메뉴 건너뛰기




Volumn 1813, Issue 8, 2011, Pages 1511-1524

Long and short distance movements of β2-adrenoceptor in cell membrane assessed by photoconvertible fluorescent protein dendra2-β2-adrenoceptor fusion

Author keywords

adrenoceptor; Compartmentalization; Dendra2; G protein coupled receptor; Lateral diffusion; Receptor mobility

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; HYBRID PROTEIN; PROTEIN; PROTEIN DENDRA2; UNCLASSIFIED DRUG;

EID: 79959354808     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.05.008     Document Type: Article
Times cited : (6)

References (57)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 1972, 175:720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 3
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig R.R. Membrane organization in G-protein mechanisms. FASEB J. 1994, 8:939-946.
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 4
    • 33746046362 scopus 로고    scopus 로고
    • Higher-order organization and regulation of adenylate cyclases
    • Cooper D.M.F., Crossthwaite A.J. Higher-order organization and regulation of adenylate cyclases. Trends. Pharmacol. Sci. 2006, 27:426-431.
    • (2006) Trends. Pharmacol. Sci. , vol.27 , pp. 426-431
    • Cooper, D.M.F.1    Crossthwaite, A.J.2
  • 5
    • 0012050693 scopus 로고
    • Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbrück equations
    • Peters R., Cherry R.J. Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbrück equations. Proc. Natl. Acad. Sci. USA 1982, 79:4317-4321.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4317-4321
    • Peters, R.1    Cherry, R.J.2
  • 6
    • 0028142423 scopus 로고
    • Lateral diffusion measurement at high spatial resolution by scanning microphotolysis in a confocal microscope
    • Kubitscheck U., Wedekind P., Peters R. Lateral diffusion measurement at high spatial resolution by scanning microphotolysis in a confocal microscope. Biophys. J. 1994, 67:948-956.
    • (1994) Biophys. J. , vol.67 , pp. 948-956
    • Kubitscheck, U.1    Wedekind, P.2    Peters, R.3
  • 7
    • 69949119573 scopus 로고    scopus 로고
    • Lateral diffusion of rhodopsin in photoreceptor membrane: a reappraisal
    • Govardovskii V.I., Korenyak D.A., Shukolyukov S.A., Zueva L.V. Lateral diffusion of rhodopsin in photoreceptor membrane: a reappraisal. Mol. Vis. 2009, 15:1717-1729.
    • (2009) Mol. Vis. , vol.15 , pp. 1717-1729
    • Govardovskii, V.I.1    Korenyak, D.A.2    Shukolyukov, S.A.3    Zueva, L.V.4
  • 8
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • Suzuki K., Ritchie K., Kajikawa E., Fujiwara T., Kusumi A. Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophys. J. 2005, 88:3659-3680.
    • (2005) Biophys. J. , vol.88 , pp. 3659-3680
    • Suzuki, K.1    Ritchie, K.2    Kajikawa, E.3    Fujiwara, T.4    Kusumi, A.5
  • 9
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy
    • Kusumi A., Shirai Y.M., Koyama-Honda I., Suzuki K.G., Fujiwara T.K. Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy. FEBS Lett. 2010, 584:1814-1823.
    • (2010) FEBS Lett. , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 11
    • 0037030721 scopus 로고    scopus 로고
    • Regulation of AMPA receptor lateral movements
    • Borgdorff A.J., Choquet D. Regulation of AMPA receptor lateral movements. Nature 2002, 417:649-653.
    • (2002) Nature , vol.417 , pp. 649-653
    • Borgdorff, A.J.1    Choquet, D.2
  • 12
    • 0037061686 scopus 로고    scopus 로고
    • Mobile NMDA receptors at hippocampal synapses
    • Tovar K.R., Westbrook G.L. Mobile NMDA receptors at hippocampal synapses. Neuron 2002, 34:255-264.
