메뉴 건너뛰기




Volumn 431, Issue 1, 2010, Pages 149-157

Characterization of an ATP-regulated DNA-processing enzyme and thermotolerant phosphoesterase in the radioresistant bacterium Deinococcus radiodurans

Author keywords

5 nucleotidase; Deinococcus radiodurans; DNA end processing; DR0505; Dual function enzyme; Thermotolerant esterase

Indexed keywords

CALCIUM; DNA; ENZYME ACTIVITY; ENZYME INHIBITION; GENES; MANGANESE; MANGANESE COMPOUNDS; SUBSTRATES;

EID: 77956643903     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100446     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 35848960127 scopus 로고    scopus 로고
    • Review of recent studies on resistance to cytotoxic deoxynucleoside analogues
    • Jordheim, L. P. and Dumontet, C. (2007) Review of recent studies on resistance to cytotoxic deoxynucleoside analogues. Biochim. Biophys. Acta 1776, 138-159
    • (2007) Biochim. Biophys. Acta , vol.1776 , pp. 138-159
    • Jordheim, L.P.1    Dumontet, C.2
  • 2
    • 0035794219 scopus 로고    scopus 로고
    • m 5′-nucleotidase and 5′(3′)-deoxyribonucleotidase in substrate cycles involved in nucleotide metabolism
    • m 5′-nucleotidase and 5′(3′)- deoxyribonucleotidase in substrate cycles involved in nucleotide metabolism. J. Biol. Chem. 276, 6185-6190
    • (2001) J. Biol. Chem. , vol.276 , pp. 6185-6190
    • Gazziola, C.1    Ferraro, P.2    Moras, M.3    Reichard, P.4    Bianchi, V.5
  • 3
    • 20444368420 scopus 로고    scopus 로고
    • The 5′-nucleotidases as regulators of nucleotide and drug metabolism
    • Hunsucker, S. A., Mitchell, B. S. and Spychala, J. (2005) The 5′-nucleotidases as regulators of nucleotide and drug metabolism. Pharmacol. Ther. 107, 1-30
    • (2005) Pharmacol. Ther. , vol.107 , pp. 1-30
    • Hunsucker, S.A.1    Mitchell, B.S.2    Spychala, J.3
  • 4
    • 14644392828 scopus 로고    scopus 로고
    • Activity profiles of deoxynucleoside kinases and 5′-nucleotidases in cultured adipocytes and myoblastic cells: Insights into mitochondrial toxicity of nucleoside analogs
    • Rylova, S. N., Albertioni, F., Flygh, G. and Eriksson, S. (2005) Activity profiles of deoxynucleoside kinases and 5′-nucleotidases in cultured adipocytes and myoblastic cells: insights into mitochondrial toxicity of nucleoside analogs. Biochem. Pharmacol. 69, 951-960
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 951-960
    • Rylova, S.N.1    Albertioni, F.2    Flygh, G.3    Eriksson, S.4
  • 5
    • 0026729643 scopus 로고
    • 5′-nucleotidase: Molecular structure and functional aspects
    • Zimmermann, H. (1992) 5′-nucleotidase: molecular structure and functional aspects. Biochem. J. 285, 345-365
    • (1992) Biochem. J. , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 6
    • 70449725150 scopus 로고    scopus 로고
    • Staphylococcus aureus synthesizes adenosine to escape host immune responses
    • Thammavongsa, V., Kern, J. W., Missiakas, D. M. and Schneewind, O. (2009) Staphylococcus aureus synthesizes adenosine to escape host immune responses. J. Exp. Med. 206, 2417-2427
