메뉴 건너뛰기




Volumn 14, Issue 5, 2015, Pages 1275-1287

Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase Pom1

Author keywords

[No Author keywords available]

Indexed keywords

CDR2 PROTEIN; CYK3 PROTEIN; MOD5 PROTEIN; PAL1 PROTEIN; POM1 PROTEIN; PROTEIN; PROTEIN KINASE; RGA7 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; CDR2 PROTEIN, S POMBE; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; MOD5 PROTEIN, S POMBE; PAL1 PROTEIN, S POMBE; PHOSPHOPROTEIN; POM1 PROTEIN, S POMBE; PROTEIN SERINE THREONINE KINASE; PROTEOME; SCHIZOSACCHAROMYCES POMBE PROTEIN; TEA4 PROTEIN, S POMBE;

EID: 84929660023     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.045245     Document Type: Article
Times cited : (75)

References (60)
  • 1
    • 0040839027 scopus 로고    scopus 로고
    • Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis
    • Bähler, J., and Pringle, J. R. (1998) Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis. Genes Dev. 12, 1356-1370
    • (1998) Genes Dev. , vol.12 , pp. 1356-1370
    • Bähler, J.1    Pringle, J.R.2
  • 2
    • 67349103338 scopus 로고    scopus 로고
    • Polar gradients of the DYRK-family kinase Pom1 couple cell length with the cell cycle
    • Martin, S. G., and Berthelot-Grosjean, M. (2009) Polar gradients of the DYRK-family kinase Pom1 couple cell length with the cell cycle. Nature 459, 852-856
    • (2009) Nature , vol.459 , pp. 852-856
    • Martin, S.G.1    Berthelot-Grosjean, M.2
  • 3
    • 67349257405 scopus 로고    scopus 로고
    • A spatial gradient coordinates cell size and mitotic entry in fission yeast
    • Moseley, J. B., Mayeux, A., Paoletti, A., and Nurse, P. (2009) A spatial gradient coordinates cell size and mitotic entry in fission yeast. Nature 459, 857-860
    • (2009) Nature , vol.459 , pp. 857-860
    • Moseley, J.B.1    Mayeux, A.2    Paoletti, A.3    Nurse, P.4
  • 5
    • 33845467072 scopus 로고    scopus 로고
    • The cell-end factor pom1p inhibits mid1p in specification of the cell division plane in fission yeast
    • Padte, N. N., Martin, S. G., Howard, M., and Chang, F. (2006) The cell-end factor pom1p inhibits mid1p in specification of the cell division plane in fission yeast. Current Biol. 16, 2480-2487
    • (2006) Current Biol. , vol.16 , pp. 2480-2487
    • Padte, N.N.1    Martin, S.G.2    Howard, M.3    Chang, F.4
  • 6
    • 0035283205 scopus 로고    scopus 로고
    • Fission yeast Pom1p kinase activity is cell cycle regulated and essential for cellular symmetry during growth and division
    • Bahler, J., and Nurse, P. (2001) Fission yeast Pom1p kinase activity is cell cycle regulated and essential for cellular symmetry during growth and division. The EMBO J. 20, 1064-1073
    • (2001) The EMBO J. , vol.20 , pp. 1064-1073
    • Bahler, J.1    Nurse, P.2
  • 7
    • 79959647018 scopus 로고    scopus 로고
    • A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane
    • Hachet, O., Berthelot-Grosjean, M., Kokkoris, K., Vincenzetti, V., Moosbrugger, J., and Martin, S. G. (2011) A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane. Cell 145, 1116-1128
    • (2011) Cell , vol.145 , pp. 1116-1128
    • Hachet, O.1    Berthelot-Grosjean, M.2    Kokkoris, K.3    Vincenzetti, V.4    Moosbrugger, J.5    Martin, S.G.6
  • 9
    • 84894291709 scopus 로고    scopus 로고
    • Dueling kinases regulate cell size at division through the SAD kinase Cdr2
    • Deng, L., Baldissard, S., Kettenbach, A. N., Gerber, S. A., and Moseley, J. B. (2014) Dueling kinases regulate cell size at division through the SAD kinase Cdr2. Current Biol. 24, 428-433
    • (2014) Current Biol. , vol.24 , pp. 428-433
    • Deng, L.1    Baldissard, S.2    Kettenbach, A.N.3    Gerber, S.A.4    Moseley, J.B.5
  • 11
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther, T. C., and Mann, M. (2010) Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 190, 491-500
    • (2010) J. Cell Biol. , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 12
  • 14
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 15
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nature Chem. Biol. 1, 252-262
    • (2005) Nature Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 18
