메뉴 건너뛰기




Volumn 20, Issue 4, 2011, Pages 811-826

Expression of functional recombinant human growth hormone in transgenic soybean seeds

Author keywords

Human growth hormone; Molecular farming; Protein storage vacuoles; Soybean seeds; Transgenic

Indexed keywords

ALPHA COIXIN PROTEIN, COIX LACRYMA JOBI; ALPHA-COIXIN PROTEIN, COIX LACRYMA-JOBI; BETA CONGLYCININ PROTEIN, GLYCINE MAX; BETA-CONGLYCININ PROTEIN, GLYCINE MAX; GLOBULIN; HUMAN GROWTH HORMONE; PLANT ANTIGEN; RECOMBINANT PROTEIN; SEED STORAGE PROTEIN; SIGNAL PEPTIDE; SOYBEAN PROTEIN; VEGETABLE PROTEIN;

EID: 79960472029     PISSN: 09628819     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11248-010-9460-z     Document Type: Article
Times cited : (41)

References (79)
  • 1
    • 33746818809 scopus 로고    scopus 로고
    • Growth hormone therapy for short stature: is the benefit worth the burden?
    • Allen DB (2006) Growth hormone therapy for short stature: is the benefit worth the burden? Pediatrics 118: 343-348.
    • (2006) Pediatrics , vol.118 , pp. 343-348
    • Allen, D.B.1
  • 2
    • 0024673625 scopus 로고
    • Nuclear factors interact with a soybean beta-conglycinin enhancer
    • Allen RD, Bernier F, Lessard PA, Beachy RN (1989) Nuclear factors interact with a soybean beta-conglycinin enhancer. Plant Cell 1: 623-1631.
    • (1989) Plant Cell , vol.1 , pp. 623-1631
    • Allen, R.D.1    Bernier, F.2    Lessard, P.A.3    Beachy, R.N.4
  • 3
    • 70649089334 scopus 로고    scopus 로고
    • Efficient expression and secretion of recombinant human growth hormone in the methylotrophic yeast Pichia pastoris: potential applications for other proteins
    • Apte-Deshpande A, Rewanwar S, Kotwal P, Raiker VA, Padmanabhan S (2009) Efficient expression and secretion of recombinant human growth hormone in the methylotrophic yeast Pichia pastoris: potential applications for other proteins. Biotechnol Appl Biochem 54: 197-205.
    • (2009) Biotechnol Appl Biochem , vol.54 , pp. 197-205
    • Apte-Deshpande, A.1    Rewanwar, S.2    Kotwal, P.3    Raiker, V.A.4    Padmanabhan, S.5
  • 4
    • 0033942273 scopus 로고    scopus 로고
    • Selection of transgenic meristematic cells utilizing a herbicidal molecule results in the recovery of fertile transgenic soybean [Glycine max (L.) Merril] plants at a high frequency
    • Aragão FJL, Sarokin L, Vianna GR, Rech EL (2000) Selection of transgenic meristematic cells utilizing a herbicidal molecule results in the recovery of fertile transgenic soybean [Glycine max (L.) Merril] plants at a high frequency. Theor Appl Genet 101: 1-6.
    • (2000) Theor Appl Genet , vol.101 , pp. 1-6
    • Aragão, F.J.L.1    Sarokin, L.2    Vianna, G.R.3    Rech, E.L.4
  • 7
    • 34250674830 scopus 로고    scopus 로고
    • RNAi-mediated resistance to Bean golden mosaic virus in genetically engineered common bean (Phaseolus vulgaris)
    • Bonfim K, Faria JC, Nogueira EOPL, Mendes E, Aragão FJL (2007) RNAi-mediated resistance to Bean golden mosaic virus in genetically engineered common bean (Phaseolus vulgaris). Mol Plant Microbe Interact 20: 717-726.
    • (2007) Mol Plant Microbe Interact , vol.20 , pp. 717-726
    • Bonfim, K.1    Faria, J.C.2    Nogueira, E.O.P.L.3    Mendes, E.4    Aragão, F.J.L.5
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0029361756 scopus 로고
    • Comparative study of the composition and nutritional value of the seeds and protein concentrations in legumes
    • Cantoral R, Fernández-Quintela A, Martínez JA, Macarulla MT (1995) Comparative study of the composition and nutritional value of the seeds and protein concentrations in legumes. Arch Latinoam Nutr 45: 242-248.