    • (2002) Neuron , vol.34 , pp. 255-264
    • Tovar, K.R.1    Westbrook, G.L.2
  • 14
    • 0035112736 scopus 로고    scopus 로고
    • Fast and reversible trapping of surface glycine receptors by gephyrin
    • Meier J., Vannier C., Sergé A., Triller A., Choquet D. Fast and reversible trapping of surface glycine receptors by gephyrin. Nat. Neurosci. 2001, 4:253-260.
    • (2001) Nat. Neurosci. , vol.4 , pp. 253-260
    • Meier, J.1    Vannier, C.2    Sergé, A.3    Triller, A.4    Choquet, D.5
  • 15
    • 77957017139 scopus 로고    scopus 로고
    • Synaptic stability and plasticity in a floating world
    • Gerrow K., Triller A. Synaptic stability and plasticity in a floating world. Curr. Opin. Neurobiol. 2010, 20:1-9.
    • (2010) Curr. Opin. Neurobiol. , vol.20 , pp. 1-9
    • Gerrow, K.1    Triller, A.2
  • 17
    • 67649871991 scopus 로고    scopus 로고
    • Quantitative microscopy: protein dynamics and membrane organisation
    • Owen D.M., Williamson D., Rentero C., Gaus K. Quantitative microscopy: protein dynamics and membrane organisation. Traffic 2009, 10:962-971.
    • (2009) Traffic , vol.10 , pp. 962-971
    • Owen, D.M.1    Williamson, D.2    Rentero, C.3    Gaus, K.4
  • 19
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • Soumpasis D.M. Theoretical analysis of fluorescence photobleaching recovery experiments. Biophys. J. 1983, 41:95-97.
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 20
    • 63849123796 scopus 로고    scopus 로고
    • Coupling of α2-adrenoceptors to XLαs and Gαs: a new insight into ligand-induced G protein activation
    • Kaya A.I., Ugur O., Oner S.S., Bastepe M., Onaran H.O. Coupling of β2-adrenoceptors to XLαs and Gα a new insight into ligand-induced G protein activation. J. Pharmacol. Exp. Ther. 2009, 329:350-359.
    • (2009) J. Pharmacol. Exp. Ther. , vol.329 , pp. 350-359
    • Kaya, A.I.1    Ugur, O.2    Oner, S.S.3    Bastepe, M.4    Onaran, H.O.5
  • 21
    • 0030999009 scopus 로고    scopus 로고
    • Allosteric equilibrium model explains steady-state coupling of β-adrenergic receptors to adenylate cyclase in turkey erythrocyte membranes
    • Ugur O., Onaran H.O. Allosteric equilibrium model explains steady-state coupling of β-adrenergic receptors to adenylate cyclase in turkey erythrocyte membranes. Biochem. J. 1997, 323:765-776.
    • (1997) Biochem. J. , vol.323 , pp. 765-776
    • Ugur, O.1    Onaran, H.O.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0034193130 scopus 로고    scopus 로고
    • Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking
    • Kallal L., Benovic J.L. Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking. Trends. Pharmacol. Sci. 2000, 21:175-180.
    • (2000) Trends. Pharmacol. Sci. , vol.21 , pp. 175-180
    • Kallal, L.1    Benovic, J.L.2
  • 25
    • 21644460729 scopus 로고    scopus 로고
    • Green fluorescent proteins in receptor research: an emerging tool for drug discovery
    • Arun K.H., Kaul C.L., Ramarao P. Green fluorescent proteins in receptor research: an emerging tool for drug discovery. Pharmacol. Toxicol. Methods 2005, 51:1-23.
    • (2005) Pharmacol. Toxicol. Methods , vol.51 , pp. 1-23
    • Arun, K.H.1    Kaul, C.L.2    Ramarao, P.3
  • 26
    • 66649126345 scopus 로고    scopus 로고
    • Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein dendra2
    • Adam V., Nienhaus K., Bourgeois D., Nienhaus G.U. Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein dendra2. Biochemistry 2009, 48:4905-4915.
