Genetics 13:227-232.
    • (2012) Nature Rev Genetics , vol.13 , pp. 227-232
    • Vogel, C.1    Marcotte, E.M.2
  • 47
    • 0020262787 scopus 로고
    • Expression of abbreviated mouse dihydrofolate reductase genes in cultured hamster cells
    • Gasser CS, Simonsen CC, Schilling JW, Schimke RT (1982) Expression of abbreviated mouse dihydrofolate reductase genes in cultured hamster cells. Proc Natl Acad Sci USA 79:6522-6526.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6522-6526
    • Gasser, C.S.1    Simonsen, C.C.2    Schilling, J.W.3    Schimke, R.T.4
  • 48
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm FM (2004) Production of recombinant protein therapeutics in cultivated mammalian cells. Nature Biotechnol 22:1393-1398.
    • (2004) Nature Biotechnol , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 49
    • 0011978456 scopus 로고
    • Recombinant shuttle vectors for the study of mutation in mammalian cells
    • DuBridge RB, Calos MP (1988) Recombinant shuttle vectors for the study of mutation in mammalian cells. Mutagenesis 3:1-9.
    • (1988) Mutagenesis , vol.3 , pp. 1-9
    • Dubridge, R.B.1    Calos, M.P.2
  • 50
    • 38449121649 scopus 로고    scopus 로고
    • High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI
    • Backliwal G, Hildinger M, Hasija V, Wurm FM (2008) High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI. Biotechnol Bioengin 99:721-727.
    • (2008) Biotechnol Bioengin , vol.99 , pp. 721-727
    • Backliwal, G.1    Hildinger, M.2    Hasija, V.3    Wurm, F.M.4
  • 51
    • 44949087903 scopus 로고    scopus 로고
    • Transfection of HEK293-EBNA1 cells in suspension with linear PEI for production of recombinant proteins
    • Pdb prot4977
    • Tom R, Bisson L, Durocher Y (2008) Transfection of HEK293-EBNA1 cells in suspension with linear PEI for production of recombinant proteins. CSH Protocols 2008:pdb prot4977.
    • (2008) CSH Protocols 2008
    • Tom, R.1    Bisson, L.2    Durocher, Y.3
  • 52
    • 71549154680 scopus 로고    scopus 로고
    • Recombinant protein production by transient gene transfer into Mammalian cells
    • Geisse S, Fux C (2009) Recombinant protein production by transient gene transfer into Mammalian cells. Methods Enzymol 463:223-238.
    • (2009) Methods Enzymol , vol.463 , pp. 223-238
    • Geisse, S.1    Fux, C.2
  • 54
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-Acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- Acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99: 13419-13424.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 55
    • 84901011429 scopus 로고    scopus 로고
    • Productivity studies utilizing recombinant CHO cells in stirred-tank bioreactors: A comparitive study between pitched-blad and packed-bed bioreactor systems
    • Hatton T, Barnett S, Benninghoff AD, Rashid K (2012) Productivity studies utilizing recombinant CHO cells in stirred-tank bioreactors: a comparitive study between pitched-blad and packed-bed bioreactor systems. BioProcessing J 11:29-36.
    • (2012) BioProcessing J , vol.11 , pp. 29-36
    • Hatton, T.1    Barnett, S.2    Benninghoff, A.D.3    Rashid, K.4
  • 56
    • 33845948561 scopus 로고    scopus 로고
    • Packed-bed bioreactors for mammalian cell culture: Bioprocess and biomedical applications
    • Meuwly F, Ruffieux PA, Kadouri A, von Stockar U (2007) Packed-bed bioreactors for mammalian cell culture: bioprocess and biomedical applications. Biotechnology Advan 25:45-56.
    • (2007) Biotechnology Advan , vol.25 , pp. 45-56
    • Meuwly, F.1    Ruffieux, P.A.2    Kadouri, A.3    Von Stockar, U.4
  • 57
    • 0029111316 scopus 로고
    • Culture of 293 cells in different culture systems: Cell growth and recombinant adenovirus production
    • Racher AJ, Fooks AR, Griffiths JB (1995) Culture of 293 cells in different culture systems: Cell growth and recombinant adenovirus production. Biotechnol Tech 9: 169-174.
    • (1995) Biotechnol Tech , vol.9 , pp. 169-174
    • Racher, A.J.1    Fooks, A.R.2    Griffiths, J.B.3
  • 58
    • 0023122268 scopus 로고
    • Growth of 293 cells in suspension culture
    • Graham FL (1987) Growth of 293 cells in suspension culture. J Gen Virology 68:937-940.
    • (1987) J Gen Virology , vol.68 , pp. 937-940
    • Graham, F.L.1
  • 59
    • 84926640250 scopus 로고    scopus 로고
    • Optimization of HEK 293 cell growth by addition of non-Animal derived components using design of experiments
    • Cervera L, Gutierrez S, Godia F, Segura MM (2011) Optimization of HEK 293 cell growth by addition of non-Animal derived components using design of experiments. BMC Proc 5 Suppl 8:P126.
    • (2011) BMC Proc 5 Suppl , vol.8
    • Cervera, L.1    Gutierrez, S.2    Godia, F.3    Segura, M.M.4
  • 62
    • 50049130165 scopus 로고    scopus 로고
    • Valproic acid: A viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures
    • Backliwal G, Hildinger M, Kuettel I, Delegrange F, Hacker DL, Wurm FM (2008) Valproic acid: a viable alternative to sodium butyrate for enhancing protein expression in mammalian cell cultures. Biotechnol Bioengin 101:182-189.
    • (2008) Biotechnol Bioengin , vol.101 , pp. 182-189
    • Backliwal, G.1    Hildinger, M.2    Kuettel, I.3    Delegrange, F.4    Hacker, D.L.5    Wurm, F.M.6
  • 63
    • 77953436494 scopus 로고    scopus 로고
    • Nutrient supplementation strategies for biopharmeceutical production Part 1: Identifying a formulation
    • Fike R (2009) Nutrient supplementation strategies for biopharmeceutical production, Part 1: Identifying a formulation. Bioprocess Internatl 7:44-51.
    • (2009) Bioprocess Internatl , vol.7 , pp. 44-51
    • Fike, R.1
  • 64


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.