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Volumn 19, Issue 31, 2013, Pages 5543-5552

Seeds as a production system for molecular pharming applications: Status and prospects

Author keywords

Infectious diseases; Plant made pharmaceuticals; Recombinant antibodies; Recombinant proteins

Indexed keywords

ANTIGEN; ENZYME INHIBITOR; GLYCOPROTEIN; GROWTH FACTOR; HORMONE; INDUSTRIAL ENZYME; PEPTIDE; RECOMBINANT PROTEIN; SEED STORAGE PROTEIN; VACCINE;

EID: 84881349732     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319310009     Document Type: Review
Times cited : (27)

References (148)
  • 1
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma JK, Drake PM, Christou P. The production of recombinant pharmaceutical proteins in plants. Nat Rev Genet 2003; 4: 794-805.
    • (2003) Nat Rev Genet , vol.4 , pp. 794-805
    • Ma, J.K.1    Drake, P.M.2    Christou, P.3
  • 4
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants
    • Stöger E, Ma JK, Fischer R, Christou P. Sowing the seeds of success: pharmaceutical proteins from plants. Curr Opin Biotechnol 2005; 16: 167-173.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 167-173
    • Stöger, E.1    Ma, J.K.2    Fischer, R.3    Christou, P.4
  • 5
    • 0342748410 scopus 로고    scopus 로고
    • Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies
    • Stöger E, Vaquero C, Torres E, et al. Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies. Plant Mol Biol 2000; 42: 583-590.
    • (2000) Plant Mol Biol , vol.42 , pp. 583-590
    • Stöger, E.1    Vaquero, C.2    Torres, E.3
  • 7
    • 0012515015 scopus 로고    scopus 로고
    • Antibody molecular farming in plants and plant cells
    • Schillberg S, Emans N, Fischer R. Antibody molecular farming in plants and plant cells. Phytochem Rev 2002; 1: 45-54.
    • (2002) Phytochem Rev , vol.1 , pp. 45-54
    • Schillberg, S.1    Emans, N.2    Fischer, R.3
  • 8
    • 79953704799 scopus 로고    scopus 로고
    • Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies
    • Peters J, Stöger E. Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies. Hum Vaccines 2011; 7: 367-374.
    • (2011) Hum Vaccines , vol.7 , pp. 367-374
    • Peters, J.1    Stöger, E.2
  • 9
    • 1542351607 scopus 로고    scopus 로고
    • Targeting transgene expression in research, agricultural, and environmental applications: Promoters used in plant transformation
    • Potenza C, Aleman L, Sengupta-Gopalan C. Targeting transgene expression in research, agricultural, and environmental applications: Promoters used in plant transformation. In vitro Cell Dev-Pl 2004; 40: 1-22.
    • (2004) In Vitro Cell Dev-Pl , vol.40 , pp. 1-22
    • Potenza, C.1    Aleman, L.2    Sengupta-Gopalan, C.3
  • 10
    • 33747599863 scopus 로고    scopus 로고
    • A KDEL-tagged monoclonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds
    • Petruccelli S, Otegui MS, Lareu F, et al. A KDEL-tagged monoclonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds. Plant Biotechnol J 2006; 4: 511-527.
    • (2006) Plant Biotechnol J , vol.4 , pp. 511-527
    • Petruccelli, S.1    Otegui, M.S.2    Lareu, F.3
  • 12
    • 0033835441 scopus 로고    scopus 로고
    • Corn seed production of therapeutic proteins moves forward
    • Baez J, Russell D, Craig J, Cass PL. Corn seed production of therapeutic proteins moves forward. Biopharm Int 2000; 13: 50-54.
    • (2000) Biopharm Int , vol.13 , pp. 50-54
    • Baez, J.1    Russell, D.2    Craig, J.3    Cass, P.L.4
  • 13
    • 0035212386 scopus 로고    scopus 로고
    • Medical molecular farming: Production of antibodies, biopharmaceuticals and edible vaccines in plants
    • Daniell H, Streatfield SJ, Wycoff K. Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci 2001; 6: 219-226.
    • (2001) Trends Plant Sci , vol.6 , pp. 219-226
    • Daniell, H.1    Streatfield, S.J.2    Wycoff, K.3
  • 14
    • 0036806486 scopus 로고    scopus 로고
    • Expression of human lactoferrin in transgenic rice grains for the application in infant formula
    • Nandi S, Suzuki YA, Huang J, et al. Expression of human lactoferrin in transgenic rice grains for the application in infant formula. Plant Sci 2002; 163: 713-722.
    • (2002) Plant Sci , vol.163 , pp. 713-722
    • Nandi, S.1    Suzuki, Y.A.2    Huang, J.3
  • 17
    • 0030895149 scopus 로고    scopus 로고
    • Human haemoglobin from transgenic tobacco
    • Dieryck W, Pagnier J, Poyart C, et al. Human haemoglobin from transgenic tobacco. Nature 1997; 386: 29-30.
    • (1997) Nature , vol.386 , pp. 29-30
    • Dieryck, W.1    Pagnier, J.2    Poyart, C.3
  • 18
    • 0033983338 scopus 로고    scopus 로고
    • Engineering the provitamin A (beta-carotene) biosynthetic pathway into (carotenoid-free) rice endosperm
    • Ye X, Al-Babili S, Kloti A, et al. Engineering the provitamin A (beta-carotene) biosynthetic pathway into (carotenoid-free) rice endosperm. Science 2000; 287: 303-305.
    • (2000) Science , vol.287 , pp. 303-305
    • Ye, X.1    Al-Babili, S.2    Kloti, A.3
  • 19
    • 34547221110 scopus 로고    scopus 로고
    • Rice-based mucosal vaccine as a global strategy for cold-chain and needle-free vaccination
    • Nochi T, Takagi H, Yuki Y, et al. Rice-based mucosal vaccine as a global strategy for cold-chain and needle-free vaccination. Proc Natl Acad Sci USA 2007; 104: 10986-10991.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10986-10991
    • Nochi, T.1    Takagi, H.2    Yuki, Y.3
  • 21
    • 34547556413 scopus 로고    scopus 로고
    • Oral immunization with transgenic rice seeds expressing VP2 protein of infectious bursal disease virus induces protective immune responses in chickens
    • Wu J, Yu L, Li L, Hu J, Zhou J, Zhou X. Oral immunization with transgenic rice seeds expressing VP2 protein of infectious bursal disease virus induces protective immune responses in chickens. Plant Biotechnol J 2007; 5: 570-578.
    • (2007) Plant Biotechnol J , vol.5 , pp. 570-578
    • Wu, J.1    Yu, L.2    Li, L.3    Hu, J.4    Zhou, J.5    Zhou, X.6
  • 22
    • 68849113455 scopus 로고    scopus 로고
    • Production of a recombinant full-length collagen type I-1 and of a 45-kDa collagen type I-1 fragment in barley seeds
    • Eskelin K, Ritala A, Suntio T, et al. Production of a recombinant full-length collagen type I-1 and of a 45-kDa collagen type I-1 fragment in barley seeds. Plant Biotechnol J 2009; 7: 657-672.
    • (2009) Plant Biotechnol J , vol.7 , pp. 657-672
    • Eskelin, K.1    Ritala, A.2    Suntio, T.3
  • 23
    • 35148831566 scopus 로고    scopus 로고
    • Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed
    • Hood EE, Love R, Lane J, et al. Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed. Plant Biotechnol J 2007; 5: 709-719.
    • (2007) Plant Biotechnol J , vol.5 , pp. 709-719
    • Hood, E.E.1    Love, R.2    Lane, J.3
  • 24
    • 0036342361 scopus 로고    scopus 로고
    • Biopharming the SimpliRED™ HIV diagnostic reagent in barley, potato and tobacco
    • Schünmann PHD, Coia G, Waterhouse PM. Biopharming the SimpliRED™ HIV diagnostic reagent in barley, potato and tobacco. Mol Breeding 2002; 9: 113-121.
