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Volumn 87, Issue 6, 2004, Pages 3703-3715

Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; GLUTAMINE; MAGNESIUM ION; NUCLEOTIDE; PROTEIN; PROTEIN HISP; UNCLASSIFIED DRUG;

EID: 10044244918     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.046870     Document Type: Article
Times cited : (40)

References (50)
  • 2
    • 0036154304 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the ligand binding domain of the ionotropic glutamate receptor, GluR2
    • Arinaminpathy, Y., M. S. P. Sansom, and P. C. Biggin. 2002. Molecular dynamics simulations of the ligand binding domain of the ionotropic glutamate receptor, GluR2. Biophys. J. 82:676-683.
    • (2002) Biophys. J. , vol.82 , pp. 676-683
    • Arinaminpathy, Y.1    Sansom, M.S.P.2    Biggin, P.C.3
  • 4
    • 0000457975 scopus 로고
    • Force-field parameterization by weak-coupling: Reengineering SPC water
    • Berweger, C. D., W. F. van Gunsteren, and F. Mullerplathe. 1995. Force-field parameterization by weak-coupling: reengineering SPC water. Chem. Phys. Lett. 232:429-436.
    • (1995) Chem. Phys. Lett. , vol.232 , pp. 429-436
    • Berweger, C.D.1    Van Gunsteren, W.F.2    Mullerplathe, F.3
  • 5
    • 0036175994 scopus 로고    scopus 로고
    • Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase
    • Bockmann, R. A., and H. Grubmuller. 2002. Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase. Nat. Struct. Biol. 9:198-202.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 198-202
    • Bockmann, R.A.1    Grubmuller, H.2
  • 6
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: Modelling and simulation studies of MsbA
    • Campbell, J. D., P. C. Biggin, M. Baaden, and M. S. P. Sansom. 2003. Extending the structure of an ABC transporter to atomic resolution: modelling and simulation studies of MsbA. Biochemistry. 42:3666-3673.
    • (2003) Biochemistry , vol.42 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.P.4
  • 7
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang, G. 2003. Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 330:419-430.
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 8
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., and C. B. Roth. 2001. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science. 293:1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 9
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., G. Lu, J. Lin, A. L. Davidson, and F. A. Quiocho. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell. 12:651-661.
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 10
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 11
    • 0029868327 scopus 로고    scopus 로고
    • The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis
    • Davidson, A. L., S. S. Laghaeian, and D. E. Mannering. 1996. The maltose transport system of Escherichia coli displays positive cooperativity in ATP hydrolysis. J. Biol. Chem. 271:4858-4863.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4858-4863
    • Davidson, A.L.1    Laghaeian, S.S.2    Mannering, D.E.3
  • 12
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs, K., J. Diez, G. Greller, C. Muller, J. Breed, C. Schnell, C. Vonrhein, W. Boos, and W. Welte. 2000. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19:5951-5961.
    • (2000) EMBO J. , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Muller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 13
    • 0035836477 scopus 로고    scopus 로고
    • Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity
    • Druley, T. E., W. D. Stein, and I. B. Roninson. 2001. Analysis of MDR1 P-glycoprotein conformational changes in permeabilized cells using differential immunoreactivity. Biochemistry. 40:4312-4322.
    • (2001) Biochemistry , vol.40 , pp. 4312-4322
    • Druley, T.E.1    Stein, W.D.2    Roninson, I.B.3
  • 14
    • 4344703330 scopus 로고    scopus 로고
    • Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: Location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations
    • Efremov, R. G., Y. A. Kosinsky, D. E. Nolde, R. Tsivkovskii, A. S. Arseniev, and S. Lutsenko. 2004. Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations. Biochem. J. 382:293-305.
    • (2004) Biochem. J. , vol.382 , pp. 293-305
    • Efremov, R.G.1    Kosinsky, Y.A.2    Nolde, D.E.3    Tsivkovskii, R.4    Arseniev, A.S.5    Lutsenko, S.6
  • 15
    • 0037162468 scopus 로고    scopus 로고
    • Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter
    • Fetsch, E. E., and A. L. Davidson. 2002. Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter. Proc. Natl. Acad. Sci. USA. 99:9685-9690.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9685-9690
    • Fetsch, E.E.1    Davidson, A.L.2
  • 17
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 18
    • 0019965825 scopus 로고
    • Complete nucleotide-sequence and identification of membrane-components of the histidine transport operon of S. typhimurium
    • Higgins, C. F., P. D. Haag, K. Nikaido, F. Ardeshir, G. Garcia, and G. F. Ames. 1982. Complete nucleotide-sequence and identification of membrane-components of the histidine transport operon of S. typhimurium. Nature. 298:723-727.
