메뉴 건너뛰기




Volumn 23, Issue 6, 2012, Pages 965-971

Pharmaceutical protein production by yeast: Towards production of human blood proteins by microbial fermentation

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD PROTEIN; CLINICAL USE; CURRENT SITUATION; GENOMICS; HIGH-THROUGHPUT ANALYSIS; HUMAN BLOOD PROTEINS; LARGE SCALE PRODUCTIONS; MICROBIAL CELLS; MICROBIAL FERMENTATION; MODEL PLATFORM; PHARMACEUTICAL PROTEIN; SYSTEMS BIOLOGY; THERAPEUTIC PROTEIN; YEAST SACCHAROMYCES CEREVISIAE;

EID: 84869870745     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2012.03.011     Document Type: Review
Times cited : (69)

References (67)
  • 2
    • 40549145848 scopus 로고    scopus 로고
    • Cumulative updating of approved biopharmaceuticals
    • Redwan E.-R. Cumulative updating of approved biopharmaceuticals. Hum Antibodies 2007, 16:22.
    • (2007) Hum Antibodies , vol.16 , pp. 22
    • Redwan, E.-R.1
  • 3
    • 70449726880 scopus 로고    scopus 로고
    • Market watch: sales of biologics to show robust growth through to 2013
    • Goodman M. Market watch: sales of biologics to show robust growth through to 2013. Nat Rev Drug Discov 2009, 8:837.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 837
    • Goodman, M.1
  • 4
    • 83255165688 scopus 로고    scopus 로고
    • What's fueling the biotech engine-2010 to 2011
    • Aggarwal S. What's fueling the biotech engine-2010 to 2011. Nat Biotechnol 2011, 29:1083-1089.
    • (2011) Nat Biotechnol , vol.29 , pp. 1083-1089
    • Aggarwal, S.1
  • 5
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 2006, 72:211-222.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 211-222
    • Terpe, K.1
  • 6
    • 0141831834 scopus 로고    scopus 로고
    • Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli
    • Panda A.K. Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli. Adv Biochem Eng Biotechnol 2003, 85:43-93.
    • (2003) Adv Biochem Eng Biotechnol , vol.85 , pp. 43-93
    • Panda, A.K.1
  • 7
    • 79952535978 scopus 로고    scopus 로고
    • Production of recombinant proteins and metabolites in yeasts: when are these systems better than bacterial production systems?
    • Porro D., Gasser B., Fossati T., Maurer M., Branduardi P., Sauer M., Mattanovich D. Production of recombinant proteins and metabolites in yeasts: when are these systems better than bacterial production systems?. Appl Microbiol Biotechnol 2011, 89:939-948.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 939-948
    • Porro, D.1    Gasser, B.2    Fossati, T.3    Maurer, M.4    Branduardi, P.5    Sauer, M.6    Mattanovich, D.7
  • 8
    • 65449176887 scopus 로고    scopus 로고
    • PVL: high yield production of heterologous proteins with Escherichia coli
    • Tripathi N.K., Jana S.K., Rao A.M. PVL: high yield production of heterologous proteins with Escherichia coli. Defence Sci J 2009, 59:137-146.
    • (2009) Defence Sci J , vol.59 , pp. 137-146
    • Tripathi, N.K.1    Jana, S.K.2    Rao, A.M.3
  • 9
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh G., Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol 2006, 24:1241-1252.
    • (2006) Nat Biotechnol , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 10
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: current state and perspectives
    • De Pourcq K., De Schutter K., Callewaert N. Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl Microbiol Biotechnol 2010, 87:1617-1631.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1617-1631
    • De Pourcq, K.1    De Schutter, K.2    Callewaert, N.3
  • 11
    • 84862810503 scopus 로고    scopus 로고
    • Dynamic model for CHO cell engineering
    • Nolan R.P., Lee K. Dynamic model for CHO cell engineering. J Biotechnol 2012, 158:24-33.
    • (2012) J Biotechnol , vol.158 , pp. 24-33
    • Nolan, R.P.1    Lee, K.2
  • 12
    • 37349024048 scopus 로고    scopus 로고
    • Improving protein production processes
    • Morrow K.J. Improving protein production processes. Gen Eng News 2007, 27:50-54.
    • (2007) Gen Eng News , vol.27 , pp. 50-54
    • Morrow, K.J.1
  • 13
    • 84857455818 scopus 로고    scopus 로고
    • Recombinant protein vaccines produced in insect cells
    • Cox M.M. Recombinant protein vaccines produced in insect cells. Vaccine 2012, 30:1759-1766.