    • (2002) Mol Breeding , vol.9 , pp. 113-121
    • Schünmann, P.H.D.1    Coia, G.2    Waterhouse, P.M.3
  • 25
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plantsmyths and realities
    • Hood EE, Woodard SL, Horn ME. Monoclonal antibody manufacturing in transgenic plantsmyths and realities. Curr Opin Biotechnol 2002; 13: 630-635.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 630-635
    • Hood, E.E.1    Woodard, S.L.2    Horn, M.E.3
  • 26
    • 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, Vaquero C, Gerrard I, 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 Breeding 2000; 6: 345-352.
    • (2000) Mol Breeding , vol.6 , pp. 345-352
    • Perrin, Y.1    Vaquero, C.2    Gerrard, I.3
  • 27
    • 0031790556 scopus 로고    scopus 로고
    • A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes
    • Zeitlin L, Olmsted SS, Moench TR, et al. A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes. Nat Biotechnol 1998; 16: 1361-1364.
    • (1998) Nat Biotechnol , vol.16 , pp. 1361-1364
    • Zeitlin, L.1    Olmsted, S.S.2    Moench, T.R.3
  • 28
    • 0033529588 scopus 로고    scopus 로고
    • Development of biopharmaceuticals in plant expression systems: Cloning, expression and immunological reactivity of human cytomegalovirus glycoprotein B (UL55) in seeds of transgenic tobacco
    • Tackaberry ES, Dudani AK, Prior F, et al. Development of biopharmaceuticals in plant expression systems: cloning, expression and immunological reactivity of human cytomegalovirus glycoprotein B (UL55) in seeds of transgenic tobacco. Vaccine 1999; 17: 3020-3029.
    • (1999) Vaccine , vol.17 , pp. 3020-3029
    • Tackaberry, E.S.1    Dudani, A.K.2    Prior, F.3
  • 29
    • 33645112928 scopus 로고    scopus 로고
    • Forcing single-chain variable fragment production in tobacco seeds by fusion to elastin-like polypeptides
    • Scheller J, Leps M, Conrad U. Forcing single-chain variable fragment production in tobacco seeds by fusion to elastin-like polypeptides. Plant Biotechnol J 2006; 4: 243-249.
    • (2006) Plant Biotechnol J , vol.4 , pp. 243-249
    • Scheller, J.1    Leps, M.2    Conrad, U.3
  • 30
    • 33645309590 scopus 로고    scopus 로고
    • Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds
    • Nykiforuk CL, Boothe JG, Murray EW, et al. Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds. Plant Biotechnol J 2006; 4: 77-85.
    • (2006) Plant Biotechnol J , vol.4 , pp. 77-85
    • Nykiforuk, C.L.1    Boothe, J.G.2    Murray, E.W.3
  • 32
    • 2442708551 scopus 로고    scopus 로고
    • Immunogenicity of recombinant LT-B delivered orally to humans in transgenic corn
    • Tacket CO, Pasetti MF, Edelman R, Howard JA, Streatfield S. Immunogenicity of recombinant LT-B delivered orally to humans in transgenic corn. Vaccine 2004; 22: 4385-4389.
    • (2004) Vaccine , vol.22 , pp. 4385-4389
    • Tacket, C.O.1    Pasetti, M.F.2    Edelman, R.3    Howard, J.A.4    Streatfield, S.5
  • 33
    • 84881349937 scopus 로고    scopus 로고
    • Accessed online 27 August 2012, Available at
    • Monsanto Protein Technology and NeoRx Corporation. [Accessed online 27 August 2012]; Available at: http: //www.mpt.monsanto.com/andhttp://www.neorx.com/.
    • Monsanto Protein Technology and NeoRx Corporation
  • 34
    • 0035412277 scopus 로고    scopus 로고
    • N-glycosylation poten-tial of maize: The human lactoferrin used as a model
    • Samyn-Petit B, Gruber V, Flahaut C, et al. N-glycosylation poten-tial of maize: The human lactoferrin used as a model. Glycoconjugate J 2001; 18: 519-527.
    • (2001) Glycoconjugate J , vol.18 , pp. 519-527
    • Samyn-Petit, B.1    Gruber, V.2    Flahaut, C.3
  • 35
    • 0033860834 scopus 로고    scopus 로고
    • Oral immunogenicity of the plant derived spike protein from swine-transmissible gastroenteritis coronavirus
    • Gomez N, Wigdorovitz A, Castanon S, et al. Oral immunogenicity of the plant derived spike protein from swine-transmissible gastroenteritis coronavirus. Arch Virol 2000; 145: 1725-1732.
    • (2000) Arch Virol , vol.145 , pp. 1725-1732
    • Gomez, N.1    Wigdorovitz, A.2    Castanon, S.3
  • 36
    • 0034081592 scopus 로고    scopus 로고
    • Expression of murine adenosine deaminase (ADA) in transgenic maize
    • Petolino JF, Young S, Hopkins N, et al. Expression of murine adenosine deaminase (ADA) in transgenic maize. Transgenic Res 2000; 9: 1-9.
    • (2000) Transgenic Res , vol.9 , pp. 1-9
    • Petolino, J.F.1    Young, S.2    Hopkins, N.3
  • 38
    • 0034817036 scopus 로고    scopus 로고
    • Large-scale production of a therapeutic protein in transgenic tobacco plants: Effect of subcellular targeting on quality of a recombinant dog gastric lipase
    • Gruber V, Berna PP, Arnaud T, et al. Large-scale production of a therapeutic protein in transgenic tobacco plants: effect of subcellular targeting on quality of a recombinant dog gastric lipase. Mol Breeding 2001; 7: 329-340.
    • (2001) Mol Breeding , vol.7 , pp. 329-340
    • Gruber, V.1    Berna, P.P.2    Arnaud, T.3
  • 39
    • 0000217415 scopus 로고    scopus 로고
    • Commercial production of avidin from transgenic maize: Characterization of transformant, production, processing, extraction and purification
    • Hood EE, Witcher DR, Maddock S, et al. Commercial production of avidin from transgenic maize: characterization of transformant, production, processing, extraction and purification. Mol Breeding 1997; 3 (4): 291-306.
    • (1997) Mol Breeding , vol.3 , Issue.4 , pp. 291-306
    • Hood, E.E.1    Witcher, D.R.2    Maddock, S.3
  • 40
    • 12444303175 scopus 로고    scopus 로고
    • Maize (Zea mays)-derived bovine trypsin: Characterization of the first large-scale, commercial protein product from transgenic plants
    • Woodard SL, Mayor JM, Bailey MR, et al. Maize (Zea mays)-derived bovine trypsin: characterization of the first large-scale, commercial protein product from transgenic plants. Biotechnol Appl Bioc 2003; 38: 123-130.
    • (2003) Biotechnol Appl Bioc , vol.38 , pp. 123-130
    • Woodard, S.L.1    Mayor, J.M.2    Bailey, M.R.3
  • 41
    • 0035925713 scopus 로고    scopus 로고
    • Plant-based vaccines: Unique advantages
    • Streatfield SJ, Jilka JM, Hood EE, et al. Plant-based vaccines: unique advantages. Vaccine 2001; 19: 2742-2748.
    • (2001) Vaccine , vol.19 , pp. 2742-2748
    • Streatfield, S.J.1    Jilka, J.M.2    Hood, E.E.3
  • 42
    • 27644494245 scopus 로고    scopus 로고
    • Expression of the sweet protein brazzein in maize for production of a new commercial sweetener
    • Lamphear BJ, Barker DK, Brooks CA, et al. Expression of the sweet protein brazzein in maize for production of a new commercial sweetener. Plant Biotechnol J 2005; 3: 103-114.
