메뉴 건너뛰기




Volumn 7, Issue 2, 2004, Pages 171-181

Posttranslational modification of therapeutic proteins in plants

Author keywords

carboxyglutamic acid; Advanced glycosylation end product; AGE; AGP; Arabinogalactan protein; Asn; Asparagine; Chinese hamster ovary; CHO; ConA; Concanavalin A; Endoplasmic reticulum; ER; Gal; Galactose; GalNAc; GLA; HRGP; N acetylgalactosamine

Indexed keywords

BIOLOGICAL FACTOR; FATTY ACID; ION; VEGETABLE PROTEIN;

EID: 1542291118     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2004.01.015     Document Type: Review
Times cited : (251)

References (49)
  • 1
    • 0242475327 scopus 로고    scopus 로고
    • Molecular farming in plants: Host systems and expression technology
    • This review summarizes recent progress in the development of expression technology for PMPs. The authors also discuss the advantages and limitations of the different plant-based production systems for therapeutic and technical proteins.
    • Twyman R.M., Stoger E., Schillberg S., Christou P., Fischer R. Molecular farming in plants: host systems and expression technology. Trends Biotechnol. 21:2003;570-578 This review summarizes recent progress in the development of expression technology for PMPs. The authors also discuss the advantages and limitations of the different plant-based production systems for therapeutic and technical proteins.
    • (2003) Trends Biotechnol , vol.21 , pp. 570-578
    • Twyman, R.M.1    Stoger, E.2    Schillberg, S.3    Christou, P.4    Fischer, R.5
  • 5
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie B., Furie B.C. The molecular basis of blood coagulation. Cell. 53:1988;505-518.
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 6
    • 0031860158 scopus 로고    scopus 로고
    • Post-translational modifications required for coagulation factor secretion and function
    • Kaufman R.J. Post-translational modifications required for coagulation factor secretion and function. Thromb Haemost. 79:1998;1068-1079.
    • (1998) Thromb Haemost , vol.79 , pp. 1068-1079
    • Kaufman, R.J.1
  • 7
    • 0035852328 scopus 로고    scopus 로고
    • Prediction of organellar targeting signals
    • Emanuelsson O., von Heijne G. Prediction of organellar targeting signals. Biochim Biophys Acta. 1541:2001;114-119.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 114-119
    • Emanuelsson, O.1    Von Heijne, G.2
  • 8
    • 0029175644 scopus 로고
    • Protein sorting signals: Simple peptides with complex functions
    • von Heijne G. Protein sorting signals: simple peptides with complex functions. EXS. 73:1995;67-76.
    • (1995) EXS , vol.73 , pp. 67-76
    • Von Heijne, G.1
  • 9
    • 0029257224 scopus 로고
    • Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells
    • Matsumoto S., Ikura K., Ueda M., Sasaki R. Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells. Plant Mol Biol. 27:1995;1163-1172.
    • (1995) Plant Mol Biol , vol.27 , pp. 1163-1172
    • Matsumoto, S.1    Ikura, K.2    Ueda, M.3    Sasaki, R.4
  • 10
    • 0035813390 scopus 로고    scopus 로고
    • Expression of recombinant human acetylcholinesterase in transgenic tomato plants
    • Mor T.S., Sternfeld M., Soreq H., Arntzen C.J., Mason H.S. Expression of recombinant human acetylcholinesterase in transgenic tomato plants. Biotechnol Bioeng. 75:2001;259-266.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 259-266
    • Mor, T.S.1    Sternfeld, M.2    Soreq, H.3    Arntzen, C.J.4    Mason, H.S.5
  • 11
    • 0034817036 scopus 로고    scopus 로고
    • Large-scale production of a therapeutic protein in transgenic tobacco plants: Effects of subcellular targeting on quality of a recombinant dog gastric lipase
    • Gruber V., Berna P., Arnaud T., Bournat P., Clement C., Mison D., Olagnier B., Philippe L., Theisen M., Baudino S.et al. Large-scale production of a therapeutic protein in transgenic tobacco plants: effects of subcellular targeting on quality of a recombinant dog gastric lipase. Mol Breed. 7:2001;329-340.
