메뉴 건너뛰기




Volumn 44, Issue 27, 2005, Pages 9538-9544

Permeabilization of raft-containing lipid vesicles by δ-lysin: A mechanism for cell sensitivity to cytotoxic peptides

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; BACTERIA; CELL MEMBRANES; CELLS; CHOLESTEROL;

EID: 21844443548     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0506371     Document Type: Article
Times cited : (64)

References (53)
  • 2
    • 0023082885 scopus 로고
    • Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles
    • Lee, K. H., Fitton, J. E., and Wüthrich, K. (1987) Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles, Biochim. Biophys. Acta 911, 144-153.
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 144-153
    • Lee, K.H.1    Fitton, J.E.2    Wüthrich, K.3
  • 3
    • 0025963949 scopus 로고
    • The amphiphilic α-helix concept. Consequences on the structure of staphylococcal δ-toxin in solution and bound to lipids
    • Thiaudière, E., Siffert, O., Talbot, J. C., Bolard, J., Alouf, J. E., and Dufourcq, J. (1991) The amphiphilic α-helix concept. Consequences on the structure of staphylococcal δ-toxin in solution and bound to lipids, Eur. J. Biochem. 195, 203-213.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 203-213
    • Thiaudière, E.1    Siffert, O.2    Talbot, J.C.3    Bolard, J.4    Alouf, J.E.5    Dufourcq, J.6
  • 5
    • 0034880883 scopus 로고    scopus 로고
    • Dynamics and orientation of amphipathic peptides in solution and bound to membranes: A steady-state and time-resolved fluorescence study of staphylococcal δ-toxin and its synthetic analogues
    • Talbot, J. C., Thiaudière, E., Vincent, M., Gallay, J., Siffert, O., and Dufourcq, J. (2001) Dynamics and orientation of amphipathic peptides in solution and bound to membranes: A steady-state and time-resolved fluorescence study of staphylococcal δ-toxin and its synthetic analogues, Eur. Biophys. J. 30, 147-161.
    • (2001) Eur. Biophys. J. , vol.30 , pp. 147-161
    • Talbot, J.C.1    Thiaudière, E.2    Vincent, M.3    Gallay, J.4    Siffert, O.5    Dufourcq, J.6
  • 6
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles
    • Pokorny, A., Birkbeck, T. H., and Almeida, P. F. F. (2002) Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles, Biochemistry 41, 11044-11056.
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 7
    • 3042818271 scopus 로고    scopus 로고
    • Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides
    • Pokorny, A., and Almeida, P. F. F. (2004) Kinetics of dye efflux and lipid flip-flop induced by δ-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, α-helical peptides, Biochemistry 43, 8846-8857.
    • (2004) Biochemistry , vol.43 , pp. 8846-8857
    • Pokorny, A.1    Almeida, P.F.F.2
  • 8
    • 1842756746 scopus 로고    scopus 로고
    • Functional roles of lipids in membranes
    • (Vance, D. E., and Vance, J. E., Eds.) 4th ed. Elsevier, Amsterdam.
    • Dowhan, W., and Bogdanov, M. (2002) Functional roles of lipids in membranes, in Biochemistry of Lipids, Lipoproteins, and Membranes (Vance, D. E., and Vance, J. E., Eds.) 4th ed., pp 1-35, Elsevier, Amsterdam.
    • (2002) Biochemistry of Lipids, Lipoproteins, and Membranes , pp. 1-35
    • Dowhan, W.1    Bogdanov, M.2
  • 9
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 10
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld, A., and Simons, K. (1998) The differential miscibility of lipids as the basis for the formation of functional membrane rafts, Biochim. Biophys. Acta 1376, 467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 11
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson, R. G., and Jacobson, K. (2002) A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains, Science 296, 1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 13
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. (2003) The state of lipid rafts: From model membranes to cells, Annu. Rev. Biophys. Biomol. Struct. 32, 257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 14
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • Simons, K., and Vaz, W. L. (2004) Model systems, lipid rafts, and cell membranes, Annu. Rev. Biophys. Biomol. Struct. 33, 269-295.
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 269-295
    • Simons, K.1    Vaz, W.L.2
  • 15
    • 0002747562 scopus 로고
    • Physical properties and functional roles of lipids in membranes
    • (Vance, D. E., and Vance, J. E., Eds.) 2nd ed., Benjamin/Cummings, Menlo Park, CA
    • Cullis, P. R., and Hope, M. J. (1985) Physical properties and functional roles of lipids in membranes, in Biochemistry of Lipids and Membranes (Vance, D. E., and Vance, J. E., Eds.) 2nd ed., pp 28-33, Benjamin/Cummings, Menlo Park, CA.
