메뉴 건너뛰기




Volumn 287, Issue 4, 2012, Pages 2877-2886

Green fluorescent protein changes the conductance of connexin 43 (Cx43) hemichannels reconstituted in planar lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

CONDUCTANCE STATE; CONNEXIN 43; DIRECT COMMUNICATIONS; EXPRESSION SYSTEM; GAP JUNCTION CHANNELS; GIANT UNILAMELLAR VESICLES; GREEN FLUORESCENT PROTEIN; HEMICHANNELS; INTERMOLECULAR INTERACTIONS; MAMMALIAN TISSUES; MEMBRANE FRACTION; OHMIC BEHAVIOR; PICHIA PASTORIS; PLANAR PATCH; SINGLE CHANNELS; SINGLE-LIPID BILAYERS;

EID: 84856068470     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.319871     Document Type: Article
Times cited : (14)

References (59)
  • 1
    • 20444397355 scopus 로고    scopus 로고
    • Structural organization of gap junction channels
    • DOI 10.1016/j.bbamem.2005.04.001, PII S0005273605000878
    • Sosinsky, G. E., and Nicholson, B. J. (2005) Structural organization of gap junction channels. Biochim. Biophys. Acta 1711, 99-125 (Pubitemid 40799287)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1711 , Issue.2 SPEC. ISS. , pp. 99-125
    • Sosinsky, G.E.1    Nicholson, B.J.2
  • 2
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris, A. L. (2001) Emerging issues of connexin channels: biophysics fills the gap. Q. Rev. Biophys. 34, 325-472
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 3
    • 1942438964 scopus 로고    scopus 로고
    • Gap junctions and the connexin protein family
    • DOI 10.1016/j.cardiores.2003.11.013, PII S0008636303007211
    • Söhl, G., and Willecke, K. (2004) Gap junctions and the connexin protein family. Cardiovasc. Res. 62, 228-232 (Pubitemid 38496536)
    • (2004) Cardiovascular Research , vol.62 , Issue.2 , pp. 228-232
    • Sohl, G.1    Willecke, K.2
  • 5
    • 33645002735 scopus 로고    scopus 로고
    • Life cycle of connexins in health and disease
    • Laird, D. W. (2006) Life cycle of connexins in health and disease. Biochem. J. 394, 527-543
    • (2006) Biochem. J. , vol.394 , pp. 527-543
    • Laird, D.W.1
  • 6
    • 0026515179 scopus 로고
    • Membrane topology and quaternary structure of cardiac gap junction ion channels
    • Yeager, M., and Gilula, N. B. (1992) Membrane topology and quaternary structure of cardiac gap junction ion channels. J. Mol. Biol. 223, 929-948
    • (1992) J. Mol. Biol. , vol.223 , pp. 929-948
    • Yeager, M.1    Gilula, N.B.2
  • 7
    • 64249170988 scopus 로고    scopus 로고
    • Connexin43 phosphorylation: Structural changes and biological effects
    • Solan, J. L., and Lampe, P. D. (2009) Connexin43 phosphorylation: structural changes and biological effects. Biochem. J. 419, 261-272
    • (2009) Biochem. J. , vol.419 , pp. 261-272
    • Solan, J.L.1    Lampe, P.D.2
  • 8
    • 70349240629 scopus 로고    scopus 로고
    • Connexin 43, a new therapeutic target for cardiovascular diseases
    • Song, Y. N., Zhang, H., Zhao, J. Y., and Guo, X. L. (2009) Connexin 43, a new therapeutic target for cardiovascular diseases. Pharmazie 64, 291-295
    • (2009) Pharmazie , vol.64 , pp. 291-295
    • Song, Y.N.1    Zhang, H.2    Zhao, J.Y.3    Guo, X.L.4
  • 9
    • 77956461991 scopus 로고    scopus 로고
    • Osteocyte: The unrecognized side of bone tissue
    • Rochefort, G. Y., Pallu, S., and Benhamou, C. L. (2010) Osteocyte: the unrecognized side of bone tissue. Osteoporos. Int. 21, 1457-1469
    • (2010) Osteoporos. Int. , vol.21 , pp. 1457-1469
    • Rochefort, G.Y.1    Pallu, S.2    Benhamou, C.L.3
  • 10
    • 0037040922 scopus 로고    scopus 로고
    • Transduction of cell survival signals by connexin-43 hemichannels
