메뉴 건너뛰기




Volumn 17, Issue 1, 2009, Pages 96-104

The Structure of the MAP2K MEK6 Reveals an Autoinhibitory Dimer

Author keywords

PROTEINS; SIGNALING

Indexed keywords

ARGININE; ASPARTIC ACID; DIMER; MICROTUBULE ASSOCIATED PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE KINASE 6; PHOSPHATE BINDING PROTEIN; PROTEIN SUBUNIT;

EID: 58149201051     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.11.007     Document Type: Article
Times cited : (28)

References (64)
  • 1
    • 33751261134 scopus 로고    scopus 로고
    • Mechanisms of MAPK signalling specificity
    • Bardwell L. Mechanisms of MAPK signalling specificity. Biochem. Soc. Trans. 34 (2006) 837-841
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 837-841
    • Bardwell, L.1
  • 2
    • 0037444809 scopus 로고    scopus 로고
    • Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity
    • Bardwell A.J., Abdollahi M., and Bardwell L. Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity. Biochem. J. 370 (2003) 1077-1085
    • (2003) Biochem. J. , vol.370 , pp. 1077-1085
    • Bardwell, A.J.1    Abdollahi, M.2    Bardwell, L.3
  • 3
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38γ is monomeric and reveals a conserved activation-loop conformation
    • Bellon S., Fitzgibbon M.J., Fox T., Hsiao H.M., and Wilson K.P. The structure of phosphorylated p38γ is monomeric and reveals a conserved activation-loop conformation. Structure 7 (1999) 1057-1065
    • (1999) Structure , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M.J.2    Fox, T.3    Hsiao, H.M.4    Wilson, K.P.5
  • 4
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi R.M., and Nebreda A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372 (2003) 1-13
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 5
    • 0021341961 scopus 로고
    • Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases
    • Braun S., Raymond W.E., and Racker E. Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases. J. Biol. Chem. 259 (1984) 2051-2054
    • (1984) J. Biol. Chem. , vol.259 , pp. 2051-2054
    • Braun, S.1    Raymond, W.E.2    Racker, E.3
  • 7
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah B.J., Khokhlatchev A., Cobb M.H., and Goldsmith E.J. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90 (1997) 859-869
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computing Project, Number 4)
    • CCP4 (Collaborative Computing Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 0036289349 scopus 로고    scopus 로고
    • Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b
    • Chang C.I., Xu B.E., Akella R., Cobb M.H., and Goldsmith E.J. Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b. Mol. Cell 9 (2002) 1241-1249
    • (2002) Mol. Cell , vol.9 , pp. 1241-1249
    • Chang, C.I.1    Xu, B.E.2    Akella, R.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 12
    • 0346463059 scopus 로고    scopus 로고
    • High intensity ras signaling induces premature senescence by activating p38 pathway in primary human fibroblasts
    • Deng Q., Liao R., Wu B.L., and Sun P. High intensity ras signaling induces premature senescence by activating p38 pathway in primary human fibroblasts. J. Biol. Chem. 279 (2004) 1050-1059
    • (2004) J. Biol. Chem. , vol.279 , pp. 1050-1059
    • Deng, Q.1    Liao, R.2    Wu, B.L.3    Sun, P.4
  • 13
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2α substrate recognition
    • Dey M., Cao C., Dar A.C., Tamura T., Ozato K., Sicheri F., and Dever T.E. Mechanistic link between PKR dimerization, autophosphorylation, and eIF2α substrate recognition. Cell 122 (2005) 901-913
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dar, A.C.3    Tamura, T.4    Ozato, K.5    Sicheri, F.6    Dever, T.E.7
  • 14
    • 0028385715 scopus 로고
    • Overcoming non-isomorphism by phase permutation and likelihood scoring: solution of the TrpRS crystal structure
    • Doublie S., Xiang S., Gilmore C.J., and Carter Jr. C.W. Overcoming non-isomorphism by phase permutation and likelihood scoring: solution of the TrpRS crystal structure. Acta Crystallogr. A 50 (1994) 164-182
    • (1994) Acta Crystallogr. A , vol.50 , pp. 164-182
    • Doublie, S.1    Xiang, S.2    Gilmore, C.J.3    Carter Jr., C.W.4
  • 15
    • 0034653850 scopus 로고    scopus 로고
    • Molecular determinants that mediate selective activation of p38 MAP kinase isoforms
    • Enslen H., Brancho D.M., and Davis R.J. Molecular determinants that mediate selective activation of p38 MAP kinase isoforms. EMBO J. 19 (2000) 1301-1311
    • (2000) EMBO J. , vol.19 , pp. 1301-1311
    • Enslen, H.1    Brancho, D.M.2    Davis, R.J.3
  • 17
    • 36849043083 scopus 로고    scopus 로고
    • Substrate and docking interactions in serine/threonine protein kinases
