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Volumn 2, Issue 12, 2001, Pages 898-907

Kinetic modelling approaches to in vivo imaging

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DNA BINDING PROTEIN, CYCLIC AMP RESPONSIVE; PROTEIN;

EID: 0035654399     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35103000     Document Type: Review
Times cited : (225)

References (66)
  • 1
    • 0035374872 scopus 로고    scopus 로고
    • Studying protein dynamics in living cells
    • A comprehensive review on kinetic imaging methods
    • Lippincott-Schwartz, J., Snapp, E. & Kenworthy, A. Studying protein dynamics in living cells. Nature Rev. Mol. Cell Biol. 2, 444-456 (2001). A comprehensive review on kinetic imaging methods.
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 444-456
    • Lippincott-Schwartz, J.1    Snapp, E.2    Kenworthy, A.3
  • 2
    • 0032622353 scopus 로고    scopus 로고
    • Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy
    • Periasamy, A. & Day, R. N. Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy. Methods Cell Biol. 58, 293-314 (1999).
    • (1999) Methods Cell Biol. , vol.58 , pp. 293-314
    • Periasamy, A.1    Day, R.N.2
  • 4
    • 0030868836 scopus 로고    scopus 로고
    • Applications of the green fluorescent protein in cell biology and biotechnology
    • Misteli, T. & Spector, D. L. Applications of the green fluorescent protein in cell biology and biotechnology. Nature Biotechnol. 15, 961-964 (1997).
    • (1997) Nature Biotechnol. , vol.15 , pp. 961-964
    • Misteli, T.1    Spector, D.L.2
  • 5
    • 0017817822 scopus 로고
    • Molecular cytochemistry: Incorporation of fluorescently labeled actin into living cells
    • Taylor, D. L. & Wang, Y. L. Molecular cytochemistry: incorporation of fluorescently labeled actin into living cells. Proc. Natl Acad. Sci. USA 75, 857-661 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 857-1661
    • Taylor, D.L.1    Wang, Y.L.2
  • 6
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 8
    • 0035839465 scopus 로고    scopus 로고
    • An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation
    • Verkhusha, V.V. et al. An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J. Biol. Chem. 276, 29621-29624 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29621-29624
    • Verkhusha, V.V.1
  • 9
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R. & Tsien, R. Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272 (1998).
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 11
    • 0030943027 scopus 로고    scopus 로고
    • Partitioning of the Golgi apparatus during mitosis in living HeLa cells
    • Shima, D. T., Haldar, K., Pepperkok, R., Watson, R. & Warren, G. Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 137, 1211-1228 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 1211-1228
    • Shima, D.T.1    Haldar, K.2    Pepperkok, R.3    Watson, R.4    Warren, G.5
  • 12
    • 0034762729 scopus 로고    scopus 로고
    • Dynamics of immature secretory granules: Role of cytoskeletal elements during transport, cortical restriction, and f-actin-dependent tethering
    • Rudolf, R., Salm, T., Rustom, A. & Gerdes, H. H. Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction, and f-actin-dependent tethering. Mol. Biol. Cell 12, 1353-1365 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1353-1365
    • Rudolf, R.1    Salm, T.2    Rustom, A.3    Gerdes, H.H.4
  • 13
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J. et al. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138, 1193-1206 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1
  • 14
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins A and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • Moir, R. D., Yoon, M., Khuon, S. & Goldman, R. D. Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells. J. Cell Biol. 151, 1155-1168 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 15
    • 0034618074 scopus 로고    scopus 로고
    • The dynamics of postmitotic reassembly of the nucleolus
    • Dundr, M., Misteli, T. & Olson, M. O. J. The dynamics of postmitotic reassembly of the nucleolus. J. Cell Biol. 150, 433-446 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 433-446
    • Dundr, M.1    Misteli, T.2    Olson, M.O.J.3
  • 16
    • 1842376906 scopus 로고    scopus 로고
    • The dynamics of a pre-mRNA splicing factor in living cells
    • Misteli, T., Cáceres, J. F. & Spector, D. L. The dynamics of a pre-mRNA splicing factor in living cells. Nature 387, 523-527 (1997).