    • (2009) J. Exp. Med. , vol.206 , pp. 2417-2427
    • Thammavongsa, V.1    Kern, J.W.2    Missiakas, D.M.3    Schneewind, O.4
  • 7
    • 0029843192 scopus 로고    scopus 로고
    • Spontaneous mutators in bacteria: Insights into pathways of mutagenesis and repair
    • Miller, J. H. (1996) Spontaneous mutators in bacteria: insights into pathways of mutagenesis and repair. Annu. Rev. Microbiol. 50, 625-643
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 625-643
    • Miller, J.H.1
  • 8
    • 33646397599 scopus 로고    scopus 로고
    • Evolution of mutation rates in bacteria
    • Denamur, E. and Matic, I. (2006) Evolution of mutation rates in bacteria. Mol. Microbiol. 60, 820-827
    • (2006) Mol. Microbiol. , vol.60 , pp. 820-827
    • Denamur, E.1    Matic, I.2
  • 9
    • 0034624671 scopus 로고    scopus 로고
    • Radiation resistance: The fragment that remain
    • Battista, J. R. (2000) Radiation resistance: the fragment that remain. Curr. Biol. 10, R204-R205
    • (2000) Curr. Biol. , vol.10
    • Battista, J.R.1
  • 10
    • 0035102449 scopus 로고    scopus 로고
    • Genome of extremely radiation-resistant bacterium Deinococcus radioduransviewed from the perspectives of comparative genomics
    • Makarova, K. S., Aravind, L., Wolf, Y. I., Tatusov, R. L., Minton, K. W., Koonin, E. V. and Daly, M. J. (2001) Genome of extremely radiation-resistant bacterium Deinococcus radioduransviewed from the perspectives of comparative genomics. Microbiol. Mol. Biol. Rev. 65, 44-79
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 44-79
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Tatusov, R.L.4    Minton, K.W.5    Koonin, E.V.6    Daly, M.J.7
  • 11
    • 0028279759 scopus 로고
    • DNA repair in the extremely radioresistant bacterium Deinococcus radiodurans
    • Minton, K. W. (1994) DNA repair in the extremely radioresistant bacterium Deinococcus radiodurans.Mol. Microbiol. 13, 9-15
    • (1994) Mol. Microbiol. , vol.13 , pp. 9-15
    • Minton, K.W.1
  • 13
    • 69949112356 scopus 로고    scopus 로고
    • DNA polymerase X from Deinococcus radiodurans implicated in bacterial tolerance to DNA damage is characterized as a short patch base excision repair polymerase
    • Khairnar, N. P. and Misra, H. S. (2009) DNA polymerase X from Deinococcus radiodurans implicated in bacterial tolerance to DNA damage is characterized as a short patch base excision repair polymerase. Microbiology 155, 3005-3014
    • (2009) Microbiology , vol.155 , pp. 3005-3014
    • Khairnar, N.P.1    Misra, H.S.2
  • 14
    • 0025854322 scopus 로고
    • AP endonuclease and uracil DNA glycosylase activities in Deinococcus radiodurans
    • Masters, C. I., Moseley, B. E. and Minton, K. W. (1991) AP endonuclease and uracil DNA glycosylase activities in Deinococcus radiodurans. Mutat. Res. 254, 263-272
    • (1991) Mutat. Res. , vol.254 , pp. 263-272
    • Masters, C.I.1    Moseley, B.E.2    Minton, K.W.3
  • 15
    • 0347990461 scopus 로고    scopus 로고
    • Multiple uracil-DNA glycosylase activities in Deinococcus radiodurans
    • Amst.
