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Volumn 21, Issue 12, 2003, Pages 570-578

Molecular farming in plants: Host systems and expression technology

Author keywords

[No Author keywords available]

Indexed keywords

BIOREACTORS; DRUG PRODUCTS; PLANTS (BOTANY); PROTEINS;

EID: 0242475327     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2003.10.002     Document Type: Review
Times cited : (547)

References (86)
  • 1
    • 0000217415 scopus 로고    scopus 로고
    • Commercial production of avidin from transgenic maize: Characterization of transformant, production, processing, extraction and purification
    • Hood E.E., et al. Commercial production of avidin from transgenic maize: characterization of transformant, production, processing, extraction and purification. Mol. Breed. 3:1997;291-306.
    • (1997) Mol. Breed. , vol.3 , pp. 291-306
    • Hood, E.E.1
  • 2
    • 0011977387 scopus 로고    scopus 로고
    • Commercial production of β-glucuronidase (GUS): A model system for the production of proteins in plants
    • Witcher D., et al. Commercial production of β-glucuronidase (GUS): a model system for the production of proteins in plants. Mol. Breed. 4:1998;301-312.
    • (1998) Mol. Breed. , vol.4 , pp. 301-312
    • Witcher, D.1
  • 3
    • 0032487368 scopus 로고    scopus 로고
    • Processing of transgenic corn seed and its effect on the recovery of recombinant β-glucuronidase
    • Kusnadi A.R., et al. Processing of transgenic corn seed and its effect on the recovery of recombinant β-glucuronidase. Biotechnol. Bioeng. 60:1998;44-52.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 44-52
    • Kusnadi, A.R.1
  • 4
    • 0032127253 scopus 로고    scopus 로고
    • Process and economic evaluation of the extraction and purification of recombinant β-glucuronidase from transgenic corn
    • Evangelista R.L., et al. Process and economic evaluation of the extraction and purification of recombinant β-glucuronidase from transgenic corn. Biotechnol. Prog. 14:1998;607-614.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 607-614
    • Evangelista, R.L.1
  • 5
    • 0033667765 scopus 로고    scopus 로고
    • Molecular farming of pharmaceutical proteins
    • Fischer R., Emans N. Molecular farming of pharmaceutical proteins. Transgenic Res. 9:2000;279-299.
    • (2000) Transgenic Res. , vol.9 , pp. 279-299
    • Fischer, R.1    Emans, N.2
  • 6
    • 0035477961 scopus 로고    scopus 로고
    • Transgenic plants as protein factories
    • Giddings G. Transgenic plants as protein factories. Curr. Opin. Biotechnol. 12:2001;450-454.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 450-454
    • Giddings, G.1
  • 7
    • 85030943990 scopus 로고    scopus 로고
    • Hood, E.E. Plants as enzyme factories. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
    • Hood, E.E. Plants as enzyme factories. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
  • 8
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plants - Myths and realities
    • Hood E.E., et al. Monoclonal antibody manufacturing in transgenic plants - myths and realities. Curr. Opin. Biotechnol. 13:2002;630-635.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 630-635
    • Hood, E.E.1
  • 9
    • 0012515015 scopus 로고    scopus 로고
    • Antibody molecular farming in plants and plant cells
    • Schillberg S., et al. Antibody molecular farming in plants and plant cells. Phytochem. Rev. 1:2002;45-54.
    • (2002) Phytochem. Rev. , vol.1 , pp. 45-54
    • Schillberg, S.1
  • 10
    • 0036305744 scopus 로고    scopus 로고
    • Edible plant vaccines: Applications for prophylactic and therapeutic molecular medicine
    • Mason H.S., et al. Edible plant vaccines: applications for prophylactic and therapeutic molecular medicine. Trends Mol. Med. 8:2002;324-329.
