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Volumn 7, Issue 10, 2012, Pages

Protein Dynamics Governed by Interfaces of High Polarity and Low Packing Density

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; LIGHT INTERFACES OF HIGH POLARITY; MOLECULAR DYNAMICS; PHYSICAL CHEMISTRY; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING;

EID: 84868117563     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0048212     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • Lange OF, Lakomek N-A, Farès C, Schröder GF, Walter KFA, et al. (2008) Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320: 1471-1475.
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1    Lakomek, N.-A.2    Farès, C.3    Schröder, G.F.4    Walter, K.F.A.5
  • 2
    • 39649103623 scopus 로고    scopus 로고
    • Thermodynamic fidelity of the mammalian cytochrome P450 2B4 active site in binding substrates and inhibitors
    • Muralidhara BK, Sun L, Negi S, Halpert JR, (2008) Thermodynamic fidelity of the mammalian cytochrome P450 2B4 active site in binding substrates and inhibitors. Journal of Molecular Biology 377: 232-245.
    • (2008) Journal of Molecular Biology , vol.377 , pp. 232-245
    • Muralidhara, B.K.1    Sun, L.2    Negi, S.3    Halpert, J.R.4
  • 3
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P, Fuxreiter M, (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33: 2-8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 4
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson CM, (2004) Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 15: 3-16.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 5
    • 36049044125 scopus 로고    scopus 로고
    • The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint
    • Mapelli M, Massimiliano L, Santaguida S, Musacchio A, (2007) The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint. Cell 131: 730-743.
    • (2007) Cell , vol.131 , pp. 730-743
    • Mapelli, M.1    Massimiliano, L.2    Santaguida, S.3    Musacchio, A.4
  • 6
    • 42449084477 scopus 로고    scopus 로고
    • Interconversion between two unrelated protein folds in the lymphotactin native state
    • Tuinstra RL, Peterson FC, Kutlesa S, Elgin ES, Kron MA, et al. (2008) Interconversion between two unrelated protein folds in the lymphotactin native state. Proc Natl Acad Sci USA 105: 5057-5062.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5057-5062
    • Tuinstra, R.L.1    Peterson, F.C.2    Kutlesa, S.3    Elgin, E.S.4    Kron, M.A.5
  • 7
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: bridging between structure and function
    • Bahar I, Lezon TR, Yang LW, Eyal E, (2010) Global dynamics of proteins: bridging between structure and function. Annu Rev Biophys 39: 23-42.
    • (2010) Annu Rev Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Yang, L.W.3    Eyal, E.4
  • 8
    • 34249930405 scopus 로고    scopus 로고
    • Protein-folding dynamics: overview of molecular simulation techniques
    • Scheraga HA, Khalili M, Liwo A, (2007) Protein-folding dynamics: overview of molecular simulation techniques. Annu Rev Phys Chem 58: 57-83.
    • (2007) Annu Rev Phys Chem , vol.58 , pp. 57-83
    • Scheraga, H.A.1    Khalili, M.2    Liwo, A.3
  • 9
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki N, Tawfik DS, (2009) Protein dynamism and evolvability. Science 324: 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 10
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James LC, Tawfik DS, (2003) Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends Biochem Sci 28: 361-368.
    • (2003) Trends Biochem Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 11
    • 33646925084 scopus 로고    scopus 로고
    • Protein folding pathways studied by pulsed- and native-state hydrogen exchange
    • Bai Y, (2006) Protein folding pathways studied by pulsed- and native-state hydrogen exchange. Chem Rev 106: 1757-1768.
    • (2006) Chem Rev , vol.106 , pp. 1757-1768
    • Bai, Y.1
  • 12
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander SW, (2000) Protein folding intermediates and pathways studied by hydrogen exchange. Annu Rev Biophys Biomol Struct 29: 213-238.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 13
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht AR, Matouschek A, Serrano L, (1992) The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. Journal of Molecular Biology 224: 771-782.
