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Volumn 56, Issue 5, 1997, Pages 473-484

Production of recombinant proteins in transgenic plants: Practical considerations

Author keywords

Downstream processing; Gene expression; Recombinant protein; Transgenic plants

Indexed keywords

CROPS; GENES; PLANTS (BOTANY); PROTEINS;

EID: 0031555505     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19971205)56:5<473::AID-BIT1>3.0.CO;2-F     Document Type: Review
Times cited : (297)

References (129)
  • 1
    • 0030267492 scopus 로고    scopus 로고
    • Control of mRNA stability in higher plants
    • Abler, M. L., Green, P. J. 1996. Control of mRNA stability in higher plants. Plant Mol. Biol. 32: 63-78.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 63-78
    • Abler, M.L.1    Green, P.J.2
  • 2
    • 0030138749 scopus 로고    scopus 로고
    • High-level transgene expression in plant cells: Effects of a strong scaffold attachment region from tobacco
    • Allen, G. C., Hall, G., Jr., Michalowskj, S., Newman, W., Steven, S., Weissinger, A. K., Thompson, W. F. 1996. High-level transgene expression in plant cells: effects of a strong scaffold attachment region from tobacco. Plant Cell 8: 899-913.
    • (1996) Plant Cell , vol.8 , pp. 899-913
    • Allen, G.C.1    Hall Jr., G.2    Michalowskj, S.3    Newman, W.4    Steven, S.5    Weissinger, A.K.6    Thompson, W.F.7
  • 3
    • 0026436250 scopus 로고
    • Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine
    • Altenbach, S. B., Kuo, C. C., Staraci, L. C., Pearson, K. W., Wainwright, C., Georgescu, A., Townsend, J. 1992. Accumulation of a Brazil nut albumin in seeds of transgenic canola results in enhanced levels of seed protein methionine. Plant Mol. Biol. 18: 235-245.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 235-245
    • Altenbach, S.B.1    Kuo, C.C.2    Staraci, L.C.3    Pearson, K.W.4    Wainwright, C.5    Georgescu, A.6    Townsend, J.7
  • 4
    • 0024767003 scopus 로고
    • Enhancement of the methionine content of seed proteins by the expression of a chimeric gene encoding a methionine-rich protein in transgenic plants
    • Altenbach, S. B., Pearson, K. W., Meeker, G., Staraci, L. C., Sun, S. S. M. 1989. Enhancement of the methionine content of seed proteins by the expression of a chimeric gene encoding a methionine-rich protein in transgenic plants. Plant Mol. Biol. 13: 513-522.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 513-522
    • Altenbach, S.B.1    Pearson, K.W.2    Meeker, G.3    Staraci, L.C.4    Sun, S.S.M.5
  • 5
    • 0028249164 scopus 로고
    • Enzyme production by recombinant Aspergillus
    • Y. Murooka and T. Amanaka (eds.), Marcel Dekker, New York
    • Archer, D. B. 1994. Enzyme production by recombinant Aspergillus, pp. 373-393. In: Y. Murooka and T. Amanaka (eds.), Recombinant microbes for industrial and agricultural applications. Marcel Dekker, New York.
    • (1994) Recombinant Microbes for Industrial and Agricultural Applications , pp. 373-393
    • Archer, D.B.1
  • 7
    • 0001404083 scopus 로고
    • Accumulation and assembly of soybean β-conglycinin in seeds of transformed petunia plants
    • Beachy, R. N., Chen, Z. L., Horsch, R. B., Rogers, S. G., Hoffmann, N. J., Fraley, R. T. 1985. Accumulation and assembly of soybean β-conglycinin in seeds of transformed petunia plants. EMBO J. 4: 3047-3053.
    • (1985) EMBO J. , vol.4 , pp. 3047-3053
    • Beachy, R.N.1    Chen, Z.L.2    Horsch, R.B.3    Rogers, S.G.4    Hoffmann, N.J.5    Fraley, R.T.6
  • 8
    • 0026930761 scopus 로고
    • Intracellular trafficking of secretory proteins
    • Bednarek, S. Y., Raikhel, N. V. 1992. Intracellular trafficking of secretory proteins. Plant Mol. Biol. 20: 133-150.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 133-150
    • Bednarek, S.Y.1    Raikhel, N.V.2
  • 9
    • 0000365607 scopus 로고
    • Regulated genes in transgenic plants
    • Benfey, P. H., Chua, N. H. 1989. Regulated genes in transgenic plants. Science 244: 174-181.
    • (1989) Science , vol.244 , pp. 174-181
    • Benfey, P.H.1    Chua, N.H.2
  • 10
    • 0028005301 scopus 로고
    • A trout growth hormone is expressed, correctly folded and partially glycosylated in the leaves but not the seeds of transgenic plants
    • Bosch, D., Smal, J., Krebbers, E. 1994. A trout growth hormone is expressed, correctly folded and partially glycosylated in the leaves but not the seeds of transgenic plants. Transgen. Res. 3: 304-310.