    • (2002) Trends Mol. Med. , vol.8 , pp. 324-329
    • Mason, H.S.1
  • 11
    • 0032088780 scopus 로고    scopus 로고
    • Soybeans transformed with fungal phytase gene improve phosphorus availability for broilers
    • Denbow D.M., et al. Soybeans transformed with fungal phytase gene improve phosphorus availability for broilers. Poult. Sci. 77:1998;878-881.
    • (1998) Poult. Sci. , vol.77 , pp. 878-881
    • Denbow, D.M.1
  • 12
    • 0033781874 scopus 로고    scopus 로고
    • Improved plant-based production of E1 endoglucanase using potato: Expression optimization and tissue targeting
    • Dai Z.Y., et al. Improved plant-based production of E1 endoglucanase using potato: expression optimization and tissue targeting. Mol. Breed. 6:2000;277-285.
    • (2000) Mol. Breed. , vol.6 , pp. 277-285
    • Dai, Z.Y.1
  • 13
    • 0033996431 scopus 로고    scopus 로고
    • Accumulation of a thermostable endo-1,4-β-D-glucanase in the apoplast of Arabidopsis thaliana leaves
    • Ziegler M.T., et al. Accumulation of a thermostable endo-1,4-β-D- glucanase in the apoplast of Arabidopsis thaliana leaves. Mol. Breed. 6:2000;37-46.
    • (2000) Mol. Breed. , vol.6 , pp. 37-46
    • Ziegler, M.T.1
  • 14
    • 0035705385 scopus 로고    scopus 로고
    • Dramatic effects of truncation and sub-cellular targeting on the accumulation of recombinant microbial cellulase in tobacco
    • Ziegelhoffer T., et al. Dramatic effects of truncation and sub-cellular targeting on the accumulation of recombinant microbial cellulase in tobacco. Mol. Breed. 8:2001;147-158.
    • (2001) Mol. Breed. , vol.8 , pp. 147-158
    • Ziegelhoffer, T.1
  • 15
    • 0033772176 scopus 로고    scopus 로고
    • Transgenic pea seeds as bioreactors for the production of a single-chain Fv fragment (scFV) antibody used in cancer diagnosis and therapy
    • Perrin Y., et al. Transgenic pea seeds as bioreactors for the production of a single-chain Fv fragment (scFV) antibody used in cancer diagnosis and therapy. Mol. Breed. 6:2000;345-352.
    • (2000) Mol. Breed. , vol.6 , pp. 345-352
    • Perrin, Y.1
  • 16
    • 0342748410 scopus 로고    scopus 로고
    • Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies
    • Stoger E., et al. Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies. Plant Mol. Biol. 42:2000;583-590.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 583-590
    • Stoger, E.1
  • 17
    • 85030948697 scopus 로고    scopus 로고
    • Moloney, M. et al. (2003) Oil bodies and associated proteins as affinity matrices. US Patent 6509453.
    • Moloney, M., et al. (2003) Oil bodies and associated proteins as affinity matrices. US Patent 6509453.
  • 18
    • 0033779268 scopus 로고    scopus 로고
    • Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus
    • Schillberg S., et al. Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus. Mol. Breed. 6:2000;317-326.
    • (2000) Mol. Breed. , vol.6 , pp. 317-326
    • Schillberg, S.1
  • 19
    • 0032916112 scopus 로고    scopus 로고
    • Production of recombinant proteins in plant root exudates
    • Borisjuk N.V., et al. Production of recombinant proteins in plant root exudates. Nat. Biotechnol. 17:1999;466-469.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 466-469
    • Borisjuk, N.V.1
  • 20
    • 0033729827 scopus 로고    scopus 로고
    • Production of recombinant proteins in tobacco guttation fluid
    • Komarnytsky S., et al. Production of recombinant proteins in tobacco guttation fluid. Plant Physiol. 124:2000;927-933.
    • (2000) Plant Physiol. , vol.124 , pp. 927-933
    • Komarnytsky, S.1
  • 21
    • 0037703161 scopus 로고    scopus 로고
    • Rhizosecretion of a monoclonal antibody protein complex from transgenic tobacco roots
    • Drake P.M.W., et al. Rhizosecretion of a monoclonal antibody protein complex from transgenic tobacco roots. Plant Mol. Biol. 52:2003;233-241.