    • (2009) Biochemistry , vol.48 , pp. 4905-4915
    • Adam, V.1    Nienhaus, K.2    Bourgeois, D.3    Nienhaus, G.U.4
  • 27
    • 0031025764 scopus 로고    scopus 로고
    • Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate
    • Barak L.S., Ferguson S.S., Zhang J., Martenson C., Meyer T., Caron M.G. Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate. Mol. Pharmacol. 1997, 51:177-184.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 177-184
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Martenson, C.4    Meyer, T.5    Caron, M.G.6
  • 28
    • 0032730974 scopus 로고    scopus 로고
    • Visualizing differences in ligand regulation of wild-type and constitutively active mutantα 2-adrenoceptor-green fluorescent protein fusion proteins
    • Mclean A.J., Bevan N., Rees S., Milligan G. Visualizing differences in ligand regulation of wild-type and constitutively active mutant α2-adrenoceptor-green fluorescent protein fusion proteins. Mol. Pharmacol. 1999, 56:1182-1191.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1182-1191
    • Mclean, A.J.1    Bevan, N.2    Rees, S.3    Milligan, G.4
  • 29
    • 0023858575 scopus 로고
    • β-Adrenergic receptor kinase activity of partial agonists for stimulation of adenylate cyclase correlates with ability to promote receptor phosphorylation
    • Benovic J.L., Staniszewski C., Mayor F., Caron M.G., Lefkowitz R.J. β-Adrenergic receptor kinase activity of partial agonists for stimulation of adenylate cyclase correlates with ability to promote receptor phosphorylation. J. Biol. Chem. 1988, 263:3893-3897.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3893-3897
    • Benovic, J.L.1    Staniszewski, C.2    Mayor, F.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 30
    • 0030593035 scopus 로고    scopus 로고
    • Role of β-arrestin in mediating agonistpromoted G protein-coupled receptor internalization
    • Ferguson S.S., Downey W.E., Colapietro A.M., Barak L.S., Ménard L., Caron M.G. Role of β-arrestin in mediating agonistpromoted G protein-coupled receptor internalization. Science 1996, 271:363-366.
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.1    Downey, W.E.2    Colapietro, A.M.3    Barak, L.S.4    Ménard, L.5    Caron, M.G.6
  • 31
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling
    • Ferguson S.S. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol. Rev. 2001, 53:1-24.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 32
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model
    • Samama P., Cotecchia S., Costa T., Lefkowitz R.J. A mutation-induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 1993, 268:4625-4636.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 33
    • 0037076531 scopus 로고    scopus 로고
    • Mutation of a single TMVI residue, Phe282, in the β2-adrenergic receptor results in structurally distinct activated receptor conformations
    • Chen S., Lin F., Xu M., Riek R.P., Novotny J., Graham R.M. Mutation of a single TMVI residue, Phe282, in the β2-adrenergic receptor results in structurally distinct activated receptor conformations. Biochemistry 2002, 41:6045-6053.
    • (2002) Biochemistry , vol.41 , pp. 6045-6053
    • Chen, S.1    Lin, F.2    Xu, M.3    Riek, R.P.4    Novotny, J.5    Graham, R.M.6
  • 34
    • 77649186796 scopus 로고    scopus 로고
    • β2-Adrenoceptor, Gs and adenylate cyclase coupling in purified detergent-resistant, low density membrane fractions
    • Oner S.S., Kaya A.I., Onaran H.O., Ozcan G., Uǧur O. β2-Adrenoceptor, Gs and adenylate cyclase coupling in purified detergent-resistant, low density membrane fractions. Eur. J. Pharmacol. 2010, 630:42-52.
    • (2010) Eur. J. Pharmacol. , vol.630 , pp. 42-52
    • Oner, S.S.1    Kaya, A.I.2    Onaran, H.O.3    Ozcan, G.4    Uǧur, O.5
  • 35
    • 0034084767 scopus 로고    scopus 로고
    • Downregulation of G protein-coupled receptors
    • Tsao P., von Zastrow M. Downregulation of G protein-coupled receptors. Curr. Opin. Neurobiol. 2000, 10:365-369.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 365-369
    • Tsao, P.1    von Zastrow, M.2
  • 36
    • 0036209874 scopus 로고    scopus 로고
    • Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and β-arrestin proteins
    • Claing A., Laporte S.A., Caron M.G., Lefkowitz R.J. Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and β-arrestin proteins. Prog. Neurobiol. 2002, 66:61-79.
