메뉴 건너뛰기




Volumn 9, Issue 8, 2014, Pages

Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases

Author keywords

[No Author keywords available]

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; RECOMBINANT PROTEIN;

EID: 84905978951     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0105290     Document Type: Article
Times cited : (45)

References (50)
  • 1
    • 33646817446 scopus 로고    scopus 로고
    • Inborn errors of sulfur-containing amino acid metabolism
    • Finkelstein JD (2006) Inborn errors of sulfur-containing amino acid metabolism. J Nutr 136: 1750S-1754S.
    • (2006) J Nutr , vol.136
    • Finkelstein, J.D.1
  • 2
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • Cooper AJL (1983) Biochemistry of sulfur-containing amino acids. Annual Review of Biochemistry 52: 187-222.
    • (1983) Annual Review of Biochemistry , vol.52 , pp. 187-222
    • Cooper, A.J.L.1
  • 3
    • 3142749051 scopus 로고    scopus 로고
    • Cystathionine beta-synthase: Structure, function, regulation, and location of homocystinuria-causing mutations
    • DOI 10.1074/jbc.R400005200
    • Miles EW, Kraus JP (2004) Cystathionine beta-synthase: structure, function, regulation, and location of homocystinuria-causing mutations. J Biol Chem 279: 29871-29874. (Pubitemid 38937904)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 29871-29874
    • Miles, E.W.1    Kraus, J.P.2
  • 4
    • 0000167774 scopus 로고    scopus 로고
    • Disorders of transsulfuration
    • Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B et al., editors. New York: McGraw-Hill
    • Mudd SH, Levy HL, Kraus JP (2001) Disorders of transsulfuration. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B et al., editors. The Metabolic and Molecular Bases of Inherited Disease. 8 ed. New York: McGraw-Hill. 2007-2056.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. 8 Ed. , pp. 2007-2056
    • Mudd, S.H.1    Levy, H.L.2    Kraus, J.P.3
  • 5
    • 9744276776 scopus 로고    scopus 로고
    • Redox regulation and reaction mechanism of human cystathionine-beta- synthase: A PLP-dependent hemesensor protein
    • DOI 10.1016/j.abb.2004.08.037, PII S0003986104004680
    • Banerjee R, Zou CG (2005) Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. Arch Biochem Biophys 433: 144-156. (Pubitemid 39586589)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 144-156
    • Banerjee, R.1    Zou, C.-G.2
  • 6
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine beta-synthase: A unique pyridoxal 5′-phosphate-dependent heme protein
    • DOI 10.1093/emboj/20.15.3910
    • Meier M, Janosik M, Kery V, Kraus JP, Burkhard P (2001) Structure of human cystathionine beta-synthase: a unique pyridoxal 5′ -phosphate-dependent heme protein. Embo J 20: 3910-3916. (Pubitemid 32751807)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 3910-3916
    • Meier, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 7
    • 58049213352 scopus 로고    scopus 로고
    • Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone
    • Majtan T, Singh LR, Wang L, Kruger WD, Kraus JP (2008) Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone. The Journal of biological chemistry 283: 34588-34595.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 34588-34595
    • Majtan, T.1    Singh, L.R.2    Wang, L.3    Kruger, W.D.4    Kraus, J.P.5
  • 8
    • 77952368285 scopus 로고    scopus 로고
    • Rescue of cystathionine betasynthase (CBS) mutants with chemical chaperones: Purification and characterization of eight CBS mutant enzymes
    • Majtan T, Liu L, Carpenter JF, Kraus JP (2010) Rescue of cystathionine betasynthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes. The Journal of biological chemistry 285: 15866-15873.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 15866-15873
    • Majtan, T.1    Liu, L.2    Carpenter, J.F.3    Kraus, J.P.4
  • 9
    • 81555228426 scopus 로고    scopus 로고
    • The CBS domain: A protein module with an emerging prominent role in regulation
    • Baykov AA, Tuominen HK, Lahti R (2011) The CBS domain: a protein module with an emerging prominent role in regulation. ACS Chem Biol 6: 1156-1163.