    • Sandigursky, M., Sandigursky, S., Sonati, P., Daly, M. J. and Franklin, W. A. (2004) Multiple uracil-DNA glycosylase activities in Deinococcus radiodurans. DNA Repair (Amst). 3, 163-169
    • (2004) DNA Repair , vol.3 , pp. 163-169
    • Sandigursky, M.1    Sandigursky, S.2    Sonati, P.3    Daly, M.J.4    Franklin, W.A.5
  • 16
    • 0030613729 scopus 로고    scopus 로고
    • The Deinococcus radiodurans uvrA gene: Identification of mutation sites in two mitomycin-sensitive strains and the first discovery of insertion sequence element from deinobacteria
    • DOI 10.1016/S0378-1119(97)00301-6, PII S0378111997003016
    • Narumi, I., Cherdchu, K., Kitayama, S. and Watanabe, H. (1997) The Deinococcus radiodurans uvrA gene: identification of mutation sites in two mitomycin-sensitive strains and the first discovery of insertion sequence element from deinobacteria. Gene 198, 115-126 (Pubitemid 27453733)
    • (1997) Gene , vol.198 , Issue.1-2 , pp. 115-126
    • Narumi, I.1    Cherdchu, K.2    Kitayama, S.3    Watanabe, H.4
  • 17
    • 0036154793 scopus 로고    scopus 로고
    • Genetic evidence that the uvsE gene product of Deinococcus radioduransR1 is a UV damage endonuclease
    • Earl, A. M., Rankin, S. K, Kim, K. P., Lamendola, O. N. and Battista, J. R. (2002) Genetic evidence that the uvsE gene product of Deinococcus radioduransR1 is a UV damage endonuclease. J. Bacteriol. 184,1003-1009
    • (2002) J. Bacteriol. , vol.184 , pp. 1003-1009
    • Earl, A.M.1    Rankin, S.K.2    Kim, K.P.3    Lamendola, O.N.4    Battista, J.R.5
  • 18
    • 0035681810 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans
    • Li, X. and Lu, A. L. (2001) Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans. J Bacteriol. 183, 6151-6158
    • (2001) J Bacteriol. , vol.183 , pp. 6151-6158
    • Li, X.1    Lu, A.L.2
  • 19
    • 11244337973 scopus 로고    scopus 로고
    • Mismatch repair ensures fidelity of replication and recombination in the radioresistant organism Deinococcus radiodurans
    • Mennecier, S., Coste, G., Servant, P., Bailone, A. and Sommer, S. (2004) Mismatch repair ensures fidelity of replication and recombination in the radioresistant organism Deinococcus radiodurans. Mol. Genet. Genomics 272, 460-469
    • (2004) Mol. Genet. Genomics , vol.272 , pp. 460-469
    • Mennecier, S.1    Coste, G.2    Servant, P.3    Bailone, A.4    Sommer, S.5
  • 20
    • 36549029300 scopus 로고    scopus 로고
    • RecBC enzyme overproduction affects UV and γ-radiation survival of Deinococcus radiodurans
    • Khairnar, N. P., Kamble, V. A. and Misra, H. S. (2008) RecBC enzyme overproduction affects UV and γ-radiation survival of Deinococcus radiodurans. DNA Repair 7, 40-47
    • (2008) DNA Repair , vol.7 , pp. 40-47
    • Khairnar, N.P.1    Kamble, V.A.2    Misra, H.S.3
  • 21
    • 62549084295 scopus 로고    scopus 로고
    • Recombination and replication in DNA repair of heavily irradiated Deinococcus radiodurans
    • Slade, D., Lindner, A. B., Paul, G. and Radman, M. (2009) Recombination and replication in DNA repair of heavily irradiated Deinococcus radiodurans. Cell 136, 1044-1055
    • (2009) Cell , vol.136 , pp. 1044-1055
    • Slade, D.1    Lindner, A.B.2    Paul, G.3    Radman, M.4
  • 22
    • 0034191838 scopus 로고    scopus 로고
    • Systematic study of parameters influencing the action of Rose Bengal with visible light on bacterial cells: Comparison between biological effect and singlet-oxygen production
