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Volumn 8, Issue 10, 2013, Pages 1203-1212

Efficient recovery of recombinant proteins from cereal endosperm is affected by interaction with endogenous storage proteins

Author keywords

Maize endosperm; Molecular farming; Plantibodies; Protein trafficking

Indexed keywords

COVALENT INTERACTIONS; INTERMOLECULAR DISULFIDE BRIDGES; MAIZE ENDOSPERM; MOLECULAR FARMING; PLANTIBODIES; PROTEIN ACCUMULATION; PROTEIN TRAFFICKING; SEED STORAGE PROTEINS;

EID: 84884988965     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201300068     Document Type: Article
Times cited : (5)

References (56)
  • 1
    • 0036901291 scopus 로고    scopus 로고
    • Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences.
    • De Jaeger, G., Scheffer, S., Jacobs, A., Zambre, M. et al., Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences. Nat. Biotechnol. 2002, 20, 1265-1268.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1265-1268
    • De Jaeger, G.1    Scheffer, S.2    Jacobs, A.3    Zambre, M.4
  • 2
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants.
    • Stoger, E., Ma, J. K., 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
    • Stoger, E.1    Ma, J.K.2    Fischer, R.3    Christou, P.4
  • 5
    • 25644440058 scopus 로고    scopus 로고
    • Plants as bioreactors: A comparative study suggests that Medicago truncatula is a promising production system.
    • Abranches, R., Marcel, S., Arcalis, E., Altmann, F. et al., Plants as bioreactors: A comparative study suggests that Medicago truncatula is a promising production system. J. Biotechnol. 2005, 120, 121-134.
    • (2005) J. Biotechnol. , vol.120 , pp. 121-134
    • Abranches, R.1    Marcel, S.2    Arcalis, E.3    Altmann, F.4
  • 8
    • 58449105435 scopus 로고    scopus 로고
    • The development of endosperm in grasses.
    • Sabelli, P. A., Larkins, B. A., The development of endosperm in grasses. Plant Physiol. 2009, 149, 14-26.
    • (2009) Plant Physiol. , vol.149 , pp. 14-26
    • Sabelli, P.A.1    Larkins, B.A.2
  • 9
    • 41649113980 scopus 로고    scopus 로고
    • Cost-effective production of a vaginal protein microbicide to prevent HIV transmission.
    • Ramessar, K., Rademacher, T., Sack, M., Stadlmann, J. 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    Stadlmann, J.4
  • 10
    • 39749140229 scopus 로고    scopus 로고
    • Maize plants: An ideal production platform for effective and safe molecular pharming.
    • Ramessar, K., Sabalza, M., Capell, T., Christou, P., Maize plants: An ideal production platform for effective and safe molecular pharming. Plant Sci. 2008, 174, 409-419.
    • (2008) Plant Sci. , vol.174 , pp. 409-419
    • Ramessar, K.1    Sabalza, M.2    Capell, T.3    Christou, P.4
  • 11
    • 76649092621 scopus 로고    scopus 로고
    • Barley as a green factory for the production of functional Flt3 ligand.
    • Erlendsson, L. S., Muench, M. O., Hellman, U., Hrafnkelsdottir, S. M. et al., Barley as a green factory for the production of functional Flt3 ligand. Biotechnol. J. 2010, 5, 163-171.
    • (2010) Biotechnol. J. , vol.5 , pp. 163-171
    • Erlendsson, L.S.1    Muench, M.O.2    Hellman, U.3    Hrafnkelsdottir, S.M.4
  • 12
    • 0002471546 scopus 로고
    • Structure and composition
    • in: Watson, S. A., Ramstad, P. T. (Ed.), Corn: Chemistry and Technology, American Association of Cereal Chemists, St. Paul, MN
    • Watson, S. A., Structure and composition, in: Watson, S. A., Ramstad, P. T. (Ed.), Corn: Chemistry and Technology, American Association of Cereal Chemists, St. Paul, MN 1987, pp. 53-82.
    • (1987) , pp. 53-82
    • Watson, S.A.1
  • 13
    • 78149482535 scopus 로고    scopus 로고
    • Cereal seed storage protein synthesis: Fundamental processes for recombinant protein production in cereal grains.