    • (1997) Nature , vol.387 , pp. 523-527
    • Misteli, T.1    Cáceres, J.F.2    Spector, D.L.3
  • 17
    • 0034739848 scopus 로고    scopus 로고
    • In vivo analysis of cajal body movement, separation, and joining in live human cells
    • Platani, M., Goldberg, I., Swedlow, J. & Lamond, A. I. In vivo analysis of cajal body movement, separation, and joining in live human cells. J. Cell Biol. 151, 1561-1574 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1561-1574
    • Platani, M.1    Goldberg, I.2    Swedlow, J.3    Lamond, A.I.4
  • 19
    • 0033535323 scopus 로고    scopus 로고
    • Direct imaging of DNA in living cells reveals the dynamics of chromosome formation
    • Manders, E. M., Kimura, H. & Cook, P. R. Direct imaging of DNA in living cells reveals the dynamics of chromosome formation. J. Cell Biol. 144, 813-821 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 813-821
    • Manders, E.M.1    Kimura, H.2    Cook, P.R.3
  • 20
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally, J. G., Muller, W. G., Walker, D., Wolford, R. & Hager, G. L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 287, 1262-1265 (2000).
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 21
    • 0030461543 scopus 로고    scopus 로고
    • In vivo localization of DNA sequences and visualisation of large-scale chromatin organisation using lac operator/repressor recognition
    • Robinett, C. et al. In vivo localization of DNA sequences and visualisation of large-scale chromatin organisation using lac operator/repressor recognition. J. Cell Biol. 135, 1685-1700 (1996). The first description of an experimental system to study a chromatin region in living cells.
    • (1996) J. Cell Biol. , vol.135 , pp. 1685-1700
    • Robinett, C.1
  • 22
    • 0031954055 scopus 로고    scopus 로고
    • Structure and dynamics of human interphase chromosome territories in vivo
    • Zink, D. et al. Structure and dynamics of human interphase chromosome territories in vivo. Hum. Genet. 102, 241-251 (1998).
    • (1998) Hum. Genet. , vol.102 , pp. 241-251
    • Zink, D.1
  • 23
    • 0033672197 scopus 로고    scopus 로고
    • Visualisation of gene activity in living cells
    • Tsukarnoto, T. et al. Visualisation of gene activity in living cells. Nature Cell Biol. 2, 871-878 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 871-878
    • Tsukarnoto, T.1
  • 24
    • 0032054173 scopus 로고    scopus 로고
    • Four-dimensional imaging: The exploration of space and time
    • Thomas, C. F. & White, J. G. Four-dimensional imaging: the exploration of space and time. Trends Biotechnol. 16, 175-182 (1998).
    • (1998) Trends Biotechnol. , vol.16 , pp. 175-182
    • Thomas, C.F.1    White, J.G.2
  • 25
    • 0032750068 scopus 로고    scopus 로고
    • Quantitative motion analysis of subchromosomal foci in living cells using four-dimensional microscopy
    • Bomfleth, H., Edelmann, P., Zink, D., Cremer, T. & Cremer, C. Quantitative motion analysis of subchromosomal foci in living cells using four-dimensional microscopy. Biophys. J. 77, 2871-2886 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 2871-2886
    • Bomfleth, H.1    Edelmann, P.2    Zink, D.3    Cremer, T.4    Cremer, C.5
  • 26
    • 0012799399 scopus 로고    scopus 로고
    • Velocity estimation of spots in three-dimensional confocal image sequences of living cells
    • Bergsma, C. B., Streekstra, G. J., Smeulders, A. W. & Manders, E. M. Velocity estimation of spots in three-dimensional confocal image sequences of living cells. Cytometry 43, 261-272 (2001).
    • (2001) Cytometry , vol.43 , pp. 261-272
    • Bergsma, C.B.1    Streekstra, G.J.2    Smeulders, A.W.3    Manders, E.M.4
  • 27
    • 0033529248 scopus 로고    scopus 로고
    • Time-resolved analysis and visualisation of dynamic processes in living cells
    • Tvarusko, W. et al. Time-resolved analysis and visualisation of dynamic processes in living cells. Proc. Natl Acad. Sci. USA 96, 7950-7955 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7950-7955
    • Tvarusko, W.1
  • 28
    • 0034852706 scopus 로고    scopus 로고
    • Four-dimensional imaging and quantitative reconstruction to analyse complex spatiotemporal processes in live cells
    • Gehrlich, D., Beaudouin, J., Gebhard, M., Ellenberg, J. & Eils, R. Four-dimensional imaging and quantitative reconstruction to analyse complex spatiotemporal processes in live cells. Nature Cell Biol. 3, 852-855 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 852-855
    • Gehrlich, D.1    Beaudouin, J.2    Gebhard, M.3    Ellenberg, J.4    Eils, R.5
  • 29
    • 0017236539 scopus 로고
    • Measurement of membrane protein lateral diffusion in single cells
    • Edidin, M., Zagyansky, Y. & Lardner, T. J. Measurement of membrane protein lateral diffusion in single cells. Science 191, 466-468 (1976).