    • (2003) Plant Mol. Biol. , vol.52 , pp. 233-241
    • Drake, P.M.W.1
  • 22
    • 0032843937 scopus 로고    scopus 로고
    • Towards molecular farming in the future: Transient protein expression in plants
    • Fischer R., et al. Towards molecular farming in the future: transient protein expression in plants. Biotechnol. Appl. Biochem. 30:1999;113-116.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 113-116
    • Fischer, R.1
  • 23
    • 0032846881 scopus 로고    scopus 로고
    • Towards molecular farming in the future: Using plant-cell-suspension cultures as bioreactors
    • Fischer R., et al. Towards molecular farming in the future: using plant-cell-suspension cultures as bioreactors. Biotechnol. Appl. Biochem. 30:1999;109-112.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 109-112
    • Fischer, R.1
  • 24
    • 0041602667 scopus 로고    scopus 로고
    • The biosafety of molecular farming in plants
    • Commandeur U., et al. The biosafety of molecular farming in plants. AgBiotechNet. 5:2003;110.
    • (2003) AgBiotechNet , vol.5 , pp. 110
    • Commandeur, U.1
  • 25
    • 0036535775 scopus 로고    scopus 로고
    • Plantibodies: Applications, advantages and bottlenecks
    • Stoger E., et al. Plantibodies: applications, advantages and bottlenecks. Curr. Opin. Biotechnol. 13:2002;161-166.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 161-166
    • Stoger, E.1
  • 26
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants
    • Ma J.K., et al. Generation and assembly of secretory antibodies in plants. Science. 268:1995;716-719.
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.1
  • 27
    • 0034825803 scopus 로고    scopus 로고
    • Production of secretory IgA antibodies in plants
    • Larrick J.W., et al. Production of secretory IgA antibodies in plants. Biomol. Eng. 18:2001;87-94.
    • (2001) Biomol. Eng. , vol.18 , pp. 87-94
    • Larrick, J.W.1
  • 28
    • 44949159085 scopus 로고    scopus 로고
    • Metabolic engineering glycosylation: Biotechnology's challenge to the glycobiologist in the new millennium
    • B. et al. Ernst. Wiley-VCH
    • Warner T.G. Metabolic engineering glycosylation: biotechnology's challenge to the glycobiologist in the new millennium. Ernst B., et al. Carbohydrates in Chemistry and Biology. 2000;1043-1064 Wiley-VCH.
    • (2000) Carbohydrates in Chemistry and Biology , pp. 1043-1064
    • Warner, T.G.1
  • 29
    • 0037157167 scopus 로고    scopus 로고
    • Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides
    • Blixt O., et al. Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides. J. Am. Chem. Soc. 124:2002;5739-5746.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5739-5746
    • Blixt, O.1
  • 30
    • 0035956939 scopus 로고    scopus 로고
    • Galactose-extended glycans of antibodies produced by transgenic plants
    • Bakker H., et al. Galactose-extended glycans of antibodies produced by transgenic plants. Proc. Natl. Acad. Sci. U. S. A. 98:2001;2899-2904.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2899-2904
    • Bakker, H.1
  • 31
    • 0033805614 scopus 로고    scopus 로고
    • A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice
    • Chargelegue D., et al. A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice. Transgenic Res. 9:2000;187-194.
    • (2000) Transgenic Res. , vol.9 , pp. 187-194
    • Chargelegue, D.1
  • 32
    • 0042907594 scopus 로고    scopus 로고
    • Plant genes and their expression
    • Tyagi A.K. Plant genes and their expression. Curr. Sci. 80:2001;161-169.
