메뉴 건너뛰기




Volumn 51, Issue 1, 2012, Pages 126-137

Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER; ALZHEIMER'S DISEASE; AMYLOID FIBRIL; CONFORMATIONAL CHANGE; CONFORMATIONAL PREFERENCES; HYDROPHOBIC ATTRACTION; MECHANISM OF ACTION; MOLECULAR MECHANISM; NEURODEGENERATIVE DISORDERS; PARKINSON'S DISEASE; PROTEIN AGGREGATES; REPRESENTATIVE COMPOUND; SMALL ORGANIC MOLECULES;

EID: 84856873078     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201745g     Document Type: Article
Times cited : (45)

References (53)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 34248190279 scopus 로고    scopus 로고
    • Aß oligomers-a decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007) Aß oligomers-a decade of discovery. J. Neurochem. 101, 1172-1184.
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 2542530161 scopus 로고    scopus 로고
    • Protein chemistry. in the footsteps of alchemists
    • Dobson, C. M. (2004) Protein chemistry. In the footsteps of alchemists. Science 304, 1259-1262.
    • (2004) Science , vol.304 , pp. 1259-1262
    • Dobson, C.M.1
  • 5
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • DOI 10.1074/jbc.M608207200
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid ß oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324. (Pubitemid 47093410)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 6
    • 69749090512 scopus 로고    scopus 로고
    • On the mechanism of nonspecific inhibitors of protein aggregation: Dissecting the interactions of a-synuclein with Congo red and Lacmoid
    • Lendel, C., Bertoncini, C. W., Cremades, N., Waudby, C. A., Vendruscolo, M., Dobson, C. M., Schenk, D., Christodoulou, J., and Toth, G. (2009) On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the interactions of a-synuclein with Congo red and Lacmoid. Biochemistry 48, 8322-8334.
    • (2009) Biochemistry , vol.48 , pp. 8322-8334
    • Lendel, C.1    Bertoncini, C.W.2    Cremades, N.3    Waudby, C.A.4    Vendruscolo, M.5    Dobson, C.M.6    Schenk, D.7    Christodoulou, J.8    Toth, G.9
  • 8
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • DOI 10.1074/jbc.M411805200
    • Ulmer, T. S., Bax, A., Cole, N. B., and Nussbaum, R. L. (2005) Structure and dynamics of micelle-bound human a-synuclein. J. Biol. Chem. 280, 9595-9603. (Pubitemid 40409655)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 9
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospholipid-binding modes of a-synuclein revealed by solution NMR spectroscopy
    • Bodner, C. R., Dobson, C. M., and Bax, A. (2009) Multiple tight phospholipid-binding modes of a-synuclein revealed by solution NMR spectroscopy. J. Mol. Biol. 390, 775-790.
    • (2009) J. Mol. Biol. , vol.390 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 10
  • 11
    • 52449099848 scopus 로고    scopus 로고
    • Secondary structure conversions of Alzheimer's Aß(1-40) peptide induced by membrane-mimicking detergents
    • Wahlström, A., Hugonin, L., Peralvarez-Marin, A., Jarvet, J., and Gräslund, A. (2008) Secondary structure conversions of Alzheimer's Aß(1-40) peptide induced by membrane-mimicking detergents. FEBS J. 275, 5117-5128.
    • (2008) FEBS J. , vol.275 , pp. 5117-5128
    • Wahlström, A.1    Hugonin, L.2    Peralvarez-Marin, A.3    Jarvet, J.4    Gräslund, A.5
  • 13
    • 77954762756 scopus 로고    scopus 로고
    • Amyloid formation in surfactants and alcohols: Membrane mimetics or structural switchers? Curr
    • Otzen, D. E. (2010) Amyloid formation in surfactants and alcohols: membrane mimetics or structural switchers? Curr. Protein Pept. Sci. 11, 355-371.
