메뉴 건너뛰기




Volumn 483, Issue , 2009, Pages 1-23

From neanderthal to nanobiotech: From plant potions to pharming with plant factories

Author keywords

Glycosylation; Molecular farming; Plant made pharmaceutical; Recombinant protein; Therapeutic protein; Transgenic plant

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 60549108896     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-407-0_1     Document Type: Review
Times cited : (21)

References (93)
  • 1
    • 33749860977 scopus 로고    scopus 로고
    • Posttranslational modifications in the context of therapeutic proteins
    • Walsh, G., and Jefferis, R. (2006) Posttranslational modifications in the context of therapeutic proteins. Nat. Biotechnol. 24, 1241-1252.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 2
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord, V., and Faye, L. (2004) Posttranslational modification of therapeutic proteins in plants. Curr. Opin. Plant Biol. 7, 171-181.
    • (2004) Curr. Opin. Plant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 5
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Cafferkey, R., and 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
  • 9
    • 26944477789 scopus 로고    scopus 로고
    • Biopharmaceutical production in plants: Problems, solutions and opportunities
    • Gomord, V., Chamberlain, P., Jefferis, R., and Faye, L. (2005) Biopharmaceutical production in plants: problems, solutions and opportunities. Trends Biotechnol. 23, 559-565.
    • (2005) Trends Biotechnol , vol.23 , pp. 559-565
    • Gomord, V.1    Chamberlain, P.2    Jefferis, R.3    Faye, L.4
  • 13
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield, S.J. (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol. J. 5, 2-15.
    • (2007) Plant Biotechnol. J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 15
    • 0029866675 scopus 로고    scopus 로고
    • Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
    • Jensen, L.G., Olsen, O., Kops, O., Wolf, N., Thomsen, K.K., and von Wettstein, D. (1996) Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination. Proc. Natl. Acad. Sci. U. S. A. 93, 3487-3491.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 3487-3491
    • Jensen, L.G.1    Olsen, O.2    Kops, O.3    Wolf, N.4    Thomsen, K.K.5    von Wettstein, D.6
  • 17
    • 27644583910 scopus 로고    scopus 로고
    • High-level production of yeast (Schwanniomyces occidentalis) phytase in transgenic rice plants by a combination of signal sequence and codon modification of the phytase gene
    • Hamada, A., Yamaguchi, K.-I., Ohnishi, N., Harada, M., Nikumaru, S., and Honda, H. (2005) High-level production of yeast (Schwanniomyces occidentalis) phytase in transgenic rice plants by a combination of signal sequence and codon modification of the phytase gene. Plant Biotechnol. J. 3, 43-55.
    • (2005) Plant Biotechnol. J , vol.3 , pp. 43-55
    • Hamada, A.1    Yamaguchi, K.-I.2    Ohnishi, N.3    Harada, M.4    Nikumaru, S.5    Honda, H.6
  • 18
    • 0033615491 scopus 로고    scopus 로고
    • A species of small antisense RNA in posttranscriptional gene silencing in plants
    • Hamilton, A.J., and Baulcombe, D.C. (1999). A species of small antisense RNA in posttranscriptional gene silencing in plants. Science 286, 950-952.
    • (1999) Science , vol.286 , pp. 950-952
    • Hamilton, A.J.1    Baulcombe, D.C.2
  • 19
    • 14344252157 scopus 로고    scopus 로고
    • Induction and suppression of RNA silencing: Insights from viral infections
    • Voinnet, O. (2005) Induction and suppression of RNA silencing: insights from viral infections. Nat. Rev. Genet. 6, 206-220.
    • (2005) Nat. Rev. Genet , vol.6 , pp. 206-220
    • Voinnet, O.1
  • 20
    • 0029347008 scopus 로고
    • Identification of tomato bushy stunt virus host-specific symptom determinants by expression of individual genes from a potato virus X vector
    • Scholthof, H.B., Scholthof, K.B., and Jackson, A.O. (1995) Identification of tomato bushy stunt virus host-specific symptom determinants by expression of individual genes from a potato virus X vector. Plant Cell 7, 1157-1172.