    • (1982) Nature , vol.298 , pp. 723-727
    • Higgins, C.F.1    Haag, P.D.2    Nikaido, K.3    Ardeshir, F.4    Garcia, G.5    Ames, G.F.6
  • 19
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I. B., and M. A. Blight. 1999. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 293:381-399.
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 21
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., I. X. Y. Wang, K. Nikaido, P. Q. Liu, G. F. L. Ames, and S. H. Kim. 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.Y.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.L.5    Kim, S.H.6
  • 22
    • 0036789902 scopus 로고    scopus 로고
    • Mechanism of ABC transporters: A molecular dynamics simulation of a well characterized nucleotide-binding subunit
    • Jones, P. M., and A. M. George. 2002. Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit. Proc. Natl. Acad. Sci. USA. 99:12639-12644.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12639-12644
    • Jones, P.M.1    George, A.M.2
  • 23
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P. M., and A. M. George. 2004. The ABC transporter structure and mechanism: perspectives on recent research. Cell. Mol. Life Sci. 61:682-699.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • Karpowich, N., O. Martsinkevich, L. Millen, Y. R. Yuan, P. L. Dai, K. MacVey, P. J. Thomas, and J. F. Hunt. 2001. Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure. 9:571-586.
    • (2001) Structure , vol.9 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Millen, L.3    Yuan, Y.R.4    Dai, P.L.5    MacVey, K.6    Thomas, P.J.7    Hunt, J.F.8
  • 26
    • 0037133735 scopus 로고    scopus 로고
    • Structure and association of ATP-binding cassette transporter nucleotide-binding domains
    • Kerr, I. D. 2002. Structure and association of ATP-binding cassette transporter nucleotide-binding domains. Biochim. Biophys. Acta. 1561: 47-64.
    • (2002) Biochim. Biophys. Acta , vol.1561 , pp. 47-64
    • Kerr, I.D.1
  • 27
    • 0034700252 scopus 로고    scopus 로고
    • Nonequivalence of the nucleotide-binding subunits of an ABC transporter, the histidine permease, and conformational changes in the membrane complex
    • Kreimer, D. I., K. P. Chai, and G. F. L. Ames. 2000. Nonequivalence of the nucleotide-binding subunits of an ABC transporter, the histidine permease, and conformational changes in the membrane complex. Biochemistry. 39:14183-14195.
    • (2000) Biochemistry , vol.39 , pp. 14183-14195
    • Kreimer, D.I.1    Chai, K.P.2    Ames, G.F.L.3
  • 28
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 29
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton, K. J., and C. F. Higgins. 1998. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28:5-13.
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 30
    • 0036120120 scopus 로고    scopus 로고
    • P-glycoprotein misfolds in Escherichia coli: Evidence against alternating-topology models of the transport cycle
    • Linton, K. J., and C. F. Higgins. 2002. P-glycoprotein misfolds in Escherichia coli: evidence against alternating-topology models of the transport cycle. Mol. Membr. Biol. 19:51-58.
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 51-58
    • Linton, K.J.1    Higgins, C.F.2
  • 31
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., A. T. Lee, and D. C. Rees. 2002. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science. 296:1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 32
    • 0036829647 scopus 로고    scopus 로고
    • The "LSGGQ" motif in each nucleotide-binding domain of human p-glycoprotein is adjacent to the opposing Walker A sequence
    • Loo, T. W., M. C. Bartlett, and D. M. Clarke. 2002. The "LSGGQ" motif in each nucleotide-binding domain of human p-glycoprotein is adjacent to the opposing Walker A sequence. J. Biol. Chem. 277:41303-41306.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 33
    • 0034601776 scopus 로고    scopus 로고
    • Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis
    • Martin, C., G. Berridge, P. Mistry, C. Higgins, P. Charlton, and R. Callaghan. 2000. Drug binding sites on P-glycoprotein are altered by ATP binding prior to nucleotide hydrolysis. Biochemistry. 39:11901-11906.
    • (2000) Biochemistry , vol.39 , pp. 11901-11906
    • Martin, C.1    Berridge, G.2    Mistry, P.3    Higgins, C.4    Charlton, P.5    Callaghan, R.6
  • 35
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose maltodextrins of Salmonella typhimurium: Characterization of the ATPase activity associated with the purified MalK subunit
    • Morbach, S., S. Tebbe, and E. Schneider. 1993. The ATP-binding cassette (ABC) transporter for maltose maltodextrins of Salmonella typhimurium: characterization of the ATPase activity associated with the purified MalK subunit. J. Biol. Chem. 268:18617-18621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18617-18621
    • Morbach, S.1    Tebbe, S.2    Schneider, E.3
  • 36
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido, K., and G. F. L. Ames. 1999. One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J. Biol. Chem. 274:26727-26735.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.L.2
  • 37
    • 0036225157 scopus 로고    scopus 로고
    • Computational studies on prion proteins: Effect of Ala117→Val mutation
    • Okimoto, N., K. Yamanaka, A. Suenaga, M. Hata, and T. Hoshino. 2002. Computational studies on prion proteins: effect of Ala117→Val mutation. Biophys. J. 82:2746-2757.
