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Volumn , Issue , 2011, Pages 73-96

Enzymology of plant cell wall breakdown: An update

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EID: 84866494059     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-92740-4_6     Document Type: Chapter
Times cited : (28)

References (107)
  • 1
    • 0842330748 scopus 로고    scopus 로고
    • Inactivated enzymes as probes of the structure of arabinoxylans as observed by atomic force microscopy
    • Adams, E. L., Kroon, P. A., Williamson, G., Gilbert, H. J., and Morrisa, V. J. 2004. Inactivated enzymes as probes of the structure of arabinoxylans as observed by atomic force microscopy. Carbohydr. Res. 339: 579-590.
    • (2004) Carbohydr. Res. , vol.339 , pp. 579-590
    • Adams, E.L.1    Kroon, P.A.2    Williamson, G.3    Gilbert, H.J.4    Morrisa, V.J.5
  • 2
    • 0020826050 scopus 로고
    • Rumen bacterial and fungal degradation of Digitaria pentzii grown with or without sulfur
    • Akin, D. E., Gordon, G. L. R., and Hogan, J. P. 1983. Rumen bacterial and fungal degradation of Digitaria pentzii grown with or without sulfur. Appl. Environ. Microbiol. 46: 738-748.
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 738-748
    • Akin, D.E.1    Gordon, G.L.R.2    Hogan, J.P.3
  • 3
    • 0037226350 scopus 로고    scopus 로고
    • Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis
    • Arai, T., Araki, R., Tanaka, A., Karita, S., Kimura, T., Sakka, K. and Ohmya, K. 2003. Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis. J. Bacteriol. 185: 504-512.
    • (2003) J. Bacteriol. , vol.185 , pp. 504-512
    • Arai, T.1    Araki, R.2    Tanaka, A.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmya, K.7
  • 4
    • 84940981726 scopus 로고
    • Structure and function of plant cell walls
    • ed. J. Preiss San Diego: Academic Press
    • Bacic, Q., Harris, P. J., and Stone, B. A. 1988. Structure and function of plant cell walls. In The Biochemistry of plants, vol.14, ed. J. Preiss, pp. 297-371. San Diego: Academic Press.
    • (1988) Biochemistry of Plants , vol.14 , pp. 297-371
    • Bacic, Q.1    Harris, P.J.2    Stone, B.A.3
  • 5
    • 0035318377 scopus 로고    scopus 로고
    • Characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii
    • Baminger, U., Subramaniam, S. S., Renganathan, V., and Haltrich, D. 2001. Characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. App. Environ. Microbiol. 67 (4): 1766-1774.
    • (2001) App. Environ. Microbiol , vol.67 , Issue.4 , pp. 1766-1774
    • Baminger, U.1    Subramaniam, S.S.2    Renganathan, V.3    Haltrich, D.4
  • 6
    • 0027240897 scopus 로고
    • A laccase associated with lignifications in loblolly pine xylem
    • Bao, W., O'Malley, D. M., Whetten, R., and Sederoff, R. R. 1993. A laccase associated with lignifications in loblolly pine xylem. Science 260: 672-674.
    • (1993) Science , vol.260 , pp. 672-674
    • Bao, W.1    O'malley, D.M.2    Whetten, R.3    Sederoff, R.R.4
  • 7
    • 34547657101 scopus 로고    scopus 로고
    • Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: Biological implications for cell wall metabolism
    • Baumann, M. J., Eklo, J. M., Michel, G., Kallas, A. M., Teeri, T. T., Czjzek, M., and Brumer III, H. 2007. Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism. The Plant Cell 19: 1947-1963.
    • (2007) The Plant Cell , vol.19 , pp. 1947-1963
    • Baumann, M.J.1    Eklo, J.M.2    Michel, G.3    Kallas, A.M.4    Teeri, T.T.5    Czjzek, M.6    Brumer Iii, H.7
  • 10
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat, M. K. 2000. Cellulases and related enzymes in biotechnology. Biotechnol. Adv. 18: 35-383.
    • (2000) Biotechnol. Adv. , vol.18 , pp. 35-383
    • Bhat, M.K.1
  • 11
    • 0343036237 scopus 로고    scopus 로고
    • Endo-b-1, 4-xylanase families: Differences in catalytic proprieties
    • Biely, P., Vrsanská, M., Tenkanen, M., and Kluepfel, D. 1997. Endo-b-1, 4-xylanase families: differences in catalytic proprieties. J. Biotechnol. 57: 151-166.
    • (1997) J. Biotechnol. , vol.57 , pp. 151-166
    • Biely, P.1    Vrsanská, M.2    Tenkanen, M.3    Kluepfel, D.4
  • 12
    • 0033983751 scopus 로고    scopus 로고
    • Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ
    • Blum, D. L., Kataeva, I. A., Li, X. L., and Ljugdahl, L. G. 2000. Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ. J. Bacteriol. 182: 1346-1351.
    • (2000) J. Bacteriol. , vol.182 , pp. 1346-1351
    • Blum, D.L.1    Kataeva, I.A.2    Li, X.L.3    Ljugdahl, L.G.4
  • 13
    • 0034747705 scopus 로고    scopus 로고
    • Comparison of three fungal laccases from Rigodoporus lignosus and Pleurotus astreatus: Correlation between conformational changes and catalytic activity
    • Bonomo, R. P., Cennamo, G., Purrello, R., Santoro, A. M., and Zappala, R. 2001. Comparison of three fungal laccases from Rigodoporus lignosus and Pleurotus astreatus: correlation between conformational changes and catalytic activity. J. Inorg. Chem. 83: 67-73.