    • (1994) Transgen. Res. , vol.3 , pp. 304-310
    • Bosch, D.1    Smal, J.2    Krebbers, E.3
  • 11
    • 0028278503 scopus 로고
    • Myb proteins 'talking' to their DNA
    • Boulikas, T. 1994. Myb proteins 'talking' to their DNA (review). Int. J. Oncol. 5: 101-109.
    • (1994) Int. J. Oncol. , vol.5 , pp. 101-109
    • Boulikas, T.1
  • 15
    • 0023503630 scopus 로고
    • Introns increase gene expression in cultured maize cells
    • Callis, J., Fromm, M., Walbot, V. 1987. Introns increase gene expression in cultured maize cells. Genes Devel. 1: 1183-1200.
    • (1987) Genes Devel. , vol.1 , pp. 1183-1200
    • Callis, J.1    Fromm, M.2    Walbot, V.3
  • 16
    • 0027564534 scopus 로고
    • Expression of the α-thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens
    • Carmona, M. J., Molina, A., Fernandez, J. A., Lopez-Fando, J. J., Garcia-Olmedo, F. 1993. Expression of the α-thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens. Plant J. 3: 457-462.
    • (1993) Plant J. , vol.3 , pp. 457-462
    • Carmona, M.J.1    Molina, A.2    Fernandez, J.A.3    Lopez-Fando, J.J.4    Garcia-Olmedo, F.5
  • 17
    • 0025879069 scopus 로고
    • Eukaryotic start and stop translation sites
    • Cavener, D. R., Ray, S. C. 1991. Eukaryotic start and stop translation sites. Nucl. Acids Res. 19: 3185-3192.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 3185-3192
    • Cavener, D.R.1    Ray, S.C.2
  • 21
    • 0001937973 scopus 로고
    • Downstream processing economics
    • J. A. Asenjo (ed.), Marcel Dekker, New York
    • Datar, R., Rosen, C.-G. 1991. Downstream processing economics, pp. 741-792. In: J. A. Asenjo (ed.), Separation processes in biotechnology. Marcel Dekker, New York.
    • (1991) Separation Processes in Biotechnology , pp. 741-792
    • Datar, R.1    Rosen, C.-G.2
  • 23
    • 0024982237 scopus 로고
    • Protein secretion in plant cells occur via a default pathway
    • Denecke, J., Botterman, J., Deblaere, R. 1990. Protein secretion in plant cells occur via a default pathway. Plant Cell 2: 51-59.
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 25
    • 0029974746 scopus 로고    scopus 로고
    • The efficient production of human epidermal growth factor by Bacillus brevis
    • Ebisu, S., Takagi, H., Kadowaki, K., Yamagata, H., Udaka, S. 1996. The efficient production of human epidermal growth factor by Bacillus brevis. Ann. NY Acad. Sci. 782: 115-122.
    • (1996) Ann. NY Acad. Sci. , vol.782 , pp. 115-122
    • Ebisu, S.1    Takagi, H.2    Kadowaki, K.3    Yamagata, H.4    Udaka, S.5
  • 27
    • 0026197108 scopus 로고
    • Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants
    • Edwards, G. A., Hepher, A., Clerk, S. P., Boulter, D. 1991. Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants. Plant Mol. Biol. 17: 89-100.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 89-100
    • Edwards, G.A.1    Hepher, A.2    Clerk, S.P.3    Boulter, D.4
  • 28
    • 0025650526 scopus 로고
    • Cell-specific gene expression in plants
    • Edwards, J. W., Coruzzi, G. M. 1990. Cell-specific gene expression in plants. Annu. Rev. Genet. 24: 275-303.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 275-303
    • Edwards, J.W.1    Coruzzi, G.M.2
  • 31
    • 0028889621 scopus 로고
    • High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds
    • Fiedler, U., Conrad, U. 1995. High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds. Bio/Technology 13: 1090-1093.
    • (1995) Bio/Technology , vol.13 , pp. 1090-1093
    • Fiedler, U.1    Conrad, U.2
  • 32
    • 0028107795 scopus 로고
    • Transgene inactivation: Plants fight back
    • Finnegan, J., McElroy, D. 1994. Transgene inactivation: plants fight back. Bio/Technology 12: 883-888.
    • (1994) Bio/Technology , vol.12 , pp. 883-888
    • Finnegan, J.1    McElroy, D.2
  • 33
    • 0028005337 scopus 로고
    • Expression of biologically active hordothionins in tobacco. Effects of pre- and pro-sequences at the amino and carboxyl termini of the hordothionin precursor on mature protein expression and sorting
    • Florack, D. E. A., Dirkse, W. G., Visser, B., Heidekamp, F., Stiekema, W. J. 1994. Expression of biologically active hordothionins in tobacco. Effects of pre- and pro-sequences at the amino and carboxyl termini of the hordothionin precursor on mature protein expression and sorting. Plant Mol. Biol. 24: 83-96.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 83-96
    • Florack, D.E.A.1    Dirkse, W.G.2    Visser, B.3    Heidekamp, F.4    Stiekema, W.J.5
  • 35
    • 0027428379 scopus 로고
    • Purification and characterization of microbially expressed neomycin phosphotransferase II (NPTII) protein and its equivalence to the plant expressed protein
    • Fuchs, R. L., Heeren, R. A., Gustafson, M. E., Rogan, G. J., Bartnicki, D. E., Leimgruber, R. M., Finn, R. F., Hershman, A., Berberich, S. A. 1993. Purification and characterization of microbially expressed neomycin phosphotransferase II (NPTII) protein and its equivalence to the plant expressed protein. Bio/Technology 11: 1537-1541.