    • Kawakatsu, T., Takaiwa, F., Cereal seed storage protein synthesis: Fundamental processes for recombinant protein production in cereal grains. Plant Biotechnol. J. 2010, 8, 939-953.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 939-953
    • Kawakatsu, T.1    Takaiwa, F.2
  • 14
    • 0000217415 scopus 로고    scopus 로고
    • Commercial production of avidin from transgenic maize: Characterization of transformant, production, processing, extraction and purification.
    • Hood, E. E., Witcher, D. R., Maddock, S., Meyer, T. et al., Commercial production of avidin from transgenic maize: Characterization of transformant, production, processing, extraction and purification. Mol. Breeding 1997, 3, 291-306.
    • (1997) Mol. Breeding , vol.3 , pp. 291-306
    • Hood, E.E.1    Witcher, D.R.2    Maddock, S.3    Meyer, T.4
  • 15
    • 0011977387 scopus 로고    scopus 로고
    • Commercial production of beta-glucuronidase (GUS): A model system for the production of proteins in plants.
    • Witcher, D. R., Hood, E. E., Peterson, D., Bailey, M. et al., Commercial production of beta-glucuronidase (GUS): A model system for the production of proteins in plants. Mol. Breeding 1998, 4, 301-312.
    • (1998) Mol. Breeding , vol.4 , pp. 301-312
    • Witcher, D.R.1    Hood, E.E.2    Peterson, D.3    Bailey, M.4
  • 16
    • 84877740389 scopus 로고    scopus 로고
    • Heterologous expression of cellobiohydrolase II (Cel6A) in maize endosperm.
    • Devaiah, S. P., Requesens, D. V., Chang, Y. K., Hood, K. R. et al., Heterologous expression of cellobiohydrolase II (Cel6A) in maize endosperm. Transgenic Res. 2013, 22, 477-488.
    • (2013) Transgenic Res. , vol.22 , pp. 477-488
    • Devaiah, S.P.1    Requesens, D.V.2    Chang, Y.K.3    Hood, K.R.4
  • 17
  • 18
    • 20944446452 scopus 로고    scopus 로고
    • Delay of HIV-1 rebound after cessation of antiretroviral therapy through passive transfer of human neutralizing antibodies.
    • Trkola, A., Kuster, H., Rusert, P., Joos, B. et al., Delay of HIV-1 rebound after cessation of antiretroviral therapy through passive transfer of human neutralizing antibodies. Nat. Med. 2005, 11, 615-622.
    • (2005) Nat. Med. , vol.11 , pp. 615-622
    • Trkola, A.1    Kuster, H.2    Rusert, P.3    Joos, B.4
  • 19
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants.
    • Ma, J. K., Hiatt, A., Hein, M., Vine, N. D. et al., Generation and assembly of secretory antibodies in plants. Science 1995, 268, 716-719.
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.1    Hiatt, A.2    Hein, M.3    Vine, N.D.4
  • 20
    • 0033836692 scopus 로고    scopus 로고
    • Assembly, secretion, and vacuolar delivery of a hybrid immunoglobulin in plants.
    • Frigerio, L., Vine, N. D., Pedrazzini, E., Hein, M. B. et al., Assembly, secretion, and vacuolar delivery of a hybrid immunoglobulin in plants. Plant Physiol. 2000, 123, 1483-1494.
    • (2000) Plant Physiol. , vol.123 , pp. 1483-1494
    • Frigerio, L.1    Vine, N.D.2    Pedrazzini, E.3    Hein, M.B.4
  • 21
    • 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., Tuck, H. et al., A recombinant multimeric immunoglobulin expressed in rice shows assembly-dependent subcellular localization in endosperm cells. Plant Biotechno. J. 2005, 3, 115-127.
    • (2005) Plant Biotechno. J. , vol.3 , pp. 115-127
    • Nicholson, L.1    Gonzalez-Melendi, P.2    van Dolleweerd, C.3    Tuck, H.4
  • 22
    • 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., Altmann, F. et al., Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds. Proc. Natl. Acad. Sci. USA 2007, 104, 1430-1435.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1430-1435
    • Van Droogenbroeck, B.1    Cao, J.2    Stadlmann, J.3    Altmann, F.4
  • 23
    • 70449370975 scopus 로고    scopus 로고
    • Influence of elastin-like peptide fusions on the quantity and quality of a tobacco-derived human immunodeficiency virus-neutralizing antibody.
