메뉴 건너뛰기




Volumn 242, Issue , 2017, Pages 111-121

Expression of α-1,6-fucosyltransferase (FUT8) in rice grain and immunogenicity evaluation of plant-specific glycans

Author keywords

Immunogenicity of plant specific glycans; Molecular pharming; N glycosylation; Plant specific glycans; Rice seed

Indexed keywords

COST EFFECTIVENESS; POLYSACCHARIDES; PROTEINS;

EID: 85007302276     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2016.12.017     Document Type: Article
Times cited : (14)

References (76)
  • 1
    • 84897485508 scopus 로고    scopus 로고
    • Relationships between starch synthase I and branching enzyme isozymes determined using double mutant rice lines
    • Abe, N., Asai, H., Yago, H., Oitome, N.F., Itoh, R., Crofts, N., Nakamura, Y., Fujita, N., Relationships between starch synthase I and branching enzyme isozymes determined using double mutant rice lines. BMC Plant Biol., 14, 2014, 80.
    • (2014) BMC Plant Biol. , vol.14 , pp. 80
    • Abe, N.1    Asai, H.2    Yago, H.3    Oitome, N.F.4    Itoh, R.5    Crofts, N.6    Nakamura, Y.7    Fujita, N.8
  • 4
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1,3)-fucose and core xylose
    • Bardor, M., Faveeuw, C., Fitchette, A.C., Gilbert, D., Galas, L., Trottein, F., Faye, L., Lerouge, P., Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1,3)-fucose and core xylose. Glycobiology 13 (2003), 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
  • 5
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: biosynthesis and biological function in mammals
    • Becker, D.J., Lowe, J.B., Fucose: biosynthesis and biological function in mammals. Glycobiology 13 (2003), 41R–53R.
    • (2003) Glycobiology , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 6
    • 2942606516 scopus 로고    scopus 로고
    • Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin
    • Bencúrová, M., Hemmer, W., Focke-Tejkl, M., Wilson, I.B., Altmann, F., Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology 14 (2004), 457–466.
    • (2004) Glycobiology , vol.14 , pp. 457-466
    • Bencúrová, M.1    Hemmer, W.2    Focke-Tejkl, M.3    Wilson, I.B.4    Altmann, F.5
  • 8
    • 84965098196 scopus 로고    scopus 로고
    • Transient expression of mammalian genes in N. benthamiana to modulate N-glycosylation
    • Castilho, A., Steinkellner, H., Transient expression of mammalian genes in N. benthamiana to modulate N-glycosylation. Methods Mol. Biol. 1385 (2016), 99–113.
    • (2016) Methods Mol. Biol. , vol.1385 , pp. 99-113
    • Castilho, A.1    Steinkellner, H.2
  • 13
    • 0033805614 scopus 로고    scopus 로고
    • A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice
    • Chargelegue, D., Vine, N.D., van Dolleweerd, C.J., Drake, P.M., Ma, J.K., A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice. Transgenic Res. 9 (2000), 187–194.
    • (2000) Transgenic Res. , vol.9 , pp. 187-194
    • Chargelegue, D.1    Vine, N.D.2    van Dolleweerd, C.J.3    Drake, P.M.4    Ma, J.K.5
  • 14
    • 30944467214 scopus 로고    scopus 로고
    • The molecular basis of coupling of translocation and N-glycosylation
    • Chavan, M., Lennarz, W., The molecular basis of coupling of translocation and N-glycosylation. Trends Bioche. Sci. 31 (2006), 17–20.
    • (2006) Trends Bioche. Sci. , vol.31 , pp. 17-20
    • Chavan, M.1    Lennarz, W.2
  • 16
    • 84881365102 scopus 로고    scopus 로고
    • Expression and characterization of recombinant molecules in transgenic soybean
    • Da Cunha, N.B., Murad, A.M., Vianna, G.R., Coelho, C., Rech, E.L., Expression and characterization of recombinant molecules in transgenic soybean. Curr. Pharm. Des. 19 (2013), 5553–5563.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5553-5563
    • Da Cunha, N.B.1    Murad, A.M.2    Vianna, G.R.3    Coelho, C.4    Rech, E.L.5
  • 17
    • 84891930928 scopus 로고    scopus 로고
    • Molecular farming of human cytokines and blood products from plants: challenges in biosynthesis and detection of plant-produced recombinant proteins
    • Da Cunha, N.B., Vianna, G.R., da Almeida Lima, T., Rech, E., Molecular farming of human cytokines and blood products from plants: challenges in biosynthesis and detection of plant-produced recombinant proteins. Biotechnol. J. 9 (2014), 39–50.
