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Volumn 409, Issue 3, 2011, Pages 399-414

Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins

Author keywords

ATPase cycle; fluorescence correlation spectroscopy; kinetics; RNA helicase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DEAD BOX PROTEIN; OXYGEN 18; PHOSPHATE; PROTEIN MSS116; UNCLASSIFIED DRUG;

EID: 79956103194     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.04.004     Document Type: Article
Times cited : (58)

References (54)
  • 1
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • DOI 10.1016/j.gene.2005.10.019, PII S0378111905006359
    • Cordin O., Banroques J., Tanner N.K., and Linder P. The DEAD-box protein family of RNA helicases Gene 367 2006 17 37 (Pubitemid 43286737)
    • (2006) Gene , vol.367 , Issue.1-2 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 2
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle A.M. Translocation and unwinding mechanisms of RNA and DNA helicases Annu. Rev. Biophys. 37 2008 317 336
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 3
    • 39649096274 scopus 로고    scopus 로고
    • The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
    • Henn A., Cao W., Hackney D.D., and De La Cruz E.M. The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA J. Mol. Biol. 377 2008 193 205
    • (2008) J. Mol. Biol. , vol.377 , pp. 193-205
    • Henn, A.1    Cao, W.2    Hackney, D.D.3    De La Cruz, E.M.4
  • 5
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F., Putnam A., and Jankowsky E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding Proc. Natl Acad. Sci. USA 105 2008 20209 20214
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 7
    • 0033010430 scopus 로고    scopus 로고
    • An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p
    • DOI 10.1016/S1097-2765(00)80174-4
    • Staley J.P., and Guthrie C. An RNA switch at the 5′ splice site requires ATP and the DEAD box protein Prp28p Mol. Cell 3 1999 55 64 (Pubitemid 29292477)
    • (1999) Molecular Cell , vol.3 , Issue.1 , pp. 55-64
    • Staley, J.P.1    Guthrie, C.2
  • 8
    • 0026418629 scopus 로고
    • RNA splicing. Alive with DEAD proteins
    • Wassarman D.A., and Steitz J.A. RNA splicing. Alive with DEAD proteins Nature 349 1991 463 464
    • (1991) Nature , vol.349 , pp. 463-464
    • Wassarman, D.A.1    Steitz, J.A.2
  • 9
    • 0025978633 scopus 로고
    • p68 RNA helicase: Identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts
    • Iggo R.D., Jamieson D.J., MacNeill S.A., Southgate J., McPheat J., and Lane D.P. p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts Mol. Cell. Biol. 11 1991 1326 1333 (Pubitemid 21895488)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.3 , pp. 1326-1333
    • Iggo, R.D.1    Jamieson, D.J.2    MacNeill, S.A.3    Southgate, J.4    McPheat, J.5    Lane, D.P.6
  • 10
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid S.R., and Linder P. D-E-A-D protein family of putative RNA helicases Mol. Microbiol. 6 1992 283 291
    • (1992) Mol. Microbiol. , vol.6 , pp. 283-291
    • Schmid, S.R.1    Linder, P.2
  • 13
    • 1542344429 scopus 로고    scopus 로고
    • Dead-box proteins: The driving forces behind RNA metabolism
    • DOI 10.1038/nrm1335
    • Rocak S., and Linder P. DEAD-box proteins: the driving forces behind RNA metabolism Nat. Rev. Mol. Cell Biol. 5 2004 232 241 (Pubitemid 38325804)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 15
    • 33847652952 scopus 로고    scopus 로고
    • A DEAD protein that activates intron self-splicing without unwinding RNA
    • DOI 10.1016/j.molcel.2006.10.032
    • Solem A., Zingler N., and Pyle A.M. A DEAD protein that activates intron self-splicing without unwinding RNA Mol. Cell 24 2006 611 617 (Pubitemid 350284227)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.3
  • 16
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box Proteins in Group I and Group II Intron Splicing. Biochemical Characterization of Mss116p, ATP Hydrolysis-dependent and -independent Mechanisms, and General RNA Chaperone Activity
    • DOI 10.1016/j.jmb.2006.09.083, PII S0022283606013076
    • Halls C., Mohr S., Del Campo M., Yang Q., Jankowsky E., and Lambowitz A.M. Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity J. Mol. Biol. 365 2007 835 855 (Pubitemid 46001664)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 835-855