    • Floss, D. M., Sack, M., Arcalis, E., Stadlmann, J. et al., Influence of elastin-like peptide fusions on the quantity and quality of a tobacco-derived human immunodeficiency virus-neutralizing antibody. Plant Biotechnol. J. 2009, 7, 899-913.
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 899-913
    • Floss, D.M.1    Sack, M.2    Arcalis, E.3    Stadlmann, J.4
  • 24
    • 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., Stadlmann, J. 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    Stadlmann, J.4
  • 25
    • 0017103920 scopus 로고
    • Genetic-regulation of storage protein-content in maize endosperm.
    • Lee, K. H., Jones, R. A., Dalby, A., Tsai, C. Y., Genetic-regulation of storage protein-content in maize endosperm. Biochem. Genet. 1976, 14, 641-650.
    • (1976) Biochem. Genet. , vol.14 , pp. 641-650
    • Lee, K.H.1    Jones, R.A.2    Dalby, A.3    Tsai, C.Y.4
  • 26
    • 0024740149 scopus 로고
    • Changes in the zein composition of protein bodies during maize endosperm development.
    • Lending, C. R., Larkins, B. A., Changes in the zein composition of protein bodies during maize endosperm development. Plant Cell 1989, 1, 1011-1023.
    • (1989) Plant Cell , vol.1 , pp. 1011-1023
    • Lending, C.R.1    Larkins, B.A.2
  • 27
    • 0036214280 scopus 로고    scopus 로고
    • Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm.
    • Kim, C. S., Woo Ym, Y. M., Clore, A. M., Burnett, R. J. et al., Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm. Plant Cell 2002, 14, 655-672.
    • (2002) Plant Cell , vol.14 , pp. 655-672
    • Kim, C.S.1    Woo Ym, Y.M.2    Clore, A.M.3    Burnett, R.J.4
  • 28
    • 0028248853 scopus 로고
    • Two structural domains mediate two sequential events in [gamma]-zein targeting: Protein endoplasmic reticulum retention and protein body formation.
    • Geli, M. I., Torrent, M., Ludevid, D., Two structural domains mediate two sequential events in [gamma]-zein targeting: Protein endoplasmic reticulum retention and protein body formation. Plant Cell 1994, 6, 1911-1922.
    • (1994) Plant Cell , vol.6 , pp. 1911-1922
    • Geli, M.I.1    Torrent, M.2    Ludevid, D.3
  • 29
    • 16544387639 scopus 로고    scopus 로고
    • Zeolin. A new recombinant storage protein constructed using maize gamma-zein and bean phaseolin.
    • Mainieri, D., Rossi, M., Archinti, M., Bellucci, M. et al., Zeolin. A new recombinant storage protein constructed using maize gamma-zein and bean phaseolin. Plant Physiol. 2004, 136, 3447-3456.
    • (2004) Plant Physiol. , vol.136 , pp. 3447-3456
    • Mainieri, D.1    Rossi, M.2    Archinti, M.3    Bellucci, M.4
  • 30
    • 77953220245 scopus 로고    scopus 로고
    • The changing fate of a secretory glycoprotein in developing maize endosperm.
    • Arcalis, E., Stadlmann, J., Marcel, S., Drakakaki, G. et al., The changing fate of a secretory glycoprotein in developing maize endosperm. Plant Physiol. 2010, 153, 693-702.
    • (2010) Plant Physiol. , vol.153 , pp. 693-702
    • Arcalis, E.1    Stadlmann, J.2    Marcel, S.3    Drakakaki, G.4
  • 31
    • 0034764976 scopus 로고    scopus 로고
    • Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression.
    • Woo, Y. M., Hu, D. W., Larkins, B. A., Jung, R., Genomics analysis of genes expressed in maize endosperm identifies novel seed proteins and clarifies patterns of zein gene expression. Plant Cell 2001, 13, 2297-2317.
    • (2001) Plant Cell , vol.13 , pp. 2297-2317
    • Woo, Y.M.1    Hu, D.W.2    Larkins, B.A.3    Jung, R.4
  • 32
    • 0032824479 scopus 로고    scopus 로고
    • Accumulation of soybean glycinin and its assembly with the glutelins in rice.