    • (2012) Vaccine , vol.30 , pp. 1759-1766
    • Cox, M.M.1
  • 14
    • 84865232198 scopus 로고    scopus 로고
    • Production of recombinant proteins by yeast cells
    • Celik E., Calik P. Production of recombinant proteins by yeast cells. Biotechnol Adv 2012, 30:1108-1118.
    • (2012) Biotechnol Adv , vol.30 , pp. 1108-1118
    • Celik, E.1    Calik, P.2
  • 15
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • Demain A.L., Vaishnav P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 2009, 27:297-306.
    • (2009) Biotechnol Adv , vol.27 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 16
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross T.U. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 2004, 22:1409-1414.
    • (2004) Nat Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 17
    • 84862781268 scopus 로고    scopus 로고
    • Engineering of vesicle trafficking improves heterologous protein secretion in Saccharomyces cerevisiae
    • Hou J., Tyo K., Liu Z., Petranovic D., Nielsen J. Engineering of vesicle trafficking improves heterologous protein secretion in Saccharomyces cerevisiae. Metab Eng 2012.
    • (2012) Metab Eng
    • Hou, J.1    Tyo, K.2    Liu, Z.3    Petranovic, D.4    Nielsen, J.5
  • 19
    • 41549115843 scopus 로고    scopus 로고
    • Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
    • Chigira Y., Oka T., Okajima T., Jigami Y. Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains. Glycobiology 2008, 18:303-314.
    • (2008) Glycobiology , vol.18 , pp. 303-314
    • Chigira, Y.1    Oka, T.2    Okajima, T.3    Jigami, Y.4
  • 20
    • 64549111428 scopus 로고    scopus 로고
    • Yeast systems biotechnology for the production of heterologous proteins
    • Graf A., Dragosits M., Gasser B., Mattanovich D. Yeast systems biotechnology for the production of heterologous proteins. FEMS Yeast Res 2009, 9:335-348.
    • (2009) FEMS Yeast Res , vol.9 , pp. 335-348
    • Graf, A.1    Dragosits, M.2    Gasser, B.3    Mattanovich, D.4
  • 21
    • 84857058761 scopus 로고    scopus 로고
    • A systems-level approach for metabolic engineering of yeast cell factories
    • Kim I.K., Roldao A., Siewers V., Nielsen J. A systems-level approach for metabolic engineering of yeast cell factories. FEMS Yeast Res 2012, 12:228-248.
    • (2012) FEMS Yeast Res , vol.12 , pp. 228-248
    • Kim, I.K.1    Roldao, A.2    Siewers, V.3    Nielsen, J.4
  • 22
    • 79952123299 scopus 로고    scopus 로고
    • Opportunities for yeast metabolic engineering: lessons from synthetic biology
    • Krivoruchko A., Siewers V., Nielsen J. Opportunities for yeast metabolic engineering: lessons from synthetic biology. Biotechnol J 2011, 6:262-276.
    • (2011) Biotechnol J , vol.6 , pp. 262-276
    • Krivoruchko, A.1    Siewers, V.2    Nielsen, J.3
  • 23
    • 0242355018 scopus 로고    scopus 로고
    • Establishing the yeast Saccharomyces cerevisiae as a system for expression of human proteins on a proteome-scale
    • Holz C., Prinz B., Bolotina N., Sievert V., Bussow K., Simon B., Stahl U., Lang C. Establishing the yeast Saccharomyces cerevisiae as a system for expression of human proteins on a proteome-scale. J Struct Funct Genomics 2003, 4:97-108.
    • (2003) J Struct Funct Genomics , vol.4 , pp. 97-108
    • Holz, C.1    Prinz, B.2    Bolotina, N.3    Sievert, V.4    Bussow, K.5    Simon, B.6    Stahl, U.7    Lang, C.8
  • 24
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schröder M. Endoplasmic reticulum stress responses. Cell Mol Life Sci 2008, 65:862-894.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 862-894
    • Schröder, M.1
  • 25
    • 84863380845 scopus 로고    scopus 로고
    • Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress
    • Tyo K., Liu Z., Petranovic D., Nielsen J. Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress. BMC Biol 2012, 10:16.
    • (2012) BMC Biol , vol.10 , pp. 16
    • Tyo, K.1    Liu, Z.2    Petranovic, D.3    Nielsen, J.4
  • 26
    • 84862807811 scopus 로고    scopus 로고
    • Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae
    • Liu Z., Tyo K., Martínez J.L., Petranovic D., Nielsen J. Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae. Biotechnol Bioeng 2012, 109:1259-1268.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 1259-1268
    • Liu, Z.1    Tyo, K.2    Martínez, J.L.3    Petranovic, D.4    Nielsen, J.5
  • 27
    • 77956690413 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2010
    • Walsh G. Biopharmaceutical benchmarks 2010. Nat Biotechnol 2010, 28:917-924.