    • (2001) J. Inorg. Chem. , vol.83 , pp. 67-73
    • Bonomo, R.P.1    Cennamo, G.2    Purrello, R.3    Santoro, A.M.4    Zappala, R.5
  • 15
    • 0025813571 scopus 로고
    • Isolation and characterization of p-coumaroyl esterase from the anaerobic fungus Neocallimastix strain MC-2
    • Borneman, W. S., Ljungdahl, L. G., Hartley, R. D., and Akin, D. E. 1991. Isolation and characterization of p-coumaroyl esterase from the anaerobic fungus Neocallimastix strain MC-2. Appl. Environ. Microbiol. 57: 2337-2344.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2337-2344
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 16
    • 0026448264 scopus 로고
    • Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2
    • Borneman, W. S., Ljungdahl, L. G., Hartley, R. D., and Akin, D. E. 1992. Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2. Appl. Environ. Microbiol. 58: 3762-3766.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3762-3766
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 17
    • 48549100257 scopus 로고    scopus 로고
    • Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization
    • Brotman, Y., Briff, E., Viterbo, A., Chet, I. 2008. Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization. Plant Physiology 147: 779-784.
    • (2008) Plant Physiology , vol.147 , pp. 779-784
    • Brotman, Y.1    Briff, E.2    Viterbo, A.3    Chet, I.4
  • 18
    • 0034082690 scopus 로고    scopus 로고
    • Expansive growth of plant cell walls
    • Cosgrove, D. J. 2000. Expansive growth of plant cell walls. Plant Physiol. Biochem. 38: 109-124.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 109-124
    • Cosgrove, D.J.1
  • 19
    • 0022051942 scopus 로고
    • Cellulases: Production, properties and applications
    • Coughlan, M. P. 1985. Cellulases: production, properties and applications. Biochem. Soc. Trans. 13: 405-406.
    • (1985) Biochem. Soc. Trans. , vol.13 , pp. 405-406
    • Coughlan, M.P.1
  • 20
    • 0001791718 scopus 로고
    • Towards an understanding of the mechanism of action of main chain cleaving xylnases
    • eds J. Visser, J. G. Beldman, M. A. K. Someren, A. G. J. van Voragen Amsterdam: Elsevier Science
    • Coughlan, M. P. 1992. Towards an understanding of the mechanism of action of main chain cleaving xylnases. In Xylans and xylanases, eds J. Visser, J. G. Beldman, M. A. K. Someren, A. G. J. van Voragen, pp. 111-139. Amsterdam: Elsevier Science.
    • (1992) Xylans and Xylanases , pp. 111-139
    • Coughlan, M.P.1
  • 23
    • 0030829984 scopus 로고    scopus 로고
    • Laccase activity could contribute to cell-wall reconstitution of regenerating protoplasts
    • de Marco, A. and Roubelakis-Angelakis, K. A. 1997. Laccase activity could contribute to cell-wall reconstitution of regenerating protoplasts. Phytochem. 46: 421-425.
    • (1997) Phytochem. , vol.46 , pp. 421-425
    • De Marco, A.1    Roubelakis-Angelakis, K.A.2
  • 24
    • 0037364791 scopus 로고    scopus 로고
    • Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes, relevance for industrial production
    • de Vries, R. P. 2003. Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes, relevance for industrial production. Appl. Micorbiol. Biotechnol. 61: 10-20.
    • (2003) Appl. Micorbiol. Biotechnol. , vol.61 , pp. 10-20
    • De Vries, R.P.1
  • 25
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries, R. P., and Visser, J. 2001. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 65: 497-522.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 26
    • 0037090961 scopus 로고    scopus 로고
    • The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds
    • de Vries, R. P., van Kuyk, P. A., Kester, H. C. M., and Visser, J. 2002. The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem. J. 363: 377-386.
    • (2002) Biochem. J. , vol.363 , pp. 377-386
    • De Vries, R.P.1    Van Kuyk, P.A.2    Kester, H.C.M.3    Visser, J.4
  • 28
    • 0030570825 scopus 로고    scopus 로고
    • A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase
    • Eggert, C., Temp, U., Dean, J. F. D., Eriksson, K. E. L. 1996. A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase. FEBS Lett. 391: 144-148.
    • (1996) FEBS Lett. , vol.391 , pp. 144-148
    • Eggert, C.1    Temp, U.2    Dean, J.F.D.3    Eriksson, K.E.L.4
  • 30
    • 24644517613 scopus 로고    scopus 로고
    • Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger
    • Faulds, C. B., Molina, R., Gonzalez, R., Husband, F., Juge, N., Sanz-Aparicio, J., and Hermoso. J. A. 2005. Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger. FEBS J. 272: 4362-4371.
    • (2005) FEBS J. , vol.272 , pp. 4362-4371
    • Faulds, C.B.1    Molina, R.2    Gonzalez, R.3    Husband, F.4    Juge, N.5    Sanz-Aparicio, J.6    Hermoso, J.A.7
  • 31
    • 0002309012 scopus 로고    scopus 로고
    • Hemicellulases and biotechnology
    • ed. S. G. Pandalai Trivandrum: Research Signpost
    • Filho, E. X. F. Hemicellulases and biotechnology. 1998. In Recent research developments in microbiology, ed. S. G. Pandalai, pp. 165-176. Trivandrum: Research Signpost.
