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Volumn 10, Issue 9, 2014, Pages 723-731

How proteins bind macrocycles

Author keywords

[No Author keywords available]

Indexed keywords

MACROCYCLIC COMPOUND; PROTEIN;

EID: 84906307859     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1584     Document Type: Article
Times cited : (327)

References (56)
  • 2
    • 50249154886 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions
    • Berg, T. Small-molecule inhibitors of protein-protein interactions. Curr. Opin. Drug Discov. Devel. 11, 666-674 (2008).
    • (2008) Curr. Opin. Drug Discov. Devel. , vol.11 , pp. 666-674
    • Berg, T.1
  • 3
    • 79951960238 scopus 로고    scopus 로고
    • Small-molecule protein-protein interaction inhibitors: Therapeutic potential in light of molecular size, chemical space, and ligand binding efficiency considerations
    • Buchwald, P. Small-molecule protein-protein interaction inhibitors: therapeutic potential in light of molecular size, chemical space, and ligand binding efficiency considerations. IUBMB Life 62, 724-731 (2010).
    • (2010) IUBMB Life , vol.62 , pp. 724-731
    • Buchwald, P.1
  • 4
    • 33646567148 scopus 로고    scopus 로고
    • Between a rock and a hard place?
    • Whitty, A. & Kumaravel, G. Between a rock and a hard place? Nat. Chem. Biol. 2, 112-118 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 112-118
    • Whitty, A.1    Kumaravel, G.2
  • 5
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J.A. & McClendon, C.L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 (2007).
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 6
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P.J. & Greer, J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 6, 211-219 (2007).
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 7
    • 84873433440 scopus 로고    scopus 로고
    • Using a fragment-based approach to target protein-protein interactions
    • Scott, D.E. et al. Using a fragment-based approach to target protein-protein interactions. ChemBioChem 14, 332-342 (2013).
    • (2013) ChemBioChem , vol.14 , pp. 332-342
    • Scott, D.E.1
  • 8
    • 79960990847 scopus 로고    scopus 로고
    • And structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • Morelli, X., Bourgeas, R. & Roche, P. Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I). Curr. Opin. Chem. Biol. 15, 475-481 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Chemical, R.P.3
  • 9
    • 84876546810 scopus 로고    scopus 로고
    • 2P2Idb: A structural database dedicated to orthosteric modulation of protein-protein interactions
    • Basse, M.J. et al. 2P2Idb: a structural database dedicated to orthosteric modulation of protein-protein interactions. Nucleic Acids Res. 41, D824-D827 (2013).
    • (2013) Nucleic Acids Res. , vol.41
    • Basse, M.J.1
  • 11
    • 4444291734 scopus 로고    scopus 로고
    • Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix
    • Walensky, L.D. et al. Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Science 305, 1466-1470 (2004).
    • (2004) Science , vol.305 , pp. 1466-1470
    • Walensky, L.D.1
  • 12
    • 35048895357 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: Lessons from p53/MDM2
    • Murray, J.K. & Gellman, S.H. Targeting protein-protein interactions: lessons from p53/MDM2. Biopolymers 88, 657-686 (2007).
    • (2007) Biopolymers , vol.88 , pp. 657-686
    • Murray, J.K.1    Gellman, S.H.2
  • 13
    • 84879020527 scopus 로고    scopus 로고
    • Plucking the high hanging fruit: A systematic approach for targeting protein-protein interactions
    • Raj, M., Bullock, B.N. & Arora, P.S. Plucking the high hanging fruit: a systematic approach for targeting protein-protein interactions. Bioorg. Med. Chem. 21, 4051-4057 (2013).
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 4051-4057
    • Raj, M.1    Bullock, B.N.2    Arora, P.S.3
  • 14
    • 46449115901 scopus 로고    scopus 로고
    • The exploration of macrocycles for drug discovery-an underexploited structural class
    • Driggers, E.M., Hale, S.P., Lee, J. & Terrett, N.K. The exploration of macrocycles for drug discovery-an underexploited structural class. Nat. Rev. Drug Discov. 7, 608-624 (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 608-624
    • Driggers, E.M.1    Hale, S.P.2    Lee, J.3    Terrett, N.K.4
  • 15
    • 15444377930 scopus 로고    scopus 로고
    • What can a chemist learn from nature's macrocycles? - A brief, conceptual view
    • Wessjohann, L.A., Ruijter, E., Garcia-Rivera, D. & Brandt, W. What can a chemist learn from nature's macrocycles?-a brief, conceptual view. Mol. Divers. 9, 171-186 (2005).
    • (2005) Mol. Divers. , vol.9 , pp. 171-186
    • Wessjohann, L.A.1    Ruijter, E.2    Garcia-Rivera, D.3    Brandt, W.4