    • (2002) Prog. Neurobiol. , vol.66 , pp. 61-79
    • Claing, A.1    Laporte, S.A.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 39
    • 77951993972 scopus 로고    scopus 로고
    • Agonist-selective dynamic compartmentalization of human mu opioid receptor as revealed by resolutive FRAP analysis
    • Saulière-Nzeh A.N., Millot C., Corbani M., Mazères S., Lopez A., Salomé L. Agonist-selective dynamic compartmentalization of human mu opioid receptor as revealed by resolutive FRAP analysis. J. Biol. Chem. 2010, 285:14514-14520.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14514-14520
    • Saulière-Nzeh, A.N.1    Millot, C.2    Corbani, M.3    Mazères, S.4    Lopez, A.5    Salomé, L.6
  • 42
    • 34547124343 scopus 로고    scopus 로고
    • Signaling through a G protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model
    • Philip F., Sengupta P., Scarlata S. Signaling through a G protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model. J. Biol. Chem. 2007, 282:19203-19216.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19203-19216
    • Philip, F.1    Sengupta, P.2    Scarlata, S.3
  • 44
    • 40449125151 scopus 로고    scopus 로고
    • Agonist-occupied A3 adenosine receptors exist within heterogeneous complexes in membrane microdomains of individual living cells
    • Cordeaux Y., Briddon S.J., Alexander S.P., Kellam B., Hill S.J. Agonist-occupied A3 adenosine receptors exist within heterogeneous complexes in membrane microdomains of individual living cells. FASEB J. 2008, 22:850-860.
    • (2008) FASEB J. , vol.22 , pp. 850-860
    • Cordeaux, Y.1    Briddon, S.J.2    Alexander, S.P.3    Kellam, B.4    Hill, S.J.5
  • 47
    • 0032961873 scopus 로고    scopus 로고
    • Characterization of an intrinsically fluorescent gonadotropinreleasing hormone receptor and effects of ligand binding on receptor lateral diffusion
    • Nelson S., Horvat R.D., Malvey J., Roess D.A., Barisas B.G., Clay C.M. Characterization of an intrinsically fluorescent gonadotropinreleasing hormone receptor and effects of ligand binding on receptor lateral diffusion. Endocrinology 1999, 140:950-957.
    • (1999) Endocrinology , vol.140 , pp. 950-957
    • Nelson, S.1    Horvat, R.D.2    Malvey, J.3    Roess, D.A.4    Barisas, B.G.5    Clay, C.M.6
  • 48
    • 0033573876 scopus 로고    scopus 로고
    • Intrinsically fluorescent luteinizing hormone receptor demonstrates hormone-driven aggregation
    • Horvat R.D., Nelson S., Clay C.M., Barisas B.G., Roess D.A. Intrinsically fluorescent luteinizing hormone receptor demonstrates hormone-driven aggregation. Biochem. Biophys. Res. Commun. 1999, 255:382-385.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 382-385
    • Horvat, R.D.1    Nelson, S.2    Clay, C.M.3    Barisas, B.G.4    Roess, D.A.5
  • 49
    • 0025182369 scopus 로고
    • Lateral mobility of the phospholipase C-activating vasopressin V1-type receptor in A7r5 smooth muscle cells: a comparison with the adenylate cyclase-coupled V2-receptor
    • Jans D.A., Peters R., Fahrenholz F. Lateral mobility of the phospholipase C-activating vasopressin V1-type receptor in A7r5 smooth muscle cells: a comparison with the adenylate cyclase-coupled V2-receptor. EMBO J. 1990, 9:2693-2699.
