메뉴 건너뛰기




Volumn 127, Issue 3, 2007, Pages 335-347

Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes

Author keywords

Comparative evaluation; Eukaryotic expression systems; Prokaryotic expression systems

Indexed keywords

BIODIVERSITY; BIOTECHNOLOGY; CELL CULTURE; MICROORGANISMS; OPTIMAL CONTROL SYSTEMS; PROTEINS; YEAST;

EID: 34548110776     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.07.012     Document Type: Review
Times cited : (279)

References (122)
  • 1
    • 0038294644 scopus 로고    scopus 로고
    • Production of Chlamydia pneumonia proteins in Bacillus subtilis and their use in characterization of immune responses in the experimental infection model
    • Airaksinen U., PenttilÄ T., WahlstrÖm E., Vuola J.M., Puolakkainen M., and Sarvas M. Production of Chlamydia pneumonia proteins in Bacillus subtilis and their use in characterization of immune responses in the experimental infection model. Clin. Diag. Lab. Immunol. 16 (2003) 367-375
    • (2003) Clin. Diag. Lab. Immunol. , vol.16 , pp. 367-375
    • Airaksinen, U.1    PenttilÄ, T.2    WahlstrÖm, E.3    Vuola, J.M.4    Puolakkainen, M.5    Sarvas, M.6
  • 2
    • 33745209693 scopus 로고    scopus 로고
    • Production of hantavirus Puumala nucleocapsid protein in Saccharomyces cerevisiae for vaccine and diagnostics
    • Antoniukas L., Grammel H., and Reichl U. Production of hantavirus Puumala nucleocapsid protein in Saccharomyces cerevisiae for vaccine and diagnostics. J. Biotechnol. 124 (2006) 347-362
    • (2006) J. Biotechnol. , vol.124 , pp. 347-362
    • Antoniukas, L.1    Grammel, H.2    Reichl, U.3
  • 3
    • 29144471178 scopus 로고    scopus 로고
    • The use of a recombinant baculovirus expressing a chitinase from the hard tick Haemaphysalis longicornis and its potential application as a bioacaricide for tick control
    • Assenga S.P., You M., Shy C.H., Yamagishi J., Sakaguchi T., Zhou J., Kibe M.K., Xuan X., and Fujisaki K. The use of a recombinant baculovirus expressing a chitinase from the hard tick Haemaphysalis longicornis and its potential application as a bioacaricide for tick control. Parasitol. Res. 98 (2006) 111-118
    • (2006) Parasitol. Res. , vol.98 , pp. 111-118
    • Assenga, S.P.1    You, M.2    Shy, C.H.3    Yamagishi, J.4    Sakaguchi, T.5    Zhou, J.6    Kibe, M.K.7    Xuan, X.8    Fujisaki, K.9
  • 5
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 6
    • 0035158317 scopus 로고    scopus 로고
    • Yeast - a panacea for the structure - function analysis of membrane proteins?
    • Bill R.M. Yeast - a panacea for the structure - function analysis of membrane proteins?. Curr. Genet. 40 (2001) 157-171
    • (2001) Curr. Genet. , vol.40 , pp. 157-171
    • Bill, R.M.1
  • 8
    • 0029898341 scopus 로고    scopus 로고
    • Expression of the green fluorescent protein-encoding gene from a tobacco mosaic virus-based vector
    • Casper S.J., and Holt C.A. Expression of the green fluorescent protein-encoding gene from a tobacco mosaic virus-based vector. Gene 173 (1996) 69-73
    • (1996) Gene , vol.173 , pp. 69-73
    • Casper, S.J.1    Holt, C.A.2
  • 10
    • 1442352581 scopus 로고    scopus 로고
    • High-level accumulation of a recombinant antibody fragment in the periplasm of Escherichia coli requires a triple-mutant (degP prc spr) host strain
    • Chen C., Snedecor B., Nishihara J.C., Joly J.C., McFarland N., Andersen D.C., Battersby J.E., and Champion K.M. High-level accumulation of a recombinant antibody fragment in the periplasm of Escherichia coli requires a triple-mutant (degP prc spr) host strain. Biotechnol. Bioeng. 85 (2004) 463-474
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 463-474
    • Chen, C.1    Snedecor, B.2    Nishihara, J.C.3    Joly, J.C.4    McFarland, N.5    Andersen, D.C.6    Battersby, J.E.7    Champion, K.M.8
  • 11
    • 0033935592 scopus 로고    scopus 로고
    • Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence
    • Choi J.H., Jeong K.J., Kim S.C., and Lee S.Y. Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence. Appl. Microbiol. Biotechnol. 53 (2000) 640-645
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 640-645
    • Choi, J.H.1    Jeong, K.J.2    Kim, S.C.3    Lee, S.Y.4
  • 12
    • 9944248057 scopus 로고    scopus 로고
    • A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor
    • Chou C.F., Shen S., Tan Y.J., Fielding B.C., Tan T.H., Fu J., Xu Q., Lim S.G., and Hong W. A novel cell-based binding assay system reconstituting interaction between SARS-CoV S protein and its cellular receptor. J. Virol. Meth. 123 (2005) 41-48
    • (2005) J. Virol. Meth. , vol.123 , pp. 41-48
    • Chou, C.F.1    Shen, S.2    Tan, Y.J.3    Fielding, B.C.4    Tan, T.H.5    Fu, J.6    Xu, Q.7    Lim, S.G.8    Hong, W.9
  • 13
    • 0032105836 scopus 로고    scopus 로고