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., Klar, A., and Nurse, P. (1991) Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194, 795-823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 20
    • 77954695928 scopus 로고    scopus 로고
    • A genetic engineering solution to the "arginine conversion problem" in stable isotope labeling by amino acids in cell culture (SILAC)
    • Bicho, C. C., de Lima Alves, F., Chen, Z. A., Rappsilber, J., and Sawin, K. E. (2010) A genetic engineering solution to the "arginine conversion problem" in stable isotope labeling by amino acids in cell culture (SILAC). Mol. Cell. Proteomics 9, 1567-1577
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1567-1577
    • Bicho, C.C.1    De Lima Alves, F.2    Chen, Z.A.3    Rappsilber, J.4    Sawin, K.E.5
  • 22
    • 55849122284 scopus 로고    scopus 로고
    • Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis
    • Villén, J., Beausoleil, S. A., and Gygi, S. P. (2008) Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation analysis. Proteomics 8, 4444-4452
    • (2008) Proteomics , vol.8 , pp. 4444-4452
    • Villén, J.1    Beausoleil, S.A.2    Gygi, S.P.3
  • 23
    • 80054698820 scopus 로고    scopus 로고
    • Rapid and reproducible singlestage phosphopeptide enrichment of complex peptide mixtures: Application to general and phosphotyrosine-specific phosphoproteomics experiments
    • Kettenbach, A. N., and Gerber, S. A. (2011) Rapid and reproducible singlestage phosphopeptide enrichment of complex peptide mixtures: Application to general and phosphotyrosine-specific phosphoproteomics experiments. Anal. Chem. 83, 7635-7644
    • (2011) Anal. Chem. , vol.83 , pp. 7635-7644
    • Kettenbach, A.N.1    Gerber, S.A.2
  • 24
    • 33847222722 scopus 로고    scopus 로고
    • Photoinduced polymerization for entrapping of octadecylsilane microsphere columns for capillary electrochromatography
    • Xie, R., and Oleschuk, R. (2007) Photoinduced polymerization for entrapping of octadecylsilane microsphere columns for capillary electrochromatography. Anal. Chem. 79, 1529-1535
    • (2007) Anal. Chem. , vol.79 , pp. 1529-1535
    • Xie, R.1    Oleschuk, R.2
  • 25
    • 84055178474 scopus 로고    scopus 로고
    • Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks
    • Magnuson, B., Ekim, B., and Fingar, D. C. (2012) Regulation and function of ribosomal protein S6 kinase (S6K) within mTOR signalling networks. Biochem. J. 441, 1-21
    • (2012) Biochem. J. , vol.441 , pp. 1-21
    • Magnuson, B.1    Ekim, B.2    Fingar, D.C.3
  • 26
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R. (1994) An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J. Am. Soc. Mass Spectrometry 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrometry , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 27
    • 77955602609 scopus 로고    scopus 로고
    • MacroSEQUEST: Efficient candidate-centric searching and high-resolution correlation analysis for large-scale proteomics data sets
    • Faherty, B. K., and Gerber, S. A. (2010) MacroSEQUEST: efficient candidate-centric searching and high-resolution correlation analysis for large-scale proteomics data sets. Anal. Chem. 82, 6821-6829
    • (2010) Anal. Chem. , vol.82 , pp. 6821-6829
    • Faherty, B.K.1    Gerber, S.A.2
  • 28
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 30
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 19, 946-951
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 31
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., and Gygi, S. P. (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 23, 1391-1398
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 33
    • 79959558401 scopus 로고    scopus 로고
    • Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast
    • Koch, A., Krug, K., Pengelley, S., Macek, B., and Hauf, S. (2011) Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast. Sci. Signal. 4, rs6
    • (2011) Sci. Signal. , vol.4 , pp. rs6
    • Koch, A.1    Krug, K.2    Pengelley, S.3    Macek, B.4    Hauf, S.5
  • 35
    • 85081860491 scopus 로고    scopus 로고
    • Absolute proteome and phosphoproteome dynamics during the cell cycle of fission yeast
    • Carpy, A., Krug, K., Graf, S., Koch, A., Popic, S., Hauf, S., and Macek, B. (2014) Absolute proteome and phosphoproteome dynamics during the cell cycle of fission yeast. Mol. Cell. Proteomics 192-1936