    • DOI 10.1074/jbc.M108625200
    • Plotkin, L. I., Manolagas, S. C., and Bellido, T. (2002) Transduction of cell survival signals by connexin-43 hemichannels. J. Biol. Chem. 277, 8648-8657 (Pubitemid 34968331)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 8648-8657
    • Plotkin, L.I.1    Manolagas, S.C.2    Bellido, T.3
  • 12
    • 0030220781 scopus 로고    scopus 로고
    • Expression of zebrafish connexin43.4 in the notochord and tail bud of wild-type and mutant no tail embryos
    • DOI 10.1006/dbio.1996.0177
    • Essner, J. J., Laing, J. G., Beyer, E. C., Johnson, R. G., and Hackett, P. B. (1996) Expression of zebrafish connexin 43.4 in the notochord and tail bud of wild-type and mutant no tail embryos. Dev. Biol. 177, 449-462 (Pubitemid 26275897)
    • (1996) Developmental Biology , vol.177 , Issue.2 , pp. 449-462
    • Essner, J.J.1    Laing, J.G.2    Beyer, E.C.3    Johnson, R.G.4    Hackett Jr., P.B.5
  • 13
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan, K., Solan, J. L., Dominguez, M., Sia, M., Hand, A., Lampe, P. D., and Laird, D. W. (1999) Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell 10, 2033-2050
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6    Laird, D.W.7
  • 15
    • 0242380301 scopus 로고    scopus 로고
    • New roles for astrocytes: Gap junction hemichannels have something to communicate
    • DOI 10.1016/j.tins.2003.09.008
    • Bennett, M. V., Contreras, J. E., Bukauskas, F. F., and Sáez, J. C. (2003) New roles for astrocytes: gap junction hemichannels have something to communicate. Trends Neurosci. 26, 610-617 (Pubitemid 37338369)
    • (2003) Trends in Neurosciences , vol.26 , Issue.11 , pp. 610-617
    • Bennett, M.V.L.1    Contreras, J.E.2    Bukauskas, F.F.3    Saez, J.C.4
  • 17
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A. B., and Tsien, R. Y. (1995) Improved green fluorescence. Nature 373, 663-664
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 18
    • 0034283554 scopus 로고    scopus 로고
    • A chip-based biosensor for the functional analysis of single ion channels
    • Schmidt, C., Mayer, M., and Vogel, H. (2000) A chip-based biosensor for the functional analysis of single ion channels. Angew. Chem. Int. Ed. Engl. 39, 3137-3140
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 3137-3140
    • Schmidt, C.1    Mayer, M.2    Vogel, H.3
  • 19
    • 0034805579 scopus 로고    scopus 로고
    • Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip
    • Pantoja, R., Sigg, D., Blunck, R., Bezanilla, F., and Heath, J. R. (2001) Bilayer reconstitution of voltage-dependent ion channels using a microfabricated silicon chip. Biophys. J. 81, 2389-2394 (Pubitemid 32917185)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2389-2394
    • Pantoja, R.1    Sigg, D.2    Blunck, R.3    Bezanilla, F.4    Heath, J.R.5
  • 20
    • 0036106307 scopus 로고    scopus 로고
    • Whole cell patch clamp recording performed on a planar glass chip
    • Fertig, N., Blick, R. H., and Behrends, J. C. (2002) Whole cell patch clamp recording performed on a planar glass chip. Biophys. J. 82, 3056-3062 (Pubitemid 34547648)
    • (2002) Biophysical Journal , vol.82 , Issue.6 , pp. 3056-3062
    • Fertig, N.1    Blick, R.H.2    Behrends, J.C.3
  • 22
    • 33646759936 scopus 로고    scopus 로고
    • High-resolution electrophysiology on a chip: Transient dynamics of alamethicin channel formation
    • DOI 10.1016/j.bbamem.2006.03.023, PII S0005273606001106