    • Halls, C.1    Mohr, S.2    Del Campo, M.3    Yang, Q.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 17
    • 0024961642 scopus 로고
    • Mitochondrial splicing requires a protein from a novel helicase family
    • Seraphin B., Simon M., Boulet A., and Faye G. Mitochondrial splicing requires a protein from a novel helicase family Nature 337 1989 84 87
    • (1989) Nature , vol.337 , pp. 84-87
    • Seraphin, B.1    Simon, M.2    Boulet, A.3    Faye, G.4
  • 18
    • 77951625452 scopus 로고    scopus 로고
    • Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing
    • Bifano A.L., Turk E.M., and Caprara M.G. Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing J. Mol. Biol. 398 2010 429 443
    • (2010) J. Mol. Biol. , vol.398 , pp. 429-443
    • Bifano, A.L.1    Turk, E.M.2    Caprara, M.G.3
  • 19
    • 0029151794 scopus 로고
    • Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing of a yeast group II intron in vitro
    • Niemer I., Schmelzer C., and Borner G.V. Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing of a yeast group II intron in vitro Nucleic Acids Res. 23 1995 2966 2972
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2966-2972
    • Niemer, I.1    Schmelzer, C.2    Borner, G.V.3
  • 20
    • 67349117103 scopus 로고    scopus 로고
    • Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones
    • Del Campo M., Mohr S., Jiang Y., Jia H., Jankowsky E., and Lambowitz A.M. Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones J. Mol. Biol. 389 2009 674 693
    • (2009) J. Mol. Biol. , vol.389 , pp. 674-693
    • Del Campo, M.1    Mohr, S.2    Jiang, Y.3    Jia, H.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 22
    • 78049293801 scopus 로고    scopus 로고
    • Dual roles for the Mss116 cofactor during splicing of the ai5gamma group II intron
    • Zingler N., Solem A., and Pyle A.M. Dual roles for the Mss116 cofactor during splicing of the ai5gamma group II intron Nucleic Acids Res. 38 2010 6602 6609
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6602-6609
    • Zingler, N.1    Solem, A.2    Pyle, A.M.3
  • 23
    • 78049234242 scopus 로고    scopus 로고
    • Single-molecule analysis of Mss116-mediated group II intron folding
    • Karunatilaka K.S., Solem A., Pyle A.M., and Rueda D. Single-molecule analysis of Mss116-mediated group II intron folding Nature 467 2010 935 939
    • (2010) Nature , vol.467 , pp. 935-939
    • Karunatilaka, K.S.1    Solem, A.2    Pyle, A.M.3    Rueda, D.4
  • 24
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • Mohr G., Del Campo M., Mohr S., Yang Q., Jia H., Jankowsky E., and Lambowitz A.M. Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro J. Mol. Biol. 375 2008 1344 1364
    • (2008) J. Mol. Biol. , vol.375 , pp. 1344-1364
    • Mohr, G.1    Del Campo, M.2    Mohr, S.3    Yang, Q.4    Jia, H.5    Jankowsky, E.6    Lambowitz, A.M.7
  • 25
    • 20544475925 scopus 로고    scopus 로고
    • Magnesium, ADP, and actin binding linkage of myosin V: Evidence for multiple myosin V-ADP and actomyosin V-ADP states
    • DOI 10.1021/bi0473509
    • Hannemann D.E., Cao W., Olivares A.O., Robblee J.P., and De La Cruz E.M. Magnesium, ADP, and actin binding linkage of myosin V: evidence for multiple myosin V-ADP and actomyosin V-ADP states Biochemistry 44 2005 8826 8840 (Pubitemid 40840448)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8826-8840
    • Hannemann, D.E.1    Cao, W.2    Olivares, A.O.3    Robblee, J.P.4    De La Cruz, E.M.5
  • 26
    • 20544449370 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to actomyosin V and VI: A positive heat capacity change accompanies strong ADP binding
    • DOI 10.1021/bi050232g
    • Robblee J.P., Cao W., Henn A., Hannemann D.E., and De La Cruz E.M. Thermodynamics of nucleotide binding to actomyosin V and VI: a positive heat capacity change accompanies strong ADP binding Biochemistry 44 2005 10238 10249 (Pubitemid 41076819)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10238-10249
    • Robblee, J.P.1    Cao, W.2    Henn, A.3    Hannemann, D.E.4    De La Cruz, E.M.5
  • 27
    • 61849174756 scopus 로고    scopus 로고
    • Kinetic and equilibrium analysis of the myosin ATPase