  • 16
    • 79953777824 scopus 로고    scopus 로고
    • Macrocycles are great cycles: Applications, opportunities, and challenges of synthetic macrocycles in drug discovery
    • Marsault, E. & Peterson, M.L. Macrocycles are great cycles: applications, opportunities, and challenges of synthetic macrocycles in drug discovery. J. Med. Chem. 54, 1961-2004 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 1961-2004
    • Marsault, E.1    Peterson, M.L.2
  • 17
    • 84864679725 scopus 로고    scopus 로고
    • Macrocycles in new drug discovery
    • Mallinson, J. & Collins, I. Macrocycles in new drug discovery. Future Med. Chem. 4, 1409-1438 (2012).
    • (2012) Future Med. Chem. , vol.4 , pp. 1409-1438
    • Mallinson, J.1    Collins, I.2
  • 18
    • 84879641206 scopus 로고    scopus 로고
    • Macrocyclic drugs and synthetic methodologies toward macrocycles
    • Yu, X. & Sun, D. Macrocyclic drugs and synthetic methodologies toward macrocycles. Molecules 18, 6230-6268 (2013).
    • (2013) Molecules , vol.18 , pp. 6230-6268
    • Yu, X.1    Sun, D.2
  • 19
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: What can medicinal chemists learn from their properties?
    • Giordanetto, F. & Kihlberg, J. Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties? J. Med. Chem. 57, 278-295 (2014).
    • (2014) J. Med. Chem. , vol.57 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 20
    • 44949134801 scopus 로고    scopus 로고
    • The impact of natural products upon modern drug discovery
    • Ganesan, A. The impact of natural products upon modern drug discovery. Curr. Opin. Chem. Biol. 12, 306-317 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 306-317
    • Ganesan, A.1
  • 21
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • Lipinski, C.A. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 44, 235-249 (2000).
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 22
    • 41549115075 scopus 로고    scopus 로고
    • Assessing drug-likeness-what are we missing?
    • Vistoli, G., Pedretti, A. & Testa, B. Assessing drug-likeness-what are we missing? Drug Discov. Today 13, 285-294 (2008).
    • (2008) Drug Discov. Today , vol.13 , pp. 285-294
    • Vistoli, G.1    Pedretti, A.2    Testa, B.3
  • 23
    • 77955615249 scopus 로고    scopus 로고
    • Chemoinformatic analysis of biologically active macrocycles
    • Brandt, W., Haupt, V.J. & Wessjohann, L.A. Chemoinformatic analysis of biologically active macrocycles. Curr. Top. Med. Chem. 10, 1361-1379 (2010).
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 1361-1379
    • Brandt, W.1    Haupt, V.J.2    Wessjohann, L.A.3
  • 24
    • 84878789554 scopus 로고    scopus 로고
    • Form and function in cyclic peptide natural products: A pharmacokinetic perspective
    • Bockus, A.T., McEwen, C.M. & Lokey, R.S. Form and function in cyclic peptide natural products: a pharmacokinetic perspective. Curr. Top. Med. Chem. 13, 821-836 (2013).
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 821-836
    • Bockus, A.T.1    McEwen, C.M.2    Lokey, R.S.3
  • 25
    • 80054853098 scopus 로고    scopus 로고
    • On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds
    • White, T.R. et al. On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat. Chem. Biol. 7, 810-817 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 810-817
    • White, T.R.1
  • 26
    • 61449104961 scopus 로고    scopus 로고
    • Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques
    • Brenke, R. et al. Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques. Bioinformatics 25, 621-627 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 621-627
    • Brenke, R.1
  • 27
    • 33947658802 scopus 로고    scopus 로고
    • Identification of hot spots within druggable binding regions by computational solvent mapping of proteins
    • Landon, M.R., Lancia, D.R. Jr., Yu, J., Thiel, S.C. & Vajda, S. Identification of hot spots within druggable binding regions by computational solvent mapping of proteins. J. Med. Chem. 50, 1231-1240 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 1231-1240
    • Landon, M.R.1    Lancia Jr., D.R.2    Yu, J.3    Thiel, S.C.4    Vajda, S.5
  • 28
    • 80051966197 scopus 로고    scopus 로고
    • Structural conservation of druggable hot spots in protein-protein interfaces
    • Kozakov, D. et al. Structural conservation of druggable hot spots in protein-protein interfaces. Proc. Natl. Acad. Sci. USA 108, 13528-13533 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13528-13533
    • Kozakov, D.1
  • 29
    • 84862192766 scopus 로고    scopus 로고
    • ChEMBL: A large-scale bioactivity database for drug discovery
    • Gaulton, A. et al. ChEMBL: a large-scale bioactivity database for drug discovery. Nucleic Acids Res. 40, D1100-D1107 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Gaulton, A.1