    • (1998) Recent Research Developments in Microbiology , pp. 165-176
    • Filho, E.X.F.1
  • 32
    • 1042278607 scopus 로고    scopus 로고
    • Primary cell wall metabolism: Tracking the careers of wall polymers in living plant cells
    • Fry, S. C. 2003. Primary cell wall metabolism: tracking the careers of wall polymers in living plant cells. New phytologist. 161: 641-675.
    • (2003) New Phytologist. , vol.161 , pp. 641-675
    • Fry, S.C.1
  • 34
    • 0032867401 scopus 로고    scopus 로고
    • Two cellobiohydrolasesencoding genes from Aspergillus niger require D-xylose and the xylanolitic transcriptional activator XlnR for their expression
    • Gielkens, M. M. C., Dekkers, E., Visser, J., and de Graaff, L. H. 1999. Two cellobiohydrolasesencoding genes from Aspergillus niger require D-xylose and the xylanolitic transcriptional activator XlnR for their expression. Appl. Environ. Microbiol. 65: 4340-4345.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4340-4345
    • Gielkens, M.M.C.1    Dekkers, E.2    Visser, J.3    De Graaff, L.H.4
  • 35
    • 0030295290 scopus 로고    scopus 로고
    • Mannan-degrading enzymes from Sclerotium rolfsii: Characterization and synergism of two endo b-mannanase and a b-mannosidase
    • Gübitz, G. M., Hayn, M., Sommerauer, M., and Steiner, W. 1996. Mannan-degrading enzymes from Sclerotium rolfsii: Characterization and synergism of two endo b-mannanase and a b-mannosidase. Biores. Technol. 58: 127-135.
    • (1996) Biores. Technol. , vol.58 , pp. 127-135
    • Gübitz, G.M.1    Hayn, M.2    Sommerauer, M.3    Steiner, W.4
  • 36
    • 0000983731 scopus 로고
    • Phenolic constituents of plant cell walls and wall biodegradability
    • eds. N. G. Lewis, M. G. Paice Washington: American Chemical Society
    • Hartley, R. D., and Ford, C. W. 1989. Phenolic constituents of plant cell walls and wall biodegradability. In Plant cell wall polymers: biogenesis and biodegradation, eds. N. G. Lewis, M. G. Paice, pp. 137-145. Washington: American Chemical Society.
    • (1989) Plant Cell Wall Polymers: Biogenesis and Biodegradation , pp. 137-145
    • Hartley, R.D.1    Ford, C.W.2
  • 37
    • 45149138620 scopus 로고
    • Cross-linking of cell wall arabinoxylans in graminaceous plants
    • Hartley, R. D., Morrison, W. H., Himmelsbach, D. S., and Borneman, W. S. 1990. Cross-linking of cell wall arabinoxylans in graminaceous plants. Phytochem. 12: 3705-3709.
    • (1990) Phytochem. , vol.12 , pp. 3705-3709
    • Hartley, R.D.1    Morrison, W.H.2    Himmelsbach, D.S.3    Borneman, W.S.4
  • 38
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 39
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 40
    • 0026579460 scopus 로고
    • Purification and characterization of an a-L-arabinofuranosidase from Butyrivibrio fibrisolvens GS113
    • Hespell, R. B., and O'Bryan, P. J. 1992. Purification and characterization of an a-L-arabinofuranosidase from Butyrivibrio fibrisolvens GS113. Appl. Environ. Microbiol. 58: 1082-1108.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1082-1108
    • Hespell, R.B.1    O'bryan, P.J.2
  • 41
    • 0033179622 scopus 로고    scopus 로고
    • Cellulase for commodity products from cellulosic biomass
    • Himmel, M. E., Ruth, M. F., and Wyman, C. E. 1999. Cellulase for commodity products from cellulosic biomass. Curr. Opin. Biotechnol. 10: 358-364.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 358-364
    • Himmel, M.E.1    Ruth, M.F.2    Wyman, C.E.3
  • 42
    • 0026245034 scopus 로고
    • Isolation and characterization of a diferuloyl arabinoxylan hexasaccharide from bamboo shoot cell-walls
    • Ishii, T. 1991. Isolation and characterization of a diferuloyl arabinoxylan hexasaccharide from bamboo shoot cell-walls. Carbohydr. Res. 219: 15-22.
    • (1991) Carbohydr. Res. , vol.219 , pp. 15-22
    • Ishii, T.1
  • 43
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: A review
    • Jayani, R. S., Saxena, S., and Gupta, R. 2005. Microbial pectinolytic enzymes: A review. Process Biochem. 40: 2931-2944.
    • (2005) Process Biochem. , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 44
    • 10044225564 scopus 로고    scopus 로고
    • Production of cellulases and hemicellulases by three Penicillium species: Effect of substrate and evaluation of cellulase adsorption by capillary electrophoresis
    • Jorgensen, H., Morkeberg, A., Krogh, K. B. R., and Olsson, L. 2005. Production of cellulases and hemicellulases by three Penicillium species: effect of substrate and evaluation of cellulase adsorption by capillary electrophoresis. Enzyme Microbiol. Technol. 36: 42-48.