    • (2014) Biotechnol. J. , vol.9 , pp. 39-50
    • Da Cunha, N.B.1    Vianna, G.R.2    da Almeida Lima, T.3    Rech, E.4
  • 18
    • 0035212386 scopus 로고    scopus 로고
    • Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants
    • Daniell, H., Streatfield, S.J., Wycoff, K., Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci. 6 (2001), 219–226.
    • (2001) Trends Plant Sci. , vol.6 , pp. 219-226
    • Daniell, H.1    Streatfield, S.J.2    Wycoff, K.3
  • 21
    • 84855802261 scopus 로고    scopus 로고
    • Overproduction of recombinant proteins in plants
    • Egelkrout, E., Rajan, V., Howard, J.A., Overproduction of recombinant proteins in plants. Plant Sci. 184 (2012), 83–101.
    • (2012) Plant Sci. , vol.184 , pp. 83-101
    • Egelkrout, E.1    Rajan, V.2    Howard, J.A.3
  • 23
    • 78650656127 scopus 로고    scopus 로고
    • Fc-glycosylation influences fc gamma receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12
    • Forthal, D.N., Gach, J.S., Landucci, G., Jez, J., Strasser, R., Kunert, R., Steinkellner, H., Fc-glycosylation influences fc gamma receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12. J. Immunol. 185 (2010), 6876–6882.
    • (2010) J. Immunol. , vol.185 , pp. 6876-6882
    • Forthal, D.N.1    Gach, J.S.2    Landucci, G.3    Jez, J.4    Strasser, R.5    Kunert, R.6    Steinkellner, H.7
  • 24
    • 57649129498 scopus 로고    scopus 로고
    • Expression of rat beta (1, 4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation
    • Frey, A.D., Karg, S.R., Kallio, P.T., Expression of rat beta (1, 4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation. Plant Biotechnol. J. 7 (2009), 33–48.
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 33-48
    • Frey, A.D.1    Karg, S.R.2    Kallio, P.T.3
  • 26
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Caffferkey, R., Bowdish, K., Production of antibodies in transgenic plants. Nature 342 (1989), 76–78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Caffferkey, R.2    Bowdish, K.3
  • 27
    • 84867369035 scopus 로고    scopus 로고
    • An evidence-based review of the potential benefits of taliglucerase alfa in the treatment of patients with Gaucher disease
    • Hollak, C.E., An evidence-based review of the potential benefits of taliglucerase alfa in the treatment of patients with Gaucher disease. Core Evid. 7 (2012), 15–20.
    • (2012) Core Evid. , vol.7 , pp. 15-20
    • Hollak, C.E.1
  • 28
    • 0037070490 scopus 로고    scopus 로고
    • From green plants to industrial enzymes
    • Hood, E.E., From green plants to industrial enzymes. Enzyme Microb. Technol. 30 (2002), 279–283.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 279-283
    • Hood, E.E.1
  • 29
    • 84879479858 scopus 로고    scopus 로고
    • Difucosylation of chitooligosaccharides by eukaryote and prokaryote α1,6-fucosyltransferases
    • Ihara, H., Hanashima, S., Tsukamoto, H., Yamaguchi, Y., Taniguchi, N., Ikeda, Y., Difucosylation of chitooligosaccharides by eukaryote and prokaryote α1,6-fucosyltransferases. Biochim. Biophys. Acta 1830 (2013), 4482–4490.
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 4482-4490
    • Ihara, H.1    Hanashima, S.2    Tsukamoto, H.3    Yamaguchi, Y.4    Taniguchi, N.5    Ikeda, Y.6
  • 30
    • 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., Bencúrová, M., Borth, N., Ferko, B., Jensen-Jarolim, E., Altmann, F., Hantusch, B., Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. Glycobiology 16 (2006), 349–357.