  • 30
    • 1642357706 scopus 로고    scopus 로고
    • The many roles of computation in drug discovery
    • Jorgensen, W.L. The many roles of computation in drug discovery. Science 303, 1813-1818 (2004).
    • (2004) Science , vol.303 , pp. 1813-1818
    • Jorgensen, W.L.1
  • 31
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C. & Janin, J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 32
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drug-binding sites
    • Nayal, M. & Honig, B. On the nature of cavities on protein surfaces: application to the identification of drug-binding sites. Proteins 63, 892-906 (2006).
    • (2006) Proteins , vol.63 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 33
    • 33746885488 scopus 로고    scopus 로고
    • Probing hot spots at protein-ligand binding sites: A fragment-based approach using biophysical methods
    • Ciulli, A., Williams, G., Smith, A.G., Blundell, T.L. & Abell, C. Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods. J. Med. Chem. 49, 4992-5000 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 4992-5000
    • Ciulli, A.1    Williams, G.2    Smith, A.G.3    Blundell, T.L.4    Abell, C.5
  • 34
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • DeLano, W.L. Unraveling hot spots in binding interfaces: progress and challenges. Curr. Opin. Struct. Biol. 12, 14-20 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • Delano, W.L.1
  • 35
    • 33947658802 scopus 로고    scopus 로고
    • Identification of hot spots within druggable binding regions by computational solvent mapping of proteins
    • Landon, M.R., Lancia, D.R. Jr., Yu, J., Thiel, S.C. & Vajda, S. Identification of hot spots within druggable binding regions by computational solvent mapping of proteins. J. Med. Chem. 50, 1231-1240 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 1231-1240
    • Landon, M.R.1    Lancia Jr., D.R.2    Yu, J.3    Thiel, S.C.4    Vajda, S.5
  • 36
    • 72149100511 scopus 로고    scopus 로고
    • Binding hot spots and amantadine orientation in the influenza A virus M2 proton channel
    • Chuang, G.Y. et al. Binding hot spots and amantadine orientation in the influenza A virus M2 proton channel. Biophys. J. 97, 2846-2853 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 2846-2853
    • Chuang, G.Y.1
  • 37
    • 84555195240 scopus 로고    scopus 로고
    • Robust identification of binding hot spots using continuum electrostatics: Application to hen egg-white lysozyme
    • Hall, D.H. et al. Robust identification of binding hot spots using continuum electrostatics: application to hen egg-white lysozyme. J. Am. Chem. Soc. 133, 20668-20671 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20668-20671
    • Hall, D.H.1
  • 38
    • 80054860512 scopus 로고    scopus 로고
    • Analysis of binding site hot spots on the surface of Ras GTPase
    • Buhrman, G. et al. Analysis of binding site hot spots on the surface of Ras GTPase. J. Mol. Biol. 413, 773-789 (2011).
    • (2011) J. Mol. Biol. , vol.413 , pp. 773-789
    • Buhrman, G.1
  • 39
    • 84865494461 scopus 로고    scopus 로고
    • Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces
    • Zerbe, B.S., Hall, D.R., Vajda, S., Whitty, A. & Kozakov, D. Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces. J. Chem. Inf. Model. 52, 2236-2244 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2236-2244
    • Zerbe, B.S.1    Hall, D.R.2    Vajda, S.3    Whitty, A.4    Kozakov, D.5
  • 40
    • 84858044079 scopus 로고    scopus 로고
    • Hot spot analysis for driving the development of hits into leads in fragment-based drug discovery
    • Hall, D.R., Ngan, C.H., Zerbe, B.S., Kozakov, D. & Vajda, S. Hot spot analysis for driving the development of hits into leads in fragment-based drug discovery. J. Chem. Inf. Model. 52, 199-209 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 199-209
    • Hall, D.R.1    Ngan, C.H.2    Zerbe, B.S.3    Kozakov, D.4    Vajda, S.5
  • 41
    • 84876706823 scopus 로고    scopus 로고
    • Comprehensive experimental and computational analysis of binding energy hot spots at the NF-κB essential modulator/IKKβ protein-protein interface
    • Golden, M.S. et al. Comprehensive experimental and computational analysis of binding energy hot spots at the NF-κB essential modulator/IKKβ protein-protein interface. J. Am. Chem. Soc. 135, 6242-6256 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 6242-6256
    • Golden, M.S.1
  • 42
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe, S.M. et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1
  • 43
    • 17144373303 scopus 로고    scopus 로고
    • Druggability indices for protein targets derived from NMR-based screening data