    • Sondermann, M., George, M., Fertig, N., and Behrends, J. C. (2006) High-resolution electrophysiology on a chip: transient dynamics of alamethicin channel formation. Biochim. Biophys. Acta 1758, 545-551 (Pubitemid 43767732)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.4 , pp. 545-551
    • Sondermann, M.1    George, M.2    Fertig, N.3    Behrends, J.C.4
  • 23
  • 25
    • 0025168284 scopus 로고
    • Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: Bovine lysozyme
    • DOI 10.1111/j.1749-6632.1990.tb24257.x
    • Brierley, R. A., Bussineau, C., Kosson, R., Melton, A., and Siegel, R. S. (1990) Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: bovine lysozyme. Ann. N.Y. Acad. Sci. 589, 350-362 (Pubitemid 20255801)
    • (1990) Annals of the New York Academy of Sciences , vol.589 , pp. 350-362
    • Brierley, R.A.1    Bussineau, C.2    Kosson, R.3    Melton, A.4    Siegel, R.S.5
  • 26
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 27
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 0242317916 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into liposomes
    • Rigaud, J. L., and Lévy, D. (2003) Reconstitution of membrane proteins into liposomes. Methods Enzymol. 372, 65-86
    • (2003) Methods Enzymol. , vol.372 , pp. 65-86
    • Rigaud, J.L.1    Lévy, D.2
  • 33
    • 0026478808 scopus 로고
    • Voltage dependence of liver gap junction channels reconstituted into liposomes and incorporated into planar bilayers
    • Mazet, J. L., Jarry, T., Gros, D., and Mazet, F. (1992) Voltage dependence of liver gap junction channels reconstituted into liposomes and incorporated into planar bilayers. Eur. J. Biochem. 210, 249-256
    • (1992) Eur. J. Biochem. , vol.210 , pp. 249-256
    • Mazet, J.L.1    Jarry, T.2    Gros, D.3    Mazet, F.4
  • 34
    • 0033525213 scopus 로고    scopus 로고
    • Regulation of connexin channels by pH: Direct action of the protonated form of taurine and other aminosulfonates
    • DOI 10.1074/jbc.274.6.3711
    • Bevans, C. G., and Harris, A. L. (1999) Regulation of connexin channels by pH. Direct action of the protonated form of taurine and other aminosulfonates. J. Biol. Chem. 274, 3711-3719 (Pubitemid 29077218)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.6 , pp. 3711-3719
    • Bevans, C.G.1    Harris, A.L.2
  • 35
    • 0033745550 scopus 로고    scopus 로고
    • Metabolic inhibition activates a nonselective current through connexin hemichannels in isolated ventricular myocytes
    • Kondo, R. P., Wang, S. Y., John, S. A., Weiss, J. N., and Goldhaber, J. I. (2000) Metabolic inhibition activates a nonselective current through connexin hemichannels in isolated ventricular myocytes. J. Mol. Cell. Cardiol. 32, 1859-1872
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1859-1872
    • Kondo, R.P.1    Wang, S.Y.2    John, S.A.3    Weiss, J.N.4    Goldhaber, J.I.5
  • 36
    • 0037531231 scopus 로고    scopus 로고
    • Functional hemichannels in astrocytes: A novel mechanism of glutamate release
    • Ye, Z. C., Wyeth, M. S., Baltan-Tekkok, S., and Ransom, B. R. (2003) Functional hemichannels in astrocytes: a novel mechanism of glutamate release. J. Neurosci. 23, 3588-3596 (Pubitemid 36958466)
    • (2003) Journal of Neuroscience , vol.23 , Issue.9 , pp. 3588-3596
    • Ye, Z.-C.1    Wyeth, M.S.2    Baltan-Tekkok, S.3    Ransom, B.R.4
  • 37
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • DOI 10.1126/science.1126241
    • Thompson, R. J., Zhou, N., and MacVicar, B. A. (2006) Ischemia opens neuronal gap junction hemichannels. Science 312, 924-927 (Pubitemid 43727327)
    • (2006) Science , vol.312 , Issue.5775 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 38