    • (1993) Bio/Technology , vol.11 , pp. 1537-1541
    • Fuchs, R.L.1    Heeren, R.A.2    Gustafson, M.E.3    Rogan, G.J.4    Bartnicki, D.E.5    Leimgruber, R.M.6    Finn, R.F.7    Hershman, A.8    Berberich, S.A.9
  • 36
    • 0030443794 scopus 로고    scopus 로고
    • Translation in plants - Rules and exceptions
    • Fütterer, J., Hohn, T. 1996. Translation in plants - rules and exceptions. Plant Mol. Biol. 32: 159-189.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 159-189
    • Fütterer, J.1    Hohn, T.2
  • 37
    • 0030267547 scopus 로고    scopus 로고
    • Translational control of cellular and viral mRNAs
    • Gallie, D. R. 1996. Translational control of cellular and viral mRNAs. Plant Mol. Biol. 32: 145-158.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 145-158
    • Gallie, D.R.1
  • 38
    • 0024067641 scopus 로고
    • Optimizing the production of recombinant proteins in microorganism
    • Georgiou, G. 1988. Optimizing the production of recombinant proteins in microorganism. AlChE J. 34: 1233-1248.
    • (1988) AlChE J. , vol.34 , pp. 1233-1248
    • Georgiou, G.1
  • 39
    • 0000573635 scopus 로고
    • Inclusion body formation and the recovery of aggregated recombinant proteins
    • C. Ho, A. Prokop, and R. Bajpaj (eds.), McGraw-Hill, New York
    • Georgiou, G., Bowden, G. A. 1991. Inclusion body formation and the recovery of aggregated recombinant proteins, pp. 333-356. In: C. Ho, A. Prokop, and R. Bajpaj (eds.), Recombinant DNA technology and applications. McGraw-Hill, New York.
    • (1991) Recombinant DNA Technology and Applications , pp. 333-356
    • Georgiou, G.1    Bowden, G.A.2
  • 41
    • 0027357154 scopus 로고
    • Insect cell culture engineering: An overview
    • M. F. A. Goosen, A. Baugulis, and P. Faulkner (eds.), Marcel Dekker, New York
    • Goosen, M. F. A. 1993. Insect cell culture engineering: an overview, pp. 1-16. In: M. F. A. Goosen, A. Baugulis, and P. Faulkner (eds.), Insect cell culture engineering. Marcel Dekker, New York.
    • (1993) Insect Cell Culture Engineering , pp. 1-16
    • Goosen, M.F.A.1
  • 42
    • 0029055060 scopus 로고
    • Oral immunization with a recombinant bacterial antigen produced in transgenic plants
    • Haq, T. A., Mason, H. S., Clements, J. D., Arntzen, C. J. 1995. Oral immunization with a recombinant bacterial antigen produced in transgenic plants. Science 268: 714-716.
    • (1995) Science , vol.268 , pp. 714-716
    • Haq, T.A.1    Mason, H.S.2    Clements, J.D.3    Arntzen, C.J.4
  • 43
    • 0028250784 scopus 로고
    • Heterologous protein production by yeast host-vector systems
    • Harashima, S. 1994. Heterologous protein production by yeast host-vector systems. Bioproc. Technol. 19: 137-158.
    • (1994) Bioproc. Technol. , vol.19 , pp. 137-158
    • Harashima, S.1
  • 44
    • 0028891888 scopus 로고
    • A thermostable xylanase from Clostridium thermocellum expressed at high levels in the apoplast of transgenic tobacco has no detrimental effects and is easily purified
    • Herbers, K., Wilke, I., Sonnewald, U. 1995. A thermostable xylanase from Clostridium thermocellum expressed at high levels in the apoplast of transgenic tobacco has no detrimental effects and is easily purified. Bio/Technology 13: 63-66.
    • (1995) Bio/Technology , vol.13 , pp. 63-66
    • Herbers, K.1    Wilke, I.2    Sonnewald, U.3
  • 45
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Cafferkey, R., Bowdish, K. 1989. Production of antibodies in transgenic plants. Nature 342: 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 46
    • 0001690688 scopus 로고
    • Synthesis and protein body deposition of maize 15-kd zein in transgenic tobacco seeds
    • Hoffman, L. M., Donaldson, D. D., Bookland, R., Rashka, K., Herman, E. M. 1987. Synthesis and protein body deposition of maize 15-kd zein in transgenic tobacco seeds. EMBO J. 6: 3213-3221.