    • (1976) Science , vol.191 , pp. 466-468
    • Edidin, M.1    Zagyansky, Y.2    Lardner, T.J.3
  • 30
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E. & Webb, W. W. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16, 1055-1069 (1976). This is the classic paper on the quantitative analysis of FRAP data for cases in which the recovery is dominated by diffusion.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 31
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits, E. A. & Neefjes, J. J. From fixed to FRAP: measuring protein mobility and activity in living cells. Nature Cell Biol. 3, 145-147 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 145-147
    • Reits, E.A.1    Neefjes, J.J.2
  • 32
    • 0029784190 scopus 로고    scopus 로고
    • Diffusion mobility of Golgi proteins in membranes of living cells
    • Cole, N. B. et al. Diffusion mobility of Golgi proteins in membranes of living cells. Science 273, 797-801 (1996).
    • (1996) Science , vol.273 , pp. 797-801
    • Cole, N.B.1
  • 33
    • 0035039981 scopus 로고    scopus 로고
    • Accessing molecular dynamics in cells by fluorescence correlation spectroscopy
    • Dittrich, P., Malvezzi-Campeggi, F., Jahnz, M. & Schwille, P. Accessing molecular dynamics in cells by fluorescence correlation spectroscopy. Biol. Chem. 382, 491-494 (2001).
    • (2001) Biol. Chem. , vol.382 , pp. 491-494
    • Dittrich, P.1    Malvezzi-Campeggi, F.2    Jahnz, M.3    Schwille, P.4
  • 34
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille, P., Haupts, U., Maiti, S. & Webb, W. W. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation. Biophys. J. 77, 2251-2265 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 35
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy
    • Wachsmuth, M., Waldeck, W. & Langowski, J. Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy. J. Mol. Biol. 298, 677-689 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 36
    • 0033621065 scopus 로고    scopus 로고
    • Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy
    • Brock, R., Vamosi, G., Vereb, G. & Jovin, T. M. Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy. Proc. Natl Acad. Sci. USA 96, 10123-10128 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10123-10128
    • Brock, R.1    Vamosi, G.2    Vereb, G.3    Jovin, T.M.4
  • 37
    • 13044253479 scopus 로고    scopus 로고
    • Specific binding of proinsulin C-peptide to human cell membranes
    • Rigler, R. et al. Specific binding of proinsulin C-peptide to human cell membranes. Proc. Natl Acad. Sci. USA 96, 13318-13323 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13318-13323
    • Rigler, R.1
  • 38
    • 0032568529 scopus 로고    scopus 로고
    • Intranuclear diffusion and hybridization state of oligonucleotides measured by fluorescence correlation spectroscopy in living cells
    • Politz, J. C., Browne, E. S., Wolf, D. E. & Pederson, T. Intranuclear diffusion and hybridization state of oligonucleotides measured by fluorescence correlation spectroscopy in living cells. Proc. Natl Acad. Sci. USA 95, 6043-6048 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6043-6048
    • Politz, J.C.1    Browne, E.S.2    Wolf, D.E.3    Pederson, T.4
  • 39
    • 0035845662 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy detects galanin receptor diversity on insulinoma cells
    • Pramanik, A., Olsson, M., Langel, U., Bartfai, T. & Rigler, R. Fluorescence correlation spectroscopy detects galanin receptor diversity on insulinoma cells. Biochemistry 40, 10839-10645 (2001).
    • (2001) Biochemistry , vol.40 , pp. 10839-110645
    • Pramanik, A.1    Olsson, M.2    Langel, U.3    Bartfai, T.4    Rigler, R.5
  • 40
    • 0032110643 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy as a tool to investigate chemical reactions in solutions and on cell surfaces
    • Widengren, J. & Rigler, R. Fluorescence correlation spectroscopy as a tool to investigate chemical reactions in solutions and on cell surfaces. Cell. Mol. Biol. (Noisy-legrand) 44, 857-879 (1998).