    • 0037449718 scopus 로고    scopus 로고
    • Roles of Met-34, Cys-64, and Arg-75 in the assembly of human connexin 26: Implication for key amino acid residues for channel formation and function
    • DOI 10.1074/jbc.M207713200
    • Oshima, A., Doi, T., Mitsuoka, K., Maeda, S., and Fujiyoshi, Y. (2003) Roles of Met-34, Cys-64, and Arg-75 in the assembly of human connexin 26. Implication for key amino acid residues for channel formation and function. J. Biol. Chem. 278, 1807-1816 (Pubitemid 36801417)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1807-1816
    • Oshima, A.1    Doi, T.2    Mitsuoka, K.3    Maeda, S.4    Fujiyoshi, Y.5
  • 39
    • 2442431501 scopus 로고    scopus 로고
    • Regulation of Purified and Reconstituted Connexin 43 Hemichannels by Protein Kinase C-mediated Phosphorylation of Serine 368
    • DOI 10.1074/jbc.M311137200
    • Bao, X., Reuss, L., and Altenberg, G. A. (2004) Regulation of purified and reconstituted connexin 43 hemichannels by protein kinase C-mediated phosphorylation of serine 368. J. Biol. Chem. 279, 20058-20066 (Pubitemid 38623450)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20058-20066
    • Bao, X.1    Reuss, L.2    Altenberg, G.A.3
  • 40
    • 0031001091 scopus 로고    scopus 로고
    • Cell-free synthesis and assembly of connexins into functional gap junction membrane channels
    • DOI 10.1093/emboj/16.10.2703
    • Falk, M. M., Buehler, L. K., Kumar, N. M., and Gilula, N. B. (1997) Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. EMBO J. 16, 2703-2716 (Pubitemid 27226209)
    • (1997) EMBO Journal , vol.16 , Issue.10 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 41
    • 0033560718 scopus 로고    scopus 로고
    • Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels
    • DOI 10.1042/0264-6021:3390247
    • Ahmad, S., Diez, J. A., George, C. H., and Evans, W. H. (1999) Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels. Biochem. J. 339, 247-253 (Pubitemid 29209954)
    • (1999) Biochemical Journal , vol.339 , Issue.2 , pp. 247-253
    • Ahmad, S.1    Diez, J.A.2    George, C.H.3    Evans, W.H.4
  • 42
    • 67349228772 scopus 로고    scopus 로고
    • Direct formation of proteo-liposomes by in vitro synthesis and cellular cytosolic delivery with connexin-expressing liposomes
    • Kaneda, M., Nomura, S. M., Ichinose, S., Kondo, S., Nakahama, K., Akiyoshi, K., and Morita, I. (2009) Direct formation of proteo-liposomes by in vitro synthesis and cellular cytosolic delivery with connexin-expressing liposomes. Biomaterials 30, 3971-3977
    • (2009) Biomaterials , vol.30 , pp. 3971-3977
    • Kaneda, M.1    Nomura, S.M.2    Ichinose, S.3    Kondo, S.4    Nakahama, K.5    Akiyoshi, K.6    Morita, I.7
  • 43
    • 77955246394 scopus 로고    scopus 로고
    • Direct integration of cell-free synthesized connexin-43 into liposomes and hemichannel formation
    • Moritani, Y., Nomura, S. M., Morita, I., and Akiyoshi, K. (2010) Direct integration of cell-free synthesized connexin-43 into liposomes and hemichannel formation. FEBS J. 277, 3343-3352
    • (2010) FEBS J. , vol.277 , pp. 3343-3352
    • Moritani, Y.1    Nomura, S.M.2    Morita, I.3    Akiyoshi, K.4
  • 45
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • DOI 10.1002/yea.1208
    • Macauley-Patrick, S., Fazenda, M. L., McNeil, B., and Harvey, L. M. (2005) Heterologous protein production using the Pichia pastoris expression system. Yeast 22, 249-270 (Pubitemid 40528349)
    • (2005) Yeast , vol.22 , Issue.4 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 50