    • (2005) Enzyme Microbiol. Technol. , vol.36 , pp. 42-48
    • Jorgensen, H.1    Morkeberg, A.2    Krogh, K.B.R.3    Olsson, L.4
  • 45
    • 24944461039 scopus 로고    scopus 로고
    • Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources
    • Juhász, T., Szengyel, Z., Réczey, K., Siika-Aho, M., and Viikari, L. 2005. Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources. Process Biochem. 40: 3519-3525.
    • (2005) Process Biochem. , vol.40 , pp. 3519-3525
    • Juhász, T.1    Szengyel, Z.2    Réczey, K.3    Siika-Aho, M.4    Viikari, L.5
  • 46
    • 52049106382 scopus 로고    scopus 로고
    • The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1
    • Karkehabadi, S., Hansson, H., Piens, K., Mitchinson, C., and Sandgren, M. 2008. The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1.6 A resolution. J. Mol. Biol. 383: 144-154.
    • (2008) 6 A Resolution. J. Mol. Biol. , vol.383 , pp. 144-154
    • Karkehabadi, S.1    Hansson, H.2    Piens, K.3    Mitchinson, C.4    Sandgren, M.5
  • 48
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinase in the commercial sector: A review
    • Kashyap, D. R., Vohra, P. K., Chopra, S., Tewari, R. 2001. Applications of pectinase in the commercial sector: a review. Biores. Technol. 77: 215-227.
    • (2001) Biores. Technol. , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 51
    • 0030847038 scopus 로고    scopus 로고
    • Methyl phenylalkanoates as substrates to probe the active sites of esterases
    • Kroon, P. A., Faulds, C. B., Brézillon, C., and Williamson, G. 1997. Methyl phenylalkanoates as substrates to probe the active sites of esterases. Eur. J. Biochem. 248: 245-251.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 245-251
    • Kroon, P.A.1    Faulds, C.B.2    Brézillon, C.3    Williamson, G.4
  • 52
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • Kumar, R., Singh, S., Singh, O. V. 2008. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J. Ind. Microbiol. Biotechnol. 35: 377-391.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 53
    • 0038754897 scopus 로고    scopus 로고
    • Cellulosic fuel ethanol-alternative fermentation process designs with wild-type and recombinant Zymomonas mobilis
    • Lawford, H. G., and Rousseau, J. D. 2003. Cellulosic fuel ethanol-alternative fermentation process designs with wild-type and recombinant Zymomonas mobilis. Appl. Biochem. Biotechnol. 106: 457-469.
    • (2003) Appl. Biochem. Biotechnol. , vol.106 , pp. 457-469
    • Lawford, H.G.1    Rousseau, J.D.2
  • 55
    • 33751501534 scopus 로고    scopus 로고
    • Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid
    • Levasseur, A., Saloheimo, M., Navarro, D., Andberg, M., Monot, F., Nakari-Setälä, T., Asther, M., and Record, E. 2006. Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid. Appl. Microbiol. Biotechnol. 73: 872-880.
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , pp. 872-880
    • Levasseur, A.1    Saloheimo, M.2    Navarro, D.3    Andberg, M.4    Monot, F.5    Nakari-Setälä, T.6    Asther, M.7    Record, E.8
  • 56
    • 31544449727 scopus 로고    scopus 로고
    • Estimation of p-coumaric acid as a metabolite of E-6-O-p-coumaroyl scandoside methyl ester in rat plasma by HPLC and its application to a pharmacokinetic study
    • Liu, K., Yan, L., Yao, G., and Guo, X. 2006. Estimation of p-coumaric acid as a metabolite of E-6-O-p-coumaroyl scandoside methyl ester in rat plasma by HPLC and its application to a pharmacokinetic study. J. Chrom. B 831: 303-306.
    • (2006) J. Chrom. B , vol.831 , pp. 303-306
    • Liu, K.1    Yan, L.2    Yao, G.3    Guo, X.4
  • 58
    • 0037255672 scopus 로고    scopus 로고
    • Regulation of gene expression in industrial fungi: Trichoderma
    • Mach, R. L., and Zeilinger, S. 2003. Regulation of gene expression in industrial fungi: Trichoderma. Appl. Microbiol. Biotechnol. 60: 515-522.
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 515-522
    • Mach, R.L.1    Zeilinger, S.2
  • 59
    • 58549087138 scopus 로고    scopus 로고
    • Biochemical properties of a b-mannanase and a b-xylanase produced by Ceriporiopsis subvermispora during biopulping conditions
    • Magalhães, P., Milagres, A. M. F. 2009. Biochemical properties of a b-mannanase and a b-xylanase produced by Ceriporiopsis subvermispora during biopulping conditions. Int. Biodeterior. Biodegradation 63: 191-195.
    • (2009) Int. Biodeterior. Biodegradation , vol.63 , pp. 191-195
    • Magalhães, P.1    Milagres, A.M.F.2
  • 60
    • 0022054102 scopus 로고
    • Applications of cellulases
    • Mandels, M. 1985. Applications of cellulases. Biochem. Soc. Trans. 13: 414-415.
    • (1985) Biochem. Soc. Trans. , vol.13 , pp. 414-415
    • Mandels, M.1
  • 61
    • 0030812766 scopus 로고    scopus 로고
    • Cellobiose Dehydrogenase, an Active Agent in Cellulose Depolymerization
    • Manfield, S. D., de Jong, E., and Saddler, J. N. 1997. Cellobiose Dehydrogenase, an Active Agent in Cellulose Depolymerization. App. Environ. Microbiol. 63(10): 3804-3809.