    • (2010) Nat Biotechnol , vol.28 , pp. 917-924
    • Walsh, G.1
  • 28
    • 33644500755 scopus 로고    scopus 로고
    • Summary of recombinant human serum albumin development
    • Kobayashi K. Summary of recombinant human serum albumin development. Biologicals 2006, 34:55-59.
    • (2006) Biologicals , vol.34 , pp. 55-59
    • Kobayashi, K.1
  • 29
    • 34948884120 scopus 로고    scopus 로고
    • Recombinant human serum albumin
    • Chuang V., Otagiri M. Recombinant human serum albumin. Drugs Today 2007, 43:547.
    • (2007) Drugs Today , vol.43 , pp. 547
    • Chuang, V.1    Otagiri, M.2
  • 30
    • 42749089626 scopus 로고    scopus 로고
    • Recombinant human fibrinogen expressed in the yeast Pichia pastoris was assembled and biologically active
    • Tojo N., Miyagi I., Miura M., Ohi H. Recombinant human fibrinogen expressed in the yeast Pichia pastoris was assembled and biologically active. Protein Expr Purif 2008, 59:289-296.
    • (2008) Protein Expr Purif , vol.59 , pp. 289-296
    • Tojo, N.1    Miyagi, I.2    Miura, M.3    Ohi, H.4
  • 31
    • 50849113047 scopus 로고    scopus 로고
    • Expression of modified gene encoding functional human α-1-antitrypsin protein in transgenic tomato plants
    • Agarwal S., Singh R., Sanyal I., Amla D. Expression of modified gene encoding functional human α-1-antitrypsin protein in transgenic tomato plants. Transgenic Res 2008, 17:881-896.
    • (2008) Transgenic Res , vol.17 , pp. 881-896
    • Agarwal, S.1    Singh, R.2    Sanyal, I.3    Amla, D.4
  • 32
    • 79251538078 scopus 로고    scopus 로고
    • Recombinant human transferrin: beyond iron binding and transport
    • Brandsma M.E., Jevnikar A.M., Ma S. Recombinant human transferrin: beyond iron binding and transport. Biotechnol Adv 2011, 29:230-238.
    • (2011) Biotechnol Adv , vol.29 , pp. 230-238
    • Brandsma, M.E.1    Jevnikar, A.M.2    Ma, S.3
  • 33
    • 0023517015 scopus 로고
    • Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli
    • Nagai K., Thøgersen H.C. Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli. Methods Enzymol 1987, 153:461-481.
    • (1987) Methods Enzymol , vol.153 , pp. 461-481
    • Nagai, K.1    Thøgersen, H.C.2
  • 36
    • 0026737980 scopus 로고
    • Human hemoglobin expression in Escherichia coli: importance of optimal codon usage
    • Hernan R., Hui H., Andracki M., Noble R., Sligar S., Walder J., Walder R. Human hemoglobin expression in Escherichia coli: importance of optimal codon usage. Biochemistry 1992, 31:8619-8628.
    • (1992) Biochemistry , vol.31 , pp. 8619-8628
    • Hernan, R.1    Hui, H.2    Andracki, M.3    Noble, R.4    Sligar, S.5    Walder, J.6    Walder, R.7
  • 39
    • 20444445134 scopus 로고    scopus 로고
    • Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem
    • Feng L., Zhou S., Gu L., Gell D.A., Mackay J.P., Weiss M.J., Gow A.J., Shi Y. Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem. Nature 2005, 435:697-701.
    • (2005) Nature , vol.435 , pp. 697-701
    • Feng, L.1    Zhou, S.2    Gu, L.3    Gell, D.A.4    Mackay, J.P.5    Weiss, M.J.6    Gow, A.J.7    Shi, Y.8
  • 40
    • 33644968962 scopus 로고    scopus 로고
    • High-yield expression in Escherichia coli of soluble human {alpha}-hemoglobin complexed with its molecular chaperone
    • Vasseur-Godbillon C., Hamdane D., Marden M., Baudin-Creuza V. High-yield expression in Escherichia coli of soluble human {alpha}-hemoglobin complexed with its molecular chaperone. Protein Eng Des Sel 2006, 19:91-97.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 91-97
    • Vasseur-Godbillon, C.1    Hamdane, D.2    Marden, M.3    Baudin-Creuza, V.4
  • 41
    • 0031879158 scopus 로고    scopus 로고
    • Correct assembly of human normal adult hemoglobin when expressed in transgenic swine: chemical, conformational and functional equivalence with the human-derived protein
    • Manjula B.N., Kumar R., Sun D.P., Ho N.T., Ho C., Rao J.M., Malavalli A., Acharya A.S. Correct assembly of human normal adult hemoglobin when expressed in transgenic swine: chemical, conformational and functional equivalence with the human-derived protein. Protein Eng 1998, 11:583-588.