    • Hajduk, P.J., Huth, J.R. & Fesik, S.W. Druggability indices for protein targets derived from NMR-based screening data. J. Med. Chem. 48, 2518-2525 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 2518-2525
    • Hajduk, P.J.1    Huth, J.R.2    Fesik, S.W.3
  • 44
    • 38549150173 scopus 로고    scopus 로고
    • Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble
    • Landon, M.R. et al. Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble. Chem. Biol. Drug Des. 71, 106-116 (2008).
    • (2008) Chem. Biol. Drug Des. , vol.71 , pp. 106-116
    • Landon, M.R.1
  • 45
    • 84867025688 scopus 로고    scopus 로고
    • Optimizing PK properties of cyclic peptides: The effect of side chain substitutions on permeability and clearance
    • Rand, A.C. et al. Optimizing PK properties of cyclic peptides: the effect of side chain substitutions on permeability and clearance. Medchemcomm. 3, 1282-1289 (2012).
    • (2012) Medchemcomm. , vol.3 , pp. 1282-1289
    • Rand, A.C.1
  • 46
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • Hopkins, A.L., Groom, C.R. & Alex, A. Ligand efficiency: a useful metric for lead selection. Drug Discov. Today 9, 430-431 (2004).
    • (2004) Drug Discov. Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 47
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • Hajduk, P.J. Fragment-based drug design: how big is too big? J. Med. Chem. 49, 6972-6976 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 6972-6976
    • Hajduk, P.J.1
  • 48
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • Veber, D.F. et al. Molecular properties that influence the oral bioavailability of drug candidates. J. Med. Chem. 45, 2615-2623 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1
  • 49
    • 17644380257 scopus 로고    scopus 로고
    • Predicting drug disposition via application of BCS: Transport/absorption/ elimination interplay and development of a biopharmaceutics drug disposition classification system
    • Wu, C.Y. & Benet, L.Z. Predicting drug disposition via application of BCS: transport/absorption/ elimination interplay and development of a biopharmaceutics drug disposition classification system. Pharm. Res. 22, 11-23 (2005).
    • (2005) Pharm. Res. , vol.22 , pp. 11-23
    • Wu, C.Y.1    Benet, L.Z.2
  • 50
    • 0347361638 scopus 로고    scopus 로고
    • Characteristic physical properties and structural fragments of marketed oral drugs
    • Vieth, M. et al. Characteristic physical properties and structural fragments of marketed oral drugs. J. Med. Chem. 47, 224-232 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 224-232
    • Vieth, M.1
  • 51
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400 (1971).
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 52
    • 33847347192 scopus 로고    scopus 로고
    • Diverse, high-quality test set for the validation of protein-ligand docking performance
    • Hartshorn, M.J. et al. Diverse, high-quality test set for the validation of protein-ligand docking performance. J. Med. Chem. 50, 726-741 (2007).
    • (2007) J. Med. Chem. , vol.50 , pp. 726-741
    • Hartshorn, M.J.1
  • 53
    • 80051966197 scopus 로고    scopus 로고
    • Structural conservation of druggable hot spots in protein-protein interfaces
    • Kozakov, D. et al. Structural conservation of druggable hot spots in protein-protein interfaces. Proc. Natl. Acad. Sci. USA 108, 13528-13533 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13528-13533
    • Kozakov, D.1
  • 54
    • 84858044079 scopus 로고    scopus 로고
    • Hot spot analysis for driving the development of hits into leads in fragment-based drug discovery
    • Hall, D.R., Ngan, C.H., Zerbe, B.S., Kozakov, D. & Vajda, S. Hot spot analysis for driving the development of hits into leads in fragment-based drug discovery. J. Chem. Inf. Model. 52, 199-209 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 199-209
    • Hall, D.R.1    Ngan, C.H.2    Zerbe, B.S.3    Kozakov, D.4    Vajda, S.5
  • 55
    • 0002322469 scopus 로고
    • On a test of whether one of two random variables is stochastically larger than the other
    • Mann, H. & Whitney, D. On a test of whether one of two random variables is stochastically larger than the other. Ann. Math. Stat. 18, 50-60 (1947).
    • (1947) Ann. Math. Stat. , vol.18 , pp. 50-60
    • Mann, H.1    Whitney, D.2
  • 56
    • 0000923503 scopus 로고
    • Asymptotic theory of certain "goodness-of-fit" criteria based on stochastic processes
    • Anderson, T. & Darling, D. Asymptotic theory of certain "goodness-of-fit" criteria based on stochastic processes. Ann. Math. Stat. 23, 193-212 (1952).
    • (1952) Ann. Math. Stat. , vol.23 , pp. 193-212
    • Anderson, T.1    Darling, D.2


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