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Volumn 19, Issue 1, 2002, Pages 105-120

A super-channel in bacteria: Macro-molecule uptake and depolymerization systems of sphingomonas sp. a1 with a special cell surface structure

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACES; SPHINGOMONAS SP; SUPERCHANNEL;

EID: 0036917063     PISSN: 02648725     EISSN: 20465556     Source Type: Journal    
DOI: 10.1080/02648725.2002.10648025     Document Type: Article
Times cited : (5)

References (59)
  • 1
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2. 2Å resolution
    • Aleshin, E. A., Golubev, A., Firsov, L. M. and Honzatko, R. B. (1992). Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2. 2Å resolution. Journal of Biological Chemistry 267, 19291-19298.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 19291-19298
    • Aleshin, E.A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 2
    • 0026638255 scopus 로고
    • ATP-dependent bacterial transporters and cystic fibrosis: Analogy between channels and transporters
    • Ames, G. F. -L. and Lecar, H. (1992). ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. FASEB Journal 6, 2660-2666.
    • (1992) FASEB Journal , vol.6 , pp. 2660-2666
    • Ames, G.F.1    Lecar, H.2
  • 4
    • 0034304901 scopus 로고    scopus 로고
    • Chunnel vision-export and efflux through bacterial channel-tunnels
    • andersen, C., Hughes, C. and Koronakis, V. (2000). Chunnel vision-export and efflux through bacterial channel-tunnels. EMBO Reports 1, 313-318.
    • (2000) EMBO Reports , vol.1 , pp. 313-318
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 5
    • 0033616141 scopus 로고    scopus 로고
    • Calcium controls the transcription of its own transporters and channels in developing neurons
    • Carafoli, E., Genazzani, A. and Guerini, D. (1999). Calcium controls the transcription of its own transporters and channels in developing neurons. Biochemical and Biophysical Research Communications 266, 624-632.
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , pp. 624-632
    • Carafoli, E.1    Genazzani, A.2    Guerini, D.3
  • 6
    • 0002001722 scopus 로고
    • Molecular genetics and environmental regulation of alginate biosynthesis
    • Chakrabarty, A. M. (1991). Molecular genetics and environmental regulation of alginate biosynthesis. Applied Phycology 8, 583-590.
    • (1991) Applied Phycology , vol.8 , pp. 583-590
    • Chakrabarty, A.M.1
  • 7
    • 85046166124 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subunits in glycosyl hydrolases
    • Davies, G. J., Wilson, K. S. and Henrissat, B. (1997). Nomenclature for sugar-binding subunits in glycosyl hydrolases. Biochemical Journal 15, 557-559.
    • (1997) Biochemical Journal , vol.15 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 9
    • 0021252896 scopus 로고
    • Sequences of the malE gene and its product, the maltose-binding protein of Escherichia coli K12
    • Duplay, P., Bedouelle, H., Fowler, A., Zabin, I., Saurin, W. and Hofnung, M. (1984). Sequences of the malE gene and its product, the maltose-binding protein of Escherichia coli K12. Journal of Biological Chemistry 259, 10606-10613.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 10606-10613
    • Duplay, P.1    Bedouelle, H.2    Fowler, A.3    Zabin, I.4    Saurin, W.5    Hofnung, M.6
  • 11
    • 0001323496 scopus 로고
    • ALGINATE-MODIFYING ENZYMES. A PROPOSED UNIFIED MECHANISM OF ACTION FOR THE LYASES AND EPIMERASES
    • Gacesa, P. (1987). ALGINATE-MODIFYING ENZYMES. A PROPOSED UNIFIED MECHANISM OF ACTION FOR THE LYASES AND EPIMERASES. FEBS Letters 212, 199-202.
    • (1987) FEBS Letters , vol.212 , pp. 199-202
    • Gacesa, P.1
  • 12
    • 0032577423 scopus 로고    scopus 로고
    • The Streptococcus agalactiae hlyB gene encoding hyaluronate lyase: Completion of the sequence and expression analysis
    • Gase, K., OzegowskI, J. and Malk, H. (1998). The Streptococcus agalactiae hlyB gene encoding hyaluronate lyase: completion of the sequence and expression analysis. Biochimica et Biophysica Acta 1398, 86-98.