    • (2005) Plant Biotechnol J , vol.3 , pp. 103-114
    • Lamphear, B.J.1    Barker, D.K.2    Brooks, C.A.3
  • 43
    • 37749007243 scopus 로고    scopus 로고
    • Recombinant antibody 2G12 produced in maize endosperm efficiently neutralizes HIV-1 and contains predominantly single-GlcNAc N-glycans
    • Rademacher T, Sack M, Arcalis E, et al. Recombinant antibody 2G12 produced in maize endosperm efficiently neutralizes HIV-1 and contains predominantly single-GlcNAc N-glycans. Plant Biotechnol J 2008; 6: 189-201.
    • (2008) Plant Biotechnol J , vol.6 , pp. 189-201
    • Rademacher, T.1    Sack, M.2    Arcalis, E.3
  • 44
    • 41649113980 scopus 로고    scopus 로고
    • Cost-effective production of a vaginal protein microbicide to prevent HIV transmission
    • Ramessar K, Rademacher T, Sack M, et al. Cost-effective production of a vaginal protein microbicide to prevent HIV transmission. Proc Natl Acad Sci USA 2008; 105: 3727-3732.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3727-3732
    • Ramessar, K.1    Rademacher, T.2    Sack, M.3
  • 45
    • 84863421717 scopus 로고    scopus 로고
    • Bioencapsulation of the hepatitis B surface antigen and its use as an effective oral immunogen
    • Hayden CA, Streatfield SJ, Lamphear BJ, et al. Bioencapsulation of the hepatitis B surface antigen and its use as an effective oral immunogen. Vaccine 2012; 30: 2937-2942.
    • (2012) Vaccine , vol.30 , pp. 2937-2942
    • Hayden, C.A.1    Streatfield, S.J.2    Lamphear, B.J.3
  • 46
    • 84881359590 scopus 로고
    • Induction of Nitrate Reductase and Peroxidase Activity in the Seedlings of Normal and High Lysine Maize
    • Srivastava HS, Asthana JS, Jain A. Induction of Nitrate Reductase and Peroxidase Activity in the Seedlings of Normal and High Lysine Maize. Physiol Plantarum 1979; 47: 119-123.
    • (1979) Physiol Plantarum , vol.47 , pp. 119-123
    • Srivastava, H.S.1    Asthana, J.S.2    Jain, A.3
  • 47
    • 33751208023 scopus 로고    scopus 로고
    • Extraction of Recombinant Dog Gastric Lipase from Transgenic Corn Seed
    • Zhong Q, Gu Z, Glatz CE. Extraction of Recombinant Dog Gastric Lipase from Transgenic Corn Seed. J Agr Food Chem 2006; 54: 8086-8092.
    • (2006) J Agr Food Chem , vol.54 , pp. 8086-8092
    • Zhong, Q.1    Gu, Z.2    Glatz, C.E.3
  • 48
    • 84881337138 scopus 로고    scopus 로고
    • Accessed online 27 August 2012, Available at
    • EPlcyte [Accessed online 27 August 2012]; Available at: http://www.epicyte.com.
    • EPlcyte
  • 49
    • 0032487368 scopus 로고    scopus 로고
    • Processing of transgenic corn seed and its effect on the recovery of recombinant beta-glucuronidase
    • Kusnadi AR, Evangelista RL, Hood EE, Howard JA, Nikolov ZL. Processing of transgenic corn seed and its effect on the recovery of recombinant beta-glucuronidase. Biotechnol Bioeng 1998; 60: 44-52.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 44-52
    • Kusnadi, A.R.1    Evangelista, R.L.2    Hood, E.E.3    Howard, J.A.4    Nikolov, Z.L.5
  • 51
    • 19944434133 scopus 로고    scopus 로고
    • Conservation of receptor antagonist antitumor activity by epidermal growth factor receptor antibody expressed in transgenic corn seed
    • Ludwig DL, Witte L, Hicklin DJ, et al. Conservation of receptor antagonist antitumor activity by epidermal growth factor receptor antibody expressed in transgenic corn seed. Hum Antibodies 2004; 13: 81-90.
    • (2004) Hum Antibodies , vol.13 , pp. 81-90
    • Ludwig, D.L.1    Witte, L.2    Hicklin, D.J.3
  • 52
    • 27944458471 scopus 로고    scopus 로고
    • Endosperm-specific coexpression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron
    • Drakakaki G, Marcel S, Glahn RP, et al. Endosperm-specific coexpression of recombinant soybean ferritin and Aspergillus phytase in maize results in significant increases in the levels of bioavailable iron. Plant Mol Biol 2005; 59: 869-880.
    • (2005) Plant Mol Biol , vol.59 , pp. 869-880
    • Drakakaki, G.1    Marcel, S.2    Glahn, R.P.3
  • 53
    • 46649102876 scopus 로고    scopus 로고
    • Transgenic maize plants expressing a fungal phytase gene
    • Chen R, Xue G, Chen P, et al. Transgenic maize plants expressing a fungal phytase gene. Transgenic Res 2008; 17: 633-643.
    • (2008) Transgenic Res , vol.17 , pp. 633-643
    • Chen, R.1    Xue, G.2    Chen, P.3
  • 54
    • 0036355659 scopus 로고    scopus 로고
    • Practical considerations for pharmaceutical antibody production in different crop systems
    • Stöger E, Sack M, Perrin Y, et al. Practical considerations for pharmaceutical antibody production in different crop systems. Mol Breeding 2002; 9: 149-158.
    • (2002) Mol Breeding , vol.9 , pp. 149-158
    • Stöger, E.1    Sack, M.2    Perrin, Y.3
  • 55
    • 54149119320 scopus 로고    scopus 로고
    • A biologically active rhIGF-1 fusion accumulated in transgenic rice seeds can reduce blood glucose in diabetic mice via oral delivery
    • Xie T, Qiu Q, Zhang W, et al. A biologically active rhIGF-1 fusion accumulated in transgenic rice seeds can reduce blood glucose in diabetic mice via oral delivery. Peptides 2008; 29: 1862-1870.
    • (2008) Peptides , vol.29 , pp. 1862-1870
    • Xie, T.1    Qiu, Q.2    Zhang, W.3
  • 56
    • 20844444481 scopus 로고    scopus 로고
    • Production and characterization of recombinant human lactoferrin in transgenic Javanica rice
    • Rachmawati D, Mori T, Hosaka T, Takaiwa F, Inoue E, Anzai H. Production and characterization of recombinant human lactoferrin in transgenic Javanica rice. Breeding Sci 2005; 55: 213-222.
    • (2005) Breeding Sci , vol.55 , pp. 213-222
    • Rachmawati, D.1    Mori, T.2    Hosaka, T.3    Takaiwa, F.4    Inoue, E.5    Anzai, H.6
  • 57
    • 4644330722 scopus 로고    scopus 로고
    • High-level protein expression system uses self-pollinating crops as hosts
    • Huang N. High-level protein expression system uses self-pollinating crops as hosts. Bioprocess Int 2004; 2: 54-59.
    • (2004) Bioprocess Int , vol.2 , pp. 54-59
    • Huang, N.1
  • 58
    • 0037977932 scopus 로고    scopus 로고
    • Expression and localization of human lysozyme in the endosperm of transgenic rice
    • Yang D, Guo F, Liu B, Huang N, Watkins S. Expression and localization of human lysozyme in the endosperm of transgenic rice. Planta 2003; 216: 597-603.
    • (2003) Planta , vol.216 , pp. 597-603
    • Yang, D.1    Guo, F.2    Liu, B.3    Huang, N.4    Watkins, S.5
  • 59
    • 34547797472 scopus 로고    scopus 로고
    • Expression of a synthetic neutralizing epitope of porcine epidemic diarrhea virus fused with synthetic B subunit of Escherichia coli heat labile enterotoxin in rice endosperm
    • Oszvald M, Kang TJ, Tomoskozi S, et al. Expression of a synthetic neutralizing epitope of porcine epidemic diarrhea virus fused with synthetic B subunit of Escherichia coli heat labile enterotoxin in rice endosperm. Mol Biotechnol 2007; 35: 215-223.