    • (2010) Protein Pept. Sci. , vol.11 , pp. 355-371
    • Otzen, D.E.1
  • 14
    • 42349111633 scopus 로고    scopus 로고
    • Characterization of α-synuclein interactions with selected aggregation-inhibiting small molecules
    • DOI 10.1021/bi8002378
    • Rao, J. N., Dua, V., and Ulmer, T. S. (2008) Characterization of a-synuclein interactions with selected aggregation-inhibiting small molecules. Biochemistry 47, 4651-4656. (Pubitemid 351555485)
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4651-4656
    • Rao, J.N.1    Dua, V.2    Ulmer, T.S.3
  • 15
    • 81855226548 scopus 로고    scopus 로고
    • NSAID-based ?-secretase modulators do not bind to the amyloid-ß polypeptide
    • Barrett, P. J., Sanders, C. R., Kaufman, S. A., Michelsen, K., and Jordan, J. B. (2011) NSAID-based ?-secretase modulators do not bind to the amyloid-ß polypeptide. Biochemistry 50, 10328-10342.
    • (2011) Biochemistry , vol.50 , pp. 10328-10342
    • Barrett, P.J.1    Sanders, C.R.2    Kaufman, S.A.3    Michelsen, K.4    Jordan, J.B.5
  • 20
    • 0000867858 scopus 로고    scopus 로고
    • 1H]-TROSY
    • Pervushin, K. V., Wider, G., and Wüthrich, K. (1998) Single Transition-to-single Transition Polarization Transfer (ST2-PT) in [15N,1H]-TROSY. J. Biomol. NMR 12, 345-348. (Pubitemid 128511298)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.2 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wuthrich, K.3
  • 21
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 23
    • 33846626899 scopus 로고    scopus 로고
    • A 1H-NMR thermometer suitable for cryoprobes
    • Findeisen, M., Brand, T., and Berger, S. (2007) A 1H-NMR thermometer suitable for cryoprobes. Magn. Reson. Chem. 45, 175-178.
    • (2007) Magn. Reson. Chem. , vol.45 , pp. 175-178
    • Findeisen, M.1    Brand, T.2    Berger, S.3
  • 24
    • 0142125805 scopus 로고    scopus 로고
    • Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length
    • DOI 10.1002/mrc.1132
    • Danielsson, J., Jarvet, J., Damberg, P., and Gräslund, A. (2002) Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aß(1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length. Magn. Reson. Chem. 40, S89-S97. (Pubitemid 37296918)
    • (2002) Magnetic Resonance in Chemistry , vol.40 , Issue.SPEC. ISS.
    • Danielsson, J.1    Jarvet, J.2    Damberg, P.3    Graslund, A.4
  • 25
    • 0347359145 scopus 로고    scopus 로고
    • Diffusion ordered nuclear magnetic resonance spectroscopy: Principles and applications
    • Johnson, C. S. J. (1999) Diffusion ordered nuclear magnetic resonance spectroscopy: principles and applications. Prog. Nucl. Magn. Reson. Spectrosc. 34, 203-256.
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 203-256
    • Johnson, C.S.J.1
  • 26
    • 43949103402 scopus 로고    scopus 로고
    • Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides
    • DOI 10.1021/jp7118718
    • Huang, H., Milojevic, J., and Melacini, G. (2008) Analysis and optimization of saturation transfer difference NMR experiments designed to map early self-association events in amyloidogenic peptides. J. Phys. Chem. B 112, 5795-5802. (Pubitemid 351704596)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.18 , pp. 5795-5802
    • Huang, H.1    Milojevic, J.2    Melacini, G.3
  • 27
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer, M., and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem., Int. Ed. 38, 1784-1788. (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 28
    • 0030797606 scopus 로고    scopus 로고
    • Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water - Protein proton exchange and intermolecular NOEs
    • DOI 10.1021/ja970160j
    • Hwang, T.-L., Mori, S., Shaka, A. J., and van Zijl, P. C. M. (1997) Application of phase-modulated CLEAN chemical EXchange Spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs. J. Am. Chem. Soc. 119, 6203-6204. (Pubitemid 27314859)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.26 , pp. 6203-6204
    • Hwang, T.-L.1    Mori, S.2    Shaka, A.J.3    Van Zijl, P.C.M.4
  • 29
    • 0031989849 scopus 로고    scopus 로고
    • Accurate quantitation of water-amide proton exchange rates using the Phase-Modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme
    • Hwang, T.-L., van Zijl, P. C. M., and Mori, S. (1998) Accurate quantitation of water-amide proton exchange rates using the Phase-Modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme. J. Biomol. NMR 11, 221-226. (Pubitemid 128511271)
    • (1998) Journal of Biomolecular NMR , vol.11 , Issue.2 , pp. 221-226
    • Hwang, T.-L.1    Van Zijl, P.C.M.2    Mori, S.3
  • 30
    • 23644452100 scopus 로고    scopus 로고
    • 1-helix, β-strand and random coil secondary structures
    • DOI 10.1111/j.1742-4658.2005.04812.x
    • Danielsson, J., Jarvet, J., Damberg, P., and Gräslund, A. (2005) The Alzheimer ß-peptide shows temperature-dependent transitions between left-handed 3-helix, ß-strand and random coil secondary structures. FEBS J. 272, 3938-3949. (Pubitemid 41117225)
    • (2005) FEBS Journal , vol.272 , Issue.15 , pp. 3938-3949
    • Danielsson, J.1    Jarvet, J.2    Damberg, P.3    Graslund, A.4
  • 31
    • 0015510189 scopus 로고
    • Effect of light scattering on the circular dichroism of biological membranes
    • Litman, B. J. (1972) Effect of light scattering on the circular dichroism of biological membranes. Biochemistry 11, 3243-3247.
    • (1972) Biochemistry , vol.11 , pp. 3243-3247
    • Litman, B.J.1
  • 32
    • 78649285837 scopus 로고    scopus 로고
    • Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors
    • Buell, A. K., Dobson, C. M., Knowles, T. P., and Welland, M. E. (2010) Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors. Biophys. J. 99, 3492-3497.
    • (2010) Biophys. J. , vol.99 , pp. 3492-3497
    • Buell, A.K.1    Dobson, C.M.2    Knowles, T.P.3    Welland, M.E.4
  • 33
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis
    • DOI 10.1006/jmbi.2001.4970
    • Kirkitadze, M. D., Condron, M. M., and Teplow, D. B. (2001) Identification and characterization of key kinetic intermediates in amyloid ß-protein fibrillogenesis. J. Mol. Biol. 312, 1103-1119. (Pubitemid 32980329)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 34
    • 34547920308 scopus 로고    scopus 로고
    • Positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes
    • DOI 10.1007/s10858-007-9176-4
    • Jarvet, J., Danielsson, J., Damberg, P., Oleszczuk, M., and Gräslund, A. (2007) Positioning of the Alzheimer Aß(1-40) peptide in SDS micelles using NMR and paramagnetic probes. J. Biomol. NMR 39, 63-72. (Pubitemid 47249695)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.1 , pp. 63-72
    • Jarvet, J.1    Danielsson, J.2    Damberg, P.3    Oleszczuk, M.4    Graslund, A.5
  • 35
    • 0347753786 scopus 로고    scopus 로고
    • Two Types of Alzheimer's β-Amyloid (1-40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation
    • DOI 10.1016/j.jmb.2003.11.046
    • Bokvist, M., Lindström, F., Watts, A., and Gröbner, G. (2004) Two types of Alzheimer's ß-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335, 1039-1049. (Pubitemid 38091609)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 36
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-β(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate
    • DOI 10.1021/bi701213s
    • Rangachari, V., Moore, B. D., Reed, D. K., Sonoda, L. K., Bridges, A. W., Conboy, E., Hartigan, D., and Rosenberry, T. L. (2007) Amyloid-ß(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. Biochemistry 46, 12451-12462. (Pubitemid 350027406)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Sonoda, L.K.4    Bridges, A.W.5    Conboy, E.6    Hartigan, D.7    Rosenberry, T.L.8
  • 39
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid ß-protein fibril assembly. Differential effects of a-helix stabilization
    • Fezoui, Y., and Teplow, D. B. (2002) Kinetic studies of amyloid ß-protein fibril assembly. Differential effects of a-helix stabilization. J. Biol. Chem. 277, 36948-36954.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 42
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808. (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 43
    • 79551687827 scopus 로고    scopus 로고
    • High-affinity amphipathic modulators of amyloid fibril nucleation and elongation
    • Ryan, T. M., Griffin, M. D., Teoh, C. L., Ooi, J., and Howlett, G. J. (2011) High-affinity amphipathic modulators of amyloid fibril nucleation and elongation. J. Mol. Biol. 406, 416-429.