    • (2001) Curr. Sci. , vol.80 , pp. 161-169
    • Tyagi, A.K.1
  • 33
    • 0030138945 scopus 로고    scopus 로고
    • Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants
    • Christensen A.H., Quail P.H. Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants. Transgenic Res. 5:1996;213-218.
    • (1996) Transgenic Res. , vol.5 , pp. 213-218
    • Christensen, A.H.1    Quail, P.H.2
  • 34
    • 0030066414 scopus 로고    scopus 로고
    • Intron-mediated enhancement of gene expression in maize (Zea mays L.) and bluegrass (Poa pratensis L.)
    • Vain P., et al. Intron-mediated enhancement of gene expression in maize (Zea mays L.) and bluegrass (Poa pratensis L.). Plant Cell Rep. 15:1996;489-494.
    • (1996) Plant Cell Rep. , vol.15 , pp. 489-494
    • Vain, P.1
  • 35
    • 0034111507 scopus 로고    scopus 로고
    • Chemical-inducible systems for regulated expression of plant genes
    • Zuo J., Chua N.-H. Chemical-inducible systems for regulated expression of plant genes. Curr. Opin. Biotechnol. 11:2000;146-151.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 146-151
    • Zuo, J.1    Chua, N.-H.2
  • 36
    • 0032952346 scopus 로고    scopus 로고
    • Transgenic plants for therapeutic proteins: Linking upstream and downstream technologies
    • Cramer C.L., et al. Transgenic plants for therapeutic proteins: linking upstream and downstream technologies. Curr. Top. Microbiol. Immunol. 240:1999;95-118.
    • (1999) Curr. Top. Microbiol. Immunol. , vol.240 , pp. 95-118
    • Cramer, C.L.1
  • 37
    • 0345411693 scopus 로고    scopus 로고
    • Current perspectives on mRNA stability in plants: Multiple levels and mechanisms of control
    • Gutiérrez R.A., et al. Current perspectives on mRNA stability in plants: multiple levels and mechanisms of control. Trends Plant Sci. 4:1999;429-438.
    • (1999) Trends Plant Sci. , vol.4 , pp. 429-438
    • Gutiérrez, R.A.1
  • 39
    • 0030266741 scopus 로고    scopus 로고
    • Optimizing expression of transgenes with an emphasis on post-transcriptional events
    • Koziel M.G., et al. Optimizing expression of transgenes with an emphasis on post-transcriptional events. Plant Mol. Biol. 32:1996;393-405.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 393-405
    • Koziel, M.G.1
  • 41
    • 0036369625 scopus 로고    scopus 로고
    • Foreign DNA: Integration and expression in transgenic plants
    • Setlow J.K. Kluwer-Plenum Press
    • Twyman R.M., et al. Foreign DNA: integration and expression in transgenic plants. Setlow J.K. Genetic Engineering: Principles and Practice. Vol. 24:2002;107-136 Kluwer-Plenum Press.
    • (2002) Genetic Engineering: Principles and Practice , vol.24 , pp. 107-136
    • Twyman, R.M.1
  • 42
    • 0036779333 scopus 로고    scopus 로고
    • RNA silencing: Small RNAs as ubiquitous regulators of gene expression
    • Voinnet O. RNA silencing: small RNAs as ubiquitous regulators of gene expression. Curr. Opin. Plant Biol. 5:2002;444-451.
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 444-451
    • Voinnet, O.1
  • 43
    • 0038199840 scopus 로고    scopus 로고
    • Transgene integration, organization and interaction in plants
    • Kohli A., et al. Transgene integration, organization and interaction in plants. Plant Mol. Biol. 52:2003;247-258.
    • (2003) Plant Mol. Biol. , vol.52 , pp. 247-258
    • Kohli, A.1
  • 44
    • 0034112666 scopus 로고    scopus 로고
    • Linear transgene constructs lacking vector backbone sequences generate low-copy-number transgenic plants with simple integration patterns
    • Fu X.D., et al. Linear transgene constructs lacking vector backbone sequences generate low-copy-number transgenic plants with simple integration patterns. Transgenic Res. 9:2000;11-19.