    • (1997) App. Environ. Microbiol. , vol.63 , Issue.10 , pp. 3804-3809
    • Manfield, S.D.1    De Jong, E.2    Saddler, J.N.3
  • 62
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: New functions for an old enzyme
    • Mayer, A. M., and Staples, R. C. 2002. Laccase: new functions for an old enzyme. Phytochem. 60: 551-565.
    • (2002) Phytochem. , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 63
    • 0036247869 scopus 로고    scopus 로고
    • The performance of fungal xylan-degrading enzyme preparations in elemental chlorine-free bleaching for Eucalyptus pulp
    • Medeiros, R. G., Silva Jr, F. G., Salles, B. C., Estelles, R. S., and Filho, E. X. F. 2002. The performance of fungal xylan-degrading enzyme preparations in elemental chlorine-free bleaching for Eucalyptus pulp. J. Ind. Microbiol. Biotechnol. 28: 204-206.
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.28 , pp. 204-206
    • Medeiros, R.G.1    Silva Jr., F.G.2    Salles, B.C.3    Estelles, R.S.4    Filho, E.X.F.5
  • 64
    • 0025058305 scopus 로고
    • The blue copper oxidases, ascorbate oxidase, laccase and ceruloplasmin: Modeling and structural relationships
    • Messerschmidt, A., and Huber, R. 1990. The blue copper oxidases, ascorbate oxidase, laccase and ceruloplasmin: modeling and structural relationships. Eur. J. Biochem. 187: 341-352.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 65
    • 33749574354 scopus 로고    scopus 로고
    • Plant glycoside hydrolases involved in cell wall polysaccharide degradation
    • Minic, Z., and Jouanin, L. 2006. Plant glycoside hydrolases involved in cell wall polysaccharide degradation. Plant Physiol. Biochem. 44: 435-449.
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 435-449
    • Minic, Z.1    Jouanin, L.2
  • 66
    • 7244254401 scopus 로고    scopus 로고
    • Crystal structure of a family 54 a-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose
    • Miyanaga, A., Koseki, T., Matsuzawa, H., Wakagi, T., Shoun, H., and Fushinobu, S. 2004. Crystal structure of a family 54 a-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J. Biol. Chem. 279: 44907-44914.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44907-44914
    • Miyanaga, A.1    Koseki, T.2    Matsuzawa, H.3    Wakagi, T.4    Shoun, H.5    Fushinobu, S.6
  • 67
    • 42649129680 scopus 로고    scopus 로고
    • An overview of mannan structure and mannandegrading enzyme systems
    • Moreira, L. R. S., and Filho, E. X. F. 2008. An overview of mannan structure and mannandegrading enzyme systems. Appl. Microbiol. Biotechnol. 79(2): 165-178.
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , Issue.2 , pp. 165-178
    • Moreira, L.R.S.1    Filho, E.X.F.2
  • 68
    • 0032615038 scopus 로고    scopus 로고
    • Reaction kinetics, molecular action, and mechanisms of cellulolytic proteins
    • Mosier N., Hall, P., Ladisch, C. M., and Ladisch, M. R. 1999. Reaction kinetics, molecular action, and mechanisms of cellulolytic proteins. Adv. Biochem. Eng. Biotechnol. 65: 23-39.
    • (1999) Adv. Biochem. Eng. Biotechnol. , vol.65 , pp. 23-39
    • Mosier, N.1    Hall, P.2    Ladisch, C.M.3    Ladisch, M.R.4
  • 69
    • 33644789042 scopus 로고    scopus 로고
    • A-L-Arabinofuranosidases: The potential applications in biotechnology
    • Numan, M. T., and Bhosle, N. B. 2006. a-L-Arabinofuranosidases: the potential applications in biotechnology. J. Ind. Microbiol. Biotechnol. 33: 247-260.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 247-260
    • Numan, M.T.1    Bhosle, N.B.2
  • 71
    • 0036616389 scopus 로고    scopus 로고
    • Biodegradation and biological treatments of cellulose, hemicellulose and lignin: An overview
    • Pérez, J., Muñoz-Dorado, J., de La Rubia, T., and Martínez, J. 2002. Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview. Int. Microbiol. 5: 53-63.
    • (2002) Int. Microbiol. , vol.5 , pp. 53-63
    • Pérez, J.1    Muñoz-Dorado, J.2    De La Rubia, T.3    Martínez, J.4
  • 72
    • 0009866976 scopus 로고
    • Enzymatic detoxication of stilbenes by Botrytis cinerea and inhibition by grape berries proanthrocyanidins
    • eds K. Verhoeff, N. E. Malathrakis, B. Williamson Wageningen: Pudoc Scientific
    • Pezet, R., Pont, V., and Hoang-Van, K. 1992. Enzymatic detoxication of stilbenes by Botrytis cinerea and inhibition by grape berries proanthrocyanidins. In Recent Advances in Botrytis Research, eds K. Verhoeff, N. E. Malathrakis, B. Williamson, pp. 87-92. Wageningen: Pudoc Scientific.