    • (1998) Cell. Mol. Biol. (Noisy-legrand) , vol.44 , pp. 857-879
    • Widengren, J.1    Rigler, R.2
  • 41
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. Protein dynamics: implications for nuclear architecture and gene expression. Science 291, 843-847 (2001).
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 42
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H. & Cook, P. R. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J. Cell Biol. 153, 1341-1353 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 43
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D. & Misteli, T. High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-60 (2000). An application of FRAP, FLIP and kinetic modelling to obtain quantitative measures of the mobility of several functionally distinct nuclear proteins.
    • (2000) Nature , vol.404 , pp. 604-660
    • Phair, R.D.1    Misteli, T.2
  • 44
    • 0033782030 scopus 로고    scopus 로고
    • Dynamics and retention of misfolded proteins in native ER membranes
    • Nehls, S. et al. Dynamics and retention of misfolded proteins in native ER membranes. Nature Cell Biol. 2, 288-295 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 288-295
    • Nehls, S.1
  • 45
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein
    • Adams, C. L. Chen, Y. T., Smith, S. J. & Nelson, W. J. Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein. J. Cell Biol. 142, 1105-1119 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 1105-1119
    • Adams, C.L.1    Chen, Y.T.2    Smith, S.J.3    Nelson, W.J.4
  • 49
    • 0029028963 scopus 로고
    • Circuit simulation of genetic networks
    • McAdams, H. H. & Shapiro, L. Circuit simulation of genetic networks. Science 269, 650-656 (1995).
    • (1995) Science , vol.269 , pp. 650-656
    • McAdams, H.H.1    Shapiro, L.2
  • 51
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla, U. S. & lyengar, R. Emergent properties of networks of biological signaling pathways. Science 283, 381-387 (1999).
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Lyengar, R.2
  • 53
    • 33645429016 scopus 로고
    • Exact stochastic simulation of coupled chemical reactions
    • Gillespie, D. T. Exact stochastic simulation of coupled chemical reactions. J. Phys. Chem. 81, 2340-2361 (1977).
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 55
    • 0031436866 scopus 로고    scopus 로고
    • Development of kinetic models in the nonlinear world of molecular cell biology
    • Phair, R. D. Development of kinetic models in the nonlinear world of molecular cell biology. Metabolism 46, 1489-1495 (1997).
    • (1997) Metabolism , vol.46 , pp. 1489-1495
    • Phair, R.D.1
  • 58
    • 0033936772 scopus 로고    scopus 로고
    • Physiological modeling with virtual cell framework
    • Schaff, J. C., Slepchenko, B. M. & Loew, L. M. Physiological modeling with virtual cell framework. Methods Enzymol. 321, 1-23 (2000).
    • (2000) Methods Enzymol. , vol.321 , pp. 1-23
    • Schaff, J.C.1    Slepchenko, B.M.2    Loew, L.M.3
  • 59
    • 0033615967 scopus 로고    scopus 로고
    • Morphological control of inositol-1,4,5-trisphosphate-dependent signals
    • Fink, C. C. et al. Morphological control of inositol-1,4,5-trisphosphate-dependent signals. J. Cell Biol. 147, 929-936 (1999). A clear and compelling examination of the importance of partial differential equation models when studying large cells or cells with long processes in which one must account for simultaneous diffusion and spatially distributed chemical reactions.
    • (1999) J. Cell Biol. , vol.147 , pp. 929-936
    • Fink, C.C.1
  • 61
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K. et al. Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485-1503 (1998). This was among the first studies to combine the power of green fluorescent protein chimaeras, photobleaching techniques and kinetic analysis to answer questions about protein transport in living cells.
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1
  • 63
    • 0035860545 scopus 로고    scopus 로고
    • Pathway databases: A case study in computational symbolic theories
    • Karp, P. D. Pathway databases: a case study in computational symbolic theories. Science 293, 2040-2044 (2001).
    • (2001) Science , vol.293 , pp. 2040-2044
    • Karp, P.D.1
  • 66
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • Mayr, B. & Montminy, M. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nature Rev. Mol. Cell Biol. 2, 599-609 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2


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