    • Schaefer, M., Schmitz, C., Facius, R., Horneck, G., Milow, B., Funken, K.-H. and Ortner, J. (2000) Systematic study of parameters influencing the action of Rose Bengal with visible light on bacterial cells: comparison between biological effect and singlet-oxygen production. Photochem. Photobiol. 71, 514-523
    • (2000) Photochem. Photobiol. , vol.71 , pp. 514-523
    • Schaefer, M.1    Schmitz, C.2    Facius, R.3    Horneck, G.4    Milow, B.5    Funken, K.-H.6    Ortner, J.7
  • 24
    • 0036189582 scopus 로고    scopus 로고
    • Inactivation of two homologous proteins presumed to be involved in the desiccation tolerance of plants sensitizes Deinococcus radioduransR1 to desiccation
    • Battista, J. R., Park, M. J. and McLemore, A. E. (2001) Inactivation of two homologous proteins presumed to be involved in the desiccation tolerance of plants sensitizes Deinococcus radioduransR1 to desiccation. Cryobiology 43, 133-139
    • (2001) Cryobiology , vol.43 , pp. 133-139
    • Battista, J.R.1    Park, M.J.2    McLemore, A.E.3
  • 25
    • 0032539658 scopus 로고    scopus 로고
    • Polyamide nucleic acid-DNA chimera lacking the phosphate backbone are novel primer for polymerase reactions catalysed by DNA polymerases
    • 998
    • Misra H.S., Pandey, P.K., Modak, M.J., Vinayak, R. and Pandey, V.N. (998) Polyamide nucleic acid-DNA chimera lacking the phosphate backbone are novel primer for polymerase reactions catalysed by DNA polymerases. Biochemistry 37, 1917-1925
    • Biochemistry , vol.37 , pp. 1917-1925
    • Misra, H.S.1    Pandey, P.K.2    Modak, M.J.3    Vinayak, R.4    Pandey, V.N.5
  • 26
    • 0015312264 scopus 로고
    • Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture
    • Bolton, P. G. and Dean, A. C. (1972) Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture. Biochem. J. 127, 87-96
    • (1972) Biochem. J. , vol.127 , pp. 87-96
    • Bolton, P.G.1    Dean, A.C.2
  • 27
    • 0347130091 scopus 로고    scopus 로고
    • Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source
    • McLoughlin, S. Y., Jackson, C., Liu, J. and Ollis, D. L. (2004) Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. Appl. Environ. Microbiol. 70, 404-412
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 404-412
    • McLoughlin, S.Y.1    Jackson, C.2    Liu, J.3    Ollis, D.L.4
  • 29
    • 4344646051 scopus 로고    scopus 로고
    • The HD domain of the Escherichia colitRNA nucleotidyltransferase has 2′,3′-cyclic phosphodiesterase, 2′-nucleotidase, and phosphatase activities
    • Yakunin, A. F., Proudfoot, M., Kuznetsova, E., Savchenko, A., Brown, G., Arrowsmith, C. H. and Edwards, A. M. (2004) The HD domain of the Escherichia colitRNA nucleotidyltransferase has 2′,3′-cyclic phosphodiesterase, 2′-nucleotidase, and phosphatase activities. J. Biol. Chem. 279, 36819-36827
    • (2004) J. Biol. Chem. , vol.279 , pp. 36819-36827
    • Yakunin, A.F.1    Proudfoot, M.2    Kuznetsova, E.3    Savchenko, A.4    Brown, G.5    Arrowsmith, C.H.6    Edwards, A.M.7
  • 30
    • 0028341657 scopus 로고
    • Isolation of active recombinant XPG protein, a human DNA repair endonuclease
    • O'Donovan, A., Scherly, D., Clarkson, S. G. and Wood, R. D. (1994) Isolation of active recombinant XPG protein, a human DNA repair endonuclease. J. Biol. Chem. 269, 15965-15968
    • (1994) J. Biol. Chem. , vol.269 , pp. 15965-15968
    • O'Donovan, A.1    Scherly, D.2    Clarkson, S.G.3    Wood, R.D.4
  • 31