    • (2000) Transgenic Res. , vol.9 , pp. 11-19
    • Fu, X.D.1
  • 45
    • 0031678633 scopus 로고    scopus 로고
    • Intracellular expression of TMV-specific single-chain Fv fragments leads to improved virus resistance in Nicotiana tabacum
    • Zimmermann S., et al. Intracellular expression of TMV-specific single-chain Fv fragments leads to improved virus resistance in Nicotiana tabacum. Mol. Breed. 4:1998;369-379.
    • (1998) Mol. Breed. , vol.4 , pp. 369-379
    • Zimmermann, S.1
  • 46
    • 0033178118 scopus 로고    scopus 로고
    • Apoplastic and cytosolic expression of full-size antibodies and antibody fragments in Nicotiana tabacum
    • Schillberg S., et al. Apoplastic and cytosolic expression of full-size antibodies and antibody fragments in Nicotiana tabacum. Transgenic Res. 8:1999;255-263.
    • (1999) Transgenic Res. , vol.8 , pp. 255-263
    • Schillberg, S.1
  • 47
    • 0001662492 scopus 로고    scopus 로고
    • High-level accumulation of single-chain variable fragments in the cytosol of transgenic Petunia hybrida
    • De Jaeger G., et al. High-level accumulation of single-chain variable fragments in the cytosol of transgenic Petunia hybrida. Eur. J. Biochem. 259:1999;426-434.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 426-434
    • De Jaeger, G.1
  • 48
    • 0037205497 scopus 로고    scopus 로고
    • Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol
    • Schouten A., et al. Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol. J. Biol. Chem. 277:2002;19339-19345.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19339-19345
    • Schouten, A.1
  • 49
    • 18744378812 scopus 로고    scopus 로고
    • ER-resident chaperone interactions with recombinant antibodies in transgenic plants
    • Nuttall J., et al. ER-resident chaperone interactions with recombinant antibodies in transgenic plants. Eur. J. Biochem. 269:2002;6042-6051.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6042-6051
    • Nuttall, J.1
  • 50
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity
    • Conrad U., Fiedler U. Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity. Plant Mol. Biol. 38:1998;101-109.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 51
    • 85030947579 scopus 로고    scopus 로고
    • Sriraman, R. et al. Glycosylation of recombinant antibodies in plants. Proceedings of the Ranbaxy Science Foundation Symposium 2002, Ranbaxy Science Foundation, New Delhi (in press).
    • Sriraman, R., et al. Glycosylation of recombinant antibodies in plants. Proceedings of the Ranbaxy Science Foundation Symposium 2002, Ranbaxy Science Foundation, New Delhi (in press).
  • 52
    • 0036481848 scopus 로고    scopus 로고
    • Milestones in chloroplast genetic engineering: An environmentally friendly era in biotechnology
    • Daniell H., et al. Milestones in chloroplast genetic engineering: an environmentally friendly era in biotechnology. Trends Plant Sci. 7:2002;84-91.
    • (2002) Trends Plant Sci. , vol.7 , pp. 84-91
    • Daniell, H.1
  • 53
    • 0034016818 scopus 로고    scopus 로고
    • High-yield production of a human therapeutic protein in tobacco chloroplasts
    • Staub J.M., et al. High-yield production of a human therapeutic protein in tobacco chloroplasts. Nat. Biotechnol. 18:2000;333-338.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 333-338
    • Staub, J.M.1
  • 54
    • 85169106486 scopus 로고    scopus 로고
    • A chloroplast transgenic approach to hyper-express and purify human serum albumin, a protein highly susceptible to proteolytic degradation
    • Millan A.F.-S., et al. A chloroplast transgenic approach to hyper-express and purify human serum albumin, a protein highly susceptible to proteolytic degradation. Plant Biotechnol. 1:2003;77-79.
