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Volumn 57, Issue 2, 2005, Pages 285-301

Characterisation and expression of the pathway from UDP-glucose to UDP-xylose in differentiating tobacco tissue

Author keywords

Hemicellulose; Tobacco; UDP glucose dehydrogenase; UDP glucuronate decarboxylase; UDP xylose; Xylan; Xylogenesis

Indexed keywords

CLONING; DNA; ENZYME KINETICS; GLUCOSE; OXIDATION; PLANT CELL CULTURE; TISSUE; XYLOSE;

EID: 17644405273     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11103-004-7795-7     Document Type: Article
Times cited : (34)

References (51)
  • 2
    • 0036798592 scopus 로고    scopus 로고
    • Trends in lignin modification: A comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity
    • A. Anterola N.G. Lewis 2002 Trends in lignin modification: a comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity Phytochemistry 61 221 294
    • (2002) Phytochemistry , vol.61 , pp. 221-294
    • Anterola, A.1    Lewis, N.G.2
  • 3
    • 0026521505 scopus 로고
    • Expansion of the mammalian 3-beta-hydroxysteroid dehydrogenase/plant dehydroflavonol reductase superfamily to include a bacterial UDP-galactose-4-epimerase and open reading frames in vaccinia virus and fish lymphocystis disease virus
    • M.E. Baker R. Blaso 1992 Expansion of the mammalian 3-beta-hydroxysteroid dehydrogenase/plant dehydroflavonol reductase superfamily to include a bacterial UDP-galactose-4-epimerase and open reading frames in vaccinia virus and fish lymphocystis disease virus FEBS Letts. 301 89 93
    • (1992) FEBS Letts. , vol.301 , pp. 89-93
    • Baker, M.E.1    Blaso, R.2
  • 4
    • 0035834048 scopus 로고    scopus 로고
    • Functional cloning and characterisation of a UDP glucuronic acid decarboxylase: The pathogenic fungus Cryptococcus neoformanselucidates UDP-xylose synthesis
    • M. Bar-Peled C.L. Griffith T.L. Doering 2001 Functional cloning and characterisation of a UDP glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformanselucidates UDP-xylose synthesis Proc. Natl. Acad. Sci. USA 98 12003 12008
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12003-12008
    • Bar-Peled, M.1    Griffith, C.L.2    Doering, T.L.3
  • 5
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: A comaparison of nucleotide binding proteins
    • C.R. Bellamacina 1996 The nicotinamide dinucleotide binding motif: a comaparison of nucleotide binding proteins FASEB J. 10 1257 1269
    • (1996) FASEB J. , vol.10 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 6
    • 1142306035 scopus 로고    scopus 로고
    • Structure and expression profile of the sucrose synthase multigene family in Arabidopsis
    • S. Baud M.N. Vaultier C. Rochat 2004 Structure and expression profile of the sucrose synthase multigene family in Arabidopsis J. Exp. Bot. 55 397 409
    • (2004) J. Exp. Bot. , vol.55 , pp. 397-409
    • Baud, S.1    Vaultier, M.N.2    Rochat, C.3
  • 7
    • 0035127302 scopus 로고    scopus 로고
    • Proteomic analysis reveals a novel set of cell wall proteins in a transformed tobacco cell culture that synthesises secondary walls as determined by biochemical and morphological parameters
    • K.A. Blee E.R. Wheatley V.A. Bonham G.P. Mitchell D. Robertson A.R. Slabas M.M. Burrell P. Wojtaszek G.P. Bolwell 2001 Proteomic analysis reveals a novel set of cell wall proteins in a transformed tobacco cell culture that synthesises secondary walls as determined by biochemical and morphological parameters Planta 212 404 415