    • Katsube, T., Kurisaka, N., Ogawa, M., Maruyama, N. et al., Accumulation of soybean glycinin and its assembly with the glutelins in rice. Plant physiology 1999, 120, 1063-1074.
    • (1999) Plant physiology , vol.120 , pp. 1063-1074
    • Katsube, T.1    Kurisaka, N.2    Ogawa, M.3    Maruyama, N.4
  • 33
    • 84858237223 scopus 로고    scopus 로고
    • Proteomic characterisation of endoplasmic reticulum-derived protein bodies in tobacco leaves.
    • Joseph, M., Ludevid, M. D., Torrent, M., Rofidal, V. et al., Proteomic characterisation of endoplasmic reticulum-derived protein bodies in tobacco leaves. BMC Plant Biol. 2012, 12, 36.
    • (2012) BMC Plant Biol. , vol.12 , pp. 36
    • Joseph, M.1    Ludevid, M.D.2    Torrent, M.3    Rofidal, V.4
  • 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. et al., Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm. Plant Physiol. 2004, 136, 3457-3466.
    • (2004) Plant Physiol. , vol.136 , pp. 3457-3466
    • Arcalis, E.1    Marcel, S.2    Altmann, F.3    Kolarich, D.4
  • 35
    • 33745646101 scopus 로고    scopus 로고
    • The intracellular fate of a recombinant protein is tissue dependent.
    • Drakakaki, G., Marcel, S., Arcalis, E., Altmann, F. et al., The intracellular fate of a recombinant protein is tissue dependent. Plant Physiol. 2006, 141, 578-586.
    • (2006) Plant Physiol. , vol.141 , pp. 578-586
    • Drakakaki, G.1    Marcel, S.2    Arcalis, E.3    Altmann, F.4
  • 36
    • 84861382637 scopus 로고    scopus 로고
    • Expression of hypoallergenic Der f 2 derivatives with altered intramolecular disulphide bonds induces the formation of novel ER-derived protein bodies in transgenic rice seeds.
    • Yang, L., Hirose, S., Suzuki, K., Hiroi, T., Takaiwa, F., Expression of hypoallergenic Der f 2 derivatives with altered intramolecular disulphide bonds induces the formation of novel ER-derived protein bodies in transgenic rice seeds. J. Exp. Bot. 2012, 63, 2947-2959.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2947-2959
    • Yang, L.1    Hirose, S.2    Suzuki, K.3    Hiroi, T.4    Takaiwa, F.5
  • 37
    • 84878884890 scopus 로고    scopus 로고
    • Transgenic rice seeds accumulating recombinant hypoallergenic birch pollen allergen bet v 1 generate giant protein bodies.
    • Wang, S., Takahashi, H., Kajiura, H., Kawakatsu, T. et al., Transgenic rice seeds accumulating recombinant hypoallergenic birch pollen allergen bet v 1 generate giant protein bodies. Plant Cell Physiol. 2013, 54, 914-933.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 914-933
    • Wang, S.1    Takahashi, H.2    Kajiura, H.3    Kawakatsu, T.4
  • 38
    • 84868528712 scopus 로고    scopus 로고
    • Recombinant protein yield in rice seed is enhanced by specific suppression of endogenous seed proteins at the same deposit site.
    • Yang, L., Hirose, S., Takahashi, H., Kawakatsu, T., Takaiwa, F., Recombinant protein yield in rice seed is enhanced by specific suppression of endogenous seed proteins at the same deposit site. Plant Biotechnol. J. 2012, 10, 1035-1045.
    • (2012) Plant Biotechnol. J. , vol.10 , pp. 1035-1045
    • Yang, L.1    Hirose, S.2    Takahashi, H.3    Kawakatsu, T.4    Takaiwa, F.5
  • 39
    • 0342748410 scopus 로고    scopus 로고
    • Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies.
    • Stoger, E., Vaquero, C., Torres, E., Sack, M. 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
    • Stoger, E.1    Vaquero, C.2    Torres, E.3    Sack, M.4
  • 40
    • 0035193739 scopus 로고    scopus 로고
    • Native and artificial reticuloplasmins co-accumulate in distinct domains of the endoplasmic reticulum and in post-endoplasmic reticulum compartments.