    • (1985) Biochemistry of Lipids and Membranes , pp. 28-33
    • Cullis, P.R.1    Hope, M.J.2
  • 16
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed, S. N., Brown, D. A., and London, E. (1997) On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes, Biochemistry 36, 10944-10953.
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 18
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/Phosphatidylcholine/Cholesterol phase diagram: Boundaries and composition of lipid rafts
    • de Almeida, R. F. M., Fedorov, A., and Prieto, M. (2003) Sphingomyelin/Phosphatidylcholine/Cholesterol phase diagram: Boundaries and composition of lipid rafts, Biophys. J. 85, 2406-2416.
    • (2003) Biophys. J. , vol.85 , pp. 2406-2416
    • De Almeida, R.F.M.1    Fedorov, A.2    Prieto, M.3
  • 19
    • 0035016931 scopus 로고    scopus 로고
    • Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: Nanoscopic domain formation driven by cholesterol
    • Feigenson, G. W., and Buboltz, J. T. (2001) Ternary phase diagram of dipalmitoyl-PC/dilauroyl-PC/cholesterol: Nanoscopic domain formation driven by cholesterol, Biophys. J. 80, 2775-2788.
    • (2001) Biophys. J. , vol.80 , pp. 2775-2788
    • Feigenson, G.W.1    Buboltz, J.T.2
  • 21
    • 0025128695 scopus 로고
    • 2H-nuclear magnetic resonance and differential scanning calorimetry
    • 2H-nuclear magnetic resonance and differential scanning calorimetry, Biochemistry 29, 451-464.
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 22
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram, M. B., and Thompson, T. E. (1990) Interaction of cholesterol with various glycerophospholipids and sphingomyelin, Biochemistry 29, 10670-10675.
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 24
    • 0026058545 scopus 로고
    • Cholesterol-induced fluid phase immiscibility in membranes, Proc
    • Sankaram, M. B., and Thompson, T. E. (1991) Cholesterol-induced fluid phase immiscibility in membranes, Proc. Natl. Acad. Sci. U.S.A. 88, 8686-8690.
    • (1991) Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8686-8690
    • Sankaram, M.B.1    Thompson, T.E.2
  • 25
    • 0026767199 scopus 로고
    • Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/ cholesterol lipid bilayers: A free volume analysis
    • Almeida, P. F. F., Vaz, W. L. C., and Thompson, T. E. (1992) Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: A free volume analysis, Biochemistry 31, 6739-6747.
    • (1992) Biochemistry , vol.31 , pp. 6739-6747
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 26
    • 0027511498 scopus 로고
    • Percolation and diffusion in three-component lipid bilayers: Effect of cholesterol on an equimolar mixture of two phosphatidylcholines
    • Almeida, P. F. F., Vaz, W. L. C., and Thompson, T. E. (1993) Percolation and diffusion in three-component lipid bilayers: Effect of cholesterol on an equimolar mixture of two phosphatidylcholines, Biophys. J. 64, 399-412.
    • (1993) Biophys. J. , vol.64 , pp. 399-412
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 27
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • Friedrich, C. L., Moyles, D., Beveridge, T. J., and Hancock, R. E. (2000) Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria, Antimicrob. Agents Chemother. 44, 2086-2092.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 29
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils, Antimicrob
    • Turner, J., Cho, Y., Dinh, N. N., Waring, A. J., and Lehrer, R. I. (1998) Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils, Antimicrob. Agents Chemother. 42, 2206-2214.
    • (1998) Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 30
    • 0024214704 scopus 로고
    • Purification and assay of staphylococcal δ-lysin
    • Birkbeck, T. H., and Freer, J. H. (1988) Purification and assay of staphylococcal δ-lysin, Methods Enzymol. 165, 16-22.
    • (1988) Methods Enzymol. , vol.165 , pp. 16-22
    • Birkbeck, T.H.1    Freer, J.H.2
  • 31
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett, G. R. (1959) Phosphorous assay in column chromatography, J. Biol. Chem. 234, 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 33
    • 0004974366 scopus 로고
    • The interpretation of single channel recordings
    • (Ogden, D., Ed.) 2nd ed., The Company of Biologists Ltd., Cambridge, U.K.
    • Colquhoun, D., and Hawkes, A. G. (1987) The interpretation of single channel recordings, in Microelectrode Techniques. The Plymouth Workshop Handbook (Ogden, D., Ed.) 2nd ed., pp 141-188, The Company of Biologists Ltd., Cambridge, U.K.