    • The mammary gland as a bioreactor: expression, processing, and production of recombinant proteins
    • Clark A.J. The mammary gland as a bioreactor: expression, processing, and production of recombinant proteins. J. Mammary Gland Biol. Neoplasia 3 (1998) 337-350
    • (1998) J. Mammary Gland Biol. Neoplasia , vol.3 , pp. 337-350
    • Clark, A.J.1
  • 14
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark E.B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9 (1998) 157-163
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 157-163
    • Clark, E.B.1
  • 15
    • 3442876757 scopus 로고    scopus 로고
    • Transgenic rice plants expressing the antifungal AFP protein from Aspergillus giganteus show enhanced resistance to the rice blast fungus Magnaporthe grisea
    • Coca M., Bortolotti C., Rufat M., Penas G., Eritja R., Tharreau D., del Pozo A.M., Messeguer J., and San Segundo B. Transgenic rice plants expressing the antifungal AFP protein from Aspergillus giganteus show enhanced resistance to the rice blast fungus Magnaporthe grisea. Plant. Mol. Biol. 54 (2004) 245-259
    • (2004) Plant. Mol. Biol. , vol.54 , pp. 245-259
    • Coca, M.1    Bortolotti, C.2    Rufat, M.3    Penas, G.4    Eritja, R.5    Tharreau, D.6    del Pozo, A.M.7    Messeguer, J.8    San Segundo, B.9
  • 16
    • 0030584654 scopus 로고    scopus 로고
    • Chaperone-assisted protein expression
    • Cole P.A. Chaperone-assisted protein expression. Structure 4 (1996) 239-242
    • (1996) Structure , vol.4 , pp. 239-242
    • Cole, P.A.1
  • 18
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • Daly R., and Hearn M.T.W. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J. Mol. Recogn. 18 (2005) 119-138
    • (2005) J. Mol. Recogn. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 19
    • 0025372845 scopus 로고
    • High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants
    • Davis S.J., Ward H.A., Puklavec M.J., Willis A.C., Williams A.F., and Barclay A.N. High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants. J. Biol. Chem. 265 (1990) 10410-10418
    • (1990) J. Biol. Chem. , vol.265 , pp. 10410-10418
    • Davis, S.J.1    Ward, H.A.2    Puklavec, M.J.3    Willis, A.C.4    Williams, A.F.5    Barclay, A.N.6
  • 20
    • 0034517030 scopus 로고    scopus 로고
    • Cloning, pharmacological characterization and brain distribution of the rat apelin receptor
    • De Mota N., Lenkei Z., and Llorens-Cortes C. Cloning, pharmacological characterization and brain distribution of the rat apelin receptor. Neuroendocrinology 72 (2000) 400-407
    • (2000) Neuroendocrinology , vol.72 , pp. 400-407
    • De Mota, N.1    Lenkei, Z.2    Llorens-Cortes, C.3
  • 21
    • 31944452398 scopus 로고    scopus 로고
    • Vaccination of yeast sensitive individuals: review of safety data in the US vaccine adverse event reporting system (VAERS)
    • V.A.E.R.S. Team
    • DiMiceli L., Pool V., Kelso J.M., Shadomy S.V., Iskander J., and V.A.E.R.S. Team. Vaccination of yeast sensitive individuals: review of safety data in the US vaccine adverse event reporting system (VAERS). Vaccine 24 (2006) 703-707
    • (2006) Vaccine , vol.24 , pp. 703-707
    • DiMiceli, L.1    Pool, V.2    Kelso, J.M.3    Shadomy, S.V.4    Iskander, J.5
  • 22
    • 0033669729 scopus 로고    scopus 로고
    • Impaired resensitization and recycling of the cholecystokinin receptor by co-expression of its second intracellular loop
    • Ding X.Q., Rao R.V., Kuntz S.M., Holicky E.L., and Miller L.J. Impaired resensitization and recycling of the cholecystokinin receptor by co-expression of its second intracellular loop. Mol. Pharmacol. 58 (2000) 1424-1433
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1424-1433
    • Ding, X.Q.1    Rao, R.V.2    Kuntz, S.M.3    Holicky, E.L.4    Miller, L.J.5
  • 23
    • 0038544334 scopus 로고    scopus 로고
    • Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
    • Donald L., and Jarvis D.L. Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production. Virology 310 (2003) 1-7
    • (2003) Virology , vol.310 , pp. 1-7
    • Donald, L.1    Jarvis, D.L.2
  • 25
    • 0030272085 scopus 로고    scopus 로고
    • Recombinant protein production in transgenic animals
    • Echelard Y. Recombinant protein production in transgenic animals. Curr. Opin. Biotechnol. 7 (1996) 536-540
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 536-540
    • Echelard, Y.1
  • 26
    • 0027451931 scopus 로고
    • Current applications of COS cell based transient expression systems
    • Edwards C.P., and Aruffo A. Current applications of COS cell based transient expression systems. Curr. Opin. Biotechnol. 4 (1993) 558-563
    • (1993) Curr. Opin. Biotechnol. , vol.4 , pp. 558-563
    • Edwards, C.P.1    Aruffo, A.2
  • 27