    • (2011) ACS Chem Biol , vol.6 , pp. 1156-1163
    • Baykov, A.A.1    Tuominen, H.K.2    Lahti, R.3
  • 10
    • 33646231787 scopus 로고    scopus 로고
    • S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity
    • Prudova A, Bauman Z, Braun A, Vitvitsky V, Lu SC, et al. (2006) S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci U S A 103: 6489-6494.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6489-6494
    • Prudova, A.1    Bauman, Z.2    Braun, A.3    Vitvitsky, V.4    Lu, S.C.5
  • 11
    • 84870860045 scopus 로고    scopus 로고
    • Human cystathionine beta-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): Complex regulation of CBS activity and stability by SAM
    • Pey AL, Majtan T, Sanchez-Ruiz JM, Kraus JP (2013) Human cystathionine beta-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM. Biochem J 449: 109-121.
    • (2013) Biochem J , vol.449 , pp. 109-121
    • Pey, A.L.1    Majtan, T.2    Sanchez-Ruiz, J.M.3    Kraus, J.P.4
  • 12
    • 0035794209 scopus 로고    scopus 로고
    • Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine beta-synthase and serine acetyltransferase from Trypanosoma
    • Nozaki T, Shigeta Y, Saito-Nakano Y, Imada M, Kruger WD (2001) Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine beta-synthase and serine acetyltransferase from Trypanosoma. J Biol Chem 276: 6516-6523.
    • (2001) J Biol Chem , vol.276 , pp. 6516-6523
    • Nozaki, T.1    Shigeta, Y.2    Saito-Nakano, Y.3    Imada, M.4    Kruger, W.D.5
  • 13
    • 17344382635 scopus 로고    scopus 로고
    • Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: Purification and characterization of recombinant yeast cystathionine beta-synthase
    • Maclean KN, Janosik M, Oliveriusova J, Kery V, Kraus JP (2000) Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: purification and characterization of recombinant yeast cystathionine beta-synthase. J Inorg Biochem 81: 161-171.
    • (2000) J Inorg Biochem , vol.81 , pp. 161-171
    • Maclean, K.N.1    Janosik, M.2    Oliveriusova, J.3    Kery, V.4    Kraus, J.P.5
  • 15
    • 84859464714 scopus 로고    scopus 로고
    • Novel structural arrangement of nematode cystathionine beta-synthases: Characterization of Caenorhabditis elegans CBS-1
    • Vozdek R, Hnizda A, Krijt J, Kostrouchova M, Kozich V (2012) Novel structural arrangement of nematode cystathionine beta-synthases: characterization of Caenorhabditis elegans CBS-1. Biochem J 443: 535-547.
    • (2012) Biochem J , vol.443 , pp. 535-547
    • Vozdek, R.1    Hnizda, A.2    Krijt, J.3    Kostrouchova, M.4    Kozich, V.5
  • 16
    • 0028127106 scopus 로고
    • Transsulfuration depends on heme in addition to pyridoxal 59-phosphate. Cystathionine beta-synthase is a heme protein
    • Kery V, Bukovska G, Kraus JP (1994) Transsulfuration depends on heme in addition to pyridoxal 59-phosphate. Cystathionine beta-synthase is a heme protein. J Biol Chem 269: 25283-25288.
    • (1994) J Biol Chem , vol.269 , pp. 25283-25288
    • Kery, V.1    Bukovska, G.2    Kraus, J.P.3
  • 17
    • 0032528375 scopus 로고    scopus 로고
    • Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: Structural and functional consequences
    • DOI 10.1006/abbi.1998.0723
    • Kery V, Poneleit L, Kraus JP (1998) Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences. Arch Biochem Biophys 355: 222-232. (Pubitemid 28364373)
    • (1998) Archives of Biochemistry and Biophysics , vol.355 , Issue.2 , pp. 222-232
    • Kery, V.1    Poneleit, L.2    Kraus, J.P.3
  • 18
    • 0034730104 scopus 로고    scopus 로고
    • Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation
    • DOI 10.1021/bi001020g
    • Jhee KH, McPhie P, Miles EW (2000) Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation. Biochemistry 39: 10548-10556. (Pubitemid 30655932)
    • (2000) Biochemistry , vol.39 , Issue.34 , pp. 10548-10556
    • Jhee, K.-H.1    McPhie, P.2    Miles, E.W.3
  • 19
    • 66949132549 scopus 로고    scopus 로고
    • Two pathways for cysteine biosynthesis in Leishmania major
    • Williams RA, Westrop GD, Coombs GH (2009) Two pathways for cysteine biosynthesis in Leishmania major. Biochem J 420: 451-462.