    • (2003) Plant Biotechnol. , vol.1 , pp. 77-79
    • Millan, A.F.-S.1
  • 55
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
    • Daniell H., et al. Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts. J. Mol. Biol. 311:2001;1001-1009.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1001-1009
    • Daniell, H.1
  • 56
    • 0037440739 scopus 로고    scopus 로고
    • Expression of tetanus toxin fragment C in tobacco chloroplasts
    • Tregoning J.S., et al. Expression of tetanus toxin fragment C in tobacco chloroplasts. Nucleic Acids Res. 31:2003;1174-1179.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1174-1179
    • Tregoning, J.S.1
  • 57
    • 0037280809 scopus 로고    scopus 로고
    • Overproduction of an alkali- and thermo-stable xylanase in tobacco chloroplasts and efficient recovery of the enzyme
    • Leelavathi S., et al. Overproduction of an alkali- and thermo-stable xylanase in tobacco chloroplasts and efficient recovery of the enzyme. Mol. Breed. 11:2003;59-67.
    • (2003) Mol. Breed. , vol.11 , pp. 59-67
    • Leelavathi, S.1
  • 58
    • 0036307494 scopus 로고    scopus 로고
    • In situ transfer of antibiotic resistance genes from transgenic (transplastomic) tobacco plants to bacteria
    • Kay E., et al. In situ transfer of antibiotic resistance genes from transgenic (transplastomic) tobacco plants to bacteria. Appl. Environ. Microbiol. 68:2002;3345-3351.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3345-3351
    • Kay, E.1
  • 59
    • 0037225784 scopus 로고    scopus 로고
    • Immunomodulation of enzyme function in plants by single domain antibody fragments
    • Jobling S.A., et al. Immunomodulation of enzyme function in plants by single domain antibody fragments. Nat. Biotechnol. 21:2003;77-80.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 77-80
    • Jobling, S.A.1
  • 60
    • 0036355659 scopus 로고    scopus 로고
    • Practical considerations for pharmaceutical antibody production in different crop systems
    • Stöger E., et al. Practical considerations for pharmaceutical antibody production in different crop systems. Mol. Breed. 9:2002;149-158.
    • (2002) Mol. Breed. , vol.9 , pp. 149-158
    • Stöger, E.1
  • 61
    • 85030953083 scopus 로고    scopus 로고
    • D'Aoust, M.A. Perennial plants as a production system for pharmaceuticals. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
    • D'Aoust, M.A. Perennial plants as a production system for pharmaceuticals. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
  • 62
    • 0031790556 scopus 로고    scopus 로고
    • A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes
    • Zeitlin L., et al. A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes. Nat. Biotechnol. 16:1998;1361-1364.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 1361-1364
    • Zeitlin, L.1
  • 63
    • 0033587793 scopus 로고    scopus 로고
    • Production of a diagnostic monoclonal antibody in perennial alfalfa plants
    • Khoudi H., et al. Production of a diagnostic monoclonal antibody in perennial alfalfa plants. Biotechnol. Bioeng. 64:1999;135-143.
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 135-143
    • Khoudi, H.1
  • 64
    • 0032863164 scopus 로고    scopus 로고
    • A plant-derived edible vaccine against hepatitis B virus
    • Kapusta J., et al. A plant-derived edible vaccine against hepatitis B virus. FASEB J. 13:1999;1796-1799.
    • (1999) FASEB J. , vol.13 , pp. 1796-1799
    • Kapusta, J.1
  • 65
    • 0037070490 scopus 로고    scopus 로고
    • From green plants to industrial enzymes
    • Hood E.E. From green plants to industrial enzymes. Enzyme & Microbial Technol. 30:2002;279-283.
    • (2002) Enzyme & Microbial Technol , vol.30 , pp. 279-283
    • Hood, E.E.1
  • 66
    • 0030460536 scopus 로고    scopus 로고
    • Microplate assay for soybean seed coat peroxidase activity
    • Vierling R.A., Wilcox J.R. Microplate assay for soybean seed coat peroxidase activity. Seed Science Technol. 24:1996;485-494.