    • 0142250913 scopus 로고    scopus 로고
    • Transgenic rabbits as therapeutic protein bioreactors and human disease models
    • Fan J., and Watanabe T. Transgenic rabbits as therapeutic protein bioreactors and human disease models. Pharmacol. Ther. 99 (2003) 261-282
    • (2003) Pharmacol. Ther. , vol.99 , pp. 261-282
    • Fan, J.1    Watanabe, T.2
  • 28
    • 13444304245 scopus 로고    scopus 로고
    • Bacillus subtilis as a tool for vaccine development: from antigen factories to delivery vectors
    • Ferreira L.C.S., Ferreira R.C.C., and Schumann W. Bacillus subtilis as a tool for vaccine development: from antigen factories to delivery vectors. Ann. Braz. Acad. Sci. 77 (2005) 113-124
    • (2005) Ann. Braz. Acad. Sci. , vol.77 , pp. 113-124
    • Ferreira, L.C.S.1    Ferreira, R.C.C.2    Schumann, W.3
  • 29
    • 0033667765 scopus 로고    scopus 로고
    • Molecular farming of pharmaceutical proteins
    • Fischer R., and Emanns N. Molecular farming of pharmaceutical proteins. Transgenic Res. 9 (2000) 279-299
    • (2000) Transgenic Res. , vol.9 , pp. 279-299
    • Fischer, R.1    Emanns, N.2
  • 31
    • 27644574423 scopus 로고    scopus 로고
    • New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolytica-a comparison
    • Gellissen G., Kunze G., Gaillardin C., Cregg J.M., Berardi E., Veenhuis M., and van der Klei I. New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolytica-a comparison. FEMS Yeast Res. 5 (2005) 1079-1096
    • (2005) FEMS Yeast Res. , vol.5 , pp. 1079-1096
    • Gellissen, G.1    Kunze, G.2    Gaillardin, C.3    Cregg, J.M.4    Berardi, E.5    Veenhuis, M.6    van der Klei, I.7
  • 32
    • 0029780708 scopus 로고    scopus 로고
    • Methylotrophic yeast Hansenula polymorpha as production organism for recombinant pharmaceuticals
    • Gellissen G., and Melber K. Methylotrophic yeast Hansenula polymorpha as production organism for recombinant pharmaceuticals. Drug Res. 46 (1996) 943-948
    • (1996) Drug Res. , vol.46 , pp. 943-948
    • Gellissen, G.1    Melber, K.2
  • 33
    • 0026452184 scopus 로고
    • Analysis of soluble human and mouse interferon-gamma receptors expressed in eukaryotic cells
    • Gentz R., Hayes A., Grau N., Fountoulakis M., Lahm H.W., Ozmen L., and Garotta G. Analysis of soluble human and mouse interferon-gamma receptors expressed in eukaryotic cells. Eur. J. Biochem. 210 (1992) 545-554
    • (1992) Eur. J. Biochem. , vol.210 , pp. 545-554
    • Gentz, R.1    Hayes, A.2    Grau, N.3    Fountoulakis, M.4    Lahm, H.W.5    Ozmen, L.6    Garotta, G.7
  • 34
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: status report and future prospects
    • Georgiou G., and Segatori L. Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr. Opin. Biotechnol. 16 (2005) 538-545
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 35
    • 0036665416 scopus 로고    scopus 로고
    • Baculovirus as mammalian cell expression vector for gene therapy: an emerging strategy
    • Ghosh S., Parvez M.K., Banerjee K., Sarin S.K., and Hasnain S.E. Baculovirus as mammalian cell expression vector for gene therapy: an emerging strategy. Mol. Ther. 6 (2002) 5-11
    • (2002) Mol. Ther. , vol.6 , pp. 5-11
    • Ghosh, S.1    Parvez, M.K.2    Banerjee, K.3    Sarin, S.K.4    Hasnain, S.E.5
  • 36
    • 0033375049 scopus 로고    scopus 로고
    • Expression system for foreign genes using the fission yeast Schizosaccharomyces pombe
    • Giga-Hama Y., and Kumagai H. Expression system for foreign genes using the fission yeast Schizosaccharomyces pombe. Biotechnol. Appl. Biochem. 30 (1999) 235-244
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 235-244
    • Giga-Hama, Y.1    Kumagai, H.2
  • 39
    • 0032581989 scopus 로고    scopus 로고
    • Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants
    • Gomez N., Carrillo C., Salinas J., Parra F., Borca M.V., and Escribano J.M. Expression of immunogenic glycoprotein S polypeptides from transmissible gastroenteritis coronavirus in transgenic plants. Virology 249 (1998) 352-358
    • (1998) Virology , vol.249 , pp. 352-358
    • Gomez, N.1    Carrillo, C.2    Salinas, J.3    Parra, F.4    Borca, M.V.5    Escribano, J.M.6
  • 40
    • 0020363515 scopus 로고
    • Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes
    • Grosjean H., and Fiers W. Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene 18 (1982) 199-209
    • (1982) Gene , vol.18 , pp. 199-209
    • Grosjean, H.1    Fiers, W.2
  • 44
    • 0001322460 scopus 로고
    • The safe and ration deployment of Bacillus thuringiensis genes in crop plant: conclusions and recommendation of OECD workshop on ecological implication of transgenic crops containing Bt toxin genes