    • (1990) EMBO J. , vol.9 , pp. 2693-2699
    • Jans, D.A.1    Peters, R.2    Fahrenholz, F.3
  • 50
    • 0024456622 scopus 로고
    • The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature
    • Jans D.A., Peters R., Zsigo J., Fahrenholz F. The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature. EMBO J. 1989, 8:2481-2488.
    • (1989) EMBO J. , vol.8 , pp. 2481-2488
    • Jans, D.A.1    Peters, R.2    Zsigo, J.3    Fahrenholz, F.4
  • 52
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess D.A., Horvat R.D., Munnelly H., Barisas B.G. Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 2000, 141:4518-4523.
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 53
    • 7244250134 scopus 로고    scopus 로고
    • Dynamic confinement of NK2 receptors in the plasma membrane: improved FRAP analysis and biological relevance
    • Cézanne L., Lecat S., Lagane B., Millot C., Vollmer J.Y., Matthes H., Galzi J.L., Lopez A. Dynamic confinement of NK2 receptors in the plasma membrane: improved FRAP analysis and biological relevance. J. Biol. Chem. 2004, 279:45057-45067.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45057-45067
    • Cézanne, L.1    Lecat, S.2    Lagane, B.3    Millot, C.4    Vollmer, J.Y.5    Matthes, H.6    Galzi, J.L.7    Lopez, A.8
  • 54
    • 23944505054 scopus 로고    scopus 로고
    • Kinetics of the initial steps of g protein-coupled receptor-mediated cellular signaling revealed by single-molecule imaging
    • Lill Y., Martinez K.L., Lill M.A., Meyer B.H., Vogel H., Hecht B. Kinetics of the initial steps of g protein-coupled receptor-mediated cellular signaling revealed by single-molecule imaging. ChemPhysChem 2005, 6:1633-1640.
    • (2005) ChemPhysChem , vol.6 , pp. 1633-1640
    • Lill, Y.1    Martinez, K.L.2    Lill, M.A.3    Meyer, B.H.4    Vogel, H.5    Hecht, B.6
  • 55
    • 0035397971 scopus 로고    scopus 로고
    • Agonist-dependent immobilization of chimeric bombesin/GRP receptors: dependence on c-Src activity and dissociation from internalization
    • Young S.H., Walsh J.H., Rozengurt E., Slice L.W. Agonist-dependent immobilization of chimeric bombesin/GRP receptors: dependence on c-Src activity and dissociation from internalization. Exp. Cell Res. 2001, 267:37-44.
    • (2001) Exp. Cell Res. , vol.267 , pp. 37-44
    • Young, S.H.1    Walsh, J.H.2    Rozengurt, E.3    Slice, L.W.4
  • 56
    • 0037095771 scopus 로고    scopus 로고
    • Receptor activation and homer differentially control the lateral mobility of metabotropic glutamate receptor 5 in the neuronal membrane
    • Sergé A., Fourgeaud L., Hémar A., Choquet D. Receptor activation and homer differentially control the lateral mobility of metabotropic glutamate receptor 5 in the neuronal membrane. J. Neurosci. 2002, 22:3910-3920.
    • (2002) J. Neurosci. , vol.22 , pp. 3910-3920
    • Sergé, A.1    Fourgeaud, L.2    Hémar, A.3    Choquet, D.4
  • 57
    • 36849019932 scopus 로고    scopus 로고
    • CD4 interacts constitutively with multiple CCR5 at the plasma membrane of living cells. A fluorescence recovery after photobleaching at variable radii approach
    • Baker A.M., Saulière A., Gaibelet G., Lagane B., Mazères S., Fourage M., Bachelerie F., Salomé L., Lopez A., Dumas F. CD4 interacts constitutively with multiple CCR5 at the plasma membrane of living cells. A fluorescence recovery after photobleaching at variable radii approach. J. Biol. Chem. 2007, 282:35163-35168.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35163-35168
    • Baker, A.M.1    Saulière, A.2    Gaibelet, G.3    Lagane, B.4    Mazères, S.5    Fourage, M.6    Bachelerie, F.7    Salomé, L.8    Lopez, A.9    Dumas, F.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.