    • (1987) EMBO J. , vol.6 , pp. 3213-3221
    • Hoffman, L.M.1    Donaldson, D.D.2    Bookland, R.3    Rashka, K.4    Herman, E.M.5
  • 47
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants
    • Hoffman, L. M., Donaldson, D. D., Herman, E. M. 1988. A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants. Plant Mol. Biol. 11: 717-729.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 717-729
    • Hoffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 48
    • 0026847823 scopus 로고
    • Novel applications of the ubiquitin-dependent proteolytic pathway in plant genetic engineering
    • Hondred, D., Vierstra, R. D. 1992. Novel applications of the ubiquitin-dependent proteolytic pathway in plant genetic engineering. Curr. Opin. Biotechnol. 3: 147-151.
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 147-151
    • Hondred, D.1    Vierstra, R.D.2
  • 50
    • 0025697895 scopus 로고
    • Proteolytic activity during senescence of plants
    • Huffaker, R. C. 1990. Proteolytic activity during senescence of plants. New Phytol. 116: 199-231.
    • (1990) New Phytol. , vol.116 , pp. 199-231
    • Huffaker, R.C.1
  • 51
    • 0342578691 scopus 로고
    • Perspectives in plant genetic engineering and biopharmacy
    • May
    • Hughes, J., Qoronfleh, M. W. 1991. Perspectives in plant genetic engineering and biopharmacy. BioPharm May: 18-28.
    • (1991) BioPharm , pp. 18-28
    • Hughes, J.1    Qoronfleh, M.W.2
  • 53
    • 0028678794 scopus 로고
    • Transcription factor 1: BZIP proteins
    • Hurst, H. C. 1994. Transcription factor 1: bZIP proteins. Prot. Profile 1: 123-124.
    • (1994) Prot. Profile , vol.1 , pp. 123-124
    • Hurst, H.C.1
  • 55
    • 0024619672 scopus 로고
    • Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco
    • Ituriaga, G., Jefferson, R. A., Bevan, M. 1989. Endoplasmic reticulum targeting and glycosylation of hybrid proteins in transgenic tobacco. Plant Cell 1: 381-390.
    • (1989) Plant Cell , vol.1 , pp. 381-390
    • Ituriaga, G.1    Jefferson, R.A.2    Bevan, M.3
  • 56
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins, N., Parekh, R. B., James, D. C. 1996. Getting the glycosylation right: implications for the biotechnology industry. Nature Biotechnol. 14: 975-981.
    • (1996) Nature Biotechnol. , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 57
    • 0024716141 scopus 로고
    • Purification technologies for plant proteins
    • Jervis, L., Pierpoint, W. S. 1989. Purification technologies for plant proteins. J. Biotechnol. 11: 161-198.
    • (1989) J. Biotechnol. , vol.11 , pp. 161-198
    • Jervis, L.1    Pierpoint, W.S.2
  • 58
    • 0027674917 scopus 로고
    • Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific
    • Kenward, K. D., Altschuler, M., Hildebrand, D., Davies, P. L. 1993. Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific. Plant Mol. Biol. 23: 377-385.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 377-385
    • Kenward, K.D.1    Altschuler, M.2    Hildebrand, D.3    Davies, P.L.4
  • 59
    • 0026648379 scopus 로고
    • A consideration of alternative models for the initiation of translation in eukaryotes
    • Kozak, M. 1992. A consideration of alternative models for the initiation of translation in eukaryotes. Crit. Rev. Biochem. Mol. Breed. 27: 385-402.
    • (1992) Crit. Rev. Biochem. Mol. Breed. , vol.27 , pp. 385-402
    • Kozak, M.1
  • 60
    • 0002603647 scopus 로고
    • Prospects and progress in the production of foreign proteins and peptides in transgenic plants
    • P. R. Shewry and S. Gutteridges (eds.), Cambridge University Press, London
    • Krebbers, E., Bosch, D., Vandekerckhove, J. 1992. Prospects and progress in the production of foreign proteins and peptides in transgenic plants, pp. 315-325. In: P. R. Shewry and S. Gutteridges (eds.), Plant protein engineering. Cambridge University Press, London.
    • (1992) Plant Protein Engineering , pp. 315-325
    • Krebbers, E.1    Bosch, D.2    Vandekerckhove, J.3
  • 61
    • 0028309911 scopus 로고
    • Escherichia coli secretion vector using the kit gene
    • Y. Murooka and T. Amanaka (eds.), Marcel Dekker, New York
    • Kudo, T. 1994. Escherichia coli secretion vector using the kit gene, pp. 291-299. In: Y. Murooka and T. Amanaka (eds.), Recombinant microbes for industrial and agricultural applications. Marcel Dekker, New York.
    • (1994) Recombinant Microbes for Industrial and Agricultural Applications , pp. 291-299
    • Kudo, T.1
  • 63
  • 64
    • 0029331455 scopus 로고
    • Prohevein is poorly processed but shows enhanced resistance to a chitin-binding fungus in transgenic tomato plants
    • Lee, H.-I., Raikhel, N. V. 1995. Prohevein is poorly processed but shows enhanced resistance to a chitin-binding fungus in transgenic tomato plants. Brazil. J. Med. Biol. Res. 28: 743-750.