    • Hokkanen H.M.T., and Wearing C.H. The safe and ration deployment of Bacillus thuringiensis genes in crop plant: conclusions and recommendation of OECD workshop on ecological implication of transgenic crops containing Bt toxin genes. Biocontrol Sci. Technol. 4 (1994) 399-403
    • (1994) Biocontrol Sci. Technol. , vol.4 , pp. 399-403
    • Hokkanen, H.M.T.1    Wearing, C.H.2
  • 45
    • 0030890431 scopus 로고    scopus 로고
    • Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered metabolite production
    • Holmberg N., Lilius G., Bailey J.E., and Bulow L. Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered metabolite production. Nat. Biotechnol. 15 (1997) 244-247
    • (1997) Nat. Biotechnol. , vol.15 , pp. 244-247
    • Holmberg, N.1    Lilius, G.2    Bailey, J.E.3    Bulow, L.4
  • 46
    • 0033672657 scopus 로고    scopus 로고
    • Transgenic animal bioreactors
    • Houdebine L.M. Transgenic animal bioreactors. Transgenic Res. 9 (2000) 305-320
    • (2000) Transgenic Res. , vol.9 , pp. 305-320
    • Houdebine, L.M.1
  • 47
    • 0033597180 scopus 로고    scopus 로고
    • Construction of modular and versatile plasmid vectors for the high-level expression of single or multiple genes in insects and insect cell lines
    • Huynh C.Q., and Zieler H. Construction of modular and versatile plasmid vectors for the high-level expression of single or multiple genes in insects and insect cell lines. Mol. Biol. 288 (1999) 13-20
    • (1999) Mol. Biol. , vol.288 , pp. 13-20
    • Huynh, C.Q.1    Zieler, H.2
  • 48
    • 0017697097 scopus 로고
    • Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin
    • Itakura K., Hirose T., Crea R., Riggs A.D., Heyneker H.L., Bolivar F., and Boyer H.W. Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin. Science 198 (1977) 1056-1063
    • (1977) Science , vol.198 , pp. 1056-1063
    • Itakura, K.1    Hirose, T.2    Crea, R.3    Riggs, A.D.4    Heyneker, H.L.5    Bolivar, F.6    Boyer, H.W.7
  • 49
    • 33644552393 scopus 로고    scopus 로고
    • Competitive bioreactor hens on the horizon
    • Ivarie R. Competitive bioreactor hens on the horizon. Trends Biotechnol. 24 (2006) 101-102
    • (2006) Trends Biotechnol. , vol.24 , pp. 101-102
    • Ivarie, R.1
  • 50
    • 0036968875 scopus 로고    scopus 로고
    • Recent studies of protein secretion by filamentous fungi
    • Iwashita K. Recent studies of protein secretion by filamentous fungi. J. Biosci. Bioeng. 94 (2002) 530-535
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 530-535
    • Iwashita, K.1
  • 51
    • 0035226492 scopus 로고    scopus 로고
    • The production of foreign proteins from genetically modified plant cells
    • James E., and Lee J.M. The production of foreign proteins from genetically modified plant cells. Adv. Biochem. Eng. Biotechnol. 72 (2001) 127-156
    • (2001) Adv. Biochem. Eng. Biotechnol. , vol.72 , pp. 127-156
    • James, E.1    Lee, J.M.2
  • 52
    • 0035839589 scopus 로고    scopus 로고
    • Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer
    • Janiyani K., Bordelon T., Waldrop G.L., and Cronan Jr. J.E. Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer. J. Biol. Chem. 276 (2001) 29864-29870
    • (2001) J. Biol. Chem. , vol.276 , pp. 29864-29870
    • Janiyani, K.1    Bordelon, T.2    Waldrop, G.L.3    Cronan Jr., J.E.4
  • 53
    • 0032539933 scopus 로고    scopus 로고
    • Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation
    • Joly J.C., Leung W.S., and Swartz J.R. Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation. Proc. Natl. Acad. Sci. 95 (1998) 2773-2777
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 2773-2777
    • Joly, J.C.1    Leung, W.S.2    Swartz, J.R.3
  • 54
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • Jonasson P., Liljeqvist S., Nygren P.A., and Stahl S. Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol. Appl. Biochem. 35 (2002) 91-105
    • (2002) Biotechnol. Appl. Biochem. , vol.35 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.A.3    Stahl, S.4
  • 55
    • 0031056155 scopus 로고    scopus 로고
    • The production of recombinant glycoproteins with special reference to simple eukaryotes including Dictyostelium discoideum
    • Jung E., and Williams K.L. The production of recombinant glycoproteins with special reference to simple eukaryotes including Dictyostelium discoideum. Biotechnol. Appl. Biochem. 25 (1997) 3-8
    • (1997) Biotechnol. Appl. Biochem. , vol.25 , pp. 3-8
    • Jung, E.1    Williams, K.L.2
  • 56
    • 0031241078 scopus 로고    scopus 로고
    • Expression of human immunodeficiency virus genes using baculovirus expression system
    • Kang C.Y. Expression of human immunodeficiency virus genes using baculovirus expression system. Mol. Biotechnol. 8 (1997) 173-187
    • (1997) Mol. Biotechnol. , vol.8 , pp. 173-187
    • Kang, C.Y.1
  • 57
    • 16844374028 scopus 로고    scopus 로고