    • (2002) Biophys. J. , vol.82 , pp. 2746-2757
    • Okimoto, N.1    Yamanaka, K.2    Suenaga, A.3    Hata, M.4    Hoshino, T.5
  • 39
    • 7244240754 scopus 로고    scopus 로고
    • Conformational transitions induced by the binding of mgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD
    • Oloo, E. O., and D. P. Tieleman. 2004. Conformational transitions induced by the binding of mgATP to the vitamin B12 ATP-binding cassette (ABC) transporter BtuCD. J. Biol. Chem. 279:45013-45019.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45013-45019
    • Oloo, E.O.1    Tieleman, D.P.2
  • 40
    • 0037671391 scopus 로고    scopus 로고
    • Interdomain dynamics and ligand binding: Molecular dynamics simulations of glutamine binding protein
    • Pang, A., Y. Arinaminpathy, M. S. P. Sansom, and P. C. Biggin. 2003. Interdomain dynamics and ligand binding: molecular dynamics simulations of glutamine binding protein. FEBS Lett. 550:168-174.
    • (2003) FEBS Lett. , vol.550 , pp. 168-174
    • Pang, A.1    Arinaminpathy, Y.2    Sansom, M.S.P.3    Biggin, P.C.4
  • 41
    • 0344119509 scopus 로고    scopus 로고
    • A computational study of the open and closed forms of the N-lobe human serum transferrin apoprotein
    • Rinaldo, D., and M. J. Field. 2003. A computational study of the open and closed forms of the N-lobe human serum transferrin apoprotein. Biophys. J. 85:3485-3501.
    • (2003) Biophys. J. , vol.85 , pp. 3485-3501
    • Rinaldo, D.1    Field, M.J.2
  • 43
    • 0028109264 scopus 로고
    • Nucleotide-induced conformational-changes of MalK, a bacterial ATP binding cassette transporter protein
    • Schneider, E., S. Wilken, and R. Schmid. 1994. Nucleotide-induced conformational-changes of MalK, a bacterial ATP binding cassette transporter protein. J. Biol. Chem. 269:20456-20461.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20456-20461
    • Schneider, E.1    Wilken, S.2    Schmid, R.3
  • 44
    • 67650047300 scopus 로고    scopus 로고
    • Probing of conformational changes, catalytic cycle and ABC transporter function
    • B. I. Holland, S. P. C. Cole, K. Kuchler, and C. F. Higgins, editors. Academic Press, London, UK
    • Sharom, F. J. 2003. Probing of conformational changes, catalytic cycle and ABC transporter function. In ABC Proteins: From Bacteria to Man. B. I. Holland, S. P. C. Cole, K. Kuchler, and C. F. Higgins, editors. Academic Press, London, UK.
    • (2003) ABC Proteins: From Bacteria to Man
    • Sharom, F.J.1
  • 45
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C., N. Karpowich, L. Millen, J. E. Moody, J. Rosen, P. J. Thomas, and J. F. Hunt. 2002. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell. 10:139-149.
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 46
    • 10044237542 scopus 로고    scopus 로고
    • Ligand-mediated structure changes of reconstituted P-glycoprotein
    • Abstr.
    • Sonveaux, N., A. B. Shapiro, C. Vigano, and J. M. Ruysschaert. 1999. Ligand-mediated structure changes of reconstituted P-glycoprotein. Biophys. J. 76:102. (Abstr.).
    • (1999) Biophys. J. , vol.76 , pp. 102
    • Sonveaux, N.1    Shapiro, A.B.2    Vigano, C.3    Ruysschaert, J.M.4
  • 47
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch, I. L., K. Gimi, S. Wilke-Mounts, and A. E. Senior. 2000. Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein. Biochemistry. 39:11921-11927.
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 48
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch, I. L., B. Sankaran, S. Bhagat, and A. E. Senior. 1995. Both P-glycoprotein nucleotide-binding sites are catalytically active. J. Biol. Chem. 270:26956-26961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 49
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-subunits and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the alpha-subunits and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 50
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette: Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter
    • Yuan, Y. R., S. Blecker, O. Martsinkevich, L. Millen, P. J. Thomas, and J. F. Hunt. 2001. The crystal structure of the MJ0796 ATP-binding cassette: implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter. J. Biol. Chem. 276:32313-32321.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.R.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6


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