    • (1998) Biochimica Et Biophysica Acta , vol.1398 , pp. 86-98
    • Gase, K.1    Ozegowski, J.2    Malk, H.3
  • 16
    • 0031783859 scopus 로고    scopus 로고
    • Sphingomonas sp. A1 lyase active on both poly-13-D-mannuronate and heteropolymeric regions in alginate
    • Hashimoto, W., Okamoto, M., Hisano, T., Momma, K. and Murata, K. (1998a). Sphingomonas sp. A1 lyase active on both poly-13-D-mannuronate and heteropolymeric regions in alginate. Journal of Fermentation and Bioengineering 86, 236-238.
    • (1998) Journal of Fermentation and Bioengineering , vol.86 , pp. 236-238
    • Hashimoto, W.1    Okamoto, M.2    Hisano, T.3    Momma, K.4    Murata, K.5
  • 17
    • 0031858250 scopus 로고    scopus 로고
    • Polysaccharide iyase: Molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1
    • Hashimoto, W., Sato, N., Kimura, S. and Murata, K. (1998b). Polysaccharide iyase: Molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1. Archives of Biochemistty and Biophysics 354, 31-39.
    • (1998) Archives of Biochemistty and Biophysics , vol.354 , pp. 31-39
    • Hashimoto, W.1    Sato, N.2    Kimura, S.3    Murata, K.4
  • 18
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. Strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto, W., Miyake, O., Momma, K., Kawai, S. and Murata, K. (2000). Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate. Journal of Bacteriology 182, 4572-4577.
    • (2000) Journal of Bacteriology , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 19
    • 0035143725 scopus 로고    scopus 로고
    • Polysaccharide lyase: Molecular cloning, sequencing, and overexpression of xanthan lyase gene of Bacillus sp. Strain GL1
    • Hashimoto, W., Miki, H., Tsuchiya, N., Nankai, H. and Murata, K. (2001). Polysaccharide lyase: molecular cloning, sequencing, and overexpression of xanthan lyase gene of Bacillus sp. strain GL1. Applied and Environmental Microbiology 67, 713-720.
    • (2001) Applied and Environmental Microbiology , vol.67 , pp. 713-720
    • Hashimoto, W.1    Miki, H.2    Tsuchiya, N.3    Nankai, H.4    Murata, K.5
  • 20
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. (1992). ABC transporters: from microorganisms to man. Annual Review of Cell Biology 8, 67-113.
    • (1992) Annual Review of Cell Biology , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 24
    • 0029159895 scopus 로고
    • Direct uptake of alginate molecules through a pit on the bacterial cell surface: A novei mechanism for the uptake of macromolecules
    • Hisano, T., Yonemoto, Y., Yamashita, T., Fukuda, Y., Kimura, A. and Murata, K. (1995). Direct uptake of alginate molecules through a pit on the bacterial cell surface: a novei mechanism for the uptake of macromolecules. Journal of Fermentation and Bioengineering 79, 538-544.
    • (1995) Journal of Fermentation and Bioengineering , vol.79 , pp. 538-544
    • Hisano, T.1    Yonemoto, Y.2    Yamashita, T.3    Fukuda, Y.4    Kimura, A.5    Murata, K.6
  • 26
    • 0027490784 scopus 로고
    • Genetic analysis of periplasmic binding protein-dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex
    • Hor, L. I. and Shuman, H. A. (1993). Genetic analysis of periplasmic binding protein-dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. Journal of Molecular Biology 233, 659-670.