    • (2001) Planta , vol.212 , pp. 404-415
    • Blee, K.A.1    Wheatley, E.R.2    Bonham, V.A.3    Mitchell, G.P.4    Robertson, D.5    Slabas, A.R.6    Burrell, M.M.7    Wojtaszek, P.8    Bolwell, G.P.9
  • 8
    • 17744390997 scopus 로고    scopus 로고
    • Protein Purification from plant sources
    • (S. Roe (ed.), Oxford University Press
    • Bolwell, G.P. 2001. Protein Purification from plant sources. In: (S. Roe (ed.), Protein Purification Applications: A Practical Approach. Oxford University Press, pp. 135-158
    • (2001) Protein Purification Applications: A Practical Approach , pp. 135-158
    • Bolwell, G.P.1
  • 10
    • 0034643813 scopus 로고    scopus 로고
    • The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation
    • R.E. Campbell S.C. Mosimann I. Vande Rijn M.E. Tanner N.C.J. Strynadka 2000 The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation Biochemistry 39 7012 7023
    • (2000) Biochemistry , vol.39 , pp. 7012-7023
    • Campbell, R.E.1    Mosimann, S.C.2    Vande Rijn, I.3    Tanner, M.E.4    Strynadka, N.C.J.5
  • 12
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • P. Chomczynsky N. Sacchi 1987 Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction Anal. Biochem. 162 156 159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynsky, P.1    Sacchi, N.2
  • 13
    • 0033212957 scopus 로고    scopus 로고
    • Arabidopsis alcohol dehydrogenase expression in both shoots and roots is conditioned by root growth environment
    • H.J. Chung R.J. Ferl 1999 Arabidopsis alcohol dehydrogenase expression in both shoots and roots is conditioned by root growth environment Plant Physiol. 121 429 436
    • (1999) Plant Physiol. , vol.121 , pp. 429-436
    • Chung, H.J.1    Ferl, R.J.2
  • 14
    • 0017774540 scopus 로고
    • Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in sycamore and poplar
    • G. Dalessandro D.H. Northcote 1977 Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in sycamore and poplar Biochem. J. 162 267 279
    • (1977) Biochem. J. , vol.162 , pp. 267-279
    • Dalessandro, G.1    Northcote, D.H.2
  • 15
    • 0037188534 scopus 로고    scopus 로고
    • An Arabidopsis gene encoding an alpha-xylosyltransferase involved in xyloglucan biosynthesis
    • A. Faik N.J. Price N.V. Raikhel K. Keegstra 2002 An Arabidopsis gene encoding an alpha-xylosyltransferase involved in xyloglucan biosynthesis Proc. Natl. Acad. Sci. USA. 99 7797 7802
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 7797-7802
    • Faik, A.1    Price, N.J.2    Raikhel, N.V.3    Keegstra, K.4
  • 16
    • 51249166384 scopus 로고
    • Microprep protocol for extraction of DNA from tomato and other herbaceous plants
    • T.M. Fulton J. Chunwongse S.D. Tanksley 1995 Microprep protocol for extraction of DNA from tomato and other herbaceous plants Plant Mol. Biol. Rep. 13 207 209
    • (1995) Plant Mol. Biol. Rep. , vol.13 , pp. 207-209
    • Fulton, T.M.1    Chunwongse, J.2    Tanksley, S.D.3
  • 17
    • 0037297226 scopus 로고    scopus 로고
    • AtBXL1, a novel higher plant (Arabidopsis thaliana) putative beta-xylosidase gene, is involved in secondary cell wall metabolism and plant development
    • T. Goujon Z. Minic A. El Amrani O. Lerouxel E. Aletti C. Lapierre 2003 AtBXL1, a novel higher plant (Arabidopsis thaliana) putative beta-xylosidase gene, is involved in secondary cell wall metabolism and plant development Plant J. 33 677 690