    • Novel poly-GalNAcbeta1-4GlcNAc (LacdiNAc) and fucosylated poly-LacdiNAc N-glycans from mammalian cells expressing beta1, 4-N-acetylgalactosaminyltransferase and alpha1,3-fucosyltransferase
    • Kawar Z.S., Haslam S.M., Morris H.R., Dell A., and Cummings R.D. Novel poly-GalNAcbeta1-4GlcNAc (LacdiNAc) and fucosylated poly-LacdiNAc N-glycans from mammalian cells expressing beta1, 4-N-acetylgalactosaminyltransferase and alpha1,3-fucosyltransferase. J. Biol. Chem. 280 (2005) 12810-12819
    • (2005) J. Biol. Chem. , vol.280 , pp. 12810-12819
    • Kawar, Z.S.1    Haslam, S.M.2    Morris, H.R.3    Dell, A.4    Cummings, R.D.5
  • 58
    • 0027651179 scopus 로고
    • The use of baculovirus as expression vectors
    • Kidd I.M., and Emery V.C. The use of baculovirus as expression vectors. Appl. Biochem. Biotechnol. 42 (1993) 137-159
    • (1993) Appl. Biochem. Biotechnol. , vol.42 , pp. 137-159
    • Kidd, I.M.1    Emery, V.C.2
  • 59
    • 0035997972 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of thermostable DNA polymerase from Thermoanaerobacter yonseiensis
    • Kim D.J., Jang H.J., Pyun Y.R., and Kim Y.S. Cloning, expression, and characterization of thermostable DNA polymerase from Thermoanaerobacter yonseiensis. J. Biochem. Mol. Biol. 35 (2002) 320-329
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 320-329
    • Kim, D.J.1    Jang, H.J.2    Pyun, Y.R.3    Kim, Y.S.4
  • 62
    • 0025766837 scopus 로고
    • Host range expansion by recombinantion of the baculovirus Bombyx mori nuclear polyhedorosis virus and Autographa californica nuclear polyhedrosis virus
    • Kondo A., and Maeda S. Host range expansion by recombinantion of the baculovirus Bombyx mori nuclear polyhedorosis virus and Autographa californica nuclear polyhedrosis virus. J. Virol. 65 (1991) 3625-3632
    • (1991) J. Virol. , vol.65 , pp. 3625-3632
    • Kondo, A.1    Maeda, S.2
  • 63
    • 0032861929 scopus 로고    scopus 로고
    • Recombinant baculoviruses as expression vectors for insect and mammalian cells
    • Kost T.A., and Condreay J.P. Recombinant baculoviruses as expression vectors for insect and mammalian cells. Curr. Opin. Biotechnol. 10 (1999) 428-433
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 428-433
    • Kost, T.A.1    Condreay, J.P.2
  • 64
    • 33645233636 scopus 로고    scopus 로고
    • Immunogenicity of a new, low-cost recombinant hepatitis B vaccine derived from Hansenula polymorpha in adults
    • Kulkarni P.S., Raut S.K., Patki P.S., Phadke M.A., Jadhav S.S., Kapre S.V., Dhorje S.P., and Godse S.R. Immunogenicity of a new, low-cost recombinant hepatitis B vaccine derived from Hansenula polymorpha in adults. Vaccine 24 (2006) 3457-3460
    • (2006) Vaccine , vol.24 , pp. 3457-3460
    • Kulkarni, P.S.1    Raut, S.K.2    Patki, P.S.3    Phadke, M.A.4    Jadhav, S.S.5    Kapre, S.V.6    Dhorje, S.P.7    Godse, S.R.8
  • 65
    • 11144262701 scopus 로고    scopus 로고
    • Expression and secretion of a prokaryotic protein streptokinase without glycosylation and degradation in Schizosaccharomyces pombe
    • Kumar R., and Singh J. Expression and secretion of a prokaryotic protein streptokinase without glycosylation and degradation in Schizosaccharomyces pombe. Yeast 21 (2004) 1343-1358
    • (2004) Yeast , vol.21 , pp. 1343-1358
    • Kumar, R.1    Singh, J.2
  • 66
    • 0034467912 scopus 로고    scopus 로고
    • A baculovirus superinfection system: efficient vehicle for gene transfer into Drosophila S2 Cells
    • Lee D.F., Chen C.C., Hsu T.A., and Juang J.L. A baculovirus superinfection system: efficient vehicle for gene transfer into Drosophila S2 Cells. J. Virol. 74 (2000) 11873-11880
    • (2000) J. Virol. , vol.74 , pp. 11873-11880
    • Lee, D.F.1    Chen, C.C.2    Hsu, T.A.3    Juang, J.L.4
  • 68
    • 17644423916 scopus 로고    scopus 로고
    • Bistability in the Bacillus subtilis K-state (competence) system requires a positive feedback loop
    • Maamar H., and Dubnau D. Bistability in the Bacillus subtilis K-state (competence) system requires a positive feedback loop. Mol. Microbiol. 56 (2005) 615-624
    • (2005) Mol. Microbiol. , vol.56 , pp. 615-624
    • Maamar, H.1    Dubnau, D.2
  • 69
    • 1842530397 scopus 로고    scopus 로고
    • Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review
    • Madzak C., Gaillardin C., and Beckerich J.M. Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review. J. Biotechnol. 8 (2004) 63-81
    • (2004) J. Biotechnol. , vol.8 , pp. 63-81
    • Madzak, C.1    Gaillardin, C.2    Beckerich, J.M.3
  • 70
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism
    • Magliery T.J., Wilson C.G., Pan W., Mishler D., Ghosh I., Hamilton A.D., and Regan L. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127 (2005) 146-157