    • (2006) Glycobiology , vol.16 , pp. 349-357
    • Jin, C.1    Bencúrová, M.2    Borth, N.3    Ferko, B.4    Jensen-Jarolim, E.5    Altmann, F.6    Hantusch, B.7
  • 32
    • 38149058818 scopus 로고    scopus 로고
    • Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins
    • Jin, C., Hantusch, B., Hemmer, W., Stadlmann, J., Altmann, F., Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins. J. Allergy Clin. Immunol. 121 (2008), 185–190.
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 185-190
    • Jin, C.1    Hantusch, B.2    Hemmer, W.3    Stadlmann, J.4    Altmann, F.5
  • 33
    • 70349765520 scopus 로고    scopus 로고
    • The production of biopharmaceuticals in plant systems
    • Karg, S.R., Kallio, P.T., The production of biopharmaceuticals in plant systems. Biotechnol. Adv. 27 (2009), 879–894.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 879-894
    • Karg, S.R.1    Kallio, P.T.2
  • 35
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alpha 1-antitrypsin and its charge isoforms
    • Kolarich, D., Weber, A., Turecek, P.L., Schwarz, H.P., Altmann, F., Comprehensive glyco-proteomic analysis of human alpha 1-antitrypsin and its charge isoforms. Proteomics 6 (2006), 3369–3380.
    • (2006) Proteomics , vol.6 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.P.4    Altmann, F.5
  • 38
    • 84907753100 scopus 로고    scopus 로고
    • Plant glyco-biotechnology on the way to synthetic biology
    • Loos, A., Steinkellner, H., Plant glyco-biotechnology on the way to synthetic biology. Front. Plant Sci., 5, 2014, 523.
    • (2014) Front. Plant Sci. , vol.5 , pp. 523
    • Loos, A.1    Steinkellner, H.2
  • 41
    • 0032168206 scopus 로고    scopus 로고
    • Deposition of storage proteins
    • Müntz, K., Deposition of storage proteins. Plant Mol. Biol. 38 (1998), 77–99.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 77-99
    • Müntz, K.1
  • 42
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma, J.K., Hikmat, B.Y., Wycoff, K., Vine, N.D., Chargelegue, D., Yu, L., Hein, M.B., Lehner, T., Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nat. Med. 4 (1998), 601–606.
    • (1998) Nat. Med. , vol.4 , pp. 601-606
    • Ma, J.K.1    Hikmat, B.Y.2    Wycoff, K.3    Vine, N.D.4    Chargelegue, D.5    Yu, L.6    Hein, M.B.7    Lehner, T.8
  • 43
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma, J.K., Drake, P.M., Christou, P., The production of recombinant pharmaceutical proteins in plants. Nat. Rev. Genet. 4 (2003), 794–805.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 794-805
    • Ma, J.K.1    Drake, P.M.2    Christou, P.3
  • 45
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O.N., Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21 (2003), 255–261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 47
    • 79952303673 scopus 로고    scopus 로고
    • Production of complex multiantennary N-glycans in Nicotiana benthamiana plants
    • Nagels, B., Van Damme, E.J., Pabst, M., Callewaert, N., Weterings, K., Production of complex multiantennary N-glycans in Nicotiana benthamiana plants. Plant Physiol. 155 (2011), 1103–1112.
    • (2011) Plant Physiol. , vol.155 , pp. 1103-1112
    • Nagels, B.1    Van Damme, E.J.2    Pabst, M.3    Callewaert, N.4    Weterings, K.5
  • 50
    • 84859781058 scopus 로고    scopus 로고
    • Development of an efficient agrobacterium-mediated gene targeting system for rice and analysis of rice knockouts lacking granule-bound starch synthase (Waxy) and beta 1,2-Xylosyltransferase
    • Ozawa, K., Wakasa, Y., Ogo, Y., Matsuo, K., Kawahigashi, H., Takaiwa, F., Development of an efficient agrobacterium-mediated gene targeting system for rice and analysis of rice knockouts lacking granule-bound starch synthase (Waxy) and beta 1,2-Xylosyltransferase. Plant Cell Physiol. 53 (2012), 755–761.