    • (2009) Biochem J , vol.420 , pp. 451-462
    • Williams, R.A.1    Westrop, G.D.2    Coombs, G.H.3
  • 20
    • 69249100078 scopus 로고    scopus 로고
    • Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions
    • Singh S, Padovani D, Leslie RA, Chiku T, Banerjee R (2009) Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions. J Biol Chem 284: 22457-22466.
    • (2009) J Biol Chem , vol.284 , pp. 22457-22466
    • Singh, S.1    Padovani, D.2    Leslie, R.A.3    Chiku, T.4    Banerjee, R.5
  • 21
    • 84866916863 scopus 로고    scopus 로고
    • Functional characterization of enzymes involved in cysteine biosynthesis and H(2)S production in Trypanosoma cruzi
    • Marciano D, Santana M, Nowicki C (2012) Functional characterization of enzymes involved in cysteine biosynthesis and H(2)S production in Trypanosoma cruzi. Mol Biochem Parasitol 185: 114-120.
    • (2012) Mol Biochem Parasitol , vol.185 , pp. 114-120
    • Marciano, D.1    Santana, M.2    Nowicki, C.3
  • 22
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo C (2007) Hydrogen sulphide and its therapeutic potential. Nat Rev Drug Discov 6: 917-935.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 917-935
    • Szabo, C.1
  • 23
    • 38349053999 scopus 로고    scopus 로고
    • Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli
    • Frank N, Kent JO, Meier M, Kraus JP (2008) Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli. Arch Biochem Biophys 470: 64-72.
    • (2008) Arch Biochem Biophys , vol.470 , pp. 64-72
    • Frank, N.1    Kent, J.O.2    Meier, M.3    Kraus, J.P.4
  • 24
    • 84873832650 scopus 로고    scopus 로고
    • Comparative Study of Enzyme Activity and Heme Reactivity in Drosophila melanogaster and Homo sapiens Cystathionine beta-Synthases
    • Su Y, Majtan T, Freeman KM, Linck R, Ponter S, et al. (2013) Comparative Study of Enzyme Activity and Heme Reactivity in Drosophila melanogaster and Homo sapiens Cystathionine beta-Synthases. Biochemistry 52: 741-751.
    • (2013) Biochemistry , vol.52 , pp. 741-751
    • Su, Y.1    Majtan, T.2    Freeman, K.M.3    Linck, R.4    Ponter, S.5
  • 25
    • 84857408197 scopus 로고    scopus 로고
    • Folding and activity of mutant cystathionine beta-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant
    • Majtan T, Kraus JP (2012) Folding and activity of mutant cystathionine beta-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant. Protein Expr Purif 82: 317-324.
    • (2012) Protein Expr Purif , vol.82 , pp. 317-324
    • Majtan, T.1    Kraus, J.P.2
  • 26
    • 0023611853 scopus 로고
    • Cystathionine beta-synthase (human)
    • Kraus JP (1987) Cystathionine beta-synthase (human). Methods Enzymol 143: 388-394.
    • (1987) Methods Enzymol , vol.143 , pp. 388-394
    • Kraus, J.P.1
  • 27
    • 0025978348 scopus 로고
    • A colorimetric assay for a pyridoxal phosphate-dependent beta-replacement reaction with L-cysteine: Application to studies of wild-type and mutant tryptophan synthase alpha 2 beta 2 complexes
    • Kayastha AM, Miles EW (1991) A colorimetric assay for a pyridoxal phosphate-dependent beta-replacement reaction with L-cysteine: application to studies of wild-type and mutant tryptophan synthase alpha 2 beta 2 complexes. Anal Biochem 193: 200-203.