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 71
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 72
    • 0344820768 scopus 로고    scopus 로고
    • Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection
    • Marheineke K., Grunewald S., Christie W., and Reilander H. Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection. FEBS Lett. 441 (1998) 49-52
    • (1998) FEBS Lett. , vol.441 , pp. 49-52
    • Marheineke, K.1    Grunewald, S.2    Christie, W.3    Reilander, H.4
  • 73
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • Marston F.A. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240 (1986) 1-12
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.1
  • 74
    • 0034609942 scopus 로고    scopus 로고
    • Correction of glycogen storage disease type II by enzyme replacement with a recombinant human acid maltase produced by over-expression in a CHO-DHFR(neg) cell line
    • Martiniuk F., Chen A., Donnabella V., Arvanitopoulos E., Slonim A.E., Raben N., Plotz P., and Rom W.N. Correction of glycogen storage disease type II by enzyme replacement with a recombinant human acid maltase produced by over-expression in a CHO-DHFR(neg) cell line. Biochem. Biophys. Res. Commun. 276 (2000) 917-923
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 917-923
    • Martiniuk, F.1    Chen, A.2    Donnabella, V.3    Arvanitopoulos, E.4    Slonim, A.E.5    Raben, N.6    Plotz, P.7    Rom, W.N.8
  • 75
    • 0036008334 scopus 로고    scopus 로고
    • Ubiquitous expression of goat cyclin T1 in transgenic mice
    • Mata X., and Vilotte J.L. Ubiquitous expression of goat cyclin T1 in transgenic mice. Transgenic Res. 11 (2002) 65-68
    • (2002) Transgenic Res. , vol.11 , pp. 65-68
    • Mata, X.1    Vilotte, J.L.2
  • 77
    • 1842817622 scopus 로고    scopus 로고
    • A Combination of the arabidopsis DREB1A gene and stress-inducible rd29A promoter improved drought-and low-temperature stress tolerance in tobacco by gene transfer
    • Mie K., Setsuko M., Kazuo S., and Kazuko Y. A Combination of the arabidopsis DREB1A gene and stress-inducible rd29A promoter improved drought-and low-temperature stress tolerance in tobacco by gene transfer. Plant Cell Physiol. 45 (2004) 346-350
    • (2004) Plant Cell Physiol. , vol.45 , pp. 346-350
    • Mie, K.1    Setsuko, M.2    Kazuo, S.3    Kazuko, Y.4
  • 78
    • 0033180105 scopus 로고    scopus 로고
    • Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast
    • Monsalve R.I., Lu G., and King T.P. Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast. Protein Express. Purif. 16 (1999) 410-416
    • (1999) Protein Express. Purif. , vol.16 , pp. 410-416
    • Monsalve, R.I.1    Lu, G.2    King, T.P.3
  • 79
    • 21644467954 scopus 로고    scopus 로고
    • Expression and one-step purification of bovine interleukin-21 (IL-21) in silkworms using a hybrid baculovirus expression system
    • Muneta Y., Nagaya H., Minagawa Y., Enomoto C., Matsumoto S., and Mori Y. Expression and one-step purification of bovine interleukin-21 (IL-21) in silkworms using a hybrid baculovirus expression system. Biotechnol. Lett. 26 (2004) 1453-1458
    • (2004) Biotechnol. Lett. , vol.26 , pp. 1453-1458
    • Muneta, Y.1    Nagaya, H.2    Minagawa, Y.3    Enomoto, C.4    Matsumoto, S.5    Mori, Y.6
  • 80
    • 11244347772 scopus 로고    scopus 로고
    • Effects of overexpression of CXCL10 (cytokine-responsive gene-2) on MA-10 mouse Leydig tumor cell steroidogenesis and proliferation
    • Nagpal M.L., Chen Y., and Lin T. Effects of overexpression of CXCL10 (cytokine-responsive gene-2) on MA-10 mouse Leydig tumor cell steroidogenesis and proliferation. J. Endocrinol. 183 (2004) 585-594
    • (2004) J. Endocrinol. , vol.183 , pp. 585-594
    • Nagpal, M.L.1    Chen, Y.2    Lin, T.3
  • 81
    • 0026745006 scopus 로고
    • High-level stable expression of recombinant 5-HT1A 5-hydroxytryptamine receptors in Chinese hamster ovary cells
    • Newman-Tancredi A., Wootton R., and Strange P.G. High-level stable expression of recombinant 5-HT1A 5-hydroxytryptamine receptors in Chinese hamster ovary cells. J. Biochem. 285 (1992) 933-938
    • (1992) J. Biochem. , vol.285 , pp. 933-938
    • Newman-Tancredi, A.1    Wootton, R.2    Strange, P.G.3
  • 83
    • 0042267949 scopus 로고    scopus 로고
    • Cell surface expression of C1qRP/CD93 is stabilized by O-glycosylation
    • Park M., and Tenner A.J. Cell surface expression of C1qRP/CD93 is stabilized by O-glycosylation. J. Cell. Physiol. 196 (2003) 512-522
    • (2003) J. Cell. Physiol. , vol.196 , pp. 512-522
    • Park, M.1    Tenner, A.J.2
  • 84
    • 33748853882 scopus 로고    scopus 로고
    • Peckham, G.D., Bugos, R.C., Su, W.W., 2006. Purification of GFP fusion proteins from transgenic plant cell cultures. Protein Express. Purif. (Epub ahead of print).