    • (2003) Plant J. , vol.33 , pp. 677-690
    • Goujon, T.1    Minic, Z.2    El Amrani, A.3    Lerouxel, O.4    Aletti, E.5    Lapierre, C.6
  • 18
    • 0026195584 scopus 로고
    • Structure, expression, chromosomal location and product of the gene encoding ADH1 in petunia
    • R. Gregerson M. McLean M. Beld A.G.M. Gerats J. Strommer 1991 Structure, expression, chromosomal location and product of the gene encoding ADH1 in petunia Plant Mol. Biol. 17 37 48
    • (1991) Plant Mol. Biol. , vol.17 , pp. 37-48
    • Gregerson, R.1    McLean, M.2    Beld, M.3    Gerats, A.G.M.4    Strommer, J.5
  • 19
    • 0036918914 scopus 로고    scopus 로고
    • Biosynthesis of UDP-Xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, Encoding Soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms
    • A.D. Harper M. Bar-Peled 2002 Biosynthesis of UDP-Xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, Encoding Soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms Plant Physiol. 130 2188 2198
    • (2002) Plant Physiol. , vol.130 , pp. 2188-2198
    • Harper, A.D.1    Bar-Peled, M.2
  • 20
    • 0028361495 scopus 로고
    • UDP-glucose dehydrogenase from bovine liver-primary structure and relationships to other dehydrogenases
    • J. Hempel J. Perozich H. Romovacek A. Hinich I. Kuo D.S. Feingold 1994 UDP-glucose dehydrogenase from bovine liver-primary structure and relationships to other dehydrogenases Protein Sci. 3 1074 1080
    • (1994) Protein Sci. , vol.3 , pp. 1074-1080
    • Hempel, J.1    Perozich, J.2    Romovacek, H.3    Hinich, A.4    Kuo, I.5    Feingold, D.S.6
  • 22
    • 0037036123 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation
    • H. Johansson F. Sterky B. Amini J. Lundeberg L.A. Kleczkowski 2002 Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation Biochim. Biophys. Acta 1576 53 58
    • (2002) Biochim. Biophys. Acta , vol.1576 , pp. 53-58
    • Johansson, H.1    Sterky, F.2    Amini, B.3    Lundeberg, J.4    Kleczkowski, L.A.5
  • 23
    • 0017692274 scopus 로고
    • Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase
    • K.V. John J.S. Schutzbach H. Ankel 1977 Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase J. Biol. Chem. 252 8013 8017
    • (1977) J. Biol. Chem. , vol.252 , pp. 8013-8017
    • John, K.V.1    Schutzbach, J.S.2    Ankel, H.3
  • 24
    • 0036857412 scopus 로고    scopus 로고
    • Purification and cloning of UDP-D-glucuronate carboxy-lyase (UDP-D-xylose synthase) from pea seedlings
    • M. Kobayashi H. Nakagawa I. Suda I. Miyagawa T. Matoh 2002 Purification and cloning of UDP-D-glucuronate carboxy-lyase (UDP-D-xylose synthase) from pea seedlings Plant Cell Physiol. 43 1259 1265
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1259-1265
    • Kobayashi, M.1    Nakagawa, H.2    Suda, I.3    Miyagawa, I.4    Matoh, T.5
  • 25
    • 0033969179 scopus 로고    scopus 로고
    • Multiple path of sugar-sensing and a sugar/oxygen overlap for genes of sucrose and ethanol metabolism
    • K.E. Koch Z. Ying Y. Wu W.T. Avigne 2000 Multiple path of sugar-sensing and a sugar/oxygen overlap for genes of sucrose and ethanol metabolism J. Exp. Bot. 51 417 427
    • (2000) J. Exp. Bot. , vol.51 , pp. 417-427
    • Koch, K.E.1    Ying, Z.2    Wu, Y.3    Avigne, W.T.4