    • (2014) Mol. Cell. Proteomics , pp. 192-1936
    • Carpy, A.1    Krug, K.2    Graf, S.3    Koch, A.4    Popic, S.5    Hauf, S.6    Macek, B.7
  • 37
    • 84859815885 scopus 로고    scopus 로고
    • Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets
    • O111.012351
    • Oppermann, F. S., Grundner-Culemann, K., Kumar, C., Gruss, O. J., Jallepalli, P. V., and Daub, H. (2012) Combination of chemical genetics and phosphoproteomics for kinase signaling analysis enables confident identification of cellular downstream targets. Mol. Cell. Proteomics 11(4): O111.012351. DOI: 10.1074/mcp.011.012351
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.4
    • Oppermann, F.S.1    Grundner-Culemann, K.2    Kumar, C.3    Gruss, O.J.4    Jallepalli, P.V.5    Daub, H.6
  • 38
    • 84868028972 scopus 로고    scopus 로고
    • Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells
    • Marguerat, S., Schmidt, A., Codlin, S., Chen, W., Aebersold, R., and Bähler, J. (2012) Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells. Cell 151, 671-683
    • (2012) Cell , vol.151 , pp. 671-683
    • Marguerat, S.1    Schmidt, A.2    Codlin, S.3    Chen, W.4    Aebersold, R.5    Bähler, J.6
  • 39
    • 0041885217 scopus 로고    scopus 로고
    • The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe
    • Carnahan, R. H., and Gould, K. L. (2003) The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe. J. Cell Biol. 162, 851-862
    • (2003) J. Cell Biol. , vol.162 , pp. 851-862
    • Carnahan, R.H.1    Gould, K.L.2
  • 40
    • 0029112482 scopus 로고
    • The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis
    • Fankhauser, C., Reymond, A., Cerutti, L., Utzig, S., Hofmann, K., and Simanis, V. (1995) The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis. Cell 82, 435-444
    • (1995) Cell , vol.82 , pp. 435-444
    • Fankhauser, C.1    Reymond, A.2    Cerutti, L.3    Utzig, S.4    Hofmann, K.5    Simanis, V.6
  • 41
    • 59849084607 scopus 로고    scopus 로고
    • The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring
    • Roberts-Galbraith, R. H., Chen, J. S., Wang, J., and Gould, K. L. (2009) The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring. J. Cell Biol. 184, 113-127
    • (2009) J. Cell Biol. , vol.184 , pp. 113-127
    • Roberts-Galbraith, R.H.1    Chen, J.S.2    Wang, J.3    Gould, K.L.4
  • 42
    • 33745612983 scopus 로고    scopus 로고
    • Cell cycle-dependent roles for the FCH-domain protein Cdc15p in formation of the actomyosin ring in Schizosaccharomyces pombe
    • Wachtler, V., Huang, Y., Karagiannis, J., and Balasubramanian, M. K. (2006) Cell cycle-dependent roles for the FCH-domain protein Cdc15p in formation of the actomyosin ring in Schizosaccharomyces pombe. Mol. Biol. Cell 17, 3254-3266
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3254-3266
    • Wachtler, V.1    Huang, Y.2    Karagiannis, J.3    Balasubramanian, M.K.4
  • 46
    • 0038172442 scopus 로고    scopus 로고
    • Fission yeast Mod5p regulates polarized growth through anchoring of Tea1p at cell tips
    • Snaith, H. A., and Sawin, K. E. (2003) Fission yeast Mod5p regulates polarized growth through anchoring of Tea1p at cell tips. Nature 423, 647-651
    • (2003) Nature , vol.423 , pp. 647-651
    • Snaith, H.A.1    Sawin, K.E.2
  • 47
    • 27744511577 scopus 로고    scopus 로고
    • Multistep and multimode cortical anchoring of tea1p at cell tips in fission yeast
    • Snaith, H. A., Samejima, I., and Sawin, K. E. (2005) Multistep and multimode cortical anchoring of tea1p at cell tips in fission yeast. The EMBO J. 24, 3690-3699
    • (2005) The EMBO J. , vol.24 , pp. 3690-3699
    • Snaith, H.A.1    Samejima, I.2    Sawin, K.E.3
  • 48
    • 16244409515 scopus 로고    scopus 로고
    • Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity
    • Martin, S. G., McDonald, W. H., Yates, J. R., 3rd, and Chang, F. (2005) Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity. Develop. Cell 8, 479-491
    • (2005) Develop. Cell , vol.8 , pp. 479-491
    • Martin, S.G.1    McDonald, W.H.2    Yates, J.R.3    Chang, F.4
  • 49
    • 20144362096 scopus 로고    scopus 로고
    • Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of Tea1 and protects cell polarity under environmental stress in S. pombe