    • 0030756165 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the SbcCD protein from Escherichia coli
    • Connelly, J. C., de Leau, E. S., Okely, E. A. and Leach, D. R. (1997) Overexpression, purification, and characterization of the SbcCD protein from Escherichia coli. J. Biol Chem. 272, 19819-19826
    • (1997) J. Biol Chem. , vol.272 , pp. 19819-19826
    • Connelly, J.C.1    De Leau, E.S.2    Okely, E.A.3    Leach, D.R.4
  • 32
    • 77952106953 scopus 로고    scopus 로고
    • The SbcCD complex of Deinococcus radiodurans contributes to radioresistance and DNA strand break repair in vivoand exhibits Mre11/Rad50 type activity in vitro
    • Kamble, V. A. and Misra, H. S. (2010) The SbcCD complex of Deinococcus radiodurans contributes to radioresistance and DNA strand break repair in vivoand exhibits Mre11/Rad50 type activity in vitro. DNA Repair 9, 488-944
    • (2010) DNA Repair , vol.9 , pp. 488-944
    • Kamble, V.A.1    Misra, H.S.2
  • 33
    • 0035929667 scopus 로고    scopus 로고
    • DNA structure specific nuclease activities in the Saccharomyces cerevisae Rad50Mre11 complex
    • Trujillo, K. M. and Sung, P. (2001) DNA structure specific nuclease activities in the Saccharomyces cerevisae Rad50Mre11 complex. J. Biol. Chem. 276, 35458-35464
    • (2001) J. Biol. Chem. , vol.276 , pp. 35458-35464
    • Trujillo, K.M.1    Sung, P.2
  • 34
    • 0033557344 scopus 로고    scopus 로고
    • DNA cleavage and degradation by the SbcCD protein complex from Escherichia coli
    • Connelly, J. C., de Leau, E. S. and Leach, D. R. F. (1999) DNA cleavage and degradation by the SbcCD protein complex from Escherichia coli. Nucleic Acids Res. 27, 1039-1046
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1039-1046
    • Connelly, J.C.1    De Leau, E.S.2    Leach, D.R.F.3
  • 35
    • 54249125124 scopus 로고    scopus 로고
    • Identification of a DNA processing complex from Deinococcus radiodurans
    • Kota, S. and Misra, H. S. (2008) Identification of a DNA processing complex from Deinococcus radiodurans. Biochem. Cell Biol. 86, 448-458
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 448-458
    • Kota, S.1    Misra, H.S.2
  • 36
    • 74349110150 scopus 로고    scopus 로고
    • Increased synthesis of signaling molecules coincides with reversible inhibition of nucleolytic activity during postirradiation recovery of Deinococcus radiodurans
    • Kamble, V. A., Rajpurohit, Y. S., Srivastava, A. K. and Misra, H. S. (2010) Increased synthesis of signaling molecules coincides with reversible inhibition of nucleolytic activity during postirradiation recovery of Deinococcus radiodurans. FEMS Microbiol. Lett. 303, 18-25
    • (2010) FEMS Microbiol. Lett. , vol.303 , pp. 18-25
    • Kamble, V.A.1    Rajpurohit, Y.S.2    Srivastava, A.K.3    Misra, H.S.4
  • 38
    • 0024372348 scopus 로고
    • Thermotolerance of adenylylsulfate reductase from Thiobacillus denitroficans
    • Taylor, B. F. (1989) Thermotolerance of adenylylsulfate reductase from Thiobacillus denitroficans. FEMS Microbiol. Lett. 59, 351-354
    • (1989) FEMS Microbiol. Lett. , vol.59 , pp. 351-354
    • Taylor, B.F.1
  • 39
    • 0024560060 scopus 로고
    • Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus
    • Lawyer, F. C., Stoffel, S., Saik, R. K., Myambo, K., Drummond, R. and Gelfand, D. H. (1989) Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus. J. Biol. Chem. 264, 6427-6437
    • (1989) J. Biol. Chem. , vol.264 , pp. 6427-6437