  • 26
    • 0034946568 scopus 로고    scopus 로고
    • A xylosyltransferase that synthesizes beta-(1->4)-xylans in wheat (Triticum aestivum L.) seedlings
    • H. Kuroyama Y. Tsumuraya 2001 A xylosyltransferase that synthesizes beta-(1->4)-xylans in wheat (Triticum aestivum L.) seedlings Planta 213 231 240
    • (2001) Planta , vol.213 , pp. 231-240
    • Kuroyama, H.1    Tsumuraya, Y.2
  • 29
    • 0019036715 scopus 로고
    • The C-5 hydrogen isotope-effect in myo-inositol 1-phosphate synthase as evidence for the myo-inositol oxidation-pathway
    • M.W. Loewus F.A. Loewus 1980 The C-5 hydrogen isotope-effect in myo-inositol 1-phosphate synthase as evidence for the myo-inositol oxidation-pathway Carbohydr. Res. 82 333 342
    • (1980) Carbohydr. Res. , vol.82 , pp. 333-342
    • Loewus, M.W.1    Loewus, F.A.2
  • 30
    • 0025429255 scopus 로고
    • Alcohol dehydrogenase gene expression in potato following elicitor and stress treatment
    • D.P. Matton P. Constabel N. Brisson 1990 Alcohol dehydrogenase gene expression in potato following elicitor and stress treatment Plant Mol. Biol. 14 775 783
    • (1990) Plant Mol. Biol. , vol.14 , pp. 775-783
    • Matton, D.P.1    Constabel, P.2    Brisson, N.3
  • 31
    • 0017335096 scopus 로고
    • UDP-apiose/UDP-xylose synthase. Subunit composition and binding studies
    • U. Matern H. Grisebach 1977 UDP-apiose/UDP-xylose synthase. Subunit composition and binding studies Eur. J. Biochem. 74 303 312
    • (1977) Eur. J. Biochem. , vol.74 , pp. 303-312
    • Matern, U.1    Grisebach, H.2
  • 32
    • 0000072518 scopus 로고
    • Cytokinin stress changes the developmental regulation of several defence-related genes in tobacco
    • J. Memelink J.H.C. Hoge R.A. Schilperoort 1987 Cytokinin stress changes the developmental regulation of several defence-related genes in tobacco EMBO J. 6 3579 3583
    • (1987) EMBO J. , vol.6 , pp. 3579-3583
    • Memelink, J.1    Hoge, J.H.C.2    Schilperoort, R.A.3
  • 34
    • 75449103970 scopus 로고    scopus 로고
    • Chemical analysis
    • J.E. Coligan, B.M. Dunn, H.L. Ploegh, D.W. Speicher and P.T. Wingfield, (Eds.), John Wiley and Sons, Inc. USA, Chapter 11.
    • Reim, D.F. and Speicher, D.W. 1997. Chemical analysis. In: J.E. Coligan, B.M. Dunn, H.L. Ploegh, D.W. Speicher and P.T. Wingfield, (Eds.), Current Protocols in Protein sciences. John Wiley and Sons, Inc. USA, Chapter 11.
    • (1997) Current Protocols in Protein Sciences
    • Reim, D.F.1    Speicher, D.W.2
  • 35
    • 0034863672 scopus 로고    scopus 로고
    • Molecular genetics of nucleotide sugar interconversion pathways in plants
    • W.D. Reiter G.F. Vanzin 2001 Molecular genetics of nucleotide sugar interconversion pathways in plants Plant Mol. Biol. 47 95 113
    • (2001) Plant Mol. Biol. , vol.47 , pp. 95-113
    • Reiter, W.D.1    Vanzin, G.F.2
  • 36
    • 0029103750 scopus 로고
    • Regulation of the enzymes of UDP-sugar metabolism during differentiation of French bean
    • D. Robertson I. Beech G.P. Bolwell 1995 Regulation of the enzymes of UDP-sugar metabolism during differentiation of French bean Phytochemistry 39 21 28
    • (1995) Phytochemistry , vol.39 , pp. 21-28
    • Robertson, D.1    Beech, I.2    Bolwell, G.P.3
  • 37
    • 0028898980 scopus 로고
    • Cell wall polysaccharide biosynthesis and related metabolismin elicitor-stressed cells of French bean (Phaseolus vulgaris L.)