    • (2012) Plant Cell Physiol. , vol.53 , pp. 755-761
    • Ozawa, K.1    Wakasa, Y.2    Ogo, Y.3    Matsuo, K.4    Kawahigashi, H.5    Takaiwa, F.6
  • 51
    • 79953704799 scopus 로고    scopus 로고
    • Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies
    • Peters, J., Stoger, E., Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies. Hum. Vaccines 7 (2011), 367–374.
    • (2011) Hum. Vaccines , vol.7 , pp. 367-374
    • Peters, J.1    Stoger, E.2
  • 54
    • 84978290995 scopus 로고    scopus 로고
    • Plant specific N-glycans do not have proven adverse effects in humans
    • Shaaltiel, Y., Tekoah, Y., Plant specific N-glycans do not have proven adverse effects in humans. Nat. Biotechnol. 34 (2016), 706–708.
    • (2016) Nat. Biotechnol. , vol.34 , pp. 706-708
    • Shaaltiel, Y.1    Tekoah, Y.2
  • 55
    • 70349759364 scopus 로고    scopus 로고
    • Plants as bioreactors: recent developments and emerging opportunities
    • Sharma, A.K., Sharma, M.K., Plants as bioreactors: recent developments and emerging opportunities. Biotechnol. Adv. 27 (2009), 811–832.
    • (2009) Biotechnol. Adv. , vol.27 , pp. 811-832
    • Sharma, A.K.1    Sharma, M.K.2
  • 56
    • 80955144306 scopus 로고    scopus 로고
    • Production of recombinant human granulocyte macrophage-colony stimulating factor in rice cell suspension culture with a human-like N-glycan structure
    • Shin, Y.J., Chong, Y.J., Yang, M.S., Kwon, T.H., Production of recombinant human granulocyte macrophage-colony stimulating factor in rice cell suspension culture with a human-like N-glycan structure. Plant Biotechnol. J. 9 (2011), 1109–1119.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 1109-1119
    • Shin, Y.J.1    Chong, Y.J.2    Yang, M.S.3    Kwon, T.H.4
  • 58
    • 84935861496 scopus 로고    scopus 로고
    • N-glyco-engineering in plants: update on strategies and major achievements
    • Steinkellner, H., Castilho, A., N-glyco-engineering in plants: update on strategies and major achievements. Methods Mol. Biol. 1321 (2015), 195–212.
    • (2015) Methods Mol. Biol. , vol.1321 , pp. 195-212
    • Steinkellner, H.1    Castilho, A.2
  • 60
    • 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. 16 (2005), 167–173.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 167-173
    • Stoger, E.1    Ma, J.K.2    Fischer, R.3    Christou, P.4
  • 61
    • 84899729872 scopus 로고    scopus 로고
    • Plant molecular pharming for the treatment of chronic and infectious diseases
    • Stoger, E., Fischer, R., Moloney, M., Ma, J.K., Plant molecular pharming for the treatment of chronic and infectious diseases. Annu. Rev. Plant Biol. 65 (2014), 743–768.
    • (2014) Annu. Rev. Plant Biol. , vol.65 , pp. 743-768
    • Stoger, E.1    Fischer, R.2    Moloney, M.3    Ma, J.K.4
  • 64
    • 0000962039 scopus 로고
    • Isolation and characterization of two types of protein bodies in the rice endosperm
    • Tanaka, K., Sugimoto, T., Ogawa, M., Kasai, Z., Isolation and characterization of two types of protein bodies in the rice endosperm. Agric. Biol. Chem. 44 (1980), 1633–1639.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 1633-1639
    • Tanaka, K.1    Sugimoto, T.2    Ogawa, M.3    Kasai, Z.4
  • 65
    • 80955158648 scopus 로고    scopus 로고
    • Differential N-glycosylation of a monoclonal antibody expressed in tobacco leaves with and without endoplasmic reticulum retention signal apparently induces similar in vivo stability in mice
    • Triguero, A., Cabrera, G., Rodríguez, M., Soto, J., Zamora, Y., Pérez, M., Wormald, M.R., Cremata, J.A., Differential N-glycosylation of a monoclonal antibody expressed in tobacco leaves with and without endoplasmic reticulum retention signal apparently induces similar in vivo stability in mice. Plant Biotechnol. J. 9 (2011), 1120–1130.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 1120-1130
    • Triguero, A.1    Cabrera, G.2    Rodríguez, M.3    Soto, J.4    Zamora, Y.5    Pérez, M.6    Wormald, M.R.7    Cremata, J.A.8
  • 69
    • 80955167004 scopus 로고    scopus 로고
    • Soybeans as bioreactors for biopharmaceuticals and industrial proteins
    • Vianna, G.R., Cunha, N.B., Murad, A.M., Rech, E.L., Soybeans as bioreactors for biopharmaceuticals and industrial proteins. Genet. Mol. Res. 10 (2011), 1733–1752.