    • (2011) J. Mol. Biol. , vol.406 , pp. 416-429
    • Ryan, T.M.1    Griffin, M.D.2    Teoh, C.L.3    Ooi, J.4    Howlett, G.J.5
  • 44
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide
    • DOI 10.1073/pnas.0605629103
    • Kim, W., and Hecht, M. H. (2006) Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aß42 peptide. Proc. Natl. Acad. Sci. U. S. A. 103, 15824-15829. (Pubitemid 44657551)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.43 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2
  • 45
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation- susceptible" regions in proteins associated with neurodegenerative diseases
    • DOI 10.1016/j.jmb.2005.04.016, PII S0022283605004262
    • Pawar, A. P., Dubay, K. F., Zurdo, J., Chiti, F., Vendruscolo, M., and Dobson, C. M. (2005) Prediction of ?aggregation-prone? and ?aggregation- susceptible? regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350, 379-392. (Pubitemid 40805470)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.2 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 46
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • DOI 10.1016/j.brainresrev.2006.08.001, PII S0165017306001019
    • Frid, P., Anisimov, S. V., and Popovic, N. (2007) Congo red and protein aggregation in neurodegenerative diseases. Brain Res. Rev. 53, 135-160. (Pubitemid 44854214)
    • (2007) Brain Research Reviews , vol.53 , Issue.1 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 47
    • 0038532258 scopus 로고    scopus 로고
    • Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
    • DOI 10.1074/jbc.M212540200
    • Kim, Y. S., Randolph, T. W., Manning, M. C., Stevens, F. J., and Carpenter, J. F. (2003) Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Biol. Chem. 278, 10842-10850. (Pubitemid 36800358)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10842-10850
    • Kim, Y.-S.1    Randolph, T.W.2    Manning, M.C.3    Stevens, F.J.4    Carpenter, J.F.5
  • 48
    • 0034109546 scopus 로고    scopus 로고
    • Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells
    • Rudyk, H., Vasiljevic, S., Hennion, R. M., Birkett, C. R., Hope, J., and Gilbert, I. H. (2000) Screening Congo red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. J. Gen. Virol. 81, 1155-1164. (Pubitemid 30189659)
    • (2000) Journal of General Virology , vol.81 , Issue.4 , pp. 1155-1164
    • Rudyk, H.1    Vasiljevic, S.2    Hennion, R.M.3    Birkett, C.R.4    Hope, J.5    Gilbert, I.H.6
  • 49
    • 23144434344 scopus 로고    scopus 로고
    • Stimulatory and inhibitory effects of alkyl bromide surfactants on β-amyloid fibrillogenesis
    • DOI 10.1021/la050472x
    • Sabaté, R., and Estelrich, J. (2005) Stimulatory and inhibitory effects of alkyl bromide surfactants on ß-amyloid fibrillogenesis. Langmuir 21, 6944-6949. (Pubitemid 41084482)
    • (2005) Langmuir , vol.21 , Issue.15 , pp. 6944-6949
    • Sabate, R.1    Estelrich, J.2
  • 52
    • 80051899060 scopus 로고    scopus 로고
    • Nucleated polymerization with secondary pathways II. Determination of self-consistent solutions to growth processes described by non-linear master equations
    • Cohen, S. I., Vendruscolo, M., Dobson, C. M., and Knowles, T. P. (2011) Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations. J. Chem. Phys. 135, 065106.
    • (2011) J. Chem. Phys. , vol.135 , pp. 065106
    • Cohen, S.I.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4
  • 53
    • 80051897336 scopus 로고    scopus 로고
    • Nucleated polymerization with secondary pathways III. Equilibrium behavior and oligomer populations
    • Cohen, S. I., Vendruscolo, M., Dobson, C. M., and Knowles, T. P. (2011) Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations. J. Chem. Phys. 135, 065107.
    • (2011) J. Chem. Phys. , vol.135 , pp. 065107
    • Cohen, S.I.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.