    • (1992) Journal of Molecular Biology , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 14
    • 7044231161 scopus 로고    scopus 로고
    • Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate
    • Campos LA, Bueno M, Lopez-Llano J, Jiménez MA, Sancho J, (2004) Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. Journal of Molecular Biology 344: 239-255.
    • (2004) Journal of Molecular Biology , vol.344 , pp. 239-255
    • Campos, L.A.1    Bueno, M.2    Lopez-Llano, J.3    Jiménez, M.A.4    Sancho, J.5
  • 15
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis T, Karplus M, (1997) "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science 278: 1928-1931.
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 16
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • Snow CD, Nguyen H, Pande VS, Gruebele M, (2002) Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420: 102-106.
    • (2002) Nature , vol.420 , pp. 102-106
    • Snow, C.D.1    Nguyen, H.2    Pande, V.S.3    Gruebele, M.4
  • 17
    • 0030580089 scopus 로고    scopus 로고
    • Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
    • Hilser VJ, Freire E, (1996) Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J Mol Biol 262: 756-772.
    • (1996) J Mol Biol , vol.262 , pp. 756-772
    • Hilser, V.J.1    Freire, E.2
  • 19
    • 84862908883 scopus 로고    scopus 로고
    • Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX
    • Liu T, Pantazatos D, Li S, Hamuro Y, Hilser VJ, et al. (2012) Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX. J Am Soc Mass Spectrom 23: 43-56.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 43-56
    • Liu, T.1    Pantazatos, D.2    Li, S.3    Hamuro, Y.4    Hilser, V.J.5
  • 20
    • 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
  • 21
    • 36549043024 scopus 로고    scopus 로고
    • Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation
    • Bahar I, Chennubhotla C, Tobi D, (2007) Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation. Curr Opin Struct Biol 17: 633-640.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 633-640
    • Bahar, I.1    Chennubhotla, C.2    Tobi, D.3
  • 22
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar I, Rader AJ, (2005) Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol 15: 586-592.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 23
    • 24644483073 scopus 로고    scopus 로고
    • Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase
    • Maragakis P, Karplus M, (2005) Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase. Journal of Molecular Biology 352: 807-822.
    • (2005) Journal of Molecular Biology , vol.352 , pp. 807-822
    • Maragakis, P.1    Karplus, M.2
  • 24
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita O, Onuchic JN, Wolynes PG, (2003) Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. Proc Natl Acad Sci USA 100: 12570-12575.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 25
    • 33645315212 scopus 로고    scopus 로고
    • Hydrogen bonding increases packing density in the protein interior
    • Schell D, Tsai J, Scholtz JM, Pace CN, (2006) Hydrogen bonding increases packing density in the protein interior. Proteins 63: 278-282.
    • (2006) Proteins , vol.63 , pp. 278-282
    • Schell, D.1    Tsai, J.2    Scholtz, J.M.3    Pace, C.N.4
  • 27
    • 34447524018 scopus 로고    scopus 로고
    • Atomic contacts in protein structures. A detailed analysis of atomic radii, packing, and overlaps
    • Seeliger D, de Groot BL, (2007) Atomic contacts in protein structures. A detailed analysis of atomic radii, packing, and overlaps. Proteins 68: 595-601.
    • (2007) Proteins , vol.68 , pp. 595-601
    • Seeliger, D.1    de Groot, B.L.2
  • 28
    • 65449171120 scopus 로고    scopus 로고
    • ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble
    • Estrada J, Bernado P, Blackledge M, Sancho J, (2009) ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble. BMC Bioinformatics 10: 104.
    • (2009) BMC Bioinformatics , vol.10 , pp. 104
    • Estrada, J.1    Bernado, P.2    Blackledge, M.3    Sancho, J.4
  • 29
    • 33845408125 scopus 로고    scopus 로고
    • Sequence-specific solvent accessibilities of protein residues in unfolded protein ensembles
    • Bernado P, Blackledge M, Sancho J, (2006) Sequence-specific solvent accessibilities of protein residues in unfolded protein ensembles. Biophys J 91: 4536-4543.