    • (1995) Plant Cell , vol.7 , pp. 1157-1172
    • Scholthof, H.B.1    Scholthof, K.B.2    Jackson, A.O.3
  • 21
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet, O., Rivas, S., Mestre, P., and Baulcombe, D. (2003) An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant J. 33, 949-956.
    • (2003) Plant J , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 22
    • 0033598840 scopus 로고    scopus 로고
    • Suppression of gene silencing: A general strategy used by diverse DNA and RNA viruses of plants
    • Voinnet, O., Pinto, Y.M., and Baulcombe, D.C. (1999) Suppression of gene silencing: a general strategy used by diverse DNA and RNA viruses of plants. Proc. Natl. Acad. Sci. U. S. A. 96, 14147-14152.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 14147-14152
    • Voinnet, O.1    Pinto, Y.M.2    Baulcombe, D.C.3
  • 23
    • 7744233197 scopus 로고    scopus 로고
    • Biopharmaceuticals derived from genetically modified plants
    • Goldstein, D.A., and Thomas, J.A. (2004) Biopharmaceuticals derived from genetically modified plants. Q. J. Med. 97, 705-716.
    • (2004) Q. J. Med , vol.97 , pp. 705-716
    • Goldstein, D.A.1    Thomas, J.A.2
  • 24
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • Hellwig, S., Drossard, J., Twyman, R.M., and Fischer, R. (2004) Plant cell cultures for the production of recombinant proteins. Nat. Biotechnol. 22, 1415-1422.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 27
    • 60549117785 scopus 로고    scopus 로고
    • A case study for plant-made pharmaceuticals comparing different plant expression and production systems
    • This issue
    • Vancanneyt, G., Dubald, M., Schröder, W., Peters, J., and Botterman, J. (2008) A case study for plant-made pharmaceuticals comparing different plant expression and production systems. This issue.
    • (2008)
    • Vancanneyt, G.1    Dubald, M.2    Schröder, W.3    Peters, J.4    Botterman, J.5
  • 28
    • 7744233197 scopus 로고    scopus 로고
    • Biopharmaceuticals derived from genetically modified plants
    • Goldstein, D.A., and Thomas, J.A. (2004) Biopharmaceuticals derived from genetically modified plants. Q. J. Med. 97, 705-716.
    • (2004) Q. J. Med , vol.97 , pp. 705-716
    • Goldstein, D.A.1    Thomas, J.A.2
  • 29
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield, S.J. (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol. J. 5, 2-15.
    • (2007) Plant Biotechnol. J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 31
    • 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., and Fiedler, U. (1998) 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, 101-109.
    • (1998) Plant Mol. Biol , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 32
    • 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., Craig, S., Schroeder, H.E., Spencer, D., and Higgins, T.J. (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.2    Craig, S.3    Schroeder, H.E.4    Spencer, D.5    Higgins, T.J.6
  • 33
    • 24144490427 scopus 로고    scopus 로고
    • Recombinant pharmaceuticals from plants: The plant endomembrane system as bioreactor
    • Vitale, A., and Pedrazzini, E. (2005) Recombinant pharmaceuticals from plants: the plant endomembrane system as bioreactor. Mol. Interv. 5, 216-225.
    • (2005) Mol. Interv , vol.5 , pp. 216-225
    • Vitale, A.1    Pedrazzini, E.2
  • 34
    • 16544390244 scopus 로고    scopus 로고
    • Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm
    • Arcalis, E., Marcel, S., Altmann, F., Kolarich, D., Drakakaki, G., Fischer, R., Christou, P., and Stoger, E. (2004) Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm. Plant Physiol. 136, 3457-3466.