    • (1995) Arch Latinoam Nutr , vol.45 , pp. 242-248
    • Cantoral, R.1    Fernández-Quintela, A.2    Martínez, J.A.3    Macarulla, M.T.4
  • 12
    • 0023270946 scopus 로고
    • High-level secretion of human growth hormone by Escherichia coli
    • Chang CN, Rey M, Bochner B, Heyneker H, Gray G (1987) High-level secretion of human growth hormone by Escherichia coli. Gene 55: 189-196.
    • (1987) Gene , vol.55 , pp. 189-196
    • Chang, C.N.1    Rey, M.2    Bochner, B.3    Heyneker, H.4    Gray, G.5
  • 13
    • 0022808468 scopus 로고
    • Functional analysis of regulatory elements in a plant embryo-specific gene
    • Chen ZL, Schuler MA, Beachy RN (1986) Functional analysis of regulatory elements in a plant embryo-specific gene. Proc Natl Acad Sci USA 83: 8560-8564.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8560-8564
    • Chen, Z.L.1    Schuler, M.A.2    Beachy, R.N.3
  • 15
    • 0035212386 scopus 로고    scopus 로고
    • Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants
    • Daniell H, Streatfield SJ, 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
  • 17
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • Demain AL, Vaishnav P (2009) Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27: 297-306.
    • (2009) Biotechnol Adv , vol.27 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 18
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming
    • Faye L, Boulaflous A, Benchabane M, Gomord V, Michaud D (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 23: 1770-1778.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 19
    • 0028889621 scopus 로고
    • High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds
    • Fiedler U, Conrad U (1995) High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds. Biotechnology (NY) 13: 1090-1093.
    • (1995) Biotechnology (NY) , vol.13 , pp. 1090-1093
    • Fiedler, U.1    Conrad, U.2
  • 21
    • 0028107795 scopus 로고
    • Transgene inactivation: plants fight back
    • Finnegan J, McElroy D (1994) Transgene inactivation: plants fight back. Nat Biotechnol 12: 883-888.
    • (1994) Nat Biotechnol , vol.12 , pp. 883-888
    • Finnegan, J.1    McElroy, D.2
  • 23
    • 0028119550 scopus 로고
    • Tissue-specific and temporal regulation of a β-conglycinin gene: roles of the RY repeat and other cis-acting elements
    • Fujiwara T, Beachy RN (1994) Tissue-specific and temporal regulation of a β-conglycinin gene: roles of the RY repeat and other cis-acting elements. Plant Mol Biol 24: 261-272.
    • (1994) Plant Mol Biol , vol.24 , pp. 261-272
    • Fujiwara, T.1    Beachy, R.N.2
  • 24
    • 0035477961 scopus 로고    scopus 로고
    • Transgenic plants as protein factories
    • Giddings G (2001) Transgenic plants as protein factories. Curr Opin Biotechnol 12: 450-454.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 450-454
    • Giddings, G.1
  • 25
    • 33744933668 scopus 로고    scopus 로고
    • High-yield production of authentic human growth hormone using a plant virus-based expression system
    • Gils M, Kandzia R, Marillonnet S, Klimyuk V, Gleba Y (2005) High-yield production of authentic human growth hormone using a plant virus-based expression system. Plant Biotechnol J 3: 613-620.
    • (2005) Plant Biotechnol J , vol.3 , pp. 613-620
    • Gils, M.1    Kandzia, R.2    Marillonnet, S.3    Klimyuk, V.4    Gleba, Y.5
  • 27
    • 0034684170 scopus 로고    scopus 로고
    • Introduction of the human growth hormone gene into the guinea pig mammary gland by in vivo transfection promotes sustained expression of human growth hormone in the milk throughout lactation
    • Hens JR, Amstutz MD, Schanbacher FL, Mather IH (2000) Introduction of the human growth hormone gene into the guinea pig mammary gland by in vivo transfection promotes sustained expression of human growth hormone in the milk throughout lactation. Biochim Biophys Acta 1523: 161-171.