    • (1993) Journal of Molecular Biology , vol.233 , pp. 659-670
    • Hor, L.I.1    Shuman, H.A.2
  • 27
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F. and Kim, S. H. (1998). Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396, 703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 28
    • 0034685825 scopus 로고    scopus 로고
    • ATP modulates the subunit-subunit interaction in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking
    • Hunke, S., Mourez, M., Jehanno, M., Dassa, E. and Schneider, E. (2000). ATP modulates the subunit-subunit interaction in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking. Journal of Biological Chemistry 275, 15526-15534.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 15526-15534
    • Hunke, S.1    Mourez, M.2    Jehanno, M.3    Dassa, E.4    Schneider, E.5
  • 30
    • 0034634335 scopus 로고    scopus 로고
    • Crystal structure of JV-acyl-D-giucosamine 2-epimerase from porcine kidney at 2. 0A resolution
    • Iron, T., Mskami, B., Maru, I., Ohta, Y., Hashimoto, W. and Murata, K. (2000). Crystal structure of JV-acyl-D-giucosamine 2-epimerase from porcine kidney at 2. 0A resolution. Journal of Molecular Biology 303, 733-744.
    • (2000) Journal of Molecular Biology , vol.303 , pp. 733-744
    • Iron, T.1    Mskami, B.2    Maru, I.3    Ohta, Y.4    Hashimoto, W.5    Murata, K.6
  • 31
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P. M. and George, A. M. (1999). Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiology Letters 179, 187-202.
    • (1999) FEMS Microbiology Letters , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 33
    • 0016151381 scopus 로고
    • Active transport of maltose in Escherichia coli K-12. Involvement of a periplasmic maltose-binding protein
    • Kellerman, O. and Szmelcman, S. (1974). Active transport of maltose in Escherichia coli K-12. Involvement of a periplasmic maltose-binding protein. European Journal of Biochemistry 47, 139-149.
    • (1974) European Journal of Biochemistry , vol.47 , pp. 139-149
    • Kellerman, O.1    Szmelcman, S.2
  • 36
    • 0034991663 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of AlgS: A bacterial ATP-binding-cassette (ABC) protein specific to macromolecule import
    • Mishima, Y., Momma, K., Hashimoto, W., Mikami, B. and Murata, K. (2001). Crystallization and preliminary X-ray analysis of AlgS: a bacterial ATP-binding-cassette (ABC) protein specific to macromolecule import. Acta Crystallographies. Section D 57 884-885.
    • (2001) Acta Crystallographies. Section D , vol.57 , pp. 884-885
    • Mishima, Y.1    Momma, K.2    Hashimoto, W.3    Mikami, B.4    Murata, K.5
  • 37
    • 0033932250 scopus 로고    scopus 로고
    • A novel bacterial ATP-binding cassette (ABC) transporter system that allows uptake of macromolecules
    • Momma, K., Okamoto, M., Mishima, Y., Mori, S., Hashimoto, W. and Murata, K. (2000). A novel bacterial ATP-binding cassette (ABC) transporter system that allows uptake of macromolecules. Journal of Bacteriology 182, 3998-4004.
    • (2000) Journal of Bacteriology , vol.182 , pp. 3998-4004
    • Momma, K.1    Okamoto, M.2    Mishima, Y.3    Mori, S.4    Hashimoto, W.5    Murata, K.6
  • 38
    • 0036304144 scopus 로고    scopus 로고
    • Crystal structure of AlgQ2, a macromolecule (Alginate)-binding protein of Sphingomonas sp. AI at 2. 0 Å resolution
    • Momma, K., Mikami, B., Mishima, Y., Hashimoto, W. and Murata, K. (2002). Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. AI at 2. 0 Å resolution. Journal of Molecular Biology 316, 1061-1069.