    • (2004) Plant Physiol , vol.136 , pp. 3457-3466
    • Arcalis, E.1    Marcel, S.2    Altmann, F.3    Kolarich, D.4    Drakakaki, G.5    Fischer, R.6    Christou, P.7    Stoger, E.8
  • 36
    • 60549089655 scopus 로고    scopus 로고
    • Protein body induction: A new tool to produce and recover recombinant proteins in plants
    • This issue
    • Torrent, M., Llop, I., and Ludevid, M.D. (2008) Protein body induction: a new tool to produce and recover recombinant proteins in plants. This issue
    • (2008)
    • Torrent, M.1    Llop, I.2    Ludevid, M.D.3
  • 37
    • 0029584041 scopus 로고
    • Structural requirements of oleosin domains for subcellular targeting to the oil body, Chapter 11 in this book
    • van Rooijen, G.J., and Moloney, M.M. (1995) Structural requirements of oleosin domains for subcellular targeting to the oil body, Chapter 11 in this book. Plant Physiol. 109, 1353-1361.
    • (1995) Plant Physiol , vol.109 , pp. 1353-1361
    • van Rooijen, G.J.1    Moloney, M.M.2
  • 38
    • 33645309590 scopus 로고    scopus 로고
    • Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds
    • Nykiforuk, C.L., Boothe, J.G., Murray, E.W., Keon, R.G., Goren, H.J., Markley, N.A., and Moloney, M.M. (2006) Transgenic expression and recovery of biologically active recombinant human insulin from Arabidopsis thaliana seeds. Plant Biotechnol. J. 4, 77-86.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 77-86
    • Nykiforuk, C.L.1    Boothe, J.G.2    Murray, E.W.3    Keon, R.G.4    Goren, H.J.5    Markley, N.A.6    Moloney, M.M.7
  • 39
    • 0036535792 scopus 로고    scopus 로고
    • Multigene engineering: Dawn of an exciting new era in biotechnology
    • Daniell, H., and Dhingra, A. (2002) Multigene engineering: dawn of an exciting new era in biotechnology. Curr. Opin. Biotechnol. 13, 136-141.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 136-141
    • Daniell, H.1    Dhingra, A.2
  • 40
    • 0035162968 scopus 로고    scopus 로고
    • Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to formation of insecticidal crystals
    • De Cosa, B., Moar, W., Lee, S.B., Miller, M., and Daniell, H. (2001) Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to formation of insecticidal crystals. Nat. Biotechnol. 19, 71-74.
    • (2001) Nat. Biotechnol , vol.19 , pp. 71-74
    • De Cosa, B.1    Moar, W.2    Lee, S.B.3    Miller, M.4    Daniell, H.5
  • 41
    • 60549114606 scopus 로고    scopus 로고
    • Chloroplast-derived vaccine antigens and biopharmaceuticals: Protocols for expression, purification or oral delivery and functional evaluation
    • This issue
    • Singh, N.D., Ding, Y., and Daniell, H. (2008) Chloroplast-derived vaccine antigens and biopharmaceuticals: protocols for expression, purification or oral delivery and functional evaluation. This issue
    • (2008)
    • Singh, N.D.1    Ding, Y.2    Daniell, H.3
  • 43
  • 44
    • 0035212386 scopus 로고    scopus 로고
    • Medical molecular farming: Production of antibodies, biopharmaceuticals and edible vaccines in plants
    • Daniell, H., Streatfield, S.J., and Wycoff, K. (2001) Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci. 6, 219-226.
    • (2001) Trends Plant Sci , vol.6 , pp. 219-226
    • Daniell, H.1    Streatfield, S.J.2    Wycoff, K.3
  • 46
    • 33645520500 scopus 로고    scopus 로고
    • Novel pathway for glycoprotein import into chloroplasts
    • Faye, L., and Daniell, H. (2006) Novel pathway for glycoprotein import into chloroplasts. Plant Biotechnol. J. 4, 275-279.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 275-279
    • Faye, L.1    Daniell, H.2
  • 48
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Michaud, D. (1998) Gel electrophoresis of proteolytic enzymes. Anal. Chim. Acta 372, 173-185.