    • (1992) Recent Advances in Botrytis Research , pp. 87-92
    • Pezet, R.1    Pont, V.2    Hoang-Van, K.3
  • 73
    • 34347354383 scopus 로고    scopus 로고
    • Cellulases from two Penicillium sp strains isolated from subtropical forest soil: Production and characterization
    • Picart, P., Diaz, P., and Pastor, F. I. J. 2007. Cellulases from two Penicillium sp. strains isolated from subtropical forest soil: production and characterization. Lett. Appl. Micobiol. 45: 108-113.
    • (2007) Lett. Appl. Micobiol. , vol.45 , pp. 108-113
    • Picart, P.1    Diaz, P.2    Pastor, F.I.J.3
  • 75
    • 84865163667 scopus 로고    scopus 로고
    • Glycosyl hydrolase genes and enzymes of Neurospora crassa
    • Radford, A. 2006. Glycosyl hydrolase genes and enzymes of Neurospora crassa. Fungal Gen. Newsletter 53: 12-14.
    • (2006) Fungal Gen. Newsletter , vol.53 , pp. 12-14
    • Radford, A.1
  • 76
    • 0026698666 scopus 로고
    • Isolation and characterisation of a cellulose-growth-specific gene from Agaricus bisporus
    • Raguz, S., Yague, E., Wood, D. A., Thurston, C. F. 1992. Isolation and characterisation of a cellulose-growth-specific gene from Agaricus bisporus. Gene (Amst.) 119: 183-190.
    • (1992) Gene (Amst.) , vol.119 , pp. 183-190
    • Raguz, S.1    Yague, E.2    Wood, D.A.3    Thurston, C.F.4
  • 77
    • 0038434063 scopus 로고    scopus 로고
    • Substrate specificity of the a-L-arabinofuranosidase from Rhizomucor pusillus HHT-1
    • Rahman, S. A. K. M., Kato, K., Kawai, S., and Takamizawa, K. 2003. Substrate specificity of the a-L-arabinofuranosidase from Rhizomucor pusillus HHT-1. Carbohydr. Res. 338: 1469-1476.
    • (2003) Carbohydr. Res. , vol.338 , pp. 1469-1476
    • Rahman, S.A.K.M.1    Kato, K.2    Kawai, S.3    Takamizawa, K.4
  • 78
    • 0029117332 scopus 로고
    • Lignin-ferulate cross-links in grasses: Active incorporation of ferulate polysaccharides esters into ryegrass lignins
    • Ralph J., Grabber, J. H., Hatfield, R. D. 1995. Lignin-ferulate cross-links in grasses: active incorporation of ferulate polysaccharides esters into ryegrass lignins. Carbohydr. Res. 275: 167-178.
    • (1995) Carbohydr. Res. , vol.275 , pp. 167-178
    • Ralph, J.1    Grabber, J.H.2    Hatfield, R.D.3
  • 80
    • 0017221817 scopus 로고
    • History of cellulose program at the US Army Natick development centre
    • Reese, E. T. 1976. History of cellulose program at the US Army Natick development centre. Biotechnol. Bioeng. Symp. 6: 9-20.
    • (1976) Biotechnol. Bioeng. Symp. , vol.6 , pp. 9-20
    • Reese, E.T.1
  • 81
    • 0036953722 scopus 로고    scopus 로고
    • The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: Current perspectives and a new unifying nomenclature
    • Rose, J. K., Braan, J., Fry, S. C., and Nishitani, K. 2002. The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature. Plant Cell Physiol. 43: 1421-1435.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1421-1435
    • Rose, J.K.1    Braan, J.2    Fry, S.C.3    Nishitani, K.4
  • 83
    • 0034253281 scopus 로고    scopus 로고
    • A-L-Arabinofuranosidases: Biochemistry, molecular biology and application in biotechnology
    • Saha, B. C. 2000. a-L-Arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotech. Adv. 18: 403-423.
    • (2000) Biotech. Adv. , vol.18 , pp. 403-423
    • Saha, B.C.1
  • 85
    • 0031975343 scopus 로고    scopus 로고
    • Purification and characterization of a novel thermostable a-L-arabinofuranosidase from a color-variant strain of a Aureobasidium pullulans
    • Saha, B. C., and Bothast, R. J. 1998. Purification and characterization of a novel thermostable a-L-arabinofuranosidase from a color-variant strain of a Aureobasidium pullulans. Appl. Environ. Microbiol. 64: 216-220.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 216-220
    • Saha, B.C.1    Bothast, R.J.2
  • 86
    • 0036046037 scopus 로고    scopus 로고
    • Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials
    • Saloheimo, M., Paloheimo, M., Hakola, S., Pere, J., Swanson, B., Nyyssönen, E., Bhatia, A., Ward, M., and Penttilä, M. 2002. Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur. J. Biochem. 269: 4202-4211.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4202-4211
    • Saloheimo, M.1    Paloheimo, M.2    Hakola, S.3    Pere, J.4    Swanson, B.5    Nyyssönen, E.6    Bhatia, A.7    Ward, M.8    Penttilä, M.9
  • 87
    • 0030669760 scopus 로고    scopus 로고
    • CDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast
    • Saloheiomo, M., Nakari-Setala, T., Tenaken, M., and Penttila, M. 1997. cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast. Eur. J. Biochem. 249: 584-591.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 584-591
    • Saloheiomo, M.1    Nakari-Setala, T.2    Tenaken, M.3    Penttila, M.4
  • 88
    • 0033059228 scopus 로고    scopus 로고
    • Ferulic acid and diferulic acids as components of sugar-beet pectins and maize bran heteroxylans J
    • Saulnier, L., and Thibault, J. F. 1999. Ferulic acid and diferulic acids as components of sugar-beet pectins and maize bran heteroxylans J. Sci. Food Agric. 79: 396-402.