  • 86
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley A.P. The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 57 (1993) 50-108
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 87
    • 0034773690 scopus 로고    scopus 로고
    • A new beta-lactoglobulin-based vector targets luciferase cDNA expression to the mammary gland of transgenic mice
    • Reichenstein M., Gottlieb H., Damari G.M., Iavnilovitch E., and Barash I. A new beta-lactoglobulin-based vector targets luciferase cDNA expression to the mammary gland of transgenic mice. Transgenic Res. 10 (2001) 445-456
    • (2001) Transgenic Res. , vol.10 , pp. 445-456
    • Reichenstein, M.1    Gottlieb, H.2    Damari, G.M.3    Iavnilovitch, E.4    Barash, I.5
  • 88
  • 89
    • 33646193336 scopus 로고    scopus 로고
    • Plant-made vaccines: biotechnology and immunology in animal health
    • Rice J., Ainley W.M., and Shewen P. Plant-made vaccines: biotechnology and immunology in animal health. Anim. Health Res. Rev. 6 (2005) 199-209
    • (2005) Anim. Health Res. Rev. , vol.6 , pp. 199-209
    • Rice, J.1    Ainley, W.M.2    Shewen, P.3
  • 91
    • 16544362909 scopus 로고    scopus 로고
    • Genetically modified plants and food safety. State of the art and discussion in the European Union
    • Schauzu M. Genetically modified plants and food safety. State of the art and discussion in the European Union. Bundesgesundheitsblatt Gesundheitsforschung Gesundheitsschutz 47 (2004) 826-833
    • (2004) Bundesgesundheitsblatt Gesundheitsforschung Gesundheitsschutz , vol.47 , pp. 826-833
    • Schauzu, M.1
  • 92
    • 6344223568 scopus 로고    scopus 로고
    • A novel sorting signal for intracellular localization is present in the S protein of a porcine coronavirus but absent from severe acute respiratory syndrome-associated coronavirus
    • Schwegmann-Wessels C., Al-Falah M., Escors D., Wang Z., Zimmer G., Deng H., Enjuanes L., Naim H.Y., and Herrler G. A novel sorting signal for intracellular localization is present in the S protein of a porcine coronavirus but absent from severe acute respiratory syndrome-associated coronavirus. J. Biol. Chem. 279 (2004) 43661-43666
    • (2004) J. Biol. Chem. , vol.279 , pp. 43661-43666
    • Schwegmann-Wessels, C.1    Al-Falah, M.2    Escors, D.3    Wang, Z.4    Zimmer, G.5    Deng, H.6    Enjuanes, L.7    Naim, H.Y.8    Herrler, G.9
  • 93
    • 33745231331 scopus 로고    scopus 로고
    • Animal models of Charcot-Marie-Tooth disease type 1A
    • Sereda M.W., and Nave K.A. Animal models of Charcot-Marie-Tooth disease type 1A. Neuromol. Med. 8 (2006) 205-216
    • (2006) Neuromol. Med. , vol.8 , pp. 205-216
    • Sereda, M.W.1    Nave, K.A.2
  • 94
    • 14844295003 scopus 로고    scopus 로고
    • CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes
    • Servant P., Le Coq D., and Aymerich S. CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression of Bacillus subtilis gluconeogenic genes. Mol. Microbiol. 55 (2005) 1435-1451
    • (2005) Mol. Microbiol. , vol.55 , pp. 1435-1451
    • Servant, P.1    Le Coq, D.2    Aymerich, S.3
  • 95
    • 18444378154 scopus 로고    scopus 로고
    • Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo
    • Sims A.H., Gent M.E., Lanthaler K., Dunn-Coleman N.S., Oliver S.G., and Robson G.D. Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo. Appl. Environ. Microbiol. 71 (2005) 2737-2747
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2737-2747
    • Sims, A.H.1    Gent, M.E.2    Lanthaler, K.3    Dunn-Coleman, N.S.4    Oliver, S.G.5    Robson, G.D.6
  • 98
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sørensen H.P., and Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115 (2005) 113-128
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 99
    • 0001615271 scopus 로고
    • Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen J. Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. 44 (1958) 1072-1078
    • (1958) Proc. Natl. Acad. Sci. , vol.44 , pp. 1072-1078
    • Spizizen, J.1
  • 100
    • 0036956671 scopus 로고    scopus 로고
    • A novel high-cell-density protein expression system based on Ralstonia eutropha
    • Srinivasan S., Barnard G.C., and Gerngross T.U. A novel high-cell-density protein expression system based on Ralstonia eutropha. Appl. Environ. Microbiol. 68 (2002) 5925-5932
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5925-5932
    • Srinivasan, S.1    Barnard, G.C.2    Gerngross, T.U.3
  • 101
    • 0025370459 scopus 로고
    • Engineering Escherichia coli to secrete heterologous gene products
    • Stader J.A., and Silhavy T.J. Engineering Escherichia coli to secrete heterologous gene products. Meth. Enzymol. 185 (1990) 166-187
    • (1990) Meth. Enzymol. , vol.185 , pp. 166-187
    • Stader, J.A.1    Silhavy, T.J.2
  • 102
    • 0033485411 scopus 로고    scopus 로고
    • Effect of foreign N-terminal residues on the conformational stability of human lysozyme
    • Takano K., Tsuchimori K., Yamagata Y., and Yutani K. Effect of foreign N-terminal residues on the conformational stability of human lysozyme. Eur. J. Biochem. 266 (1999) 675-682
    • (1999) Eur. J. Biochem. , vol.266 , pp. 675-682
    • Takano, K.1    Tsuchimori, K.2    Yamagata, Y.3    Yutani, K.4
  • 103
    • 0030298385 scopus 로고    scopus 로고
    • Heterologous expression of G protein-coupled receptors
    • Tate C.G., and Grisshammer R. Heterologous expression of G protein-coupled receptors. Trends Biotechnol. 14 (1996) 426-430
    • (1996) Trends Biotechnol. , vol.14 , pp. 426-430
    • Tate, C.G.1    Grisshammer, R.2
  • 104
    • 0028815071 scopus 로고