    • (1995) Brazil. J. Med. Biol. Res. , vol.28 , pp. 743-750
    • Lee, H.-I.1    Raikhel, N.V.2
  • 65
    • 0027419308 scopus 로고
    • Comparison of soluble and secreted forms of human parainfluenza virus type 3 glycoproteins expressed from mammalian and insect cells as subunit vaccines
    • Lehman, D. J., Roof, L. L., Brideau, R. J., Aeed, P. A., Thomsen, D. R., Elhammer, A. P., Wathen, M. W., Homa, F. L. 1993. Comparison of soluble and secreted forms of human parainfluenza virus type 3 glycoproteins expressed from mammalian and insect cells as subunit vaccines. J. Gen. Virol. 74: 459-469.
    • (1993) J. Gen. Virol. , vol.74 , pp. 459-469
    • Lehman, D.J.1    Roof, L.L.2    Brideau, R.J.3    Aeed, P.A.4    Thomsen, D.R.5    Elhammer, A.P.6    Wathen, M.W.7    Homa, F.L.8
  • 66
    • 0026454405 scopus 로고
    • Rational design of purification processes for recombinant proteins
    • Lesser, E. W., Asenjo, J. A. 1992. Rational design of purification processes for recombinant proteins. J. Chromatogr. 584: 43-57.
    • (1992) J. Chromatogr. , vol.584 , pp. 43-57
    • Lesser, E.W.1    Asenjo, J.A.2
  • 69
    • 0023881356 scopus 로고
    • Trends in the development of baculovirus expression vectors
    • Luckow, V. A., Summers, M. D. 1988. Trends in the development of baculovirus expression vectors. Bio/Technology 6: 47-55.
    • (1988) Bio/Technology , vol.6 , pp. 47-55
    • Luckow, V.A.1    Summers, M.D.2
  • 72
    • 0029411968 scopus 로고
    • Immunotherapeutic potential of antibodies produced in plants
    • Ma, J. K.-C., Hein, M. B. 1995. Immunotherapeutic potential of antibodies produced in plants. Trends Biotechnol. 13: 522-527.
    • (1995) Trends Biotechnol. , vol.13 , pp. 522-527
    • Ma, J.K.-C.1    Hein, M.B.2
  • 74
    • 0026113341 scopus 로고
    • The combination of a novel stimulatory element in the first exon of the maize Shrunken-1 gene with the following intron 1 enhances reporter gene expression up to 1000-fold
    • Maas, C., Laufs, J., Grant, S., Korfhage, C., Werr, W. 1991. The combination of a novel stimulatory element in the first exon of the maize Shrunken-1 gene with the following intron 1 enhances reporter gene expression up to 1000-fold. Plant Mol. Biol. 16: 199-207.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 199-207
    • Maas, C.1    Laufs, J.2    Grant, S.3    Korfhage, C.4    Werr, W.5
  • 75
    • 0008619890 scopus 로고
    • Expression of heterologous proteins in yeast
    • A. Prokop, R. K. Bajpal, and C. S. Ha (eds.), McGraw-Hill, New York
    • Marino, M. M. 1991. Expression of heterologous proteins in yeast, pp. 29-65. In: A. Prokop, R. K. Bajpal, and C. S. Ha (eds.), Recombinant DNA technology and applications. McGraw-Hill, New York.
    • (1991) Recombinant DNA Technology and Applications , pp. 29-65
    • Marino, M.M.1
  • 76
    • 0029891823 scopus 로고    scopus 로고
    • Expression of Norwalk virus capsid protein in transgenic tobacco and its oral immunogenicity in mice
    • Mason, H. S., Ball, J. M., Shi, J.-J., Jiang, X., Estes, M. K., Arntzen, C. J. 1996. Expression of Norwalk virus capsid protein in transgenic tobacco and its oral immunogenicity in mice. Proc. Natl. Acad. Sci. USA 93: 5335-5340.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5335-5340
    • Mason, H.S.1    Ball, J.M.2    Shi, J.-J.3    Jiang, X.4    Estes, M.K.5    Arntzen, C.J.6
  • 77
    • 0027048769 scopus 로고
    • Expression of hepatitis B surface antigen in transgenic plants
    • Mason, H. S., Lam, D. M.-K., Arntzen, D. J. 1992. Expression of hepatitis B surface antigen in transgenic plants. Proc. Natl. Acad. Sci. USA 89: 11745-11749.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11745-11749
    • Mason, H.S.1    Lam, D.M.-K.2    Arntzen, D.J.3
  • 78
    • 0029257224 scopus 로고
    • Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells
    • Matsumoto, S., Ikura, K., Ueada, M., Sasaki, R. 1995. Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells. Plant Mol. Biol. 27: 1163-1172.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 1163-1172
    • Matsumoto, S.1    Ikura, K.2    Ueada, M.3    Sasaki, R.4
  • 79
    • 0027502723 scopus 로고
    • Nutritional improvement of the aspartate family of amino acids in edible crop plants
    • Matthews, B. F., Hughes, C. A. 1993. Nutritional improvement of the aspartate family of amino acids in edible crop plants. Amino Acids 4: 21-34.