    • (1999) Sci. Food Agric. , vol.79 , pp. 396-402
    • Saulnier, L.1    Thibault, J.F.2
  • 89
    • 46549102057 scopus 로고
    • Ether linkage between phenolic acids and lignin fractions from wheat straw
    • Scalbert, A., Monties, B., Lallemand, J. Y., Guittet, E., and Rolando, C. 1985. Ether linkage between phenolic acids and lignin fractions from wheat straw. Phytochem. 24: 1359-1362.
    • (1985) Phytochem. , vol.24 , pp. 1359-1362
    • Scalbert, A.1    Monties, B.2    Lallemand, J.Y.3    Guittet, E.4    Rolando, C.5
  • 90
    • 0037070548 scopus 로고    scopus 로고
    • The identification of the acid-base catalyst of a-arabinofuranosidase from Geobacillus stearothermopuhilus T-6, a family 51 glycoside hydrolase
    • Shallom, D., Belakhov, V., Solomon, D., Gilead-Gropper, S., Baasov, T., Shoham, G., and Shohama, Y. 2002. The identification of the acid-base catalyst of a-arabinofuranosidase from Geobacillus stearothermopuhilus T-6, a family 51 glycoside hydrolase. FEBS Lett. 514: 163-167.
    • (2002) FEBS Lett. , vol.514 , pp. 163-167
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Gilead-Gropper, S.4    Baasov, T.5    Shoham, G.6    Shohama, Y.7
  • 91
    • 77949644999 scopus 로고    scopus 로고
    • Plant cell wall as substrate for production of enzymes with industrial applications
    • Siqueira, F.G.S. and Filho, E. X. F. 2010. Plant cell wall as substrate for production of enzymes with industrial applications. MROC 7: 54-60.
    • (2010) MROC , vol.7 , pp. 54-60
    • Siqueira, F.G.S.1    Filho, E.X.F.2
  • 92
    • 70449527713 scopus 로고    scopus 로고
    • Cellulase production from Aspergillus niger MS82: Effect of temperature and pH
    • Sohail, M., Siddiqi, R., Ahmad, A., and Khan, S. A. 2009. Cellulase production from Aspergillus niger MS82: effect of temperature and pH. N Biotechnol. 25: 437-441.
    • (2009) N Biotechnol. , vol.25 , pp. 437-441
    • Sohail, M.1    Siddiqi, R.2    Ahmad, A.3    Khan, S.A.4
  • 93
    • 0027914978 scopus 로고
    • Electronic structure contributions to function in bioinorganic chemistry
    • Solomon, E. I., and Lowery, M. D. 1993. Electronic structure contributions to function in bioinorganic chemistry. Science. 259: 1575-1581.
    • (1993) Science , vol.259 , pp. 1575-1581
    • Solomon, E.I.1    Lowery, M.D.2
  • 94
    • 14544285489 scopus 로고    scopus 로고
    • Efficiencies of designed enzyme combinations in releasing arabinose and xylose from wheat arabinoxylan in an industrial ethanol fermentation residue
    • Sorensen, H. R., Pedersen, S., Vikso-Nielsen, A., Meyer, A. S. 2005. Efficiencies of designed enzyme combinations in releasing arabinose and xylose from wheat arabinoxylan in an industrial ethanol fermentation residue. Enzyme Microb. Technol. 36: 773-784.
    • (2005) Enzyme Microb. Technol. , vol.36 , pp. 773-784
    • Sorensen, H.R.1    Pedersen, S.2    Vikso-Nielsen, A.3    Meyer, A.S.4
  • 95
    • 0035983948 scopus 로고    scopus 로고
    • Gibberellic acid, synthetic auxins, and ethylene differentially modulate a-L-arabinofuranosidase activities in antisense 1-aminocyclopropane-1-carboxylic acid synthase Tomato Pericarp
    • Sozzi, G. O., Greve, L. C., Prody, G. A., and Labavitch, J. M. 2002. Gibberellic acid, synthetic auxins, and ethylene differentially modulate a-L-arabinofuranosidase activities in antisense 1-aminocyclopropane-1-carboxylic acid synthase Tomato Pericarp. Discs. Plant Physiol. 129: 1330-1340.
    • (2002) Discs. Plant Physiol. , vol.129 , pp. 1330-1340
    • Sozzi, G.O.1    Greve, L.C.2    Prody, G.A.3    Labavitch, J.M.4
  • 96
    • 0032214527 scopus 로고    scopus 로고
    • Immobilization of the glycosidases: A-L-arabinofuranosidase and b-D-glucopyranosidase from Aspergillus niger on a chitosan derivative to increase the aroma of wine
    • Spagna, G., Andreani, F., Salatelli, E., Romagnoli, D., Casarini, D., and Pifferi, P. G. 1998. Immobilization of the glycosidases: a-L- arabinofuranosidase and b-D-glucopyranosidase from Aspergillus niger on a chitosan derivative to increase the aroma of wine. Part II. Enzyme Microb. Technol. 23: 413-421.