    • Murine T and B cell responses to natural and recombinant hornet venom allergen Dol m 5.02 and its recombinant fragments
    • Te P., King Kochoumian L., and Lu G. Murine T and B cell responses to natural and recombinant hornet venom allergen Dol m 5.02 and its recombinant fragments. J. Immunol. 154 (1995) 577-584
    • (1995) J. Immunol. , vol.154 , pp. 577-584
    • Te, P.1    King Kochoumian, L.2    Lu, G.3
  • 106
    • 0034003792 scopus 로고    scopus 로고
    • Immunogenicity of porcine transmissible gastroenteritis virus spike protein expressed in plants
    • Tuboly T., Yu W., Bailey A., Degrandis S., Du S., Erickson L., and Nagy E. Immunogenicity of porcine transmissible gastroenteritis virus spike protein expressed in plants. Vaccine 18 (2000) 2023-2028
    • (2000) Vaccine , vol.18 , pp. 2023-2028
    • Tuboly, T.1    Yu, W.2    Bailey, A.3    Degrandis, S.4    Du, S.5    Erickson, L.6    Nagy, E.7
  • 110
    • 17044373656 scopus 로고    scopus 로고
    • The role of sigma (B) in the stress response of Gram-positive bacteria-targets for food preservation and safety
    • van Schaik W., and Abee T. The role of sigma (B) in the stress response of Gram-positive bacteria-targets for food preservation and safety. Curr. Opin. Biotechnol. 16 (2005) 218-224
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 218-224
    • van Schaik, W.1    Abee, T.2
  • 111
    • 14744296298 scopus 로고    scopus 로고
    • The development of a plant-based vaccine for measles
    • Webster D.E., Thomas M.C., Huang Z., and Wesselingh S.L. The development of a plant-based vaccine for measles. Vaccine 23 (2005) 1859-1865
    • (2005) Vaccine , vol.23 , pp. 1859-1865
    • Webster, D.E.1    Thomas, M.C.2    Huang, Z.3    Wesselingh, S.L.4
  • 113
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • Wildt S., and Gerngross T.U. The humanization of N-glycosylation pathways in yeast. Nat. Rev. Microbiol. 3 (2005) 119-128
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 119-128
    • Wildt, S.1    Gerngross, T.U.2
  • 114
    • 21644448789 scopus 로고    scopus 로고
    • Construction of a host range-expanded hybrid baculovirus of BmNPV and AcNPV, and knockout of cysteinase gene for more efficient expression
    • Wu X., Cao C., Xu Y., and Lu X. Construction of a host range-expanded hybrid baculovirus of BmNPV and AcNPV, and knockout of cysteinase gene for more efficient expression. Sci. China C: Life Sci. 47 (2004) 406-415
    • (2004) Sci. China C: Life Sci. , vol.47 , pp. 406-415
    • Wu, X.1    Cao, C.2    Xu, Y.3    Lu, X.4
  • 115
    • 30344488701 scopus 로고    scopus 로고
    • Improving rice nutrition: challenges and practical approaches for iron fortification
    • Yoshihara T., Takaiwa F., and Goto F. Improving rice nutrition: challenges and practical approaches for iron fortification. Food Nutr. Bull. 26 (2005) 416-418
    • (2005) Food Nutr. Bull. , vol.26 , pp. 416-418
    • Yoshihara, T.1    Takaiwa, F.2    Goto, F.3
  • 117
    • 0034695494 scopus 로고    scopus 로고
    • Trienoic fatty acids and plant tolerance of high temperature
    • Yuuki M., Michito T., Yoshichika K., Hiroaki K., and Koh I. Trienoic fatty acids and plant tolerance of high temperature. Science 287 (2000) 476-479
    • (2000) Science , vol.287 , pp. 476-479
    • Yuuki, M.1    Michito, T.2    Yoshichika, K.3    Hiroaki, K.4    Koh, I.5
  • 119
    • 0029998886 scopus 로고    scopus 로고
    • Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants
    • Zeng C.Q.Y., Wentz M.J., Cohen J., Estes M.K., and Ramig R.F. Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants. J. Virol. 70 (1996) 2736-2742
    • (1996) J. Virol. , vol.70 , pp. 2736-2742
    • Zeng, C.Q.Y.1    Wentz, M.J.2    Cohen, J.3    Estes, M.K.4    Ramig, R.F.5
  • 120
    • 33745637253 scopus 로고    scopus 로고
    • Secreted expression and purification of dengue 2 virus full-length nonstructural glycoprotein NS1 in Pichia pastoris
    • Zhou J.M., Tang Y.X., Fang D.Y., Zhou J.J., Liang Y., Guo H.Y., and Jiang L.F. Secreted expression and purification of dengue 2 virus full-length nonstructural glycoprotein NS1 in Pichia pastoris. Virus Genes 33 (2006) 27-32
    • (2006) Virus Genes , vol.33 , pp. 27-32
    • Zhou, J.M.1    Tang, Y.X.2    Fang, D.Y.3    Zhou, J.J.4    Liang, Y.5    Guo, H.Y.6    Jiang, L.F.7
  • 121
    • 0344443709 scopus 로고    scopus 로고
    • Virokinin, a bioactive peptide of the tachykinin family, is released from the fusion protein of bovine respiratory syncytial virus
    • Zimmer G., Rohn M., McGregor G.P., Schemann M., Conzelmann K.K., and Herrler G. Virokinin, a bioactive peptide of the tachykinin family, is released from the fusion protein of bovine respiratory syncytial virus. J. Biol. Chem. 278 (2003) 46854-46861
    • (2003) J. Biol. Chem. , vol.278 , pp. 46854-46861
    • Zimmer, G.1    Rohn, M.2    McGregor, G.P.3    Schemann, M.4    Conzelmann, K.K.5    Herrler, G.6
  • 122
    • 16844381561 scopus 로고    scopus 로고
    • Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy
    • Zullo S.J., Parks W.T., Chloupkova M., Wei B., Weiner H., Fenton W.A., Eisenstadt J.M., and Merril C.R. Stable transformation of CHO Cells and human NARP cybrids confers oligomycin resistance (oli(r)) following transfer of a mitochondrial DNA-encoded oli(r) ATPase6 gene to the nuclear genome: a model system for mtDNA gene therapy. Rejuvenation Res. 8 (2005) 18-28
    • (2005) Rejuvenation Res. , vol.8 , pp. 18-28
    • Zullo, S.J.1    Parks, W.T.2    Chloupkova, M.3    Wei, B.4    Weiner, H.5    Fenton, W.A.6    Eisenstadt, J.M.7    Merril, C.R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.