    • (2006) Biophys J , vol.91 , pp. 4536-4543
    • Bernado, P.1    Blackledge, M.2    Sancho, J.3
  • 30
    • 1842788912 scopus 로고    scopus 로고
    • Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins
    • Eyal E, Najmanovich R, McConkey BJ, Edelman M, Sobolev V, (2004) Importance of solvent accessibility and contact surfaces in modeling side-chain conformations in proteins. J Comput Chem 25: 712-724.
    • (2004) J Comput Chem , vol.25 , pp. 712-724
    • Eyal, E.1    Najmanovich, R.2    McConkey, B.J.3    Edelman, M.4    Sobolev, V.5
  • 31
    • 77954383580 scopus 로고    scopus 로고
    • Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins
    • Ayuso-Tejedor S, Angarica VE, Bueno M, Campos LA, Abián O, et al. (2010) Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins. Journal of Molecular Biology 400: 922-934.
    • (2010) Journal of Molecular Biology , vol.400 , pp. 922-934
    • Ayuso-Tejedor, S.1    Angarica, V.E.2    Bueno, M.3    Campos, L.A.4    Abián, O.5
  • 32
    • 79951675082 scopus 로고    scopus 로고
    • Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering
    • Ayuso-Tejedor S, Garcia-Fandino R, Orozco M, Sancho J, Bernado P, (2011) Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering. J Mol Biol 406: 604-619.
    • (2011) J Mol Biol , vol.406 , pp. 604-619
    • Ayuso-Tejedor, S.1    Garcia-Fandino, R.2    Orozco, M.3    Sancho, J.4    Bernado, P.5
  • 33
    • 0035371555 scopus 로고    scopus 로고
    • Anabaena apoflavodoxin hydrogen exchange: on the stable exchange core of the alpha/beta(21345) flavodoxin-like family
    • Langdon GM, Jimenez MA, Genzor CG, Maldonado S, Sancho J, et al. (2001) Anabaena apoflavodoxin hydrogen exchange: on the stable exchange core of the alpha/beta(21345) flavodoxin-like family. Proteins 43: 476-488.
    • (2001) Proteins , vol.43 , pp. 476-488
    • Langdon, G.M.1    Jimenez, M.A.2    Genzor, C.G.3    Maldonado, S.4    Sancho, J.5
  • 35
    • 52949132638 scopus 로고    scopus 로고
    • Cavities and atomic packing in protein structures and interfaces
    • Sonavane S, Chakrabarti P, (2008) Cavities and atomic packing in protein structures and interfaces. PLoS Comput Biol 4: e1000188.
    • (2008) PLoS Comput Biol , vol.4
    • Sonavane, S.1    Chakrabarti, P.2
  • 38
    • 0029643523 scopus 로고
    • Protein folding intermediates: native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW, (1995) Protein folding intermediates: native-state hydrogen exchange. Science 269: 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 39
    • 34548406580 scopus 로고    scopus 로고
    • Branching in the sequential folding pathway of cytochrome c
    • Krishna MM, Maity H, Rumbley JN, Englander SW, (2007) Branching in the sequential folding pathway of cytochrome c. Protein Sci 16: 1946-1956.
    • (2007) Protein Sci , vol.16 , pp. 1946-1956
    • Krishna, M.M.1    Maity, H.2    Rumbley, J.N.3    Englander, S.W.4
  • 40
    • 8744301024 scopus 로고    scopus 로고
    • The long and short flavodoxins: I. The role of the differentiating loop in apoflavodoxin structure and FMN binding
    • Lopez-Llano J, Maldonado S, Bueno M, Lostao A, Angeles-Jimenez M, et al. (2004) The long and short flavodoxins: I. The role of the differentiating loop in apoflavodoxin structure and FMN binding. J Biol Chem 279: 47177-47183.
    • (2004) J Biol Chem , vol.279 , pp. 47177-47183
    • Lopez-Llano, J.1    Maldonado, S.2    Bueno, M.3    Lostao, A.4    Angeles-Jimenez, M.5
  • 41
    • 0021114569 scopus 로고
    • Molten-globule state': a compact form of globular proteins with mobile side-chains
    • Ohgushi M, Wada A, (1983) 'Molten-globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett 164: 21-24.