    • (2007) Mol Biotechnol , vol.35 , pp. 215-223
    • Oszvald, M.1    Kang, T.J.2    Tomoskozi, S.3
  • 60
    • 33845807398 scopus 로고    scopus 로고
    • Endosperm tissue is good production platform for artificial recombinant proteins in transgenic rice
    • Takaiwa F, Takagi H, Hirose S, Wakasa Y. Endosperm tissue is good production platform for artificial recombinant proteins in transgenic rice. Plant Biotechnol J 2007; 5: 84-92.
    • (2007) Plant Biotechnol J , vol.5 , pp. 84-92
    • Takaiwa, F.1    Takagi, H.2    Hirose, S.3    Wakasa, Y.4
  • 61
    • 0041634710 scopus 로고    scopus 로고
    • Pharming vaccines for hepatitis and cytomegalovirus: Towards the development of multivalent and subunit vaccines for oral delivery of antigens
    • Alli Z, Sardana RK, Pierre B, et al. Pharming vaccines for hepatitis and cytomegalovirus: Towards the development of multivalent and subunit vaccines for oral delivery of antigens. Phytochemistry Rev 2002; 1: 55-66.
    • (2002) Phytochemistry Rev , vol.1 , pp. 55-66
    • Alli, Z.1    Sardana, R.K.2    Pierre, B.3
  • 62
    • 79961154061 scopus 로고    scopus 로고
    • Antihypertensive activity of transgenic rice seed containing an 18-repeat novokinin peptide localized in the nucleolus of endosperm cells
    • Wakasa Y, Zhao H, Hirose S, et al. Antihypertensive activity of transgenic rice seed containing an 18-repeat novokinin peptide localized in the nucleolus of endosperm cells. Plant Biotechnol J 2011; 9: 729-735.
    • (2011) Plant Biotechnol J , vol.9 , pp. 729-735
    • Wakasa, Y.1    Zhao, H.2    Hirose, S.3
  • 63
    • 40849083328 scopus 로고    scopus 로고
    • Expression of Recombinant Phytase in Transgenic Rice
    • Qian-feng L, Qiao-quan L, Da-jiang Z, et al. Expression of Recombinant Phytase in Transgenic Rice. Chinese J Rice Sci 2006; 20: 243-247.
    • (2006) Chinese J Rice Sci , vol.20 , pp. 243-247
    • Qian-Feng, L.1    Qiao-Quan, L.2    Da-Jiang, Z.3
  • 64
    • 4143061287 scopus 로고    scopus 로고
    • Producing transglutaminases by molecular farming in plants: Minireview article
    • Capell T, Claparols I, Del Duca S, et al. Producing transglutaminases by molecular farming in plants: Minireview article. Amino Acids 2004; 26: 419-423.
    • (2004) Amino Acids , vol.26 , pp. 419-423
    • Capell, T.1    Claparols, I.2    Del Duca, S.3
  • 65
    • 77957884786 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant human transferrin from rice (Oryza sativa L.)
    • Zhang D, Nandi S, Bryan P, et al. Expression, purification, and characterization of recombinant human transferrin from rice (Oryza sativa L.). Protein Expres Purif 2010; 74: 69-79.
    • (2010) Protein Expres Purif , vol.74 , pp. 69-79
    • Zhang, D.1    Nandi, S.2    Bryan, P.3
  • 66
    • 35848945914 scopus 로고    scopus 로고
    • Biologically active human GM-CSF produced in the seeds of transgenic rice plants
    • Sardana R, Dudani AK, Tackaberry E, et al. Biologically active human GM-CSF produced in the seeds of transgenic rice plants. Transgenic Res 2007; 16: 713-721.
    • (2007) Transgenic Res , vol.16 , pp. 713-721
    • Sardana, R.1    Dudani, A.K.2    Tackaberry, E.3
  • 67
    • 17044434158 scopus 로고    scopus 로고
    • A recombinant multimeric immunoglobulin expressed in rice shows assembly dependent subcellular localization in endosperm cells
    • Nicholson L, Gonzalez-Melendi P, van Dolleweerd C, et al. A recombinant multimeric immunoglobulin expressed in rice shows assembly dependent subcellular localization in endosperm cells. Plant Biotechnol J 2005; 3: 115-127.
    • (2005) Plant Biotechnol J , vol.3 , pp. 115-127
    • Nicholson, L.1    Gonzalez-Melendi, P.2    van Dolleweerd, C.3
  • 68
    • 84881335689 scopus 로고    scopus 로고
    • Transgenic expression of the recombinant phytase in rice (Oryza sativa)
    • Qiao-quan L, Qian-feng L, Li J, et al. Transgenic expression of the recombinant phytase in rice (Oryza sativa). IRRN 2007; 32: 44.
    • (2007) IRRN , vol.32 , pp. 44
    • Qiao-Quan, L.1    Qian-Feng, L.2    Li, J.3
  • 69
    • 63349084378 scopus 로고    scopus 로고
    • Deposition of a recombinant peptide in ER-derived protein bodies by retention with cysteine-rich prolamins in transgenic rice seed
    • Takaiwa F, Hirose S, Takagi H, Yang L, Wakasa Y. Deposition of a recombinant peptide in ER-derived protein bodies by retention with cysteine-rich prolamins in transgenic rice seed. Planta 2009; 229: 1147-1158.
    • (2009) Planta , vol.229 , pp. 1147-1158
    • Takaiwa, F.1    Hirose, S.2    Takagi, H.3    Yang, L.4    Wakasa, Y.5
  • 70
    • 79953730113 scopus 로고    scopus 로고
    • Prevention of allergic asthma by vaccination with transgenic rice seed expressing mite allergen: Induction of allergen-specific oral tolerance without by stander suppression
    • Suzuki K, Kaminuma O, Yang L, et al. Prevention of allergic asthma by vaccination with transgenic rice seed expressing mite allergen: induction of allergen-specific oral tolerance without by stander suppression. Plant Biotechnol J 2011; 9: 982-990.
    • (2011) Plant Biotechnol J , vol.9 , pp. 982-990
    • Suzuki, K.1    Kaminuma, O.2    Yang, L.3
  • 71
    • 84856968665 scopus 로고    scopus 로고
    • Production of human growth hormone in transgenic rice seeds: Cointroduction of RNA interference cassette for suppressing the gene expression of endogenous storage proteins
    • Shigemitsu T, Ozaki S, Saito Y, et al. Production of human growth hormone in transgenic rice seeds: cointroduction of RNA interference cassette for suppressing the gene expression of endogenous storage proteins. Plant Cell Rep 2012; 31: 539-549.
    • (2012) Plant Cell Rep , vol.31 , pp. 539-549
    • Shigemitsu, T.1    Ozaki, S.2    Saito, Y.3
  • 72
    • 0035077846 scopus 로고    scopus 로고
    • Sorting of glycoprotein B from human cytomegalovirus to protein storage vesicles in seeds of transgenic tobacco
    • Wright KE, Prior F, Sardana R, et al. Sorting of glycoprotein B from human cytomegalovirus to protein storage vesicles in seeds of transgenic tobacco. Transgenic Res 2001; 10: 177-181.
    • (2001) Transgenic Res , vol.10 , pp. 177-181
    • Wright, K.E.1    Prior, F.2    Sardana, R.3
  • 73
    • 0034000123 scopus 로고    scopus 로고
    • Expression of correctly processed human growth hormone in seeds of transgenic tobacco plants
    • Leite A, Kemper EL, da Silva MJ, et al. Expression of correctly processed human growth hormone in seeds of transgenic tobacco plants. Mol Breeding 2000; 6: 47-53.