    • (2001) Mol Breed , vol.7 , pp. 329-340
    • Gruber, V.1    Berna, P.2    Arnaud, T.3    Bournat, P.4    Clement, C.5    Mison, D.6    Olagnier, B.7    Philippe, L.8    Theisen, M.9    Baudino, S.10
  • 12
    • 0032966917 scopus 로고    scopus 로고
    • Cis-elements of protein transport to the plant vacuoles
    • Matsuoka K., Neuhaus J.M. Cis-elements of protein transport to the plant vacuoles. J Exp Bot. 50:1999;165-174.
    • (1999) J Exp Bot , vol.50 , pp. 165-174
    • Matsuoka, K.1    Neuhaus, J.M.2
  • 13
    • 0022001083 scopus 로고
    • Polypeptide ligation occurs during post-translational modification of concanavalin a
    • Carrington D.M., Auffret A., Hanke D.E. Polypeptide ligation occurs during post-translational modification of concanavalin A. Nature. 313:1985;64-67.
    • (1985) Nature , vol.313 , pp. 64-67
    • Carrington, D.M.1    Auffret, A.2    Hanke, D.E.3
  • 14
    • 0001142403 scopus 로고
    • Transport and processing of the glycosylated precursor of concanavalin a in jack-bean
    • Faye L., Chrispeels M.J. Transport and processing of the glycosylated precursor of concanavalin A in jack-bean. Planta. 170:1987;217-224.
    • (1987) Planta , vol.170 , pp. 217-224
    • Faye, L.1    Chrispeels, M.J.2
  • 15
    • 0034945644 scopus 로고    scopus 로고
    • Deglycosylation is necessary but not sufficient for activation of proconcanavalin a
    • Ramis C., Gomord V., Lerouge P., Faye L. Deglycosylation is necessary but not sufficient for activation of proconcanavalin A. J Exp Bot. 52:2001;911-917.
    • (2001) J Exp Bot , vol.52 , pp. 911-917
    • Ramis, C.1    Gomord, V.2    Lerouge, P.3    Faye, L.4
  • 17
    • 0034993922 scopus 로고    scopus 로고
    • High-level expression in mammalian cells of recombinant house dust mite allergen ProDer p 1 with optimized codon usage
    • Massaer M., Mazzu P., Haumont M., Magi M., Daminet V., Bollen A., Jacquet A. High-level expression in mammalian cells of recombinant house dust mite allergen ProDer p 1 with optimized codon usage. Int Arch Allergy Immunol. 125:2001;32-43.
    • (2001) Int Arch Allergy Immunol , vol.125 , pp. 32-43
    • Massaer, M.1    Mazzu, P.2    Haumont, M.3    Magi, M.4    Daminet, V.5    Bollen, A.6    Jacquet, A.7
  • 18
    • 0034124315 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of a recombinant precursor form of the house dust mite allergen der p 1 produced by Drosophila cells
    • Jacquet A., Haumont M., Massaer M., Daminet V., Garcia L., Mazzu P., Jacobs P., Bollen A. Biochemical and immunological characterization of a recombinant precursor form of the house dust mite allergen Der p 1 produced by Drosophila cells. Clin Exp Allergy. 30:2000;677-684.
    • (2000) Clin Exp Allergy , vol.30 , pp. 677-684
    • Jacquet, A.1    Haumont, M.2    Massaer, M.3    Daminet, V.4    Garcia, L.5    Mazzu, P.6    Jacobs, P.7    Bollen, A.8
  • 19
    • 0026023554 scopus 로고
    • Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting
    • Matsuoka K., Nakamura K. Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc Natl Acad Sci USA. 88:1991;834-838.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 20
    • 0031080071 scopus 로고    scopus 로고
    • The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER
    • Gomord V., Denmat L.A., Fitchette-Laine A.C., Satiat-Jeunemaitre B., Hawes C., Faye L. The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER. Plant J. 11:1997;313-325.