    • (1998) Anal. Chim. Acta , vol.372 , pp. 173-185
    • Michaud, D.1
  • 50
    • 0034129161 scopus 로고    scopus 로고
    • Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention
    • Pagny, S., Cabanes-Macheteau, M., Gillikin, J.W., Leborgne-Castel, N., Lerouge, P., Boston, R.S., Faye, L., and Gomord, V. (2000) Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention. Plant Cell 12, 739-756.
    • (2000) Plant Cell , vol.12 , pp. 739-756
    • Pagny, S.1    Cabanes-Macheteau, M.2    Gillikin, J.W.3    Leborgne-Castel, N.4    Lerouge, P.5    Boston, R.S.6    Faye, L.7    Gomord, V.8
  • 51
    • 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., and 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
  • 52
    • 60549092771 scopus 로고    scopus 로고
    • (XXXX) Companion protease inhibitors to protect recombinant proteins in transgenic plant extracts
    • This issue
    • Benchabane, M., Rivard, D., Girard, C., and Michaud, D. (XXXX) Companion protease inhibitors to protect recombinant proteins in transgenic plant extracts. This issue
    • Benchabane, M.1    Rivard, D.2    Girard, C.3    Michaud, D.4
  • 53
    • 33645503258 scopus 로고    scopus 로고
    • An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants
    • Rivard, D., Anguenot, R., Brunelle, F., Le, V.Q., Vézina, L.P., Trépanier, S., Michaud, D. (2006) An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants. Plant Biotechnol. J. 4, 359-368.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 359-368
    • Rivard, D.1    Anguenot, R.2    Brunelle, F.3    Le, V.Q.4    Vézina, L.P.5    Trépanier, S.6    Michaud, D.7
  • 54
    • 0037181489 scopus 로고    scopus 로고
    • Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant
    • Merle, C., Perret, S., Lacour, T., Jonval, V., Hudaverdian, S., Garrone, R., Ruggiero, F., and Theisen, M. (2002) Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant. FEBS Lett. 515, 114-118.
    • (2002) FEBS Lett , vol.515 , pp. 114-118
    • Merle, C.1    Perret, S.2    Lacour, T.3    Jonval, V.4    Hudaverdian, S.5    Garrone, R.6    Ruggiero, F.7    Theisen, M.8
  • 55
    • 34250346068 scopus 로고    scopus 로고
    • From planta to pharma with glycosylation in the toolbox
    • Saint-Jore-Dupas, C., Faye, L., and Gomord, V. (2007) From planta to pharma with glycosylation in the toolbox. Trends Biotechnol. 25, 317-323.
    • (2007) Trends Biotechnol , vol.25 , pp. 317-323
    • Saint-Jore-Dupas, C.1    Faye, L.2    Gomord, V.3
  • 56
    • 0019859015 scopus 로고
    • Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom
    • Aalberse, R.C., Koshte, V., and Clemens, J.G. (1981) Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom. J. Allergy Clin. Immunol. 68, 356-364.
    • (1981) J. Allergy Clin. Immunol , vol.68 , pp. 356-364
    • Aalberse, R.C.1    Koshte, V.2    Clemens, J.G.3
  • 57
    • 0022186574 scopus 로고
    • Characterization of N-linked oligosaccharides by affinoblotting with concanavalin A- peroxidase and treatment of the blots with glycosidases
    • Faye, L., and Chrispeels, M.J. (1985) Characterization of N-linked oligosaccharides by affinoblotting with concanavalin A- peroxidase and treatment of the blots with glycosidases. Anal. Biochem. 149, 218-224.
    • (1985) Anal. Biochem , vol.149 , pp. 218-224
    • Faye, L.1    Chrispeels, M.J.2
  • 58
    • 0019283013 scopus 로고
    • Cross-reactions between vegetable foods, pollen and bee venom due to IgE antibodies to a ubiquitous carbohydrate determinant
    • Aalberse, R.C., Koshte, V., and Clemens, J.G. (1981) Cross-reactions between vegetable foods, pollen and bee venom due to IgE antibodies to a ubiquitous carbohydrate determinant. Int. Arch. Allergy Appl. Immunol. 66, 259-260.