    • (2000) Mol Breeding , vol.6 , pp. 47-53
    • Leite, A.1    Kemper, E.L.2    da Silva, M.J.3
  • 74
    • 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 SB, Pearson KW, Meeker G, Staraci LC, Sun SM. 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 1989; 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.M.5
  • 75
    • 33747599863 scopus 로고    scopus 로고
    • A KDEL tagged mono-clonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds
    • Petruccelli S, Otegui MS, Lareu F, et al. A KDEL tagged mono-clonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds. Plant Biotechnol J 2006; 4: 511-527.
    • (2006) Plant Biotechnol J , vol.4 , pp. 511-527
    • Petruccelli, S.1    Otegui, M.S.2    Lareu, F.3
  • 77
    • 0028889621 scopus 로고
    • High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds
    • Fiedler U, Conrad U. High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds. Biotechnology (NY) 1995; 13: 1090-1093.
    • (1995) Biotechnology (NY) , vol.13 , pp. 1090-1093
    • Fiedler, U.1    Conrad, U.2
  • 79
    • 84865978982 scopus 로고    scopus 로고
    • Production of different glycosylation variants of the tumourtargeting mAb H10 in Nicotiana benthamiana: Influence on expression yield and antibody degradation
    • Lombardi R, Donini M, Villani ME, et al. Production of different glycosylation variants of the tumourtargeting mAb H10 in Nicotiana benthamiana: influence on expression yield and antibody degradation. Transgenic Res 2012: 1-17.
    • (2012) Transgenic Res , pp. 1-17
    • Lombardi, R.1    Donini, M.2    Villani, M.E.3
  • 80
    • 0346266176 scopus 로고    scopus 로고
    • Expression & immunogenicity of malaria merozoite peptides displayed on the small coat protein of chimaeric cowpea mosaic virus
    • Yasawardene SG, Lomonossoff GP, Ramasamy R. Expression & immunogenicity of malaria merozoite peptides displayed on the small coat protein of chimaeric cowpea mosaic virus. Indian J Med Res 2003; 118: 115-124.
    • (2003) Indian J Med Res , vol.118 , pp. 115-124
    • Yasawardene, S.G.1    Lomonossoff, G.P.2    Ramasamy, R.3
  • 81
    • 0031907101 scopus 로고    scopus 로고
    • Protective Immune Response to Foot and Mouth Disease Virus with VP1 Expressed in Transgenic Plants
    • Carrillo C, Wigdorovitz A, Oliveros JC, et al. Protective Immune Response to Foot and Mouth Disease Virus with VP1 Expressed in Transgenic Plants. J Virol 1998; 72: 1688-1690.
    • (1998) J Virol , vol.72 , pp. 1688-1690
    • Carrillo, C.1    Wigdorovitz, A.2    Oliveros, J.C.3
  • 82
    • 27444440300 scopus 로고    scopus 로고
    • Development of cowpea mosaic virus-based vectors for the production of vaccines in plants
    • Canizares MC, Lomonossoff GP, Nicholson L. Development of cowpea mosaic virus-based vectors for the production of vaccines in plants. Expert Rev Vaccines 2005; 4: 687-697.
    • (2005) Expert Rev Vaccines , vol.4 , pp. 687-697
    • Canizares, M.C.1    Lomonossoff, G.P.2    Nicholson, L.3
  • 83
    • 33846210581 scopus 로고    scopus 로고
    • Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine
    • Moravec T, Schmidt MA, Herman EM, Woodford-Thomas T. Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine. Vaccine 2007; 25: 1647-1657.
    • (2007) Vaccine , vol.25 , pp. 1647-1657
    • Moravec, T.1    Schmidt, M.A.2    Herman, E.M.3    Woodford-Thomas, T.4
  • 84
    • 79960472029 scopus 로고    scopus 로고
    • Expression of functional recombinant human growth hormone in transgenic soybean seeds
    • Cunha N, Murad A, Cipriano T, et al. Expression of functional recombinant human growth hormone in transgenic soybean seeds. Transgenic Res 2011; 20: 811-826.
    • (2011) Transgenic Res , vol.20 , pp. 811-826
    • Cunha, N.1    Murad, A.2    Cipriano, T.3
  • 85
    • 84857637180 scopus 로고    scopus 로고
    • Expression of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus in soybean seed yields an immunogenic antigenic protein
    • Vimolmangkang S, Gasic K, Soria-Guerra R, Rosales-Mendoza S, Moreno-Fierros L, Korban SS. Expression of the nucleocapsid protein of porcine reproductive and respiratory syndrome virus in soybean seed yields an immunogenic antigenic protein. Planta 2012; 235: 513-522.
    • (2012) Planta , vol.235 , pp. 513-522
    • Vimolmangkang, S.1    Gasic, K.2    Soria-Guerra, R.3    Rosales-Mendoza, S.4    Moreno-Fierros, L.5    Korban, S.S.6
  • 86
    • 39649090699 scopus 로고    scopus 로고
    • Anti-hypertensive activity of genetically modified soybean seeds accumulating novokinin
    • Yamada Y, Nishizawa K, Yokoo M, et al. Anti-hypertensive activity of genetically modified soybean seeds accumulating novokinin. Peptides 2008; 29: 331-337.
    • (2008) Peptides , vol.29 , pp. 331-337
    • Yamada, Y.1    Nishizawa, K.2    Yokoo, M.3
  • 87
    • 84970050981 scopus 로고
    • En-kephalins Prouduced in Transgenic Plants Using Modified 2S Seed Storage Proteins
    • Vandekerckhove J, van Damme J, van Lijsebettens M, et al. En-kephalins Prouduced in Transgenic Plants Using Modified 2S Seed Storage Proteins. Nat Biotechnol 1989; 7: 929-932.
    • (1989) Nat Biotechnol , vol.7 , pp. 929-932
    • Vandekerckhove, J.1    van Damme, J.2    van Lijsebettens, M.3
  • 88
    • 78149486704 scopus 로고    scopus 로고
    • Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds
    • Lau OS, Ng DW, Chan WW, Chang SP, Sun SS. Production of the 42-kDa fragment of Plasmodium falciparum merozoite surface protein 1, a leading malaria vaccine antigen, in Arabidopsis thaliana seeds. Plant Biotechnol J 2010; 8: 994-1004.
    • (2010) Plant Biotechnol J , vol.8 , pp. 994-1004
    • Lau, O.S.1    Ng, D.W.2    Chan, W.W.3    Chang, S.P.4    Sun, S.S.5
  • 89
    • 78650892991 scopus 로고    scopus 로고
    • Production of monoclonal antibodies with a controlled N-glycosylation pattern in seeds of Arabidopsis thaliana
    • Loos A, van Droogenbroeck B, Hillmer S, et al. Production of monoclonal antibodies with a controlled N-glycosylation pattern in seeds of Arabidopsis thaliana. Plant Biotechnol J 2011; 9: 179-192.
    • (2011) Plant Biotechnol J , vol.9 , pp. 179-192
    • Loos, A.1    van Droogenbroeck, B.2    Hillmer, S.3
  • 90
    • 33744971907 scopus 로고    scopus 로고
    • Producing Proteins Using Transgenic Oilbody-Oleosin Technology
    • Markley N, Nykiforuk C, Boothe J, Moloney M. Producing Proteins Using Transgenic Oilbody-Oleosin Technology. BioPharm Int 2006; 19: 34.
    • (2006) BioPharm Int , vol.19 , pp. 34
    • Markley, N.1    Nykiforuk, C.2    Boothe, J.3    Moloney, M.4
  • 91
    • 33846614234 scopus 로고    scopus 로고
    • Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds
    • van Droogenbroeck B, Cao J, Stadlmann J, et al. Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds. Proc Natl Acad Sci 2007; 104: 1430-1435.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 1430-1435
    • van Droogenbroeck, B.1    Cao, J.2    Stadlmann, J.3
  • 92
    • 33947428691 scopus 로고    scopus 로고
    • Aptamers improve the expression of a human granulocyte macrophage colony stimulating factor in transgenic Arabidopsis thaliana seeds
    • Wang B, Ma M, Wu T. Aptamers improve the expression of a human granulocyte macrophage colony stimulating factor in transgenic Arabidopsis thaliana seeds. J Plant Biol 2007; 50: 29-37.