    • (1998) Part II. Enzyme Microb. Technol. , vol.23 , pp. 413-421
    • Spagna, G.1    Andreani, F.2    Salatelli, E.3    Romagnoli, D.4    Casarini, D.5    Pifferi, P.G.6
  • 98
    • 14544302286 scopus 로고    scopus 로고
    • Comparison of mesophilic and thermophilic feruloyl esterases: Characterization of their substrate specificity for methyl phenylalkanoates
    • Topakas, E., Christakopoulos, P, and Faulds, C. B. 2005. Comparison of mesophilic and thermophilic feruloyl esterases: characterization of their substrate specificity for methyl phenylalkanoates. J. Biotechnol. 115: 355-366.
    • (2005) J. Biotechnol. , vol.115 , pp. 355-366
    • Topakas, E.1    Christakopoulos, P.2    Faulds, C.B.3
  • 99
    • 33947214919 scopus 로고    scopus 로고
    • Microbial production, characterization and applications of feruloyl esterases
    • Topakas, E.,Vafiadi, C., Christakopoulos, P. 2007. Microbial production, characterization and applications of feruloyl esterases. Proc. Biochem. 42: 497-509.
    • (2007) Proc. Biochem. , vol.42 , pp. 497-509
    • Topakas, E.1    Vafiadi, C.2    Christakopoulos, P.3
  • 100
    • 34147150667 scopus 로고    scopus 로고
    • Potential and utilization of thermophiles and thermostable enzymes in biorefining
    • Turner, P., Mamo, G., Karlsson, E. N. 2007. Potential and utilization of thermophiles and thermostable enzymes in biorefining. Microb. Cell Fact. 6: 1-23.
    • (2007) Microb. Cell Fact. , vol.6 , pp. 1-23
    • Turner, P.1    Mamo, G.2    Karlsson, E.N.3
  • 101
    • 33947586316 scopus 로고    scopus 로고
    • Pectinases: Aplicações industriais e perspectivas
    • Uenojo, M., Pastore, G. M. 2007. Pectinases: aplicações industriais e perspectivas. Quim. Nova, 30: 388-394.
    • (2007) Quim. Nova , vol.30 , pp. 388-394
    • Uenojo, M.1    Pastore, G.M.2
  • 102
    • 12944324721 scopus 로고    scopus 로고
    • Mapping the hydrolytic and synthetic selectivity of a type c feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates
    • Vafiadi, C., Topakas, E., Wong, K. K. Y., Suckling, I. D., and Christakopoulos, P. 2005. Mapping the hydrolytic and synthetic selectivity of a type c feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates. Tetrahed. Asym. 16: 373-379.
    • (2005) Tetrahed. Asym. , vol.16 , pp. 373-379
    • Vafiadi, C.1    Topakas, E.2    Wong, K.K.Y.3    Suckling, I.D.4    Christakopoulos, P.5
  • 103
    • 33746919075 scopus 로고    scopus 로고
    • The feruloyl esterase system of Talaromyces stipitatus: Determining the hydrolytic and synthetic specificity of TsFaeC
    • Vafiadi, C., Topakas, E., Christakopoulos, P., and Faulds, C. B. 2006. The feruloyl esterase system of Talaromyces stipitatus: determining the hydrolytic and synthetic specificity of TsFaeC. J. Biotechnol. 125: 210-221.
    • (2006) J. Biotechnol. , vol.125 , pp. 210-221
    • Vafiadi, C.1    Topakas, E.2    Christakopoulos, P.3    Faulds, C.B.4
  • 104
    • 0032714960 scopus 로고    scopus 로고
    • Action of diverse peroxidases and laccases on six cell wall-related phenolic compounds
    • Wallace, G., and Fry, S. C. 1999. Action of diverse peroxidases and laccases on six cell wall-related phenolic compounds. Phytochem. 52: 769-773.
    • (1999) Phytochem. , vol.52 , pp. 769-773
    • Wallace, G.1    Fry, S.C.2
  • 105
    • 0024575448 scopus 로고
    • Degradation of cell wall and related plant polysaccharides
    • Ward, O. P., and Moo-Young, M. 1989. Degradation of cell wall and related plant polysaccharides. Crit. Rev. Biotechnol. 8: 237-274.
    • (1989) Crit. Rev. Biotechnol. , vol.8 , pp. 237-274
    • Ward, O.P.1    Moo-Young, M.2
  • 106
    • 0037126853 scopus 로고    scopus 로고
    • Endo-b-1,4-Mannanases from blue mussel, Mytilus edulis: Purification, characterization, and mode of action
    • Xu, B., Hägglund, P., Stalbrand, H., Janson, J. 2002. Endo-b-1,4-Mannanases from blue mussel, Mytilus edulis: purification, characterization, and mode of action. J. of Biotechnol. 92: 267-277.
    • (2002) J. of Biotechnol. , vol.92 , pp. 267-277
    • Xu, B.1    Hägglund, P.2    Stalbrand, H.3    Janson, J.4
  • 107
    • 56749155915 scopus 로고    scopus 로고
    • Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38
    • Yao, Q., Sun, T., Liu, W., Chen, G. 2008. Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38. Biosci Biotechnol. Biochem. 72: 2799-2805.
    • (2008) Biosci Biotechnol. Biochem. , vol.72 , pp. 2799-2805
    • Yao, Q.1    Sun, T.2    Liu, W.3    Chen, G.4


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