    • (1981) Int. Arch. Allergy Appl. Immunol , vol.66 , pp. 259-260
    • Aalberse, R.C.1    Koshte, V.2    Clemens, J.G.3
  • 59
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glycoepitopes, core alpha(1,3)-fucose and core xylose
    • Bardor, M., Faveeuw, C., Fitchette, A.C., Gilbert, D., Galas, L., Trottein, F., Faye, L., and Lerouge, P. (2003) Immunoreactivity in mammals of two typical plant glycoepitopes, core alpha(1,3)-fucose and core xylose. Glycobiology 13, 427-434.
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.C.3    Gilbert, D.4    Galas, L.5    Trottein, F.6    Faye, L.7    Lerouge, P.8
  • 60
    • 33645109820 scopus 로고    scopus 로고
    • Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice
    • Jin, C., Bencurova, M., Borth, N., Ferko, B., Jensen-Jarolim, E., Altmann, F., and Hantusch, B. (2006) Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. Glycobiology 16, 349-357.
    • (2006) Glycobiology , vol.16 , pp. 349-357
    • Jin, C.1    Bencurova, M.2    Borth, N.3    Ferko, B.4    Jensen-Jarolim, E.5    Altmann, F.6    Hantusch, B.7
  • 61
    • 33845621148 scopus 로고    scopus 로고
    • A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts
    • Nuttall, J., Ma, J.K., and Frigerio, L. (2005) A functional antibody lacking N-linked glycans is efficiently folded, assembled and secreted by tobacco mesophyll protoplasts. Plant Biotechnol. J. 3, 497-504.
    • (2005) Plant Biotechnol. J , vol.3 , pp. 497-504
    • Nuttall, J.1    Ma, J.K.2    Frigerio, L.3
  • 62
    • 5644303930 scopus 로고    scopus 로고
    • Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha(1,3)-fucose residues
    • Sriraman, R., Bardor, M., Sack, M., Vaquero, C., Faye, L., Fischer, R., Finnern, R., and Lerouge, P. (2004) Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha(1,3)-fucose residues. Plant Biotechnol. J. 2, 279-287.
    • (2004) Plant Biotechnol. J , vol.2 , pp. 279-287
    • Sriraman, R.1    Bardor, M.2    Sack, M.3    Vaquero, C.4    Faye, L.5    Fischer, R.6    Finnern, R.7    Lerouge, P.8
  • 63
    • 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, M.S., Lareu, F., Tran Dinh, O., Fitchette, A.-C., Circosta, A., Rumbo, M., Bardor, M., Carcamo, R., Gomord, V., and Beachy, R.N. (2006) 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. 4, 511-527.
    • (2006) Plant Biotechnol. J , vol.4 , pp. 511-527
    • Petruccelli, S.1    Otegui, M.S.2    Lareu, F.3    Tran Dinh, O.4    Fitchette, A.-C.5    Circosta, A.6    Rumbo, M.7    Bardor, M.8    Carcamo, R.9    Gomord, V.10    Beachy, R.N.11
  • 64
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser, R., Altmann, F., Mach, L., Glossl, J., and Steinkellner, H. (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett. 561, 132-136.
    • (2004) FEBS Lett , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    Mach, L.3    Glossl, J.4    Steinkellner, H.5
  • 67
    • 60549083580 scopus 로고    scopus 로고
    • Sourrouille, C. (2005) Inactivation de l'alpha (1,3)- fucosyltransférase et de la beta (1,2)-xylosyltransferase, en vue de la production de protéines recombinantes d'intérêt thérapeutique chez la luzerne (Université de Rouen), pp. 164.
    • Sourrouille, C. (2005) Inactivation de l'alpha (1,3)- fucosyltransférase et de la beta (1,2)-xylosyltransferase, en vue de la production de protéines recombinantes d'intérêt thérapeutique chez la luzerne (Université de Rouen), pp. 164.