    • (2007) J Plant Biol , vol.50 , pp. 29-37
    • Wang, B.1    Ma, M.2    Wu, T.3
  • 93
    • 79961191023 scopus 로고    scopus 로고
    • CESA5 is required for the synthesis of cellulose with a role in structuring the adherent mucilage of Arabidopsis seeds
    • Sullivan S, Ralet MC, Berger A, et al. CESA5 is required for the synthesis of cellulose with a role in structuring the adherent mucilage of Arabidopsis seeds. Plant Physiol 2011; 156: 1725-1739.
    • (2011) Plant Physiol , vol.156 , pp. 1725-1739
    • Sullivan, S.1    Ralet, M.C.2    Berger, A.3
  • 94
    • 33645112692 scopus 로고    scopus 로고
    • Synthesis of enzymatically active human-l-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds
    • Downing WL, Galpin JD, Clemens S, et al. Synthesis of enzymatically active human-l-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds. Plant Biotechnol J 2006; 4: 169-181.
    • (2006) Plant Biotechnol J , vol.4 , pp. 169-181
    • Downing, W.L.1    Galpin, J.D.2    Clemens, S.3
  • 95
    • 0035033768 scopus 로고    scopus 로고
    • Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix
    • Stöger E, Parker M, Christou P, Casey R. Pea legumin overexpressed in wheat endosperm assembles into an ordered paracrystalline matrix. Plant Physiol 2001; 125: 1732-1742.
    • (2001) Plant Physiol , vol.125 , pp. 1732-1742
    • Stöger, E.1    Parker, M.2    Christou, P.3    Casey, R.4
  • 96
    • 0034117707 scopus 로고    scopus 로고
    • Generation of transgenic wheat (Triticum aestivum L.) for constitutive accumulation of an Aspergillus phytase
    • Brinch-Pedersen H, Olesen A, Rasmussen SK, Holm PB. Generation of transgenic wheat (Triticum aestivum L.) for constitutive accumulation of an Aspergillus phytase. Mol Breeding 2000; 6: 195-206.
    • (2000) Mol Breeding , vol.6 , pp. 195-206
    • Brinch-Pedersen, H.1    Olesen, A.2    Rasmussen, S.K.3    Holm, P.B.4
  • 97
    • 78650956114 scopus 로고    scopus 로고
    • Expression and recovery of biologically active recombinant Apolipoprotein AI(Milano) from transgenic safflower (Carthamus tinctorius) seeds
    • Nykiforuk CL, Shen Y, Murray EW, et al. Expression and recovery of biologically active recombinant Apolipoprotein AI(Milano) from transgenic safflower (Carthamus tinctorius) seeds. Plant Biotechnol J 2011; 9: 250-263.
    • (2011) Plant Biotechnol J , vol.9 , pp. 250-263
    • Nykiforuk, C.L.1    Shen, Y.2    Murray, E.W.3
  • 98
    • 0031391390 scopus 로고    scopus 로고
    • Molecular farming in plants: Oilseeds as vehicles for the production of pharmaceutical proteins
    • Boothe JG, Saponja JA, Parmenter DL. Molecular farming in plants: Oilseeds as vehicles for the production of pharmaceutical proteins. Drug Develop Res 1997; 42: 172-181.
    • (1997) Drug Develop Res , vol.42 , pp. 172-181
    • Boothe, J.G.1    Saponja, J.A.2    Parmenter, D.L.3
  • 100
    • 28444466635 scopus 로고    scopus 로고
    • Transgenic expression of bean alphaamylase inhibitor in peas results in altered structure and immunogenicity
    • Prescott VE, Campbell PM, Moore A, et al. Transgenic expression of bean alphaamylase inhibitor in peas results in altered structure and immunogenicity. J Agr Food Chem 2005; 53: 9023-9030.
    • (2005) J Agr Food Chem , vol.53 , pp. 9023-9030
    • Prescott, V.E.1    Campbell, P.M.2    Moore, A.3
  • 101
    • 76649092621 scopus 로고    scopus 로고
    • Barley as a green factory for the production of functional Flt3 ligand
    • Erlendsson LS, Muench MO, Hellman U, et al. Barley as a green factory for the production of functional Flt3 ligand. Biotechnology J 2010; 5: 163-171.
    • (2010) Biotechnology J , vol.5 , pp. 163-171
    • Erlendsson, L.S.1    Muench, M.O.2    Hellman, U.3
  • 102
    • 51649090968 scopus 로고    scopus 로고
    • Production of recombinant human lactoferrin from transgenic plants
    • Stefanova G, Vlahova M, Atanassov A. Production of recombinant human lactoferrin from transgenic plants. Biol Plantarum 2008; 52: 423-428.
    • (2008) Biol Plantarum , vol.52 , pp. 423-428
    • Stefanova, G.1    Vlahova, M.2    Atanassov, A.3
  • 103
    • 84881354831 scopus 로고    scopus 로고
    • accessed online 1 September, Available at
    • TAIR (The Arabidopsis Information Resource) [accessed online 1 September 2012]; Available at http://www.arabidopsis.org/
    • (2012) TAIR (The Arabidopsis Information Resource)
  • 104
    • 0034928217 scopus 로고    scopus 로고
    • Growth stage-based phenotypic analysis of Arabidopsis: A model for high throughput functional genomics in plants
    • Boyes DC, Zayed AM, Ascenzi R, McCaskill AJ, Hoffman NE, Davis KR, Gorlach J. Growth stage-based phenotypic analysis of Arabidopsis: a model for high throughput functional genomics in plants. Plant Cell 2001; 13: 1499-1510.
    • (2001) Plant Cell , vol.13 , pp. 1499-1510
    • Boyes, D.C.1    Zayed, A.M.2    Ascenzi, R.3    McCaskill, A.J.4    Hoffman, N.E.5    Davis, K.R.6    Gorlach, J.7
  • 105
    • 33645758314 scopus 로고    scopus 로고
    • Application of two dimensional gel electrophoresis to interrogate alterations in the proteome of genetically modified crops. 2. Assessing natural variability
    • Ruebelt MC, Lipp M, Reynolds TL, Astwood JD, Engel KH, Jany KD. Application of two dimensional gel electrophoresis to interrogate alterations in the proteome of genetically modified crops. 2. Assessing natural variability. J Agric Food Chem 2006; 54: 2162-2168.
    • (2006) J Agric Food Chem , vol.54 , pp. 2162-2168
    • Ruebelt, M.C.1    Lipp, M.2    Reynolds, T.L.3    Astwood, J.D.4    Engel, K.H.5    Jany, K.D.6
  • 106
    • 81555201437 scopus 로고    scopus 로고
    • Exploiting the natural variation of Arabidopsis thaliana for the seed-specific production of proteins
    • Demeyer R, De Loose M, Van Bockstaele E, Van Droogenbroeck B. Exploiting the natural variation of Arabidopsis thaliana for the seed-specific production of proteins. Euphytica 2012; 183: 83-93.
    • (2012) Euphytica , vol.183 , pp. 83-93
    • Demeyer, R.1    de Loose, M.2    van Bockstaele, E.3    van Droogenbroeck, B.4
  • 108
    • 39749140229 scopus 로고    scopus 로고
    • An ideal production platform for effective and safe molecular pharming
    • Ramessar K, Sabalza M, Capell T, Christou P. An ideal production platform for effective and safe molecular pharming. Plant Science 2008; 174: 409-419.