    • Lawyer, F.C.1    Stoffel, S.2    Saik, R.K.3    Myambo, K.4    Drummond, R.5    Gelfand, D.H.6
  • 40
  • 41
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan, A. G. (2006) The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63, 123-143
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 42
    • 38549172995 scopus 로고    scopus 로고
    • Strucural and enzymatic characterization of DR1281: A calcineurin-like phosphoesterase from Deinococcus radiodurans
    • Shin, D. H., Proudfoot, M., Lim, H. J., Choi, I. K., Yokota, H., Yakunin, A. F., Kim, R. and Kim, S. H. (2008) Strucural and enzymatic characterization of DR1281: a calcineurin-like phosphoesterase from Deinococcus radiodurans. Proteins 70, 1000-1009
    • (2008) Proteins , vol.70 , pp. 1000-1009
    • Shin, D.H.1    Proudfoot, M.2    Lim, H.J.3    Choi, I.K.4    Yokota, H.5    Yakunin, A.F.6    Kim, R.7    Kim, S.H.8
  • 43
    • 70349243062 scopus 로고    scopus 로고
    • Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans
    • Hawwa, R., Larsen, S. D., Ratia, K. and Mesecar, A. D. (2009) Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans. J. Mol. Biol. 393, 36-57
    • (2009) J. Mol. Biol. , vol.393 , pp. 36-57
    • Hawwa, R.1    Larsen, S.D.2    Ratia, K.3    Mesecar, A.D.4
  • 44
    • 77956645364 scopus 로고    scopus 로고
    • ATP-type DNA ligase requires other proteins for its activity in vitroand its operon components for radiation resistance in Deinococcus radiodurans in vivo
    • in the press
    • Kota, S., Kamble, V. A., Rajpurohit, Y. S. and Misra, H. S. (2010) ATP-type DNA ligase requires other proteins for its activity in vitroand its operon components for radiation resistance in Deinococcus radiodurans in vivo. Biochem. Cell Biol., in the press
    • (2010) Biochem. Cell Biol.
    • Kota, S.1    Kamble, V.A.2    Rajpurohit, Y.S.3    Misra, H.S.4
  • 45
    • 0025231804 scopus 로고
    • Biochemical and physical characterization of exonuclease V from Escherichia coli: Comparison of the catalytic activity of RecBCD and RecBC enzymes
    • Palas, K. M. and Kushner, S. R. (1990) Biochemical and physical characterization of exonuclease V from Escherichia coli: comparison of the catalytic activity of RecBCD and RecBC enzymes. J. Biol. Chem. 265, 3447-3454
    • (1990) J. Biol. Chem. , vol.265 , pp. 3447-3454
    • Palas, K.M.1    Kushner, S.R.2
  • 46
    • 34347379540 scopus 로고    scopus 로고
    • Additive effects of SbcCD and PolX deficiencies in the in vivo repair of DNA double-strand breaks in Deinococcus radiodurans
    • DOI 10.1128/JB.00452-07
    • Bentchikou, E., Servant, P., Coste, G. and Sommer, S. (2007) Additive effects of SbcCD and PolX deficiencies in the in vivo repair of DNA double-strand breaks in Deinococcus radiodurans. J. Bacteriol. 189, 4784-90 (Pubitemid 47025590)
    • (2007) Journal of Bacteriology , vol.189 , Issue.13 , pp. 4784-4790
    • Bentchikou, E.1    Servant, P.2    Coste, G.3    Sommer, S.4
  • 47
    • 77249170247 scopus 로고    scopus 로고
    • Characteristics of nuclease activity of the SbcCD complex from Deinococcus radiodurans
    • Hu, Y., Tian, B., Xu, G., Yin, L., Hua, X., Lin, J. and Hua, Y. (2010) Characteristics of nuclease activity of the SbcCD complex from Deinococcus radiodurans. J. Biochem. 147, 307-315
    • (2010) J. Biochem. , vol.147 , pp. 307-315
    • Hu, Y.1    Tian, B.2    Xu, G.3    Yin, L.4    Hua, X.5    Lin, J.6    Hua, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.