    • (1991) Anal Biochem , vol.193 , pp. 200-203
    • Kayastha, A.M.1    Miles, E.W.2
  • 28
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde MK (1967) A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J 104: 627-633.
    • (1967) Biochem J , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 29
    • 0024276839 scopus 로고
    • A Fourier-transform infrared spectroscopic study of the phosphoserine residues in hen egg phosvitin and ovalbumin
    • Sanchez-Ruiz JM, Martinez-Carrion M (1988) A Fourier-transform infrared spectroscopic study of the phosphoserine residues in hen egg phosvitin and ovalbumin. Biochemistry 27: 3338-3342.
    • (1988) Biochemistry , vol.27 , pp. 3338-3342
    • Sanchez-Ruiz, J.M.1    Martinez-Carrion, M.2
  • 31
    • 0000159569 scopus 로고    scopus 로고
    • Protein Structure and the Energetics of Protein Stability
    • Robertson AD, Murphy KP (1997) Protein Structure and the Energetics of Protein Stability. Chem Rev 97: 1251-1268.
    • (1997) Chem Rev , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 32
    • 77949314227 scopus 로고    scopus 로고
    • Binding of S-methyl-5′-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair
    • Lucas M, Encinar JA, Arribas EA, Oyenarte I, Garcia IG, et al. (2010) Binding of S-methyl-5′-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair. J Mol Biol 396: 800-820.
    • (2010) J Mol Biol , vol.396 , pp. 800-820
    • Lucas, M.1    Encinar, J.A.2    Arribas, E.A.3    Oyenarte, I.4    Garcia, I.G.5
  • 33
    • 84885071800 scopus 로고    scopus 로고
    • Structural basis of regulation and oligomerization of human cystathionine beta-synthase, the central enzyme of transsulfuration
    • Ereno-Orbea J, Majtan T, Oyenarte I, Kraus JP, Martinez-Cruz LA (2013) Structural basis of regulation and oligomerization of human cystathionine beta-synthase, the central enzyme of transsulfuration. Proc Natl Acad Sci U S A 110: E3790-3799.
    • (2013) Proc Natl Acad Sci U S A , vol.110
    • Ereno-Orbea, J.1    Majtan, T.2    Oyenarte, I.3    Kraus, J.P.4    Martinez-Cruz, L.A.5
  • 34
    • 0033153361 scopus 로고    scopus 로고
    • Erratum: Characterization of the heme and pyridoxal phosphate cofactors of human cystathionine beta-synthase reveals nonequivalent active sites (Biochemistry (March 2, 1999) 38:9 (2738-2744))
    • DOI 10.1021/bi995077i
    • Taoka S, West M, Banerjee R (1999) Characterization of the heme and pyridoxal phosphate cofactors of human cystathionine beta-synthase reveals nonequivalent active sites. Biochemistry 38: 7406. (Pubitemid 29262803)
    • (1999) Biochemistry , vol.38 , Issue.22 , pp. 7406
    • Taoka, S.1    West, M.2    Banerjee, R.3
  • 35
    • 0035807013 scopus 로고    scopus 로고
    • Regulation of human cystathionine beta-synthase by S-adenosyl-L- methionine: Evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region
    • DOI 10.1021/bi010711p
    • Janosik M, Kery V, Gaustadnes M, Maclean KN, Kraus JP (2001) Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Biochemistry 40: 10625-10633. (Pubitemid 32816674)
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10625-10633
    • Janosik, M.1    Kery, V.2    Gaustadnes, M.3    Maclean, K.N.4    Kraus, J.P.5
  • 38
    • 84905983688 scopus 로고    scopus 로고
    • Stopped-flow kinetic analysis of the reaction catalyzed by yeast cystathionine beta - synthase
    • Taoka S, Banerjee R (2002) Stopped-flow kinetic analysis of the reaction catalyzed by yeast cystathionine beta - synthase. J Biol Chem 10: 10.