    • (1997) Plant J , vol.11 , pp. 313-325
    • Gomord, V.1    Denmat, L.A.2    Fitchette-Laine, A.C.3    Satiat-Jeunemaitre, B.4    Hawes, C.5    Faye, L.6
  • 21
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro R.G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology. 12:2002;43R-56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 22
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1,3)-fucose and core xylose
    • The work described in this paper shows that plant-specific N-glycans are immunogenic in both rodents, except in BALB/c mice, and non-allergic humans.
    • 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 The work described in this paper shows that plant-specific N-glycans are immunogenic in both rodents, except in BALB/c mice, and non-allergic humans.
    • (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
  • 23
    • 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., Lommen A. Influence of growth conditions and developmental stage on N-glycan heterogeneity of transgenic immunoglobulin G and endogenous proteins in tobacco leaves. Plant Physiol. 126:2001;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
  • 29
    • 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.W., Ma J. 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.W.4    Ma, J.5
  • 30
    • 0038105203 scopus 로고    scopus 로고
    • Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy
    • Chenu S., Gregoire A., Malykh Y., Visvikis A., Monaco L., Shaw L., Schauer R., Marc A., Goergen J.L. Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy. Biochim Biophys Acta. 1622:2003;133-144.
    • (2003) Biochim Biophys Acta , vol.1622 , pp. 133-144
    • Chenu, S.1    Gregoire, A.2    Malykh, Y.3    Visvikis, A.4    Monaco, L.5    Shaw, L.6    Schauer, R.7    Marc, A.8    Goergen, J.L.9
  • 31
    • 0038270847 scopus 로고    scopus 로고
    • Function and glycosylation of plant-derived antiviral monoclonal antibody
    • A human anti-rabies antibody that contains a carboxy-terminal KDEL/ER retention signal on the heavy chains is produced in tobacco plants. This antibody contains mainly high-mannose-type N-glycans. The authors discuss the advantage of the shorter half-life of this type of plant-made antibody (which is caused by the presence of high-mannose-type N-glycans) in providing passive immunity against rabies.
    • Ko K., Tekoah Y., Rudd P.M., Harvey D.J., Dwek R.A., Spitsin S., Hanlon C.A., Rupprecht C., Dietzschold B., Golovkin M., Koprowski H. Function and glycosylation of plant-derived antiviral monoclonal antibody. Proc Natl Acad Sci USA. 100:2003;8013-8018 A human anti-rabies antibody that contains a carboxy-terminal KDEL/ER retention signal on the heavy chains is produced in tobacco plants. This antibody contains mainly high-mannose-type N-glycans. The authors discuss the advantage of the shorter half-life of this type of plant-made antibody (which is caused by the presence of high-mannose-type N-glycans) in providing passive immunity against rabies.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8013-8018
    • Ko, K.1    Tekoah, Y.2    Rudd, P.M.3    Harvey, D.J.4    Dwek, R.A.5    Spitsin, S.6    Hanlon, C.A.7    Rupprecht, C.8    Dietzschold, B.9    Golovkin, M.10    Koprowski, H.11
  • 32
    • 0032055988 scopus 로고    scopus 로고
    • Effect of C2-associated carbohydrate structure on Ig effector function: Studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells
    • Wright A., Morrison S.L. Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells. J Immunol. 160:1998;3393-3402.
    • (1998) J Immunol , vol.160 , pp. 3393-3402
    • Wright, A.1    Morrison, S.L.2
  • 33
    • 0037237680 scopus 로고    scopus 로고
    • Structural requirements for Arabidopsis beta1,2-xylosyltransferase activity and targeting to the Golgi
    • The most typical plant glycosyltransferase, the β1,2 xylosyltransferase from A. thaliana, is analyzed in this study. The authors identified a Golgi-retention determinant that is sufficient to localize a protein specifically to the medial cisternae of Golgi. This study provides the first detailed characterization of a plant glycosyltransferase at the molecular level.