    • (1993) Amino Acids , vol.4 , pp. 21-34
    • Matthews, B.F.1    Hughes, C.A.2
  • 82
    • 0027025565 scopus 로고
    • Differential expression of a chimeric CaMV-tomato proteinase inhibitor I gene in leaves of transformed nightshade, tobacco and alfalfa
    • Narvaez-Vasquez, J., Orozco-Cardenas, M. L., Ryan, C. A. 1992. Differential expression of a chimeric CaMV-tomato proteinase inhibitor I gene in leaves of transformed nightshade, tobacco and alfalfa. Plant Mol. Biol. 20: 1149-1157.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 1149-1157
    • Narvaez-Vasquez, J.1    Orozco-Cardenas, M.L.2    Ryan, C.A.3
  • 83
    • 14744306138 scopus 로고
    • Production of cyclodextrins, a novel carbohydrate, in the tubers of transgenic potato plants
    • Oakes, J. V., Shewmaker, C. K., Stalker, D. M. 1991. Production of cyclodextrins, a novel carbohydrate, in the tubers of transgenic potato plants. Bio/Technology 9: 982-986.
    • (1991) Bio/Technology , vol.9 , pp. 982-986
    • Oakes, J.V.1    Shewmaker, C.K.2    Stalker, D.M.3
  • 84
    • 0026066777 scopus 로고
    • Normal and lysine-containing zeins are unstable in transgenic tobacco seeds
    • Ohtani, T., Galili, G., Wallace, J. C., Thompson, G. A., Larkins, B. A. 1991. Normal and lysine-containing zeins are unstable in transgenic tobacco seeds. Plant Mol. Biol. 16: 117-128.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 117-128
    • Ohtani, T.1    Galili, G.2    Wallace, J.C.3    Thompson, G.A.4    Larkins, B.A.5
  • 85
    • 0030087727 scopus 로고    scopus 로고
    • Gene silencing mediated by promoter homology occurs at the level of transcription and results in meiotically heritable alterations in methylation and gene activity
    • Park, Y.-D., Papp, I., Moscone, E. A., Iglesias, V. A., Vaucheret, H., Matzke, A. J. M., Matzke, M. A. 1996. Gene silencing mediated by promoter homology occurs at the level of transcription and results in meiotically heritable alterations in methylation and gene activity. Plant J. 9: 183-194.
    • (1996) Plant J. , vol.9 , pp. 183-194
    • Park, Y.-D.1    Papp, I.2    Moscone, E.A.3    Iglesias, V.A.4    Vaucheret, H.5    Matzke, A.J.M.6    Matzke, M.A.7
  • 87
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in j stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A., Lindquist, S. 1993. The function of heat-shock proteins in j stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Gen. 27: 437-496.
    • (1993) Annu. Rev. Gen. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 89
    • 0002437697 scopus 로고
    • Protein production in transgenic crops: Analysis of plant molecular farming
    • A. Hiatt (ed.), Marcel Dekker, New York
    • Pen, J., Sijmons, P. C., van Ooijen, A. J. J., Hoekema, A. 1993a. Protein production in transgenic crops: analysis of plant molecular farming, pp. 239-251. In: A. Hiatt (ed.), Transgenic plants fundamentals and applications. Marcel Dekker, New York.
    • (1993) Transgenic Plants Fundamentals and Applications , pp. 239-251
    • Pen, J.1    Sijmons, P.C.2    Van Ooijen, A.J.J.3    Hoekema, A.4
  • 91
    • 0029637157 scopus 로고
    • Computer-aided process analysis and economic evaluation for biosynthetic human insulin production - A study case
    • Petridis, D., Sapidou, E., Calandranis, J. 1995. Computer-aided process analysis and economic evaluation for biosynthetic human insulin production - a study case. Biotechnol. Bioeng. 48: 529-541.
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 529-541
    • Petridis, D.1    Sapidou, E.2    Calandranis, J.3
  • 93
    • 0026111169 scopus 로고
    • Ion exchange and affinity chromatography in the scaleup of the purification of α-galactosidase from soybean seeds
    • Porter, J. E., Ladisch, M. R., Herrmann, K. M. 1991. Ion exchange and affinity chromatography in the scaleup of the purification of α-galactosidase from soybean seeds. Biotechnol. Bioeng. 37: 356-364.
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 356-364
    • Porter, J.E.1    Ladisch, M.R.2    Herrmann, K.M.3
  • 96
  • 97
    • 0028243830 scopus 로고
    • Mechanism of assembly of wheat high molecular weight glutenins inferred from expression of wild-type and mutant subunits in transgenic tobacco
    • Shani, N., Rosenberg, N., Kasarda, D. D., Galili, G. 1994. Mechanism of assembly of wheat high molecular weight glutenins inferred from expression of wild-type and mutant subunits in transgenic tobacco. J. Biol. Chem. 269: 8924-8930.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8924-8930
    • Shani, N.1    Rosenberg, N.2    Kasarda, D.D.3    Galili, G.4
  • 98
    • 0001685824 scopus 로고
    • Feedback control of gene expression
    • Sheen, J. 1994. Feedback control of gene expression. Photosynth. Res. 39: 427-438.