    • (1983) FEBS Lett , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 42
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • Kuwajima K, (1996) The molten globule state of alpha-lactalbumin. Faseb J 10: 102-109.
    • (1996) Faseb J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 43
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman BA, Kim PS, Dobson CM, Redfield C, (1997) A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat Struct Biol 4: 630-634.
    • (1997) Nat Struct Biol , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 44
    • 35548965931 scopus 로고    scopus 로고
    • Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Go model simulation
    • Gu Z, Rao MK, Forsyth WR, Finke JM, Matthews CR, (2007) Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Go model simulation. J Mol Biol 374: 528-546.
    • (2007) J Mol Biol , vol.374 , pp. 528-546
    • Gu, Z.1    Rao, M.K.2    Forsyth, W.R.3    Finke, J.M.4    Matthews, C.R.5
  • 45
    • 33947593231 scopus 로고    scopus 로고
    • Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus
    • Gu Z, Zitzewitz JA, Matthews CR, (2007) Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus. J Mol Biol 368: 582-594.
    • (2007) J Mol Biol , vol.368 , pp. 582-594
    • Gu, Z.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 46
    • 0036071577 scopus 로고    scopus 로고
    • Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels
    • Forsyth WR, Matthews CR, (2002) Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels. J Mol Biol 320: 1119-1133.
    • (2002) J Mol Biol , vol.320 , pp. 1119-1133
    • Forsyth, W.R.1    Matthews, C.R.2
  • 47
    • 24644462765 scopus 로고    scopus 로고
    • Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values
    • Salvatella X, Dobson CM, Fersht AR, Vendruscolo M, (2005) Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values. Proc Natl Acad Sci U S A 102: 12389-12394.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12389-12394
    • Salvatella, X.1    Dobson, C.M.2    Fersht, A.R.3    Vendruscolo, M.4
  • 48
    • 25144442821 scopus 로고    scopus 로고
    • COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures
    • Vertrees J, Barritt P, Whitten S, Hilser VJ, (2005) COREX/BEST server: a web browser-based program that calculates regional stability variations within protein structures. Bioinformatics 21: 3318-3319.
    • (2005) Bioinformatics , vol.21 , pp. 3318-3319
    • Vertrees, J.1    Barritt, P.2    Whitten, S.3    Hilser, V.J.4
  • 49
    • 66349132195 scopus 로고    scopus 로고
    • Relating protein conformational changes to packing efficiency and disorder
    • Bhardwaj N, Gerstein M, (2009) Relating protein conformational changes to packing efficiency and disorder. Protein Sci 18: 1230-1240.
    • (2009) Protein Sci , vol.18 , pp. 1230-1240
    • Bhardwaj, N.1    Gerstein, M.2
  • 50
    • 0000627329 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and molecular recognition
    • Freire E, (1997) Thermodynamics of protein folding and molecular recognition. Pure & Appl Chem 69: 2253-2261.
    • (1997) Pure & Appl Chem , vol.69 , pp. 2253-2261
    • Freire, E.1
  • 52
    • 0003742069 scopus 로고
    • University College London, London, UK. NACCESS Computer Program Department of Biochemistry and Molecular Biology University College London, London, UK
    • Hubbard SJ, Thornton JM (1993) NACCESS Computer Program Department of Biochemistry and Molecular Biology. University College London, London, UK. NACCESS Computer Program Department of Biochemistry and Molecular Biology University College London, London, UK.
    • (1993) NACCESS Computer Program Department of Biochemistry and Molecular Biology
    • Hubbard, S.J.1    Thornton, J.M.2
  • 53
    • 12544256134 scopus 로고    scopus 로고
    • Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly
    • Voss NR, Gerstein M, (2005) Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly. J Mol Biol 346: 477-492.
    • (2005) J Mol Biol , vol.346 , pp. 477-492
    • Voss, N.R.1    Gerstein, M.2
  • 55
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels
    • Russell RB, Barton GJ, (1992) Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14: 309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2


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