    • Pagny S., Bouissonnie F., Sarkar M., Follet-Gueye M.L., Driouich A., Schachter H., Faye L., Gomord V. Structural requirements for Arabidopsis beta1,2-xylosyltransferase activity and targeting to the Golgi. Plant J. 33:2003;189-203 The most typical plant glycosyltransferase, the β1,2 xylosyltransferase from A. thaliana, is analyzed in this study. The authors identified a Golgi-retention determinant that is sufficient to localize a protein specifically to the medial cisternae of Golgi. This study provides the first detailed characterization of a plant glycosyltransferase at the molecular level.
    • (2003) Plant J , vol.33 , pp. 189-203
    • Pagny, S.1    Bouissonnie, F.2    Sarkar, M.3    Follet-Gueye, M.L.4    Driouich, A.5    Schachter, H.6    Faye, L.7    Gomord, V.8
  • 36
    • 0034788422 scopus 로고    scopus 로고
    • Arabinogalactan-proteins: Structure, expression and function
    • Showalter A.M. Arabinogalactan-proteins: structure, expression and function. Cell Mol Life Sci. 58:2001;1399-1417.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1399-1417
    • Showalter, A.M.1
  • 37
    • 1542367698 scopus 로고    scopus 로고
    • Novel glycan structures on the endogenous glycoconjugates of higher plants
    • Shah M., Fujiyama K., Flynn C., Joshi L. Novel glycan structures on the endogenous glycoconjugates of higher plants. Glycobiology. 13:2003;876R.
    • (2003) Glycobiology , vol.13
    • Shah, M.1    Fujiyama, K.2    Flynn, C.3    Joshi, L.4
  • 38
    • 0037181489 scopus 로고    scopus 로고
    • Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant
    • The authors describe the simultaneous expression of human collagen I and proline-4-hydroxylase. Their results demonstrate that it is possible to engineer the proline hydroxylation pathway to provide increased quality and conformity of recombinant collagen in plants.
    • Merle C., Perret S., Lacour T., Jonval V., Hudaverdian S., Garrone R., Ruggiero F., Theisen M. Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant. FEBS Lett. 515:2002;114-118 The authors describe the simultaneous expression of human collagen I and proline-4-hydroxylase. Their results demonstrate that it is possible to engineer the proline hydroxylation pathway to provide increased quality and conformity of recombinant collagen in plants.
    • (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
  • 39
    • 0037022383 scopus 로고    scopus 로고
    • Gamma-glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates
    • Bandyopadhyay P.K., Garrett J.E., Shetty R.P., Keate T., Walker C.S., Olivera B.M. Gamma-glutamyl carboxylation: an extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates. Proc Natl Acad Sci USA. 99:2002;1264-1269.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1264-1269
    • Bandyopadhyay, P.K.1    Garrett, J.E.2    Shetty, R.P.3    Keate, T.4    Walker, C.S.5    Olivera, B.M.6
  • 40
    • 0035896551 scopus 로고    scopus 로고
    • On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila
    • Walker C.S., Shetty R.P., Clark K., Kazuko S.G., Letsou A., Olivera B.M., Bandyopadhyay P.K. On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila. J Biol Chem. 276:2001;7769-7774.
    • (2001) J Biol Chem , vol.276 , pp. 7769-7774
    • Walker, C.S.1    Shetty, R.P.2    Clark, K.3    Kazuko, S.G.4    Letsou, A.5    Olivera, B.M.6    Bandyopadhyay, P.K.7
  • 41
    • 0027155879 scopus 로고
    • In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells
    • Rehemtulla A., Roth D.A., Wasley L.C., Kuliopulos A., Walsh C.T., Furie B., Furie B.C., Kaufman R.J. In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells. Proc Natl Acad Sci USA. 90:1993;4611-4615.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4611-4615
    • Rehemtulla, A.1    Roth, D.A.2    Wasley, L.C.3    Kuliopulos, A.4    Walsh, C.T.5    Furie, B.6    Furie, B.C.7    Kaufman, R.J.8
  • 43
    • 0027293993 scopus 로고
    • Expression of bovine vitamin K-dependent carboxylase activity in baculovirus-infected insect cells
    • Roth D.A., Rehemtulla A., Kaufman R.J., Walsh C.T., Furie B., Furie B.C. Expression of bovine vitamin K-dependent carboxylase activity in baculovirus-infected insect cells. Proc Natl Acad Sci USA. 90:1993;8372-8376.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8372-8376
    • Roth, D.A.1    Rehemtulla, A.2    Kaufman, R.J.3    Walsh, C.T.4    Furie, B.5    Furie, B.C.6
  • 44
    • 0032840232 scopus 로고    scopus 로고
    • Age-induced protein modifications and increased proteolysis in potato seed-tubers
    • Kumar G.N., Houtz R.L., Knowles N.R. Age-induced protein modifications and increased proteolysis in potato seed-tubers. Plant Physiol. 119:1999;89-100.