    • (2008) Plant Science , vol.174 , pp. 409-419
    • Ramessar, K.1    Sabalza, M.2    Capell, T.3    Christou, P.4
  • 109
    • 0002471546 scopus 로고
    • Corn: Chemistry and Technology
    • S.A. Watson, P.T. Ramstad (Eds.), Cereal Chemists, St. Paul, MN
    • Watson SA. in: S.A. Watson, P.T. Ramstad (Eds.) Corn: Chemistry and Technology. Am. Assoc. Cereal Chemists, St. Paul, MN; 1987: 53-82.
    • (1987) Am. Assoc , pp. 53-82
    • Watson, S.A.1
  • 110
    • 0033758021 scopus 로고    scopus 로고
    • Transgenic plants as factories for biopharmaceuticals
    • Giddings G, Allison G, Brooks D, Carter A. Transgenic plants as factories for biopharmaceuticals. Nat Biotechnol 2000; 18: 1151-1155.
    • (2000) Nat Biotechnol , vol.18 , pp. 1151-1155
    • Giddings, G.1    Allison, G.2    Brooks, D.3    Carter, A.4
  • 111
    • 0011977387 scopus 로고    scopus 로고
    • Commercial production of b-glucuronidase (GUS): A model system for the production of proteins in plants
    • Witcher DR, Hood EE, Peterson D, et al. Commercial production of b-glucuronidase (GUS): a model system for the production of proteins in plants. Mol Breed 1998; 4: 301-412.
    • (1998) Mol Breed , vol.4 , pp. 301-412
    • Witcher, D.R.1    Hood, E.E.2    Peterson, D.3
  • 113
    • 77957181613 scopus 로고
    • The site of synthesis and accumulation of rice storage proteins
    • Yamagata H, Tanaka K. The site of synthesis and accumulation of rice storage proteins. Plant Cell Physiol 1986; 27: 135-145.
    • (1986) Plant Cell Physiol , vol.27 , pp. 135-145
    • Yamagata, H.1    Tanaka, K.2
  • 114
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • Müntz K. Deposition of storage proteins. Plant Mol Biol 1998; 38: 77-99.
    • (1998) Plant Mol Biol , vol.38 , pp. 77-99
    • Müntz, K.1
  • 115
    • 0035949562 scopus 로고    scopus 로고
    • Expression of the REB transcriptional activator in rice grains improves the yield of recombinant proteins whose genes are controlled by a Reb-responsive promoter
    • Yang D, Wu L, Hwang YS, Chen L, Huang N. Expression of the REB transcriptional activator in rice grains improves the yield of recombinant proteins whose genes are controlled by a Reb-responsive promoter. Proc Natl Acad Sci USA (PNAS) 2001; 98: 11438-11443.
    • (2001) Proc Natl Acad Sci USA (PNAS) , vol.98 , pp. 11438-11443
    • Yang, D.1    Wu, L.2    Hwang, Y.S.3    Chen, L.4    Huang, N.5
  • 116
    • 27144463587 scopus 로고    scopus 로고
    • Improvement of human lysozyme expression in transgenic rice grain by combining wheat (Triticum aestivum) puroindoline b and rice (Oryza sativa) Gt1 promoters and signal peptides
    • Hennegan K, Yang D, Nguyen D, et al. Improvement of human lysozyme expression in transgenic rice grain by combining wheat (Triticum aestivum) puroindoline b and rice (Oryza sativa) Gt1 promoters and signal peptides. Transgenic Res 2005; 14: 583-592.
    • (2005) Transgenic Res , vol.14 , pp. 583-592
    • Hennegan, K.1    Yang, D.2    Nguyen, D.3
  • 117
    • 70349778691 scopus 로고    scopus 로고
    • Plant seeds as bioreactors for recombinant protein production
    • Lau OS, Sun SSM. Plant seeds as bioreactors for recombinant protein production. Biotechnol Adv 2009; 27: 015-022.
    • (2009) Biotechnol Adv , vol.27 , pp. 015-022
    • Lau, O.S.1    Sun, S.S.M.2
  • 118
    • 77954018329 scopus 로고    scopus 로고
    • Success stories in molecular farming a brief overview
    • Faye L, Gomord V. Success stories in molecular farming a brief overview. Plant Biotechnol J 2010; 8: 525-528.
    • (2010) Plant Biotechnol J , vol.8 , pp. 525-528
    • Faye, L.1    Gomord, V.2
  • 119
    • 0034903585 scopus 로고    scopus 로고
    • Processing and localization of bovine bcasein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette
    • Philip R, Darnowski DW, Maughan PJ, Vodkin LO. Processing and localization of bovine bcasein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette. Plant Science 2001; 161: 323-335.
    • (2001) Plant Science , vol.161 , pp. 323-335
    • Philip, R.1    Darnowski, D.W.2    Maughan, P.J.3    Vodkin, L.O.4
  • 120
    • 33846210581 scopus 로고    scopus 로고
    • Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine
    • Moravec T, Schmidt MA, Herman EM, Woodford-Thomas T. Production of Escherichia coli heat labile toxin (LT) B subunit in soybean seed and analysis of its immunogenicity as an oral vaccine. Vaccine 2007; 25: 1647-1657.
    • (2007) Vaccine , vol.25 , pp. 1647-1657
    • Moravec, T.1    Schmidt, M.A.2    Herman, E.M.3    Woodford-Thomas, T.4
  • 121
    • 79960467709 scopus 로고    scopus 로고
    • Accumulation of functional recombinant human coagulation factor IX in transgenic soybean seeds
    • Cunha NB, Murad A, Ramos GL, et al. Accumulation of functional recombinant human coagulation factor IX in transgenic soybean seeds. Transgenic Res 2011; 20: 841-855.
    • (2011) Transgenic Res , vol.20 , pp. 841-855
    • Cunha, N.B.1    Murad, A.2    Ramos, G.L.3
  • 122
    • 0035034943 scopus 로고    scopus 로고
    • High-level expression of a single-chain Fv fragment (scFv) antibody in transgenic pea seeds
    • Saalbach I, Giersberg M, Conrad U. High-level expression of a single-chain Fv fragment (scFv) antibody in transgenic pea seeds. J Plant Physiol 2001; 158: 529-533.
    • (2001) J Plant Physiol , vol.158 , pp. 529-533
    • Saalbach, I.1    Giersberg, M.2    Conrad, U.3
  • 123
    • 84864046231 scopus 로고    scopus 로고
    • Feasibility of Pisum sativum as an expression system for pharmaceuticals
    • DOI 10.1007/s11248-011-9573-z
    • Mikschofsky H, Broer I. Feasibility of Pisum sativum as an expression system for pharmaceuticals. Transgenic Res 2011; DOI 10.1007/s11248-011-9573-z.
    • (2011) Transgenic Res
    • Mikschofsky, H.1    Broer, I.2
  • 124
    • 77954003389 scopus 로고    scopus 로고
    • Seed-based expression systems for plant molecular farming
    • Boothe J, Nykiforuk C, Shen Y, et al. Seed-based expression systems for plant molecular farming. Plant Biotechnol J 2010; 8: 588-606.
    • (2010) Plant Biotechnol J , vol.8 , pp. 588-606
    • Boothe, J.1    Nykiforuk, C.2    Shen, Y.3
  • 125
    • 0028859854 scopus 로고
    • Plant seed oil-bodies as carriers for foreign proteins
    • Van Rooijen GJH, Moloney MM. Plant seed oil-bodies as carriers for foreign proteins. Nat Biotechnol 1995; 13: 72-77.
    • (1995) Nat Biotechnol , vol.13 , pp. 72-77
    • van Rooijen, G.J.H.1    Moloney, M.M.2
  • 126
    • 79953234180 scopus 로고    scopus 로고
    • Plant-made pharmaceuticals: Leading products and production platforms
    • Paul M, Ma JKC. Plant-made pharmaceuticals: Leading products and production platforms. Biotechnol Appl Biochem 2011; 58: 58-67.