    • Tatebe, H., Shimada, K., Uzawa, S., Morigasaki, S., and Shiozaki, K. (2005) Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of Tea1 and protects cell polarity under environmental stress in S. pombe. Current Biol. 15, 1006-1015
    • (2005) Current Biol. , vol.15 , pp. 1006-1015
    • Tatebe, H.1    Shimada, K.2    Uzawa, S.3    Morigasaki, S.4    Shiozaki, K.5
  • 50
    • 24344499517 scopus 로고    scopus 로고
    • The novel fission yeast protein Pal1p interacts with Hip1-related Sla2p/End4p and is involved in cellular morphogenesis
    • Ge, W., Chew, T. G., Wachtler, V., Naqvi, S. N., and Balasubramanian, M. K. (2005) The novel fission yeast protein Pal1p interacts with Hip1-related Sla2p/End4p and is involved in cellular morphogenesis. Mol. Biol. Cell 16, 4124-4138
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4124-4138
    • Ge, W.1    Chew, T.G.2    Wachtler, V.3    Naqvi, S.N.4    Balasubramanian, M.K.5
  • 51
    • 77951219431 scopus 로고    scopus 로고
    • Rga4 modulates the activity of the fission yeast cell integrity MAPK pathway by acting as a Rho2 GTPase-activating protein
    • Soto, T., Villar-Tajadura, M. A., Madrid, M., Vicente, J., Gacto, M., Pérez, P., and Cansado, J. (2010) Rga4 modulates the activity of the fission yeast cell integrity MAPK pathway by acting as a Rho2 GTPase-activating protein. J. Biolog. Chem. 285, 11516-11525
    • (2010) J. Biolog. Chem. , vol.285 , pp. 11516-11525
    • Soto, T.1    Villar-Tajadura, M.A.2    Madrid, M.3    Vicente, J.4    Gacto, M.5    Pérez, P.6    Cansado, J.7
  • 53
    • 84913616885 scopus 로고    scopus 로고
    • F-BAR domain protein Rga7 collaborates with Cdc15 and Imp2 to ensure proper cytokinesis in fission yeast
    • Martin-Garcia, R., Coll, P. M., and Perez, P. (2014) F-BAR domain protein Rga7 collaborates with Cdc15 and Imp2 to ensure proper cytokinesis in fission yeast. J. Cell Sci. 4146-4158
    • (2014) J. Cell Sci. , pp. 4146-4158
    • Martin-Garcia, R.1    Coll, P.M.2    Perez, P.3
  • 54
    • 64549151622 scopus 로고    scopus 로고
    • Fission yeast syt22 protein, a putative Arf guanine nucleotide exchange factor, is necessary for new end take off
    • Fujita, A., and Misumi, Y. (2009) Fission yeast syt22 protein, a putative Arf guanine nucleotide exchange factor, is necessary for new end take off. FEMS Microbiol. Lett. 294, 191-197
    • (2009) FEMS Microbiol. Lett. , vol.294 , pp. 191-197
    • Fujita, A.1    Misumi, Y.2
  • 55
    • 84863509406 scopus 로고    scopus 로고
    • Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis
    • Pollard, L. W., Onishi, M., Pringle, J. R., and Lord, M. (2012) Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis. Mol. Biol. Cell 23, 2433-2444
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2433-2444
    • Pollard, L.W.1    Onishi, M.2    Pringle, J.R.3    Lord, M.4
  • 56
    • 0032547838 scopus 로고    scopus 로고
    • Imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe
    • Demeter, J., and Sazer, S. (1998) imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe. J. Cell Biol. 143, 415-427
    • (1998) J. Cell Biol. , vol.143 , pp. 415-427
    • Demeter, J.1    Sazer, S.2
  • 57
    • 80052820010 scopus 로고    scopus 로고
    • Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast
    • Arasada, R., and Pollard, T. D. (2011) Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast. Current Biol. 21, 1450-1459
    • (2011) Current Biol. , vol.21 , pp. 1450-1459
    • Arasada, R.1    Pollard, T.D.2
  • 58
    • 0035462362 scopus 로고    scopus 로고
    • A journey into space
    • Hayles, J., and Nurse, P. (2001) A journey into space. Mol. Cell Biol. 2, 647-656
    • (2001) Mol. Cell Biol. , vol.2 , pp. 647-656
    • Hayles, J.1    Nurse, P.2
  • 60
    • 77957828789 scopus 로고    scopus 로고
    • A catalytic role for Mod5 in the formation of the Tea1 cell polarity landmark
    • Bicho, C. C., Kelly, D. A., Snaith, H. A., Goryachev, A. B., and Sawin, K. E. (2010) A catalytic role for Mod5 in the formation of the Tea1 cell polarity landmark. Current Biol. 20, 1752-1757
    • (2010) Current Biol. , vol.20 , pp. 1752-1757
    • Bicho, C.C.1    Kelly, D.A.2    Snaith, H.A.3    Goryachev, A.B.4    Sawin, K.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.