    • (1999) Plant Physiol , vol.119 , pp. 89-100
    • Kumar, G.N.1    Houtz, R.L.2    Knowles, N.R.3
  • 45
    • 0001465386 scopus 로고
    • Changes in lipid peroxidation and lipolytic and free-radical scavenging enzyme activities during aging and sprouting of potato (Solanum tuberosum) seed-tubers
    • Kumar G., Knowles N.R. Changes in lipid peroxidation and lipolytic and free-radical scavenging enzyme activities during aging and sprouting of potato (Solanum tuberosum) seed-tubers. Plant Physiol. 102:1993;115-124.
    • (1993) Plant Physiol , vol.102 , pp. 115-124
    • Kumar, G.1    Knowles, N.R.2
  • 46
    • 0027415273 scopus 로고
    • Protein sorting by high-performance liquid chromatography. I. Biomimetic interaction chromatography of recombinant human deoxyribonuclease I on polyionic stationary phases
    • Cacia J., Quan C.P., Vasser M., Sliwkowski M.B., Frenz J. Protein sorting by high-performance liquid chromatography. I. Biomimetic interaction chromatography of recombinant human deoxyribonuclease I on polyionic stationary phases. J Chromatogr. 634:1993;229-239.
    • (1993) J Chromatogr , vol.634 , pp. 229-239
    • Cacia, J.1    Quan, C.P.2    Vasser, M.3    Sliwkowski, M.B.4    Frenz, J.5
  • 47
    • 0025853823 scopus 로고
    • Deamidation of soluble CD4 at asparagine-52 results in reduced binding capacity for the HIV-1 envelope glycoprotein gp120
    • Shima G., Porter J., Yim K., Ling V., Guzzetta A. Deamidation of soluble CD4 at asparagine-52 results in reduced binding capacity for the HIV-1 envelope glycoprotein gp120. Biochemistry. 30:1991;3916-3922.
    • (1991) Biochemistry , vol.30 , pp. 3916-3922
    • Shima, G.1    Porter, J.2    Yim, K.3    Ling, V.4    Guzzetta, A.5
  • 48
    • 0023801411 scopus 로고
    • Isolation and characterization of a sulfoxide and a desamido derivative of biosynthetic human growth hormone
    • Becker G.W., Tackitt P.M., Bromer W.W., Lefeber D.S., Riggin R.M. Isolation and characterization of a sulfoxide and a desamido derivative of biosynthetic human growth hormone. Biotechnol Appl Biochem. 10:1988;326-337.
    • (1988) Biotechnol Appl Biochem , vol.10 , pp. 326-337
    • Becker, G.W.1    Tackitt, P.M.2    Bromer, W.W.3    Lefeber, D.S.4    Riggin, R.M.5
  • 49
    • 1542307901 scopus 로고    scopus 로고
    • Optimizing glycan processing in plants. 25 September, 2003; Patent WO 03/078637. Plant Research International B.V.
    • Bakker H, Florack D, Bosch H, Rouwendal G: Optimizing glycan processing in plants. 25 September, 2003; Patent WO 03/078637. Plant Research International B.V. ( http://www.plant.wageningen-ur.nl/ ).
    • Bakker, H.1    Florack, D.2    Bosch, H.3    Rouwendal, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.