    • (1987) Microelectrode Techniques. The Plymouth Workshop Handbook , pp. 141-188
    • Colquhoun, D.1    Hawkes, A.G.2
  • 34
    • 0034030262 scopus 로고    scopus 로고
    • Kinetics of amphiphile association with two-phase lipid bilayer vesicles
    • Pokorny, A., Almeida, P. F. F., Melo, E. C. C., and Vaz, W. L. C. (2000) Kinetics of amphiphile association with two-phase lipid bilayer vesicles, Biophys. J. 78, 267-280.
    • (2000) Biophys. J. , vol.78 , pp. 267-280
    • Pokorny, A.1    Almeida, P.F.F.2    Melo, E.C.C.3    Vaz, W.L.C.4
  • 35
    • 4444293957 scopus 로고    scopus 로고
    • SNAREs prefer liquid-disordered over 'raft' (liquid-ordered) domains when reconstituted into giant unilamellar vesicles
    • Bacia, K., Schuette, C. G., Kahya, N., Jahn, R., and Schwille, P. (2004) SNAREs prefer liquid-disordered over 'raft' (liquid-ordered) domains when reconstituted into giant unilamellar vesicles, J. Biol. Chem. 279, 37951-37955.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37951-37955
    • Bacia, K.1    Schuette, C.G.2    Kahya, N.3    Jahn, R.4    Schwille, P.5
  • 36
    • 0142063411 scopus 로고    scopus 로고
    • Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: Extension of quenching analysis to account for the effects of domain size and domain boundaries
    • Fastenberg, M. E., Shogomori, H., Xu, X., Brown, D. A., and London, E. (2003) Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: Extension of quenching analysis to account for the effects of domain size and domain boundaries, Biochemistry 42, 12376-12390.
    • (2003) Biochemistry , vol.42 , pp. 12376-12390
    • Fastenberg, M.E.1    Shogomori, H.2    Xu, X.3    Brown, D.A.4    London, E.5
  • 37
    • 0036194867 scopus 로고    scopus 로고
    • Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts
    • Gandhavadi, M., Allende, D., Vidal, A., Simon, S. A., and McIntosh, T. J. (2002) Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts, Biophys. J. 82, 1469-1482.
    • (2002) Biophys. J. , vol.82 , pp. 1469-1482
    • Gandhavadi, M.1    Allende, D.2    Vidal, A.3    Simon, S.A.4    McIntosh, T.J.5
  • 38
    • 0041821501 scopus 로고    scopus 로고
    • Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts
    • McIntosh, T. J., Vidal, A., and Simon, S. A. (2003) Sorting of lipids and transmembrane peptides between detergent-soluble bilayers and detergent-resistant rafts, Biophys. J. 85, 1656-1666.
    • (2003) Biophys. J. , vol.85 , pp. 1656-1666
    • McIntosh, T.J.1    Vidal, A.2    Simon, S.A.3
  • 39
    • 13544250497 scopus 로고    scopus 로고
    • Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes
    • Abraham, T., Lewis, R. N. A. H., Hodges, R. S., and McElhaney, R. N. (2005) Isothermal titration calorimetry studies of the binding of a rationally designed analogue of the antimicrobial peptide gramicidin S to phospholipid bilayer membranes, Biochemistry 44, 2103-2112.
    • (2005) Biochemistry , vol.44 , pp. 2103-2112
    • Abraham, T.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 40
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms, Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 41
    • 0000420475 scopus 로고
    • Gram-positive bacteria
    • (Ratledge, C., and Wilkinson, S. G., Eds.) Academic Press, San Diego
    • O'Leary, W. M., and Wilkinson, S. G. (1988) Gram-positive bacteria, in Microbial Lipids (Ratledge, C., and Wilkinson, S. G., Eds.) Vol. 1, pp 117-201, Academic Press, San Diego.
    • (1988) Microbial Lipids , vol.1 , pp. 117-201
    • O'Leary, W.M.1    Wilkinson, S.G.2
  • 42
    • 0000420475 scopus 로고
    • Gram-negative bacteria
    • (Ratledge, C., and Wilkinson, S. G., Eds.) Academic Press, San Diego
    • Wilkinson, S. G. (1988) Gram-negative bacteria, in Microbial Lipids (Ratledge, C., and Wilkinson, S. G., Eds.) Vol. 1, pp 299-488, Academic Press, San Diego.
    • (1988) Microbial Lipids , vol.1 , pp. 299-488
    • Wilkinson, S.G.1
  • 43
    • 15744398051 scopus 로고    scopus 로고
    • Role of membrane lipids in bacterial division-site selection
    • Mileykovskaya, E., and Dowhan, W. (2005) Role of membrane lipids in bacterial division-site selection, Curr. Opin. Microbiol. 8, 135-142.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 135-142
    • Mileykovskaya, E.1    Dowhan, W.2
  • 44
    • 0035799334 scopus 로고    scopus 로고
    • Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif
    • Hinderliter, A., Almeida, P. F. F., Creutz, C. E., and Biltonen, R. L. (2001) Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif, Biochemistry 40, 4181-4191.