  • 70
    • 0242500989 scopus 로고    scopus 로고
    • Plant cultured cells expressing human beta1,4- galactosyltransferase secrete glycoproteins with galactose-extended N-linked glycans
    • Misaki, R., Kimura, Y., Palacpac, N.Q., Yoshida, S., Fujiyama, K., and Seki, T. (2003) Plant cultured cells expressing human beta1,4- galactosyltransferase secrete glycoproteins with galactose-extended N-linked glycans. Glycobiology 13, 199-205.
    • (2003) Glycobiology , vol.13 , pp. 199-205
    • Misaki, R.1    Kimura, Y.2    Palacpac, N.Q.3    Yoshida, S.4    Fujiyama, K.5    Seki, T.6
  • 75
    • 33744484016 scopus 로고    scopus 로고
    • Sialic acid concentrations in plants are in the range of inadvertent contamination
    • Zeleny, R., Kolarich, D., Strasser, R., and Altmann, F. (2006) Sialic acid concentrations in plants are in the range of inadvertent contamination. Planta 224, 222-227.
    • (2006) Planta , vol.224 , pp. 222-227
    • Zeleny, R.1    Kolarich, D.2    Strasser, R.3    Altmann, F.4
  • 76
    • 0038544334 scopus 로고    scopus 로고
    • Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
    • Jarvis, D.L. (2003) Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production. Virology 310, 1-7.
    • (2003) Virology , vol.310 , pp. 1-7
    • Jarvis, D.L.1
  • 77
    • 0032191992 scopus 로고    scopus 로고
    • Targeting of active sialyltransferase to the plant Golgi apparatus
    • Wee, E.G., Sherrier, D.J., Prime, T.A., and Dupree, P. (1998) Targeting of active sialyltransferase to the plant Golgi apparatus. Plant Cell 10, 1759-1768.
    • (1998) Plant Cell , vol.10 , pp. 1759-1768
    • Wee, E.G.1    Sherrier, D.J.2    Prime, T.A.3    Dupree, P.4
  • 78
    • 29044433720 scopus 로고    scopus 로고
    • ExpressionofhumanCMP-N- acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell
    • Misaki, R., Fujiyama, K., and Seki, T. (2006) ExpressionofhumanCMP-N- acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell. Biochem. Biophys. Res. Commun. 339, 1184-1189.
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , pp. 1184-1189
    • Misaki, R.1    Fujiyama, K.2    Seki, T.3
  • 80
    • 60549105461 scopus 로고    scopus 로고
    • (XXXX) Glycosylation of antibody therapeutics: Optimisation for purpose
    • This issue
    • Jefferis, R. (XXXX) Glycosylation of antibody therapeutics: optimisation for purpose. This issue
    • Jefferis, R.1
  • 81
    • 0025884282 scopus 로고
    • Stable transformation of the moss Physcomitrella patens
    • Schaefer, D., Zryd, J.P., Knight, C.D., and Cove, D.J. (1991) Stable transformation of the moss Physcomitrella patens. Mol. Gen. Genet. 226, 418-424.
    • (1991) Mol. Gen. Genet , vol.226 , pp. 418-424
    • Schaefer, D.1    Zryd, J.P.2    Knight, C.D.3    Cove, D.J.4
  • 82
    • 0031170922 scopus 로고    scopus 로고
    • Efficient gene targeting in the moss Physcomitrella patens
    • Schaefer, D.G., and Zryd, J.P. (1997) Efficient gene targeting in the moss Physcomitrella patens. Plant J. 11, 1195-1206.
    • (1997) Plant J , vol.11 , pp. 1195-1206
    • Schaefer, D.G.1    Zryd, J.P.2
  • 83
    • 60549099831 scopus 로고    scopus 로고
    • (XXXX) Physcomitrella patens: A non-vascular plant for recombinant protein production
    • This issue
    • Lienard, D., and Nogué, F. (XXXX) Physcomitrella patens: a non-vascular plant for recombinant protein production. This issue.