    • (2000) Biochim Biophys Acta , vol.1523 , pp. 161-171
    • Hens, J.R.1    Amstutz, M.D.2    Schanbacher, F.L.3    Mather, I.H.4
  • 28
    • 58849122869 scopus 로고    scopus 로고
    • Production of pharmaceutical proteins by transgenic animals
    • Houdebine LM (2009) Production of pharmaceutical proteins by transgenic animals. Comp Immunol Microbiol Infect Dis 32: 107-121.
    • (2009) Comp Immunol Microbiol Infect Dis , vol.32 , pp. 107-121
    • Houdebine, L.M.1
  • 29
    • 63849201516 scopus 로고    scopus 로고
    • Spatial and temporal control of transcription of the soybean beta-conglycinin alpha subunit gene is conferred by its proximal promoter region and accounts for the unequal distribution of the protein during embryogenesis
    • Imoto Y, Yamada T, Kitamura K, Kanazawa A (2008) Spatial and temporal control of transcription of the soybean beta-conglycinin alpha subunit gene is conferred by its proximal promoter region and accounts for the unequal distribution of the protein during embryogenesis. Genes Genet Syst 83: 469-476.
    • (2008) Genes Genet Syst , vol.83 , pp. 469-476
    • Imoto, Y.1    Yamada, T.2    Kitamura, K.3    Kanazawa, A.4
  • 30
    • 27844451115 scopus 로고    scopus 로고
    • Pathways for protein transport to seed storage vacuoles
    • Jolliffe NA, Craddock CP, Frigerio L (2005) Pathways for protein transport to seed storage vacuoles. Biochem Soc Trans 33: 1016-1018.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1016-1018
    • Jolliffe, N.A.1    Craddock, C.P.2    Frigerio, L.3
  • 32
    • 13444256318 scopus 로고    scopus 로고
    • Expression of an 11 kDa methionine-rich delta-zein in transgenic soybean results in the formation of two types of novel protein bodies in transitional cells situated between the vascular tissue and storage parenchyma cells
    • Kim W-S, Krishnan HB (2004) Expression of an 11 kDa methionine-rich delta-zein in transgenic soybean results in the formation of two types of novel protein bodies in transitional cells situated between the vascular tissue and storage parenchyma cells. Plant Biotechnol J 2: 199-210.
    • (2004) Plant Biotechnol J , vol.2 , pp. 199-210
    • Kim, W.-S.1    Krishnan, H.B.2
  • 33
    • 42149153938 scopus 로고    scopus 로고
    • Expression of human growth hormone in transgenic rice cell suspension culture
    • Kim TG, Baek MY, Lee EK, Kwon TH, Yang MS (2008) Expression of human growth hormone in transgenic rice cell suspension culture. Plant Cell Rep 27: 885-891.
    • (2008) Plant Cell Rep , vol.27 , pp. 885-891
    • Kim, T.G.1    Baek, M.Y.2    Lee, E.K.3    Kwon, T.H.4    Yang, M.S.5
  • 34
    • 24644434888 scopus 로고    scopus 로고
    • Epi-CHO, an episomal expression system for recombinant protein production in CHO cells
    • Kunaparaju R, Liao M, Sunstrom N-A (2005) Epi-CHO, an episomal expression system for recombinant protein production in CHO cells. Biotechnol Bioeng 91: 670-677.
    • (2005) Biotechnol Bioeng , vol.91 , pp. 670-677
    • Kunaparaju, R.1    Liao, M.2    Sunstrom, N.-A.3
  • 35
    • 0031555505 scopus 로고    scopus 로고
    • Production of recombinant proteins in transgenic plants: practical considerations
    • Kusnadi AR, Nikolov ZL, Howard JA (1997) Production of recombinant proteins in transgenic plants: practical considerations. Biotechnol Bioeng 56: 473-484.
    • (1997) Biotechnol Bioeng , vol.56 , pp. 473-484
    • Kusnadi, A.R.1    Nikolov, Z.L.2    Howard, J.A.3
  • 37
    • 0035423688 scopus 로고    scopus 로고
    • Producing proteins in transgenic plants and animals
    • Larrick JW, Thomas DW (2001) Producing proteins in transgenic plants and animals. Curr Opin Biotechnol 12: 411-418.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 411-418
    • Larrick, J.W.1    Thomas, D.W.2
  • 39
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans
    • Lerouge P, Bardor M, Pagny S, Gomord V, Faye L (2000) N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Curr Pharm Biotechnol 4: 347-354.