    • (2011) Biotechnol Appl Biochem , vol.58 , pp. 58-67
    • Paul, M.1    Ma, J.K.C.2
  • 127
    • 48849103075 scopus 로고    scopus 로고
    • Evolution of a regulatory framework for pharmaceuticals derived from genetically modified plants
    • Spök A, Twyman RM, Fischer R, Ma JKC, Sparrow PAC. Evolution of a regulatory framework for pharmaceuticals derived from genetically modified plants. Trends Biotechnol 2008; 26: 506-517.
    • (2008) Trends Biotechnol , vol.26 , pp. 506-517
    • Spök, A.1    Twyman, R.M.2    Fischer, R.3    Ma, J.K.C.4    Sparrow, P.A.C.5
  • 128
    • 84881352694 scopus 로고    scopus 로고
    • Accessed online 1 September 2012, Available at
    • SemBioSys Genetics Inc. 2010; [Accessed online 1 September 2012] Available at http://micro.newswire.ca/36078-0.html?Start=15
    • (2010) SemBioSys Genetics Inc
  • 129
    • 84856960863 scopus 로고    scopus 로고
    • Recovery and purification of plant-made recombinant proteins
    • Wilken LR, Nikolov ZL. Recovery and purification of plant-made recombinant proteins. Biotechnol Adv 2012; 30: 419-433.
    • (2012) Biotechnol Adv , vol.30 , pp. 419-433
    • Wilken, L.R.1    Nikolov, Z.L.2
  • 130
    • 0036305744 scopus 로고    scopus 로고
    • Edible plant vaccines: Applications for prophylactic and therapeutic molecular medicine
    • Mason HS, Warzecha H, Mor T, Arntzen CJ. Edible plant vaccines: applications for prophylactic and therapeutic molecular medicine. Trends Mol Med 2002; 8: 324-329.
    • (2002) Trends Mol Med , vol.8 , pp. 324-329
    • Mason, H.S.1    Warzecha, H.2    Mor, T.3    Arntzen, C.J.4
  • 131
    • 28444454488 scopus 로고    scopus 로고
    • A rice-based edible vaccine expressing multiple T cell epitopes induces oral tolerance for inhibition of Th2-mediated IgE responses
    • Takagi H, Hiroi T, Yang L, et al. A rice-based edible vaccine expressing multiple T cell epitopes induces oral tolerance for inhibition of Th2-mediated IgE responses. Proc Natl Acad Sci USA (PNAS) 2005; 102: 17525-17530.
    • (2005) Proc Natl Acad Sci USA (PNAS) , vol.102 , pp. 17525-17530
    • Takagi, H.1    Hiroi, T.2    Yang, L.3
  • 133
    • 65549099593 scopus 로고    scopus 로고
    • Scaleable manufacture of HIV-1 entry inhibitor griffithsin and validation of its safety and efficacy as a topical microbicide component
    • O'Keefe BR, Vojdani F, Buffa V, et al. Scaleable manufacture of HIV-1 entry inhibitor griffithsin and validation of its safety and efficacy as a topical microbicide component. Proc Natl Acad Sci USA (PNAS) 2009; 106: 6099-6104.
    • (2009) Proc Natl Acad Sci USA (PNAS) , vol.106 , pp. 6099-6104
    • O'Keefe, B.R.1    Vojdani, F.2    Buffa, V.3
  • 134
    • 78649834556 scopus 로고    scopus 로고
    • High-value products from transgenic maize
    • Naqvi S, Ramessar K, Farré G, et al. High-value products from transgenic maize. Biotechnol Adv 2011; 29: 40-53.
    • (2011) Biotechnol Adv , vol.29 , pp. 40-53
    • Naqvi, S.1    Ramessar, K.2    Farré, G.3
  • 138
    • 84881332519 scopus 로고    scopus 로고
    • Transgenic multivitamin corn through biofortification of endosperm with three vitamins representing three distinct metabolic pathways
    • Naqvi S, Zhu C, Farre G, et al. Transgenic multivitamin corn through biofortification of endosperm with three vitamins representing three distinct metabolic pathways. Proc Natl Acad Sci USA (PNAS) 2009; 108: 1-6.
    • (2009) Proc Natl Acad Sci USA (PNAS) , vol.108 , pp. 1-6
    • Naqvi, S.1    Zhu, C.2    Farre, G.3
  • 139
    • 57449119110 scopus 로고    scopus 로고
    • Combinatorial Genetic Transformation of Cereals and the Creation of Metabolic Libraries for the Carotenoid Pathway
    • Zhu C, Naqvi S, Breitenbach J, Sandman G, Christou P, Capell T. Combinatorial Genetic Transformation of Cereals and the Creation of Metabolic Libraries for the Carotenoid Pathway. Proc Natl Acad Sci USA (PNAS) 2008; 105: 18232-18237.
    • (2008) Proc Natl Acad Sci USA (PNAS) , vol.105 , pp. 18232-18237
    • Zhu, C.1    Naqvi, S.2    Breitenbach, J.3    Sandman, G.4    Christou, P.5    Capell, T.6
  • 140
    • 77249152189 scopus 로고    scopus 로고
    • Expression and purification of pharmaceutical proteins in plants
    • Chen Q. Expression and purification of pharmaceutical proteins in plants. Biol Engineering 2008; 2: 291-321.
    • (2008) Biol Engineering , vol.2 , pp. 291-321
    • Chen, Q.1
  • 141
    • 0033779268 scopus 로고    scopus 로고
    • Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus
    • Schillberg S, Zimmermann S, Findlay K, Fischer R. Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus. Mol Breed 2000; 6: 317-326.
    • (2000) Mol Breed , vol.6 , pp. 317-326
    • Schillberg, S.1    Zimmermann, S.2    Findlay, K.3    Fischer, R.4
  • 142
    • 77950088155 scopus 로고    scopus 로고
    • Purification of recombinant plant-made proteins from corn extracts by ultrafiltration
    • Aspelund MT, Glatz CE. Purification of recombinant plant-made proteins from corn extracts by ultrafiltration. J Membr Sci 2010; 353: 103-110.
    • (2010) J Membr Sci , vol.353 , pp. 103-110
    • Aspelund, M.T.1    Glatz, C.E.2
  • 143
    • 79954426300 scopus 로고    scopus 로고
    • Nutritionally enhanced crops and food security: Scientific achievements versus political expediency
    • Farre G, Twyman RM, Zhu C, Capell T, Christou P. Nutritionally enhanced crops and food security: scientific achievements versus political expediency. Curr Opi Biotechnol 2011; 22: 245-251.
    • (2011) Curr Opi Biotechnol , vol.22 , pp. 245-251
    • Farre, G.1    Twyman, R.M.2    Zhu, C.3    Capell, T.4    Christou, P.5
  • 145
    • 76349083333 scopus 로고    scopus 로고
    • Going to ridiculous lengths-European coexistence regulations for GM crops
    • Ramessar K, Capell T, Twyman RM, Christou P. Going to ridiculous lengths-European coexistence regulations for GM crops. Nat Biotechnol 2010; 28: 133-136.
    • (2010) Nat Biotechnol , vol.28 , pp. 133-136
    • Ramessar, K.1    Capell, T.2    Twyman, R.M.3    Christou, P.4
  • 148
    • 56649099066 scopus 로고    scopus 로고
    • Calling the tunes on transgenic crops: The case for regulatory harmony
    • Ramessar K, Capell T, Twyman RM, Quemada H, Christou P. Calling the tunes on transgenic crops: the case for regulatory harmony. Mol Breed 2009; 23: 99-112.
    • (2009) Mol Breed , vol.23 , pp. 99-112
    • Ramessar, K.1    Capell, T.2    Twyman, R.M.3    Quemada, H.4    Christou, P.5


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