    • Goldsmith E.J., Akella R., Min X., Zhou T., and Humphreys J.M. Substrate and docking interactions in serine/threonine protein kinases. Chem. Rev. 107 (2007) 5065-5081
    • (2007) Chem. Rev. , vol.107 , pp. 5065-5081
    • Goldsmith, E.J.1    Akella, R.2    Min, X.3    Zhou, T.4    Humphreys, J.M.5
  • 19
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAP kinase kinase (MKK6)
    • Han J., Lee J.D., Jiang Y., Li Z., Feng L., and Ulevitch R.J. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J. Biol. Chem. 271 (1996) 2886-2891
    • (1996) J. Biol. Chem. , vol.271 , pp. 2886-2891
    • Han, J.1    Lee, J.D.2    Jiang, Y.3    Li, Z.4    Feng, L.5    Ulevitch, R.J.6
  • 22
    • 0028916307 scopus 로고
    • Biochemical and biological analysis of Mek1 phosphorylation site mutants
    • Huang W., Kessler D.S., and Erikson R.L. Biochemical and biological analysis of Mek1 phosphorylation site mutants. Mol. Biol. Cell 6 (1995) 237-245
    • (1995) Mol. Biol. Cell , vol.6 , pp. 237-245
    • Huang, W.1    Kessler, D.S.2    Erikson, R.L.3
  • 23
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16 (1997) 5572-5581
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 24
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 25
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., and Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298 (2002) 1911-1912
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G., Willett P., Glen R.C., Leach A.R., and Taylor R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267 (1997) 727-748
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 28
  • 29
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch M.H., Vachette P., and Svergun D.I. Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36 (2003) 147-227
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 30
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M., Lu W., Meng W., Parrini M.C., Eck M.J., Mayer B.J., and Harrison S.C. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102 (2000) 387-397
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 31
    • 0022981913 scopus 로고
    • Loops in globular proteins: a novel category of secondary structure
    • Leszczynski J.F., and Rose G.D. Loops in globular proteins: a novel category of secondary structure. Science 234 (1986) 849-855
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.F.1    Rose, G.D.2
  • 32
    • 33645765166 scopus 로고    scopus 로고
    • Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3
    • Liu S., Sun J.P., Zhou B., and Zhang Z.Y. Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3. Proc. Natl. Acad. Sci. USA 103 (2006) 5326-5331
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5326-5331
    • Liu, S.1    Sun, J.P.2    Zhou, B.3    Zhang, Z.Y.4
  • 33
    • 0028351165 scopus 로고
    • Contribution of unusual arginine-arginine short-range interactions to stabilization and recognition in proteins
    • Magalhaes A., Maigret B., Hoflack J., Gomes J.N., and Scheraga H.A. Contribution of unusual arginine-arginine short-range interactions to stabilization and recognition in proteins. J. Protein Chem. 13 (1994) 195-215
    • (1994) J. Protein Chem. , vol.13 , pp. 195-215
    • Magalhaes, A.1    Maigret, B.2    Hoflack, J.3    Gomes, J.N.4    Scheraga, H.A.5
  • 34
    • 0038004740 scopus 로고    scopus 로고
    • Targeting JNK for therapeutic benefit: from junk to gold?
    • Manning A.M., and Davis R.J. Targeting JNK for therapeutic benefit: from junk to gold?. Nat. Rev. Drug Discov. 2 (2003) 554-565
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 554-565
    • Manning, A.M.1    Davis, R.J.2
  • 37
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., and Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 375 (1995) 554-560
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 439-450
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 43
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam C.D., Hammel M., Hura G.L., and Tainer J.A. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40 (2007) 191-285
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 44
    • 0026345260 scopus 로고
    • Use of synthetic amino acid polymers for assay of protein-tyrosine and protein-serine kinases
    • Racker E. Use of synthetic amino acid polymers for assay of protein-tyrosine and protein-serine kinases. Methods Enzymol. 200 (1991) 107-111
    • (1991) Methods Enzymol. , vol.200 , pp. 107-111
    • Racker, E.1
  • 45
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman M., Chen W., and Cobb M.H. Differential regulation and properties of MAPKs. Oncogene 26 (2007) 3100-3112
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 46
    • 29144502234 scopus 로고    scopus 로고