    • (2000) Curr Pharm Biotechnol , vol.4 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 41
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma JKC, Drake PMW, Christou P (2003) The production of recombinant pharmaceutical proteins in plants. Nat Rev Genet 4: 794-805.
    • (2003) Nat Rev Genet , vol.4 , pp. 794-805
    • Ma, J.K.C.1    Drake, P.M.W.2    Christou, P.3
  • 43
    • 3242774747 scopus 로고    scopus 로고
    • High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification
    • Mooney BP, Krishnan HB, Thelen JJ (2004) High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. Phytochemistry 65: 1733-1744.
    • (2004) Phytochemistry , vol.65 , pp. 1733-1744
    • Mooney, B.P.1    Krishnan, H.B.2    Thelen, J.J.3
  • 45
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • Müntz K (1998) Deposition of storage proteins. Plant Mol Biol 38: 77-99.
    • (1998) Plant Mol Biol , vol.38 , pp. 77-99
    • Müntz, K.1
  • 46
    • 0141497248 scopus 로고    scopus 로고
    • Protein transport in plant cells: in and out of the Golgi
    • Neumann U, Brandizzi F, Hawes C (2003) Protein transport in plant cells: in and out of the Golgi. Ann Bot 92: 167-180.
    • (2003) Ann Bot , vol.92 , pp. 167-180
    • Neumann, U.1    Brandizzi, F.2    Hawes, C.3
  • 47
    • 0027567216 scopus 로고
    • Sequence analysis of 22 kDa-like alpha-Coixin genes and their comparison with homologous zein and kafirin genes reveals highly conserved protein structure and regulatory elements
    • Ottoboni LM, Leite A, Yunes JA, Targon ML, Souza Filho GA, Arruda P (1993) Sequence analysis of 22 kDa-like alpha-Coixin genes and their comparison with homologous zein and kafirin genes reveals highly conserved protein structure and regulatory elements. Plant Mol Biol 21: 765-778.
    • (1993) Plant Mol Biol , vol.21 , pp. 765-778
    • Ottoboni, L.M.1    Leite, A.2    Yunes, J.A.3    Targon, M.L.4    Souza Filho, G.A.5    Arruda, P.6
  • 48
    • 64549120754 scopus 로고    scopus 로고
    • Expression system for recombinant human growth hormone production from Bacillus subtilis
    • Ozdamar TH, Sentürk B, Yilmaz OD, Calik G, Celik E, Calik P (2009) Expression system for recombinant human growth hormone production from Bacillus subtilis. Biotechnol Prog 25: 75-84.
    • (2009) Biotechnol Prog , vol.25 , pp. 75-84
    • Ozdamar, T.H.1    Sentürk, B.2    Yilmaz, O.D.3    Calik, G.4    Celik, E.5    Calik, P.6
  • 49
    • 0037325964 scopus 로고    scopus 로고
    • Fusion with HDEL protects cell wall invertase from early degradation when N-glycosylation is inhibited
    • Pagny S, Denmat-Ouisse LA, Gomord V, Faye L (2003) Fusion with HDEL protects cell wall invertase from early degradation when N-glycosylation is inhibited. Plant Cell Physiol 44: 173-182.
    • (2003) Plant Cell Physiol , vol.44 , pp. 173-182
    • Pagny, S.1    Denmat-Ouisse, L.A.2    Gomord, V.3    Faye, L.4
  • 50
    • 1342265970 scopus 로고    scopus 로고
    • Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species
    • Park M, Kim SJ, Vitale A, Hwang I (2004) Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species. Plant Physiol 134: 625-639.
    • (2004) Plant Physiol , vol.134 , pp. 625-639
    • Park, M.1    Kim, S.J.2    Vitale, A.3    Hwang, I.4
  • 52
    • 0035137450 scopus 로고    scopus 로고
    • Expression and long-term stability of a recombinant single-chain Fv antibody fragment in transgenic Nicotiana tabacum seeds
    • Ramírez N, Oramas P, Ayala M, Rodríguez M, Pérez M, Gavilondo J (2001) Expression and long-term stability of a recombinant single-chain Fv antibody fragment in transgenic Nicotiana tabacum seeds. Biotechnol Lett 23: 47-49.