    • (2001) Biochemistry , vol.40 , pp. 4181-4191
    • Hinderliter, A.1    Almeida, P.F.F.2    Creutz, C.E.3    Biltonen, R.L.4
  • 45
    • 2642533608 scopus 로고    scopus 로고
    • Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction
    • Hinderliter, A., Biltonen, R. L., and Almeida, P. F. F. (2004) Lipid modulation of protein-induced membrane domains as a mechanism for controlling signal transduction, Biochemistry 43, 7102-7110.
    • (2004) Biochemistry , vol.43 , pp. 7102-7110
    • Hinderliter, A.1    Biltonen, R.L.2    Almeida, P.F.F.3
  • 47
    • 0642338937 scopus 로고    scopus 로고
    • DmAMP1, an antifungal plant defensin from dahlia (Dahlia merckii), interacts with sphingolipids from Saccharomyces cerevisiae
    • Thevissen, K., Francois, I. E., Takemoto, J. Y., Ferket, K. K., Meert, E. M., and Cammue, B. P. (2003) DmAMP1, an antifungal plant defensin from dahlia (Dahlia merckii), interacts with sphingolipids from Saccharomyces cerevisiae, FEMS Microbiol. Lett. 226, 169-173.
    • (2003) FEMS Microbiol. Lett. , vol.226 , pp. 169-173
    • Thevissen, K.1    Francois, I.E.2    Takemoto, J.Y.3    Ferket, K.K.4    Meert, E.M.5    Cammue, B.P.6
  • 48
    • 0141627480 scopus 로고    scopus 로고
    • Isolation and characterization of Neurospora crassa mutants resistant to antifungal plant defensins
    • Ferket, K. K., Levery, S. B., Park, C., Cammue, B. P., and Thevissen, K. (2003) Isolation and characterization of Neurospora crassa mutants resistant to antifungal plant defensins, Fungal Genet. Biol. 40, 176-185.
    • (2003) Fungal Genet. Biol. , vol.40 , pp. 176-185
    • Ferket, K.K.1    Levery, S.B.2    Park, C.3    Cammue, B.P.4    Thevissen, K.5
  • 49
    • 0001075893 scopus 로고
    • Yeasts
    • (Ratledge, C., and Wilkinson, S. G., Eds.) Academic Press, San Diego
    • Rattray, J. M. B. (1988) Yeasts, in Microbial Lipids (Ratledge, C., and Wilkinson, S. G., Eds.) Vol. 1, pp 555-697, Academic Press, San Diego.
    • (1988) Microbial Lipids , vol.1 , pp. 555-697
    • Rattray, J.M.B.1
  • 50
    • 0001507976 scopus 로고
    • Fungal Lipids
    • (Ratledge, C., and Wilkinson, S. G., Eds.) Academic Press, San Diego
    • Lösel, D. M. (1988) Fungal Lipids, in Microbial Lipids (Ratledge, C., and Wilkinson, S. G., Eds.) Vol. 1, pp 699-806, Academic Press, San Diego.
    • (1988) Microbial Lipids , vol.1 , pp. 699-806
    • Lösel, D.M.1
  • 51
    • 21144453569 scopus 로고    scopus 로고
    • The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: A deuterium NMR and calorimetric study
    • Hsueh, Y.-W., Gilbert, K., Trandum, C., Zuckermann, M., and Thewalt, J. (2005) The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: A deuterium NMR and calorimetric study, Biophys. J. 88, 1799-1808.
    • (2005) Biophys. J. , vol.88 , pp. 1799-1808
    • Hsueh, Y.-W.1    Gilbert, K.2    Trandum, C.3    Zuckermann, M.4    Thewalt, J.5
  • 52
    • 0025760201 scopus 로고
    • The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane
    • Patton, J. L., and Lester, R. L. (1991) The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane, J. Bacteriol. 173, 3101-3108.
    • (1991) J. Bacteriol. , vol.173 , pp. 3101-3108
    • Patton, J.L.1    Lester, R.L.2
  • 53
    • 0038039171 scopus 로고    scopus 로고
    • Recently discovered functions of glucosylceramides in plants and fungi
    • Warnecke, D., and Heinz, E. (2003) Recently discovered functions of glucosylceramides in plants and fungi, Cell. Mol. Life Sci. 60, 919-941.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 919-941
    • Warnecke, D.1    Heinz, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.