    • (1998) Protein Eng , vol.11 , pp. 583-588
    • Manjula, B.N.1    Kumar, R.2    Sun, D.P.3    Ho, N.T.4    Ho, C.5    Rao, J.M.6    Malavalli, A.7    Acharya, A.S.8
  • 42
    • 0035093694 scopus 로고    scopus 로고
    • Enhanced transformation efficiency of an anticoagulant hirudin gene into Saccharomyces cerevisiae by a double delta-sequence
    • Kim M.D., Yoo Y.J., Rhee S.K., Seo J.H. Enhanced transformation efficiency of an anticoagulant hirudin gene into Saccharomyces cerevisiae by a double delta-sequence. J Microbiol Biotechnol 2001, 11:61-64.
    • (2001) J Microbiol Biotechnol , vol.11 , pp. 61-64
    • Kim, M.D.1    Yoo, Y.J.2    Rhee, S.K.3    Seo, J.H.4
  • 45
    • 0027451963 scopus 로고
    • Effects of beta 6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast
    • Adachi K., Konitzer P., Kim J., Welch N., Surrey S. Effects of beta 6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast. J Biol Chem 1993, 268:21650-21656.
    • (1993) J Biol Chem , vol.268 , pp. 21650-21656
    • Adachi, K.1    Konitzer, P.2    Kim, J.3    Welch, N.4    Surrey, S.5
  • 47
    • 84869877819 scopus 로고    scopus 로고
    • Enhancing recombinant hemoglobin production by co-expression with alpha hemoglobin stabilizing protein
    • Google Patents
    • Olson JS, Weiss MJ, Enhancing recombinant hemoglobin production by co-expression with alpha hemoglobin stabilizing protein. Google Patents; 2010.
    • (2010)
    • Olson, J.S.1    Weiss, M.J.2
  • 48
    • 77949497124 scopus 로고    scopus 로고
    • The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly
    • Mollan T.L., Yu X., Weiss M.J., Olson J.S. The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly. Antioxid Redox signal 2010, 12:219-231.
    • (2010) Antioxid Redox signal , vol.12 , pp. 219-231
    • Mollan, T.L.1    Yu, X.2    Weiss, M.J.3    Olson, J.S.4
  • 49
    • 0029022510 scopus 로고
    • Hemin-induced acceleration of hemoglobin production in immature cultured erythroid cells: preferential enhancement of fetal hemoglobin
    • Fibach E., Kollia P., Schechter A., Noguchi C., Rodgers G. Hemin-induced acceleration of hemoglobin production in immature cultured erythroid cells: preferential enhancement of fetal hemoglobin. Blood 1995, 85:2967-2974.
    • (1995) Blood , vol.85 , pp. 2967-2974
    • Fibach, E.1    Kollia, P.2    Schechter, A.3    Noguchi, C.4    Rodgers, G.5
  • 50
    • 0031574266 scopus 로고    scopus 로고
    • Turnover of recombinant human hemoglobin in Escherichia coli occurs rapidly for insoluble and slowly for soluble globin
    • Weickert M.J., Curry S.R. Turnover of recombinant human hemoglobin in Escherichia coli occurs rapidly for insoluble and slowly for soluble globin. Arch Biochem Biophys 1997, 348:337-346.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 337-346
    • Weickert, M.J.1    Curry, S.R.2
  • 52
    • 0141996306 scopus 로고    scopus 로고
    • Identification of rate-limiting steps in yeast heme biosynthesis
    • Hoffman M., Góra M., Rytka J. Identification of rate-limiting steps in yeast heme biosynthesis. Biochem Biophys Res Commun 2003, 310:1247-1253.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 1247-1253
    • Hoffman, M.1    Góra, M.2    Rytka, J.3
  • 53
    • 4544275383 scopus 로고    scopus 로고
    • Production of antithrombotic hirudin in GAL1-disrupted Saccharomyces cerevisiae
    • Kim M.D., Lee T.H., Lim H.K., Seo J.H. Production of antithrombotic hirudin in GAL1-disrupted Saccharomyces cerevisiae. Appl Microbiol Biotechnol 2004, 65:259-262.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 259-262
    • Kim, M.D.1    Lee, T.H.2    Lim, H.K.3    Seo, J.H.4
  • 56
    • 33750587201 scopus 로고    scopus 로고
    • Manufacturing of recombinant therapeutic proteins in microbial systems
    • Graumann K., Premstaller A. Manufacturing of recombinant therapeutic proteins in microbial systems. Biotechnol J 2006, 1:164-186.