    • Torres, E., Gonzalez-Melendi, P., Stoger, E., Shaw, P. et al., Native and artificial reticuloplasmins co-accumulate in distinct domains of the endoplasmic reticulum and in post-endoplasmic reticulum compartments. Plant Physiol. 2001, 127, 1212-1223.
    • (2001) Plant Physiol. , vol.127 , pp. 1212-1223
    • Torres, E.1    Gonzalez-Melendi, P.2    Stoger, E.3    Shaw, P.4
  • 41
    • 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., Tuck, H. 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    Tuck, H.4
  • 42
    • 0031420939 scopus 로고    scopus 로고
    • Coexpression of the maize delta-zein and beta-zein genes results in stable accumulation of delta-zein in endoplasmic reticulum-derived protein bodies formed by beta-zein.
    • Bagga, S., Adams, H. P., Rodriguez, F. D., Kemp, J. D., Sengupta-Gopalan, C., Coexpression of the maize delta-zein and beta-zein genes results in stable accumulation of delta-zein in endoplasmic reticulum-derived protein bodies formed by beta-zein. Plant Cell 1997, 9, 1683-1696.
    • (1997) Plant Cell , vol.9 , pp. 1683-1696
    • Bagga, S.1    Adams, H.P.2    Rodriguez, F.D.3    Kemp, J.D.4    Sengupta-Gopalan, C.5
  • 43
    • 0029105386 scopus 로고
    • Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco.
    • Bagga, S., Adams, H., Kemp, J. D., Sengupta-Gopalan, C., Accumulation of 15-kilodalton zein in novel protein bodies in transgenic tobacco. Plant Physiol 1995, 107, 13-23.
    • (1995) Plant Physiol , vol.107 , pp. 13-23
    • Bagga, S.1    Adams, H.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 44
    • 0024299371 scopus 로고
    • Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes.
    • Wallace, J. C., Galili, G., Kawata, E. E., Cuellar, R. E. et al., Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes. Science 1988, 240, 662-664.
    • (1988) Science , vol.240 , pp. 662-664
    • Wallace, J.C.1    Galili, G.2    Kawata, E.E.3    Cuellar, R.E.4
  • 45
    • 4344706600 scopus 로고    scopus 로고
    • The accumulation of alpha-zein in transgenic tobacco endosperm is stabilized by co-expression of beta-zein.
    • Coleman, C. E., Yoho, P. R., Escobar, S., Ogawa, M., The accumulation of alpha-zein in transgenic tobacco endosperm is stabilized by co-expression of beta-zein. Plant Cell Physiol. 2004, 45, 864-871.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 864-871
    • Coleman, C.E.1    Yoho, P.R.2    Escobar, S.3    Ogawa, M.4
  • 46
    • 0000031926 scopus 로고
    • Increases in binding-protein (Bip) accompany changes in protein body morphology in 3 high-lysine mutants of maize.
    • Zhang, F., Boston, R. S., Increases in binding-protein (Bip) accompany changes in protein body morphology in 3 high-lysine mutants of maize. Protoplasma 1992, 171, 142-152.
    • (1992) Protoplasma , vol.171 , pp. 142-152
    • Zhang, F.1    Boston, R.S.2
  • 47
    • 84873254593 scopus 로고    scopus 로고
    • Recombinant antibody production in Arabidopsis seeds triggers an unfolded protein response.
    • De Wilde, K., De Buck, S., Vanneste, K., Depicker, A., Recombinant antibody production in Arabidopsis seeds triggers an unfolded protein response. Plant Physiol. 2013, 161, 1021-1033.
    • (2013) Plant Physiol. , vol.161 , pp. 1021-1033
    • De Wilde, K.1    De Buck, S.2    Vanneste, K.3    Depicker, A.4
  • 48
    • 35148888987 scopus 로고    scopus 로고
    • Development of transgenic rice seed accumulating a major Japanese cedar pollen allergen (Cry j 1) structurally disrupted for oral immunotherapy.
    • Yang, L., Suzuki, K., Hirose, S., Wakasa, Y., Takaiwa, F., Development of transgenic rice seed accumulating a major Japanese cedar pollen allergen (Cry j 1) structurally disrupted for oral immunotherapy. Plant Biotechnol. J. 2007, 5, 815-826.