    • D. Robertson B.A. McCormack G.P. Bolwell 1995 Cell wall polysaccharide biosynthesis and related metabolismin elicitor-stressed cells of French bean (Phaseolus vulgaris L.) Biochem. J. 306 745 750
    • (1995) Biochem. J. , vol.306 , pp. 745-750
    • Robertson, D.1    McCormack, B.A.2    Bolwell, G.P.3
  • 38
    • 0030064506 scopus 로고    scopus 로고
    • Inducible UDP-glucose dehydrogenase from French bean (Phaseolus vulgaris L.) locates to vascular tissue and has alcohol dehydrogenase activity
    • D. Robertson C. Smith G.P. Bolwell 1996 Inducible UDP-glucose dehydrogenase from French bean (Phaseolus vulgaris L.) locates to vascular tissue and has alcohol dehydrogenase activity Biochem. J. 313 311 317
    • (1996) Biochem. J. , vol.313 , pp. 311-317
    • Robertson, D.1    Smith, C.2    Bolwell, G.P.3
  • 39
    • 0027095610 scopus 로고
    • Partial purification of Golgi-bound arabinosyl transferase and two isoforms of xylosyl transferase from French Bean (Phaseolus vulgaris L.)
    • M.W. Rodgers G.P. Bolwell 1992 Partial purification of Golgi-bound arabinosyl transferase and two isoforms of xylosyl transferase from French Bean (Phaseolus vulgaris L.) Biochem. J. 288 817 822
    • (1992) Biochem. J. , vol.288 , pp. 817-822
    • Rodgers, M.W.1    Bolwell, G.P.2
  • 40
    • 2442434678 scopus 로고    scopus 로고
    • Nucleotide sugar interconversions and cell wall biosynthesis: How to bring the inside to the outside
    • G.J. Seifert 2004 Nucleotide sugar interconversions and cell wall biosynthesis: how to bring the inside to the outside Curr. Opp. Plant Biol. 7 277 284
    • (2004) Curr. Opp. Plant Biol. , vol.7 , pp. 277-284
    • Seifert, G.J.1
  • 41
    • 0033998513 scopus 로고    scopus 로고
    • Matrix polysaccharide precursors in Arabidopsis cell walls are synthesized by alternate pathways with organ-specific expression patterns
    • B. Seitz C. Klos M. Wurm R. Tenhaken 2000 Matrix polysaccharide precursors in Arabidopsis cell walls are synthesized by alternate pathways with organ-specific expression patterns Plant J. 21 537 546
    • (2000) Plant J. , vol.21 , pp. 537-546
    • Seitz, B.1    Klos, C.2    Wurm, M.3    Tenhaken, R.4
  • 42
    • 0036916853 scopus 로고    scopus 로고
    • Proteomic study of the soluble proteins of the unicellular cyanobacterium Synechocytis sp PCC6803 using automated matrix automated matrix-assisted laser desorption/ionization-time of flight peptide mass fingerprinting
    • W.J. Simon J.J. Hall I. Suzuki N. Murata A.R. Slabas 2002 Proteomic study of the soluble proteins of the unicellular cyanobacterium Synechocytis sp PCC6803 using automated matrix automated matrix-assisted laser desorption/ionization-time of flight peptide mass fingerprinting Proteomics 2 1735 1742
    • (2002) Proteomics , vol.2 , pp. 1735-1742
    • Simon, W.J.1    Hall, J.J.2    Suzuki, I.3    Murata, N.4    Slabas, A.R.5
  • 43
    • 0000854293 scopus 로고    scopus 로고
    • Genetic manipulation of alcohol dehydrogenase levels in ripening tomato fruit affects the balance of some flavor aldehydes and alcohols
    • J. Speirs E. Lee K. Holt K. Yong-Duk N. Steele Scott B. Loveys W. Schuch 1998 Genetic manipulation of alcohol dehydrogenase levels in ripening tomato fruit affects the balance of some flavor aldehydes and alcohols Plant Physiol 117 1047 1058