    • (1996) Seed Science Technol. , vol.24 , pp. 485-494
    • Vierling, R.A.1    Wilcox, J.R.2
  • 67
    • 0031863854 scopus 로고    scopus 로고
    • Immunogenicity in humans of a recombinant bacterial-antigen delivered in transgenic potato
    • Tacket C.O., et al. Immunogenicity in humans of a recombinant bacterial-antigen delivered in transgenic potato. Nat. Med. 4:1998;607-609.
    • (1998) Nat. Med. , vol.4 , pp. 607-609
    • Tacket, C.O.1
  • 68
    • 0013651896 scopus 로고    scopus 로고
    • Human immune responses to a novel Norwalk virus vaccine delivered in transgenic potatoes
    • Tacket C.O., et al. Human immune responses to a novel Norwalk virus vaccine delivered in transgenic potatoes. J. Infect. Dis. 182:2000;302-305.
    • (2000) J. Infect. Dis. , vol.182 , pp. 302-305
    • Tacket, C.O.1
  • 69
    • 0033758177 scopus 로고    scopus 로고
    • Production of hepatitis B surface antigen in transgenic plants for oral immunization
    • Richter L.J., et al. Production of hepatitis B surface antigen in transgenic plants for oral immunization. Nat. Biotechnol. 18:2000;1167-1171.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1167-1171
    • Richter, L.J.1
  • 70
    • 0038732769 scopus 로고    scopus 로고
    • Expression of rotavirus capsid protein VP6 in transgenic potato and its oral immunogenicity in mice
    • Yu J., Langridge W. Expression of rotavirus capsid protein VP6 in transgenic potato and its oral immunogenicity in mice. Transgenic Res. 12:2003;163-169.
    • (2003) Transgenic Res. , vol.12 , pp. 163-169
    • Yu, J.1    Langridge, W.2
  • 71
    • 0031711457 scopus 로고    scopus 로고
    • Potato tubers as a biofactory for recombinant antibodies
    • Artsaenko O., et al. Potato tubers as a biofactory for recombinant antibodies. Mol. Breed. 4:1998;313-319.
    • (1998) Mol. Breed. , vol.4 , pp. 313-319
    • Artsaenko, O.1
  • 72
    • 0036383059 scopus 로고    scopus 로고
    • Expression of antibodies and Fab fragments in transgenic potato plants: A case study for bulk production in crop plants
    • De Wilde C., et al. Expression of antibodies and Fab fragments in transgenic potato plants: a case study for bulk production in crop plants. Mol. Breed. 9:2002;2871-2882.
    • (2002) Mol. Breed. , vol.9 , pp. 2871-2882
    • De Wilde, C.1
  • 73
    • 0036342361 scopus 로고    scopus 로고
    • Biopharming the SimpliRED™ HIV diagnostic reagent in barley, potato and tobacco
    • Schunmann P.H.D., et al. Biopharming the SimpliRED™ HIV diagnostic reagent in barley, potato and tobacco. Mol. Breed. 9:2002;113-121.
    • (2002) Mol. Breed. , vol.9 , pp. 113-121
    • Schunmann, P.H.D.1
  • 74
    • 0034030703 scopus 로고    scopus 로고
    • Expression of full-length bioactive antimicrobial human lactoferrin in potato plants
    • Chong D.K.X., Langridge W.H.R. Expression of full-length bioactive antimicrobial human lactoferrin in potato plants. Transgenic Res. 9:2000;71-78.
    • (2000) Transgenic Res. , vol.9 , pp. 71-78
    • Chong, D.K.X.1    Langridge, W.H.R.2
  • 75
    • 0031194819 scopus 로고    scopus 로고
    • Expression of the human milk protein β-casein in transgenic potato plants
    • Chong D.K.X., et al. Expression of the human milk protein β-casein in transgenic potato plants. Transgenic Res. 6:1997;289-296.