    • (2002) Journal of Molecular Biology , vol.316 , pp. 1061-1069
    • Momma, K.1    Mikami, B.2    Mishima, Y.3    Hashimoto, W.4    Murata, K.5
  • 39
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase acti vi ty associated with the purified MalK subunit
    • Morbach, S., Tebbe, S. and Schneider, E. (1993). The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase acti vi ty associated with the purified MalK subunit. Journal of Biological Chemistry 268, 18617-18621.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 18617-18621
    • Morbach, S.1    Tebbe, S.2    Schneider, E.3
  • 40
    • 0002870071 scopus 로고
    • BACTERIAL ALGINATE LYASE: ENZYMATIC AND GENETIC ASPECTS OF THE LYASE AND ITS APPLICATION TO AGRICULTURAL, FOOD, AND PHARMACEUTICAL PROCESSES
    • Murata, K, (1994). BACTERIAL ALGINATE LYASE: ENZYMATIC AND GENETIC ASPECTS OF THE LYASE AND ITS APPLICATION TO AGRICULTURAL, FOOD, AND PHARMACEUTICAL PROCESSES. Comments on Agricultural and Food Chemistry 3, 87-110.
    • (1994) Comments on Agricultural and Food Chemistry , vol.3 , pp. 87-110
    • Murata, K.1
  • 42
    • 0030822352 scopus 로고    scopus 로고
    • Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of
    • Nikaido, K., Liu, P. -Q. and Ames, G. F. -L. (1997). Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Journal of Biological Chemistry 272, 27745-27752.
    • (1997) Salmonella Typhimurium. Journal of Biological Chemistry , vol.272 , pp. 27745-27752
    • Nikaido, K.1    Liu, P.-Q.2    Ames, G.F.3
  • 43
    • 0024120551 scopus 로고
    • Nucleotide sequences of the ugp genes of Escherichia coli K-12: Homology to the maltose system
    • Overduin, P., Boos, W. and Tommassen, J. (1988). Nucleotide sequences of the ugp genes of Escherichia coli K-12: homology to the maltose system. Molecular Microbiology 2, 767-775.
    • (1988) Molecular Microbiology , vol.2 , pp. 767-775
    • Overduin, P.1    Boos, W.2    Tommassen, J.3
  • 44
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch, M. C. (1996). ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochemical Society Transactions 24, 274-279.
    • (1996) Biochemical Society Transactions , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 45
    • 0034674165 scopus 로고    scopus 로고
    • MECHANISM OF HYALURONAN BINDING AND DEGRADATION STRUCTURE of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at i. 7 A resolution
    • Ponnuraj, K. and Jedrzejas, M. J. (2000). MECHANISM OF HYALURONAN BINDING AND DEGRADATION STRUCTURE of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at i. 7 A resolution. Journal of Molecular Biology 299, 885-895.
    • (2000) Journal of Molecular Biology , vol.299 , pp. 885-895
    • Ponnuraj, K.1    Jedrzejas, M.J.2
  • 47
    • 0021971601 scopus 로고
    • Role of Pseudomonas aeruginosa mucoid exopolysaccharide in adherence to tracheal cells
    • Rampiial, R. and Pier, G. B. (1985). Role of Pseudomonas aeruginosa mucoid exopolysaccharide in adherence to tracheal cells. Infection and Immunity 47, 1-4.
    • (1985) Infection and Immunity , vol.47 , pp. 1-4
    • Rampiial, R.1    Pier, G.B.2
  • 48
    • 0028215587 scopus 로고
    • SEQUENCE RELATIONSHIPS BETWEEN INTEGRAL INNER MEMBRANE PROTEINS OF BINDING PROTEIN-DEPENDENT TRANSPORT SYSTEMS: EVOLUTION BY RECURRENT GENE DUPLICATIONS
    • Saurin, W. and Dassa, E. (1994). SEQUENCE RELATIONSHIPS BETWEEN INTEGRAL INNER MEMBRANE PROTEINS OF BINDING PROTEIN-DEPENDENT TRANSPORT SYSTEMS: EVOLUTION BY RECURRENT GENE DUPLICATIONS. Protein Science 3, 325-344.