    • (1998) Plant Physiol , vol.117 , pp. 1047-1058
    • Speirs, J.1    Lee, E.2    Holt, K.3    Yong-Duk, K.4    Steele Scott, N.5    Loveys, B.6    Schuch, W.7
  • 44
    • 0031728483 scopus 로고    scopus 로고
    • Uridine 5′-diphosphate-glucose dehydrogenase from soybean nodules
    • D.C. Stewart L. Copeland 1998 Uridine 5′-diphosphate-glucose dehydrogenase from soybean nodules Plant Physiol. 116 349 355
    • (1998) Plant Physiol. , vol.116 , pp. 349-355
    • Stewart, D.C.1    Copeland, L.2
  • 45
    • 0033600769 scopus 로고    scopus 로고
    • Kinetic properties of UDP-glucose dehydrogenase from soybean nodules
    • D.C. Stewart L. Copeland 1999 Kinetic properties of UDP-glucose dehydrogenase from soybean nodules Plant Sci. 147 119 125
    • (1999) Plant Sci. , vol.147 , pp. 119-125
    • Stewart, D.C.1    Copeland, L.2
  • 46
    • 0019395149 scopus 로고
    • 2 stress on tomato alcohol dehydrogenase activity - Description of a second ADH coding gene
    • 2 stress on tomato alcohol dehydrogenase activity - description of a second ADH coding gene Biochem. Genet. 19 397 409
    • (1981) Biochem. Genet. , vol.19 , pp. 397-409
    • Tanksley, S.D.1    Jones, R.A.2
  • 47
    • 0030296227 scopus 로고    scopus 로고
    • Cloning of an enzyme that synthesises a key nucleotide sugar precursor of hemicellulose biosynthesis from soybean: UDP-glucose dehydrogenase
    • R. Tenhaken O. Thulke 1996 Cloning of an enzyme that synthesises a key nucleotide sugar precursor of hemicellulose biosynthesis from soybean: UDP-glucose dehydrogenase Plant Physiol. 112 1127 1134
    • (1996) Plant Physiol. , vol.112 , pp. 1127-1134
    • Tenhaken, R.1    Thulke, O.2
  • 48
    • 0036431530 scopus 로고    scopus 로고
    • Purification and kinetic properties of UDP-glucose dehydrogenase from sugarcane
    • W. Turner F.C. Botha 2002 Purification and kinetic properties of UDP-glucose dehydrogenase from sugarcane Arch. Biochem. Biophys. 407 209 216
    • (2002) Arch. Biochem. Biophys. , vol.407 , pp. 209-216
    • Turner, W.1    Botha, F.C.2
  • 50
    • 0036898058 scopus 로고    scopus 로고
    • Characterisation and immunolocation of an 87 kDa polypeptide associated with UDP-glucuronic acid decarboxylase activity from differentiating tobacco cells (Nicotiana tabacum L.)
    • E.R. Wheatley D.R. Davies G.P. Bolwell 2002 Characterisation and immunolocation of an 87 kDa polypeptide associated with UDP-glucuronic acid decarboxylase activity from differentiating tobacco cells (Nicotiana tabacum L.) Phytochemistry 61 771 780
    • (2002) Phytochemistry , vol.61 , pp. 771-780
    • Wheatley, E.R.1    Davies, D.R.2    Bolwell, G.P.3
  • 51
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding beta alpha beta fold in proteins, using an amino acid sequence fingerprint
    • R.K. Wierenga P. Terpstra W.G.J. Hol 1986 Prediction of the occurrence of the ADP-binding beta alpha beta fold in proteins, using an amino acid sequence fingerprint J. Mol. Biol. 187 101 107
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3


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