    • (2007) Plant Biotechnol. J. , vol.5 , pp. 815-826
    • Yang, L.1    Suzuki, K.2    Hirose, S.3    Wakasa, Y.4    Takaiwa, F.5
  • 49
    • 78649798754 scopus 로고    scopus 로고
    • Reducing rice seed storage protein accumulation leads to changes in nutrient quality and storage organelle formation.
    • Kawakatsu, T., Hirose, S., Yasuda, H., Takaiwa, F., Reducing rice seed storage protein accumulation leads to changes in nutrient quality and storage organelle formation. Plant Physiol. 2010, 154, 1842-1854.
    • (2010) Plant Physiol. , vol.154 , pp. 1842-1854
    • Kawakatsu, T.1    Hirose, S.2    Yasuda, H.3    Takaiwa, F.4
  • 50
    • 79956043300 scopus 로고    scopus 로고
    • Silencing of soybean seed storage proteins results in a rebalanced protein composition preserving seed protein content without major collateral changes in the metabolome and transcriptome.
    • Schmidt, M. A., Barbazuk, W. B., Sandford, M., May, G. et al., Silencing of soybean seed storage proteins results in a rebalanced protein composition preserving seed protein content without major collateral changes in the metabolome and transcriptome. Plant Physiol. 2011, 156, 330-345.
    • (2011) Plant Physiol. , vol.156 , pp. 330-345
    • Schmidt, M.A.1    Barbazuk, W.B.2    Sandford, M.3    May, G.4
  • 51
    • 13844274216 scopus 로고    scopus 로고
    • Foreign gene products can be enhanced by introduction into low storage protein mutants.
    • Tada, Y., Utsumi, S., Takaiwa, F., Foreign gene products can be enhanced by introduction into low storage protein mutants. Plant Biotechnol. J. 2003, 1, 411-422.
    • (2003) Plant Biotechnol. J. , vol.1 , pp. 411-422
    • Tada, Y.1    Utsumi, S.2    Takaiwa, F.3
  • 52
    • 84868528712 scopus 로고    scopus 로고
    • Yang, L., Hirose, S., Takahashi, H., Kawakatsu, T., Takaiwa, F., Recombinant protein yield in rice seed is enhanced by specific suppression of endogenous seed proteins at the same deposit site. Plant Biotechnol. J. 2012, 10, 1035-1045.
    • Yang, L., Hirose, S., Takahashi, H., Kawakatsu, T., Takaiwa, F., Recombinant protein yield in rice seed is enhanced by specific suppression of endogenous seed proteins at the same deposit site. Plant Biotechnol. J. 2012, 10, 1035-1045.
  • 53
    • 78149472034 scopus 로고    scopus 로고
    • Rice seed ER-derived protein body as an efficient deliver vehicle for oral tolerogenic peptides.
    • Takagi, H., Hiroi, T., Hirose, S., Yang, L., Takaiwa, F., Rice seed ER-derived protein body as an efficient deliver vehicle for oral tolerogenic peptides. Peptides 2010, 31, 1421-1425.
    • (2010) Peptides , vol.31 , pp. 1421-1425
    • Takagi, H.1    Hiroi, T.2    Hirose, S.3    Yang, L.4    Takaiwa, F.5
  • 54
    • 79953698171 scopus 로고    scopus 로고
    • Seed-based oral vaccines as allergen-specific immunotherapies.
    • Takaiwa, F., Seed-based oral vaccines as allergen-specific immunotherapies. Hum. Vaccines 2011, 7, 357-366.
    • (2011) Hum. Vaccines , vol.7 , pp. 357-366
    • Takaiwa, F.1
  • 55
    • 84884923204 scopus 로고    scopus 로고
    • The use of rice seeds to produce human pharmaceuticals for oral therapy.
    • DOI: 10.1002/biot.201200065.
    • Wakasa, Y., Takaiwa, F., The use of rice seeds to produce human pharmaceuticals for oral therapy. Biotechnol. J. 2013, 8, DOI: 10.1002/biot.201200065.
    • (2013) Biotechnol. J. , vol.8
    • Wakasa, Y.1    Takaiwa, F.2
  • 56
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.