    • (1997) Transgenic Res. , vol.6 , pp. 289-296
    • Chong, D.K.X.1
  • 76
    • 0028863460 scopus 로고
    • Expression of the rabies virus glycoprotein in transgenic tomatoes
    • McGarvey P.B., et al. Expression of the rabies virus glycoprotein in transgenic tomatoes. Biotechnology (N.Y.). 13:1995;1484-1487.
    • (1995) Biotechnology (N.Y.) , vol.13 , pp. 1484-1487
    • Mcgarvey, P.B.1
  • 77
    • 0037472387 scopus 로고    scopus 로고
    • Vaccine antigen production in transgenic plants: Strategies, gene constructs and perspectives
    • Sala F., et al. Vaccine antigen production in transgenic plants: strategies, gene constructs and perspectives. Vaccine. 21:2003;803-808.
    • (2003) Vaccine , vol.21 , pp. 803-808
    • Sala, F.1
  • 78
    • 0000146626 scopus 로고    scopus 로고
    • An agrobacterium-mediated transient gene expression system for intact leaves
    • Kapila J., et al. An agrobacterium-mediated transient gene expression system for intact leaves. Plant Sci. 122:1997;101-108.
    • (1997) Plant Sci. , vol.122 , pp. 101-108
    • Kapila, J.1
  • 79
    • 0036515168 scopus 로고    scopus 로고
    • A carcinoembryonic antigen-specific diabody produced in tobacco
    • Vaquero C., et al. A carcinoembryonic antigen-specific diabody produced in tobacco. FASEB J. 16:2002;408-410.
    • (2002) FASEB J. , vol.16 , pp. 408-410
    • Vaquero, C.1
  • 80
    • 0031732939 scopus 로고    scopus 로고
    • Expression and assembly of a full-length monoclonal antibody in plants using a plant virus vector
    • Verch T., et al. Expression and assembly of a full-length monoclonal antibody in plants using a plant virus vector. J. Immunol. Methods. 220:1998;69-75.
    • (1998) J. Immunol. Methods , vol.220 , pp. 69-75
    • Verch, T.1
  • 81
    • 0033582277 scopus 로고    scopus 로고
    • Rapid production of specific vaccines for lymphoma by expression of the tumor-derived single-chain Fv epitopes in tobacco plants
    • McCormick A.A., et al. Rapid production of specific vaccines for lymphoma by expression of the tumor-derived single-chain Fv epitopes in tobacco plants. Proc. Natl. Acad. Sci. U. S. A. 96:1999;703-708.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 703-708
    • Mccormick, A.A.1
  • 82
    • 85030947537 scopus 로고    scopus 로고
    • Mor, T.S. and Mason, H.S. Plants as a source of subunit vaccines. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
    • Mor, T.S. and Mason, H.S. Plants as a source of subunit vaccines. In Handbook of Plant Biotechnology (Christou, P. and Klee, H., eds), Wiley-VCH (in press).
  • 83
    • 0034026065 scopus 로고    scopus 로고
    • Foreign protein production in plant tissue cultures
    • Doran P.M. Foreign protein production in plant tissue cultures. Curr. Opin. Biotechnol. 11:2000;199-204.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 199-204
    • Doran, P.M.1
  • 84
    • 0033498455 scopus 로고    scopus 로고
    • Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies
    • Torres E., et al. Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies. Transgenic Res. 8:1999;441-449.
    • (1999) Transgenic Res. , vol.8 , pp. 441-449
    • Torres, E.1
  • 85
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose
    • Bardor M., et al. Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose. Glycobiology. 13:2003;427-434.
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1
  • 86
    • 0032169762 scopus 로고    scopus 로고
    • N-glycoprotein biosynthesis in plants: Recent developments and future trends
    • Lerouge P., et al. N-glycoprotein biosynthesis in plants: recent developments and future trends. Plant Mol. Biol. 38:1998;31-48.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 31-48
    • Lerouge, P.1


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