    • Lienard, D.1    Nogué, F.2
  • 84
    • 27644576554 scopus 로고    scopus 로고
    • Enhanced recovery of a secreted recombinant human growth factor using stabilizing additives and by co-expression of human serum albumin in the moss Physcomitrella patens
    • Baur, A., Reski, R., and Gorr, G. (2005) Enhanced recovery of a secreted recombinant human growth factor using stabilizing additives and by co-expression of human serum albumin in the moss Physcomitrella patens. Plant Biotechnol. J. 3, 331-340.
    • (2005) Plant Biotechnol. J , vol.3 , pp. 331-340
    • Baur, A.1    Reski, R.2    Gorr, G.3
  • 85
    • 60549092180 scopus 로고    scopus 로고
    • Schaefer, D.G., Bisztray, G., and Zrÿd, J.-P. (1994) Genetic transformation of the moss Physcomitrella patens. In Plant protoplasts and genetic engineering, V, Y.P.S. Bajaj, ed. (Berlin, Heidelberg, New York: Springer Verlag), pp. 349-364.
    • Schaefer, D.G., Bisztray, G., and Zrÿd, J.-P. (1994) Genetic transformation of the moss Physcomitrella patens. In Plant protoplasts and genetic engineering, V, Y.P.S. Bajaj, ed. (Berlin, Heidelberg, New York: Springer Verlag), pp. 349-364.
  • 86
    • 9144237471 scopus 로고    scopus 로고
    • Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants
    • Vietor, R., Loutelier, B.C., Fitchette, A., Margerie, P., Gonneau, M., Faye, L., and Lerouge, P. (2003) Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants. Planta 218, 269-275.
    • (2003) Planta , vol.218 , pp. 269-275
    • Vietor, R.1    Loutelier, B.C.2    Fitchette, A.3    Margerie, P.4    Gonneau, M.5    Faye, L.6    Lerouge, P.7
  • 87
    • 1542321146 scopus 로고    scopus 로고
    • Prospects for molecular farming in the green alga Chlamydomonas
    • Franklin, S.E., and Mayfield, S.P. (2004) Prospects for molecular farming in the green alga Chlamydomonas. Curr. Opin. Plant Biol. 7, 159-165.
    • (2004) Curr. Opin. Plant Biol , vol.7 , pp. 159-165
    • Franklin, S.E.1    Mayfield, S.P.2
  • 90
    • 14744293443 scopus 로고    scopus 로고
    • Expression of human antibodies in eukaryotic micro-algae
    • Mayfield, S.P., and Franklin, S.E. (2005) Expression of human antibodies in eukaryotic micro-algae. Vaccine 23, 1828-1832.
    • (2005) Vaccine , vol.23 , pp. 1828-1832
    • Mayfield, S.P.1    Franklin, S.E.2
  • 91
    • 1542278229 scopus 로고    scopus 로고
    • Advantages of therapeutic protein production in the aquatic plant Lemna
    • Gasdaska, J.R., Spencer, D., and Dickey, L.F. (2003) Advantages of therapeutic protein production in the aquatic plant Lemna. Bioprocessing J. 3, 50-56.
    • (2003) Bioprocessing J , vol.3 , pp. 50-56
    • Gasdaska, J.R.1    Spencer, D.2    Dickey, L.F.3
  • 93
    • 0034959745 scopus 로고    scopus 로고
    • Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves
    • Elbers, I.J., Stoopen, G.M., Bakker, H., Stevens, L.H., Bardor, M., Molthoff, J.W., Jordi, W.J., Bosch, D., and Lommen, A. (2001) Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves. Plant Physiol. 126, 1314-1322.
    • (2001) Plant Physiol , vol.126 , pp. 1314-1322
    • Elbers, I.J.1    Stoopen, G.M.2    Bakker, H.3    Stevens, L.H.4    Bardor, M.5    Molthoff, J.W.6    Jordi, W.J.7    Bosch, D.8    Lommen, A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.