    • The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network
    • Remenyi A., Good M.C., Bhattacharyya R.P., and Lim W.A. The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. Mol. Cell 20 (2005) 951-962
    • (2005) Mol. Cell , vol.20 , pp. 951-962
    • Remenyi, A.1    Good, M.C.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 48
    • 33745325007 scopus 로고    scopus 로고
    • Mechanisms of drug inhibition of signalling molecules
    • Sebolt-Leopold J.S., and English J.M. Mechanisms of drug inhibition of signalling molecules. Nature 441 (2006) 457-462
    • (2006) Nature , vol.441 , pp. 457-462
    • Sebolt-Leopold, J.S.1    English, J.M.2
  • 49
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of parallel expression vectors
    • Sheffield P., Garrard S., and Derewenda Z. Overcoming expression and purification problems of RhoGDI using a family of parallel expression vectors. Protein Expr. Purif. 15 (1999) 34-39
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 50
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 51
    • 20844449066 scopus 로고    scopus 로고
    • Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases
    • Takekawa M., Tatebayashi K., and Saito H. Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases. Mol. Cell 18 (2005) 295-306
    • (2005) Mol. Cell , vol.18 , pp. 295-306
    • Takekawa, M.1    Tatebayashi, K.2    Saito, H.3
  • 52
    • 0037400611 scopus 로고    scopus 로고
    • Molecular recognitions in the MAP kinase cascades
    • Tanoue T., and Nishida E. Molecular recognitions in the MAP kinase cascades. Cell. Signal. 15 (2003) 455-462
    • (2003) Cell. Signal. , vol.15 , pp. 455-462
    • Tanoue, T.1    Nishida, E.2
  • 53
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • Tsutakawa S.E., Hura G.L., Frankel K.A., Cooper P.K., and Tainer J.A. Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography. J. Struct. Biol. 158 (2007) 214-223
    • (2007) J. Struct. Biol. , vol.158 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 55
    • 32144436881 scopus 로고    scopus 로고
    • Regulation of cellular functions by the ERK5 signalling pathway
    • Wang X., and Tournier C. Regulation of cellular functions by the ERK5 signalling pathway. Cell. Signal. 18 (2006) 753-760
    • (2006) Cell. Signal. , vol.18 , pp. 753-760
    • Wang, X.1    Tournier, C.2
  • 57
    • 27744602322 scopus 로고    scopus 로고
    • Structural comparison of p38 inhibitor-protein complexes: a review of recent p38 inhibitors having unique binding interactions
    • Wrobleski S.T., and Doweyko A.M. Structural comparison of p38 inhibitor-protein complexes: a review of recent p38 inhibitors having unique binding interactions. Curr. Top. Med. Chem. 5 (2005) 1005-1016
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 1005-1016
    • Wrobleski, S.T.1    Doweyko, A.M.2
  • 59
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions
    • Yoon S., and Seger R. The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24 (2006) 21-44
    • (2006) Growth Factors , vol.24 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 60
    • 19644367000 scopus 로고    scopus 로고
    • Activation and signaling of the p38 MAP kinase pathway
    • Zarubin T., and Han J. Activation and signaling of the p38 MAP kinase pathway. Cell Res. 15 (2005) 11-18
    • (2005) Cell Res. , vol.15 , pp. 11-18
    • Zarubin, T.1    Han, J.2
  • 61
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang F., Strand A., Robbins D., Cobb M.H., and Goldsmith E.J. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367 (1994) 704-711
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 62
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X., Gureasko J., Shen K., Cole P.A., and Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125 (2006) 1137-1149
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 63
    • 4644232397 scopus 로고    scopus 로고
    • Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K
    • Zhou T., Raman M., Gao Y., Earnest S., Chen Z., Machius M., Cobb M.H., and Goldsmith E.J. Crystal structure of the TAO2 kinase domain: activation and specificity of a Ste20p MAP3K. Structure 12 (2004) 1891-1900
    • (2004) Structure , vol.12 , pp. 1891-1900
    • Zhou, T.1    Raman, M.2    Gao, Y.3    Earnest, S.4    Chen, Z.5    Machius, M.6    Cobb, M.H.7    Goldsmith, E.J.8
  • 64
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • Zhou T., Sun L., Humphreys J., and Goldsmith E.J. Docking interactions induce exposure of activation loop in the MAP kinase ERK2. Structure 14 (2006) 1011-1019
    • (2006) Structure , vol.14 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3    Goldsmith, E.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.