    • (1994) Photosynth. Res. , vol.39 , pp. 427-438
    • Sheen, J.1
  • 100
    • 0028150850 scopus 로고
    • Molecular regulation of amino acid biosynthesis in plants
    • Singh, B. K., Matthews, B. F. 1994. Molecular regulation of amino acid biosynthesis in plants. Amino Acids 7: 165-174.
    • (1994) Amino Acids , vol.7 , pp. 165-174
    • Singh, B.K.1    Matthews, B.F.2
  • 101
    • 0343884449 scopus 로고
    • Effect of transit and storage conditions on potatoes
    • W. F. Talburt and O. Smith (eds.), AVI, Westport, CT
    • Smith, O. 1975. Effect of transit and storage conditions on potatoes, pp. 171-235. In: W. F. Talburt and O. Smith (eds.), Potato processing. AVI, Westport, CT.
    • (1975) Potato Processing , pp. 171-235
    • Smith, O.1
  • 102
    • 0025655342 scopus 로고
    • Similarities and dissimilarities between plant UsnRNAs and their equivalents in other eukaryotes with respect to structure, complexing with proteins, gene organization and function
    • Solymosy, F. 1990. Similarities and dissimilarities between plant UsnRNAs and their equivalents in other eukaryotes with respect to structure, complexing with proteins, gene organization and function. Acta Biochim. Biophys. Hung. 25: 67-85.
    • (1990) Acta Biochim. Biophys. Hung. , vol.25 , pp. 67-85
    • Solymosy, F.1
  • 103
    • 0003229971 scopus 로고
    • Uridylate-rich small nuclear RNAs (Usn-RNAs). their genes and pseudogenes, and UsnRNPs in plants: Structure and function. A comparative approach
    • Solymosy, F., Pollak. T. 1993. Uridylate-rich small nuclear RNAs (Usn-RNAs). their genes and pseudogenes, and UsnRNPs in plants: structure and function. A comparative approach. Crit. Rev. Plant Sci. 12: 275-369.
    • (1993) Crit. Rev. Plant Sci. , vol.12 , pp. 275-369
    • Solymosy, F.1    Pollak, T.2
  • 104
    • 0027720289 scopus 로고
    • Post-transcriptional regulation of nuclear-encoded genes in higher plants: The roles of mRNA stability and translation
    • Sullivan, M. L., Green, P. J. 1993. Post-transcriptional regulation of nuclear-encoded genes in higher plants: the roles of mRNA stability and translation. Plant Mol. Biol. 23: 1091-1104.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1091-1104
    • Sullivan, M.L.1    Green, P.J.2
  • 105
    • 0029278093 scopus 로고
    • Identification and characterization of genes with unstable transcripts (GUTs) in tobacco
    • Taylor, C.B., Green, P. J. 1995. Identification and characterization of genes with unstable transcripts (GUTs) in tobacco. Plant Mol. Biol. 28: 27-38.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 27-38
    • Taylor, C.B.1    Green, P.J.2
  • 107
    • 0027154583 scopus 로고
    • Expression vectors for high-level gene expression in dicotyledonous and monocotyledonous plants
    • Topfer, R., Maas, C., Horicke-Grandpierre, C., Schell, J., Steinbiss, H. H. 1993. Expression vectors for high-level gene expression in dicotyledonous and monocotyledonous plants. Meth. Enzymol. 217: 66-79.
    • (1993) Meth. Enzymol. , vol.217 , pp. 66-79
    • Topfer, R.1    Maas, C.2    Horicke-Grandpierre, C.3    Schell, J.4    Steinbiss, H.H.5
  • 108
    • 0001809359 scopus 로고
    • Expression of active hen egg white lysozyme in transgenic tobacco
    • Trudel, J., Potvin, C., Asselin, A. 1992. Expression of active hen egg white lysozyme in transgenic tobacco. Plant Sci. 87: 55-67.
    • (1992) Plant Sci. , vol.87 , pp. 55-67
    • Trudel, J.1    Potvin, C.2    Asselin, A.3
  • 110
    • 0027297667 scopus 로고
    • High-level secretion of heterologous proteins by Bacillus brevis
    • Udaka, S., Yamagata, H. 1993. High-level secretion of heterologous proteins by Bacillus brevis. Meth. Enzymol. 217: 23-33.
    • (1993) Meth. Enzymol. , vol.217 , pp. 23-33
    • Udaka, S.1    Yamagata, H.2
  • 111
    • 0028140751 scopus 로고
    • Expression and accumulation of normal and modified soybean glycinins in potato tubers
    • Utsumi, S., Kitagawa, S., Katsube, T., Higasa, T., Kito, M., Takaiwa, F., Ishige, T. 1994. Expression and accumulation of normal and modified soybean glycinins in potato tubers. Plant Sci. 102: 181-188.