    • (2011) Genet. Mol. Res. , vol.10 , pp. 1733-1752
    • Vianna, G.R.1    Cunha, N.B.2    Murad, A.M.3    Rech, E.L.4
  • 70
    • 21444434554 scopus 로고    scopus 로고
    • Sorting of proteins to storage vacuoles: how many mechanisms?
    • Vitale, A., Hinz, G., Sorting of proteins to storage vacuoles: how many mechanisms?. Trends Plant Sci. 10 (2005), 316–323.
    • (2005) Trends Plant Sci. , vol.10 , pp. 316-323
    • Vitale, A.1    Hinz, G.2
  • 71
    • 84921051387 scopus 로고    scopus 로고
    • Fast-tracking determination of homozygous transgenic lines and transgene stacking using a reliable quantitative real-time PCR assay
    • Wang, X.H., Jiang, D.M., Yang, D.C., Fast-tracking determination of homozygous transgenic lines and transgene stacking using a reliable quantitative real-time PCR assay. Appl. Biochem. Biotechnol. 175 (2015), 996–1006.
    • (2015) Appl. Biochem. Biotechnol. , vol.175 , pp. 996-1006
    • Wang, X.H.1    Jiang, D.M.2    Yang, D.C.3
  • 72
    • 84908003879 scopus 로고    scopus 로고
    • Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines
    • Ward, B.J., Landry, N., Trépanier, S., Mercier, G., Dargis, M., Couture, M., D'Aoust, M.A., Vézina, L.P., Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines. Vaccine 32 (2014), 6098–6106.
    • (2014) Vaccine , vol.32 , pp. 6098-6106
    • Ward, B.J.1    Landry, N.2    Trépanier, S.3    Mercier, G.4    Dargis, M.5    Couture, M.6    D'Aoust, M.A.7    Vézina, L.P.8
  • 73
    • 71749094615 scopus 로고    scopus 로고
    • Production of therapeutic antibodies with controlled fucosylation
    • Yamane-Ohnuki, N., Satoh, M., Production of therapeutic antibodies with controlled fucosylation. MAbs 1 (2009), 230–236.
    • (2009) MAbs , vol.1 , pp. 230-236
    • Yamane-Ohnuki, N.1    Satoh, M.2
  • 74
    • 84875248958 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human alpha-antitrypsin in transgenic rice seed
    • Zhang, L., Shi, J., Jiang, D., Stupak, J., Ou, J., Qiu, Q., An, N., Li, J., Yang, D., Expression and characterization of recombinant human alpha-antitrypsin in transgenic rice seed. J. Biotechnol. 164 (2012), 300–308.
    • (2012) J. Biotechnol. , vol.164 , pp. 300-308
    • Zhang, L.1    Shi, J.2    Jiang, D.3    Stupak, J.4    Ou, J.5    Qiu, Q.6    An, N.7    Li, J.8    Yang, D.9
  • 75
    • 42449143890 scopus 로고    scopus 로고
    • Branched N-glycans regulate the biological functions of integrins and cadherins
    • Zhao, Y., Sato, Y., Isaji, T., Fukuda, T., Matsumoto, A., Miyoshi, E., Gu, J., Taniguchi, N., Branched N-glycans regulate the biological functions of integrins and cadherins. FEBS J. 275 (2008), 1939–1948.
    • (2008) FEBS J. , vol.275 , pp. 1939-1948
    • Zhao, Y.1    Sato, Y.2    Isaji, T.3    Fukuda, T.4    Matsumoto, A.5    Miyoshi, E.6    Gu, J.7    Taniguchi, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.