    • 0037155841 scopus 로고    scopus 로고
    • Intercellular calcium signaling in astrocytes via ATP release through connexin hemichannels
    • DOI 10.1074/jbc.M109902200
    • Stout, C. E., Costantin, J. L., Naus, C. C., and Charles, A. C. (2002) Intercellular calcium signaling in astrocytes via ATP release through connexin hemichannels. J. Biol. Chem. 277, 10482-10488 (Pubitemid 34968170)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10482-10488
    • Stout, C.E.1    Costantin, J.L.2    Naus, C.C.G.3    Charles, A.C.4
  • 53
    • 0035195813 scopus 로고    scopus 로고
    • Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons
    • Cottrell, G. T., and Burt, J. M. (2001) Heterotypic gap junction channel formation between heteromeric and homomeric Cx40 and Cx43 connexons. Am. J. Physiol. Cell Physiol. 281, C1559-C1567
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Cottrell, G.T.1    Burt, J.M.2
  • 54
    • 0036083484 scopus 로고    scopus 로고
    • Cx40 and Cx43 expression ratio influences heteromeric/heterotypic gap junction channel properties
    • Cottrell, G. T., Wu, Y., and Burt, J. M. (2002) Cx40 and Cx43 expression ratio influences heteromeric/heterotypic gap junction channel properties. Am. J. Physiol. Cell Physiol. 282, C1469-C1482 (Pubitemid 34663096)
    • (2002) American Journal of Physiology - Cell Physiology , vol.282 , Issue.6
    • Trevor, C.G.1    Wu, Y.2    Burt, J.M.3
  • 55
    • 0346496133 scopus 로고    scopus 로고
    • Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells
    • Hunter, A. W., Jourdan, J., and Gourdie, R. G. (2003) Fusion of GFP to the carboxyl terminus of connexin43 increases gap junction size in HeLa cells. Cell Commun. Adhes. 10, 211-214 (Pubitemid 38081374)
    • (2003) Cell Communication and Adhesion , vol.10 , Issue.4-6 , pp. 211-214
    • Hunter, A.W.1    Jourdan, J.2    Gourdie, R.G.3
  • 56
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • DOI 10.1091/mbc.E05-08-0737
    • Hunter, A. W., Barker, R. J., Zhu, C., and Gourdie, R. G. (2005) Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion. Mol. Biol. Cell 16, 5686-5698 (Pubitemid 41752218)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 57
    • 71749094770 scopus 로고    scopus 로고
    • Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains
    • Bouvier, D., Spagnol, G., Chenavas, S., Kieken, F., Vitrac, H., Brownell, S., Kellezi, A., Forge, V., and Sorgen, P. L. (2009) Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. J. Biol. Chem. 284, 34257-34271
    • (2009) J. Biol. Chem. , vol.284 , pp. 34257-34271
    • Bouvier, D.1    Spagnol, G.2    Chenavas, S.3    Kieken, F.4    Vitrac, H.5    Brownell, S.6    Kellezi, A.7    Forge, V.8    Sorgen, P.L.9
  • 58
    • 0031830342 scopus 로고    scopus 로고
    • Structure of cardiac gap junction intercellular channels
    • Yeager, M. (1998) Structure of cardiac gap junction intercellular channels. J. Struct. Biol. 121, 231-245
    • (1998) J. Struct. Biol. , vol.121 , pp. 231-245
    • Yeager, M.1
  • 59
    • 11144230049 scopus 로고    scopus 로고
    • Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1
    • DOI 10.1074/jbc.M409552200
    • Sorgen, P. L., Duffy, H. S., Sahoo, P., Coombs, W., Delmar, M., and Spray, D. C. (2004) Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. J. Biol. Chem. 279, 54695-54701 (Pubitemid 40053213)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54695-54701
    • Sorgen, P.L.1    Duffy, H.S.2    Sahoo, P.3    Coombs, W.4    Delmar, M.5    Spray, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.