    • (1994) Plant Sci. , vol.102 , pp. 181-188
    • Utsumi, S.1    Kitagawa, S.2    Katsube, T.3    Higasa, T.4    Kito, M.5    Takaiwa, F.6    Ishige, T.7
  • 112
    • 0027145384 scopus 로고
    • Synthesis, processing and accumulation of modified glycinins of soybean in the seeds, leaves and stems of transgenic tobacco
    • Utsumi, S., Kitagawa, S., Katsube, T., Kang, I. J., Gidamis, A. B., Takaiwa, F., Kito, M. 1993. Synthesis, processing and accumulation of modified glycinins of soybean in the seeds, leaves and stems of transgenic tobacco. Plant Sci. 92: 191-202.
    • (1993) Plant Sci. , vol.92 , pp. 191-202
    • Utsumi, S.1    Kitagawa, S.2    Katsube, T.3    Kang, I.J.4    Gidamis, A.B.5    Takaiwa, F.6    Kito, M.7
  • 116
    • 0028859854 scopus 로고
    • Plant seed oil-bodies as carriers for foreign proteins
    • Van Rooijen, G. J. H., Moloney, M. M. 1995. Plant seed oil-bodies as carriers for foreign proteins. Bio/Technology 13: 72-77.
    • (1995) Bio/Technology , vol.13 , pp. 72-77
    • Van Rooijen, G.J.H.1    Moloney, M.M.2
  • 117
    • 0030614584 scopus 로고    scopus 로고
    • Transgenic livestock as drug factories
    • Velander, W. H., Lubon, H., Drohan, W. N. 1997. Transgenic livestock as drug factories. Sci. Am. 276: 70-74.
    • (1997) Sci. Am. , vol.276 , pp. 70-74
    • Velander, W.H.1    Lubon, H.2    Drohan, W.N.3
  • 120
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification, and intracellular transport
    • Vitale, A., Ceriotti, A., Denecke, J. 1993. The role of the endoplasmic reticulum in protein synthesis, modification, and intracellular transport. J. Exp. Botany 44: 1417-1444.
    • (1993) J. Exp. Botany , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 121
    • 0024301301 scopus 로고
    • In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: Role of glycans in protein targeting and stability
    • Voelker, T. A., Herman, E. M., Chrispeels, M. J. 1989. In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: role of glycans in protein targeting and stability. Plant Cell 1: 95-104.
    • (1989) Plant Cell , vol.1 , pp. 95-104
    • Voelker, T.A.1    Herman, E.M.2    Chrispeels, M.J.3
  • 122
    • 0026834063 scopus 로고
    • Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants
    • Wandelt, C. I., Khan, M. R. I., Craig, S., Schroeder, H. E., Spencer, D., Higgins, T. J. V. 1992. Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants. Plant J. 2: 181-192.
    • (1992) Plant J. , vol.2 , pp. 181-192
    • Wandelt, C.I.1    Khan, M.R.I.2    Craig, S.3    Schroeder, H.E.4    Spencer, D.5    Higgins, T.J.V.6
  • 123
    • 0342578671 scopus 로고
    • Strategies for production of proteins in mammalian cells
    • A. Prokop, R. K. Bajpai, and C. S. Ho (eds.), McGraw-Hill, New York
    • Warren, T. G., Krivi, G. G. 1991. Strategies for production of proteins in mammalian cells, pp. 66-96. In: A. Prokop, R. K. Bajpai, and C. S. Ho (eds.), Recombinant DNA technology and applications. McGraw-Hill, New York.
    • (1991) Recombinant DNA Technology and Applications , pp. 66-96
    • Warren, T.G.1    Krivi, G.G.2
  • 124
    • 0009357696 scopus 로고
    • Successful products and future business prospects
    • R. E. Spier, J. B. Griffiths, and W. Berthold (eds.), Butterworth-Heinemann, Oxford
    • Werner, R. G., Thomae, K. 1994. Successful products and future business prospects, pp. 573-578. In: R. E. Spier, J. B. Griffiths, and W. Berthold (eds.), Animal cell technology products of today prospects for tomorrow. Butterworth-Heinemann, Oxford.
    • (1994) Animal Cell Technology Products of Today Prospects for Tomorrow , pp. 573-578
    • Werner, R.G.1    Thomae, K.2
  • 128
    • 0026930457 scopus 로고
    • Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants
    • Wong, E. Y., Hironaka, C. M., Fischhoff, D. A. 1992. Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants. Plant Mol. Biol. 20: 81-93.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 81-93
    • Wong, E.Y.1    Hironaka, C.M.2    Fischhoff, D.A.3
  • 129
    • 0000929420 scopus 로고
    • Ti plasmid vector for the introduction of DNA into plant cells without alteration of their normal regeneration capacity
    • Zambryski, P., Joss, H., Genetello, C., Leemans, J., van Montagu, M., Schell, J. 1983. Ti plasmid vector for the introduction of DNA into plant cells without alteration of their normal regeneration capacity. EMBO J. 2: 2143-2150.
    • (1983) EMBO J. , vol.2 , pp. 2143-2150
    • Zambryski, P.1    Joss, H.2    Genetello, C.3    Leemans, J.4    Van Montagu, M.5    Schell, J.6


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