    • (1994) Protein Science , vol.3 , pp. 325-344
    • Saurin, W.1    Dassa, E.2
  • 49
    • 0026493924 scopus 로고
    • Cryslallographic evidence of a large ligand induced high-twist motion between the two domains of the mahodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A. I., Rodseth, L. E., Spuruno, J. C. and Quiocho, F. A. (1992). Cryslallographic evidence of a large ligand induced high-twist motion between the two domains of the mahodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31, 10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.I.1    Rodseth, L.E.2    Spuruno, J.C.3    Quiocho, F.A.4
  • 50
    • 0025754301 scopus 로고
    • The 2. 3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G. -Y. and Quiocho, F. A. (1991). The 2. 3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. Journal of Biological Chemistry 266, 5202-5219.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 52
    • 0001607723 scopus 로고
    • Distantly related sequences in the a- and (I-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes, and a common nucleotide-binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. and Gay, N. J. (1982). Distantly related sequences in the a- and i-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes, and a common nucleotide-binding fold. EMBO Journal 1, 945-951.
    • (1982) EMBO Journal , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 53
    • 0026051791 scopus 로고
    • Bacterial Alginate Lyase: Characterization Of Alginate Lyase-Producing Bacteria And Purification Of The Enzyme
    • Yonemoto, Y., Murata, K., Kimura, A., Yamaguchi, H. and Okayama, K. (1991). Bacterial Alginate Lyase: Characterization Of Alginate Lyase-Producing Bacteria And Purification Of The Enzyme. Journal Of Fermentation And Bioengineering 72, 152-157.
    • (1991) Journal of Fermentation and Bioengineering , vol.72 , pp. 152-157
    • Yonemoto, Y.1    Murata, K.2    Kimura, A.3    Yamaguchi, H.4    Okayama, K.5
  • 56
    • 0033538420 scopus 로고    scopus 로고
    • Crystal structure of alginate lyase Al-HI from Sphingomonas species Al at 1. 78A resolution
    • Yoon, H. -J., Mikami, B., Hashimoto, W. and Murata, K. (1999). Crystal structure of alginate lyase Al-HI from Sphingomonas species Al at 1. 78A resolution. Journal of Molecular Biology 290. 505-514.
    • (1999) Journal of Molecular Biology , vol.290 , pp. 505-514
    • Yoon, H.-J.1    Mikami, B.2    Hashimoto, W.3    Murata, K.4
  • 57
    • 0034084571 scopus 로고    scopus 로고
    • OVEREXPRESSION IN Escherichia coli, purification, and characterization of Sphingomonas sp. Al alginate lyases
    • Yoon, H. -J., Hashimoto, W., Miyake, O., Okamoto, M., Mikami, B. and Murata, K. (2000a). OVEREXPRESSION IN Escherichia coli, purification, and characterization of Sphingomonas sp. Al alginate lyases. Protein Expression and Purification 19, 84-90.
    • (2000) Protein Expression and Purification , vol.19 , pp. 84-90
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Okamoto, M.4    Mikami, B.5    Murata, K.6
  • 58
    • 0033962604 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of alginate lyase Al-II from Sphingomonas species Al
    • Yoon, H. -J., Hashimoto, W., Katsuya, Y., Mezaki, Y., Murata, K. and Mikami, B. (2000b). Crystallization and preliminary X-ray crystallographic analysis of alginate lyase Al-II from Sphingomonas species Al. Biochimica et Biophysica Acta 1476. 382-385.
    • (2000) Biochimica Et Biophysica Acta , vol.1476 , pp. 382-385
    • Yoon, H.-J.1    Hashimoto, W.2    Katsuya, Y.3    Mezaki, Y.4    Murata, K.5    Mikami, B.6
  • 59
    • 0035896032 scopus 로고    scopus 로고
    • CRYSTAL STRUCTURE OF ALGINATE LYASE A1-IH COMPLEXED WITH TRISACCHARIDE PRODUCT AT 2. 0A RESOLUTION
    • Yoon, H. -J., Hashimoto, W., Miyake, O., Murata, K. and Mikami, B. (2001). CRYSTAL STRUCTURE OF ALGINATE LYASE A1-IH COMPLEXED WITH TRISACCHARIDE PRODUCT AT 2. 0A RESOLUTION. Journal of Molecular Biology 307. 9-16.
    • (2001) Journal of Molecular Biology , vol.307 , pp. 9-16
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Murata, K.4    Mikami, B.5


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