    • (2002) J Biol Chem , vol.10 , pp. 10
    • Taoka, S.1    Banerjee, R.2
  • 39
    • 84856890456 scopus 로고    scopus 로고
    • Redox outside the box: Linking extracellular redox remodeling with intracellular redox metabolism
    • Banerjee R (2012) Redox outside the box: linking extracellular redox remodeling with intracellular redox metabolism. J Biol Chem 287: 4397-4402.
    • (2012) J Biol Chem , vol.287 , pp. 4397-4402
    • Banerjee, R.1
  • 40
    • 33645864368 scopus 로고    scopus 로고
    • Methionine flux to transsulfuration is enhanced in the long living Ames dwarf mouse
    • Uthus EO, Brown-Borg HM (2006) Methionine flux to transsulfuration is enhanced in the long living Ames dwarf mouse. Mech Ageing Dev 127: 444-450.
    • (2006) Mech Ageing Dev , vol.127 , pp. 444-450
    • Uthus, E.O.1    Brown-Borg, H.M.2
  • 41
    • 50949130722 scopus 로고    scopus 로고
    • Mitochondrial dysfunction increases oxidative stress and decreases chronological life span in fission yeast
    • Zuin A, Gabrielli N, Calvo IA, Garcia-Santamarina S, Hoe KL, et al. (2008) Mitochondrial dysfunction increases oxidative stress and decreases chronological life span in fission yeast. PLoS One 3: e2842.
    • (2008) PLoS One , vol.3
    • Zuin, A.1    Gabrielli, N.2    Calvo, I.A.3    Garcia-Santamarina, S.4    Hoe, K.L.5
  • 43
    • 33748558473 scopus 로고    scopus 로고
    • Hydrogen sulfide: Clandestine microbial messenger?
    • Lloyd D (2006) Hydrogen sulfide: clandestine microbial messenger? Trends Microbiol 14: 456-462.
    • (2006) Trends Microbiol , vol.14 , pp. 456-462
    • Lloyd, D.1
  • 45
    • 0035755593 scopus 로고    scopus 로고
    • From cofactor to enzymes. The molecular evolution of pyridoxal-s'- pliosphate-dependent enzymes
    • Christen P, Mehta PK (2001) From cofactor to enzymes. The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes. Chem Rec 1: 436-447. (Pubitemid 33771590)
    • (2001) Chemical Records , vol.1 , Issue.6 , pp. 436-447
    • Christen, P.1    Mehta, P.K.2
  • 46
    • 0032566713 scopus 로고    scopus 로고
    • Evidence for heme-mediated redox regulation of human cystathionine beta- synthase activity
    • DOI 10.1074/jbc.273.39.25179
    • Taoka S, Ojha S, Shan X, Kruger WD, Banerjee R (1998) Evidence for heme-mediated redox regulation of human cystathionine b-synthase activity. Journal of Biological Chemistry 273: 25179-25184. (Pubitemid 28443278)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.39 , pp. 25179-25184
    • Taoka, S.1    Ohja, S.2    Shan, X.3    Kruger, W.D.4    Banerjee, R.5
  • 48
    • 0027320121 scopus 로고
    • Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment
    • Cherest H, Thomas D, Surdin-Kerjan Y (1993) Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment. Journal of Bacteriology 175: 5366-5374. (Pubitemid 23264431)
    • (1993) Journal of Bacteriology , vol.175 , Issue.17 , pp. 5366-5374
    • Cherest, H.1    Thomas, D.2    Surdin-Kerjan, Y.3
  • 49
    • 79955717081 scopus 로고    scopus 로고
    • Biodiversity in sulfur metabolism in hemiascomycetous yeasts
    • Hebert A, Casaregola S, Beckerich JM (2011) Biodiversity in sulfur metabolism in hemiascomycetous yeasts. FEMS Yeast Res 11: 366-378.
    • (2011) FEMS Yeast Res , vol.11 , pp. 366-378
    • Hebert, A.1    Casaregola, S.2    Beckerich, J.M.3
  • 50
    • 80051929163 scopus 로고    scopus 로고
    • PLP-dependent H(2)S biogenesis
    • Singh S, Banerjee R (2011) PLP-dependent H(2)S biogenesis. Biochim Biophys Acta 1814: 1518-1527.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1518-1527
    • Singh, S.1    Banerjee, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.