    • (2006) Biotechnol J , vol.1 , pp. 164-186
    • Graumann, K.1    Premstaller, A.2
  • 57
    • 0037275711 scopus 로고    scopus 로고
    • Angiostatin production in cultivation of recombinant Pichia pastoris fed with mixed carbon sources
    • Xie J., Zhang L., Ye Q., Zhou Q., Xin L., Du P., Gan R. Angiostatin production in cultivation of recombinant Pichia pastoris fed with mixed carbon sources. Biotechnol Lett 2003, 25:173-177.
    • (2003) Biotechnol Lett , vol.25 , pp. 173-177
    • Xie, J.1    Zhang, L.2    Ye, Q.3    Zhou, Q.4    Xin, L.5    Du, P.6    Gan, R.7
  • 60
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • Schmidt F.R. Recombinant expression systems in the pharmaceutical industry. Appl Microbiol Biotechnol 2004, 65:363-372.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 61
    • 0033975293 scopus 로고    scopus 로고
    • High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation
    • Kobayashi K., Kuwae S., Ohya T., Ohda T., Ohyama M., Ohi H., Tomomitsu K., Ohmura T. High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation. J Biosci Bioeng 2000, 89:55-61.
    • (2000) J Biosci Bioeng , vol.89 , pp. 55-61
    • Kobayashi, K.1    Kuwae, S.2    Ohya, T.3    Ohda, T.4    Ohyama, M.5    Ohi, H.6    Tomomitsu, K.7    Ohmura, T.8
  • 63
    • 0031194183 scopus 로고    scopus 로고
    • Expression and purification of recombinant human apolipoprotein A-I in Chinese hamster ovary cells
    • Schmidt H.H., Genschel J., Haas R., Buttner C., Manns M.P. Expression and purification of recombinant human apolipoprotein A-I in Chinese hamster ovary cells. Protein Expr Purif 1997, 10:226-236.
    • (1997) Protein Expr Purif , vol.10 , pp. 226-236
    • Schmidt, H.H.1    Genschel, J.2    Haas, R.3    Buttner, C.4    Manns, M.P.5
  • 64
    • 77951999991 scopus 로고    scopus 로고
    • Application of simple fed-batch technique to high-level secretory production of insulin precursor using Pichia pastoris with subsequent purification and conversion to human insulin
    • Gurramkonda C., Polez S., Skoko N., Adnan A., Gabel T., Chugh D., Swaminathan S., Khanna N., Tisminetzky S., Rinas U. Application of simple fed-batch technique to high-level secretory production of insulin precursor using Pichia pastoris with subsequent purification and conversion to human insulin. Microb Cell Fact 2010, 9:31.
    • (2010) Microb Cell Fact , vol.9 , pp. 31
    • Gurramkonda, C.1    Polez, S.2    Skoko, N.3    Adnan, A.4    Gabel, T.5    Chugh, D.6    Swaminathan, S.7    Khanna, N.8    Tisminetzky, S.9    Rinas, U.10
  • 65
    • 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
  • 66
    • 77949500672 scopus 로고    scopus 로고
    • Cervarix: a vaccine for the prevention of HPV 16, 18-associated cervical cancer
    • Monie A., Hung C.F., Roden R., Wu T.C. Cervarix: a vaccine for the prevention of HPV 16, 18-associated cervical cancer. Biologics 2008, 2:97-105.
    • (2008) Biologics , vol.2 , pp. 97-105
    • Monie, A.1    Hung, C.F.2    Roden, R.3    Wu, T.C.4
  • 67
    • 0028884983 scopus 로고
    • Secretion of biologically active human proapolipoprotein A-I in a baculovirus-insect cell system: protection from degradation by protease inhibitors
    • Pyle L.E., Barton P., Fujiwara Y., Mitchell A., Fidge N. Secretion of biologically active human proapolipoprotein A-I in a baculovirus-insect cell system: protection from degradation by protease inhibitors. J Lipid Res 1995, 36:2355-2361.
    • (1995) J Lipid Res , vol.36 , pp. 2355-2361
    • Pyle, L.E.1    Barton, P.2    Fujiwara, Y.3    Mitchell, A.4    Fidge, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.