    • (2001) Biotechnol Lett , vol.23 , pp. 47-49
    • Ramírez, N.1    Oramas, P.2    Ayala, M.3    Rodríguez, M.4    Pérez, M.5    Gavilondo, J.6
  • 53
    • 40649104816 scopus 로고    scopus 로고
    • High-efficiency transformation by biolistics of soybean, common bean and cotton transgenic plants
    • Rech EL, Vianna GR, Aragão FJL (2008) High-efficiency transformation by biolistics of soybean, common bean and cotton transgenic plants. Nat Protoc 3: 410-418.
    • (2008) Nat Protoc , vol.3 , pp. 410-418
    • Rech, E.L.1    Vianna, G.R.2    Aragão, F.J.L.3
  • 54
    • 69949187516 scopus 로고    scopus 로고
    • A stepwise increase in recombinant human growth hormone dosing during puberty achieves improved pubertal growth: a National Cooperative Growth Study report
    • Riddick L, Alter C, Davis DA, Frane J, Lippe B, Bakker B (2009) A stepwise increase in recombinant human growth hormone dosing during puberty achieves improved pubertal growth: a National Cooperative Growth Study report. J Pediatr Endocrinol Metab 22: 623-628.
    • (2009) J Pediatr Endocrinol Metab , vol.22 , pp. 623-628
    • Riddick, L.1    Alter, C.2    Davis, D.A.3    Frane, J.4    Lippe, B.5    Bakker, B.6
  • 55
    • 21844450852 scopus 로고    scopus 로고
    • Protein sorting to the storage vacuoles of plants: a critical appraisal
    • Robinson DG, Oliviusson P, Hinz G (2005) Protein sorting to the storage vacuoles of plants: a critical appraisal. Traffic 6: 615-625.
    • (2005) Traffic , vol.6 , pp. 615-625
    • Robinson, D.G.1    Oliviusson, P.2    Hinz, G.3
  • 59
    • 79960451768 scopus 로고    scopus 로고
    • In: Sambrook J, Russell DW (ed) Molecular cloning: a laboratory manual, 3rd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Sambrook J, Russell DW (2001) Commonly used techniques in molecular cloning. In: Sambrook J, Russell DW (ed) Molecular cloning: a laboratory manual, 3rd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp A8-A8. 20.
    • (2001) Commonly used techniques in molecular cloning , pp. 8
    • Sambrook, J.1    Russell, D.W.2
  • 60
    • 4644346842 scopus 로고    scopus 로고
    • Adenoviral vector mediates high expression levels of human growth hormone in the milk of mice and goats
    • Sanchez O, Toledo JR, Rodriguez MP, Castro FO (2004) Adenoviral vector mediates high expression levels of human growth hormone in the milk of mice and goats. J Biotechnol 114: 89-97.
    • (2004) J Biotechnol , vol.114 , pp. 89-97
    • Sanchez, O.1    Toledo, J.R.2    Rodriguez, M.P.3    Castro, F.O.4
  • 61
    • 0000611828 scopus 로고
    • Molecular basis of Imidazolinone herbicide resistance in Arabidopsis thaliana var Columbia
    • Sathasivan K, Haughn GW, Murai N (1991) Molecular basis of Imidazolinone herbicide resistance in Arabidopsis thaliana var Columbia. Plant Physiol 97: 1044-1050.
    • (1991) Plant Physiol , vol.97 , pp. 1044-1050
    • Sathasivan, K.1    Haughn, G.W.2    Murai, N.3
  • 62
    • 0012515015 scopus 로고    scopus 로고
    • Antibody molecular farming in plants and plant cells
    • Schillberg S, Emans N, Fischer R (2002) Antibody molecular farming in plants and plant cells. Phytochem Rev 1: 45-54.
    • (2002) Phytochem Rev , vol.1 , pp. 45-54
    • Schillberg, S.1    Emans, N.2    Fischer, R.3
  • 63
    • 33746750608 scopus 로고    scopus 로고
    • Challenges in therapeutic glycoprotein production
    • Sethuraman N, Stadheim TA (2006) Challenges in therapeutic glycoprotein production. Curr Opin Biotechnol 17: 341-346.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 341-346
    • Sethuraman, N.1    Stadheim, T.A.2
  • 64
    • 0344625372 scopus 로고    scopus 로고
    • High-level production of human growth hormone in Escherichia coli by a simple recombinant process
    • Shin NK, Kim DY, Shin CS, Hong MS, Lee J, Shin HC (1998) High-level production of human growth hormone in Escherichia coli by a simple recombinant process. J Biotechnol 62: 143-151.
    • (1998) J Biotechnol , vol.62 , pp. 143-151
    • Shin, N.K.1    Kim, D.Y.2    Shin, C.S.3    Hong, M.S.4    Lee, J.5    Shin, H.C.6
  • 70
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: pharmaceutical proteins from plants
    • Stoger E, Ma JK, Fischer R, Christou P (2005) Sowing the seeds of success: pharmaceutical proteins from plants. Curr Opin Biotechnol 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
  • 71
    • 0030151988 scopus 로고    scopus 로고
    • Expression of human growth hormone in silkworn larvae through recombinant Bombyx mori nuclear polyhedrosis virus
    • Sumathy S, Palhn VB, Gopinathan KP (1996) Expression of human growth hormone in silkworn larvae through recombinant Bombyx mori nuclear polyhedrosis virus. Protein Express Purif 7: 262-268.
    • (1996) Protein Express Purif , vol.7 , pp. 262-268
    • Sumathy, S.1    Palhn, V.B.2    Gopinathan, K.P.3
  • 73
    • 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 (2007) Endosperm tissue is good production platform for artificial recombinant proteins in transgenic rice. Plant Biotechnol J 5: 84-92.
    • (2007) Plant Biotechnol J , vol.5 , pp. 84-92
    • Takaiwa, F.1    Takagi, H.2    Hirose, S.3    Wakasa, Y.4
  • 75
    • 46649085694 scopus 로고    scopus 로고
    • Systemic overexpression of growth hormone (GH) in transgenic FVB/N inbred mice: an optimized model for holistic studies of molecular mechanisms underlying GH-induced kidney pathology
    • Waldthausen D von, Schneider M, Renner-Müller I, Rauleder D, Herbach N, Aigner B, Wanke R, Wolf E (2008) Systemic overexpression of growth hormone (GH) in transgenic FVB/N inbred mice: an optimized model for holistic studies of molecular mechanisms underlying GH-induced kidney pathology. Transgenic Res 17: 479-488.
    • (2008) Transgenic Res , vol.17 , pp. 479-488
    • von Waldthausen, D.1    Schneider, M.2    Renner-Müller, I.3    Rauleder, D.4    Herbach, N.5    Aigner, B.6    Wanke, R.7    Wolf, E.8
  • 76
    • 0033928343 scopus 로고    scopus 로고
    • Isolation and characterization of plant N-acetyl glucosaminyltransferase I (GntI) cDNA sequences. Functional analyses in the Arabidopsis cgl mutant and in antisense plants
    • Wenderoth I, von Schaewen A (2000) Isolation and characterization of plant N-acetyl glucosaminyltransferase I (GntI) cDNA sequences. Functional analyses in the Arabidopsis cgl mutant and in antisense plants. Plant Physiol 123: 1097-1108.
    • (2000) Plant Physiol , vol.123 , pp. 1097-1108
    • Wenderoth, I.1    von Schaewen, A.2
  • 78
    • 0007412271 scopus 로고
    • The origin of protein bodies in developing soybean cotyledons: a proposal
    • Yoo BY, Chrispeels MJ (1980) The origin of protein bodies in developing soybean cotyledons: a proposal. Protoplasma 103: 201-204.
    • (1980) Protoplasma , vol.103 , pp. 201-204
    • Yoo, B.Y.1    Chrispeels, M.J.2
  • 79
    • 34548611034 scopus 로고    scopus 로고
    • Hereditary behavior of bar gene cassette is complex in rice mediated by particle bombardment
    • Zhao Y, Qian Q, Wang H, Huang D (2007) Hereditary behavior of bar gene cassette is complex in rice mediated by particle bombardment. J Genet Genomics 34: 824-835.
    • (2007) J Genet Genomics , vol.34 , pp. 824-835
    • Zhao, Y.1    Qian, Q.2    Wang, H.3    Huang, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.