    • De La Cruz E.M., and Ostap E.M. Kinetic and equilibrium analysis of the myosin ATPase Methods Enzymol. 455 2009 157 192
    • (2009) Methods Enzymol. , vol.455 , pp. 157-192
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 28
    • 0028566711 scopus 로고
    • Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer: 1. Use of fluorescent nucleotide analogues
    • Moore K.J., and Lohman T.M. Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer: 1. Use of fluorescent nucleotide analogues Biochemistry 33 1994 14550 14564
    • (1994) Biochemistry , vol.33 , pp. 14550-14564
    • Moore, K.J.1    Lohman, T.M.2
  • 29
    • 12344279980 scopus 로고    scopus 로고
    • Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA
    • DOI 10.1021/bi048253i
    • Talavera M.A., and De La Cruz E.M. Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA Biochemistry 44 2005 959 970 (Pubitemid 40129656)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 959-970
    • Talavera, M.A.1    De La Cruz, E.M.2
  • 30
    • 65549101787 scopus 로고    scopus 로고
    • Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange factor
    • Chin H.F., Cai Y., Menon S., Ferro-Novick S., Reinisch K.M., and De La Cruz E.M. Kinetic analysis of the guanine nucleotide exchange activity of TRAPP, a multimeric Ypt1p exchange factor J. Mol. Biol. 389 2009 275 288
    • (2009) J. Mol. Biol. , vol.389 , pp. 275-288
    • Chin, H.F.1    Cai, Y.2    Menon, S.3    Ferro-Novick, S.4    Reinisch, K.M.5    De La Cruz, E.M.6
  • 31
    • 29444437883 scopus 로고    scopus 로고
    • The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP
    • DOI 10.1073/pnas.0505288102
    • Hackney D.D. The tethered motor domain of a kinesin-microtubule complex catalyzes reversible synthesis of bound ATP Proc. Natl Acad. Sci. USA 102 2005 18338 18343 (Pubitemid 43011227)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.51 , pp. 18338-18343
    • Hackney, D.D.1
  • 32
    • 0018817999 scopus 로고
    • Oxygen-18 probes of enzymic reactions of phosphate compounds
    • Hackney D.D., Stempel K.E., and Boyer P.D. Oxygen-18 probes of enzymic reactions of phosphate compounds Methods Enzymol. 64 1980 60 83
    • (1980) Methods Enzymol. , vol.64 , pp. 60-83
    • Hackney, D.D.1    Stempel, K.E.2    Boyer, P.D.3
  • 33
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • DOI 10.1529/biophysj.105.079251
    • Rhoades E., Ramlall T.F., Webb W.W., and Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy Biophys. J. 90 2006 4692 4700 (Pubitemid 43830913)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 34
    • 0001579306 scopus 로고
    • Fluorescence correlation spectroscopy
    • Thompson N.L. Fluorescence correlation spectroscopy J.R. Lakowicz, Topics in Fluorescence Microscopy 1991 Plenum Press New York, NY 337 378
    • (1991) Topics in Fluorescence Microscopy , pp. 337-378
    • Thompson, N.L.1
  • 35
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • Rigler R., Mets Ü., Widengren J., and Kask P. Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion Eur. Biophys. J. 22 1993 169 175 (Pubitemid 23279495)
    • (1993) European Biophysics Journal , vol.22 , Issue.3 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, J.3    Kask, P.4
  • 37
    • 70449584733 scopus 로고    scopus 로고
    • The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis
    • Aregger R., and Klostermeier D. The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis Biochemistry 48 2009 10679 10681
    • (2009) Biochemistry , vol.48 , pp. 10679-10681
    • Aregger, R.1    Klostermeier, D.2
  • 39
    • 78751584740 scopus 로고    scopus 로고
    • Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV
    • Appleby T.C., Anderson R., Fedorova O., Pyle A.M., Wang R., and Liu X. Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV J. Mol. Biol. 405 2011 1139 1153
    • (2011) J. Mol. Biol. , vol.405 , pp. 1139-1153
    • Appleby, T.C.1    Anderson, R.2    Fedorova, O.3    Pyle, A.M.4    Wang, R.5    Liu, X.6
  • 40
    • 79956071179 scopus 로고    scopus 로고
    • DEAD-box proteins as RNA helicases and chaperones
    • Jarmoskaite I., and Russell R. DEAD-box proteins as RNA helicases and chaperones WIREs RNA 2 2011 135 152
    • (2011) WIREs RNA , vol.2 , pp. 135-152
    • Jarmoskaite, I.1    Russell, R.2
  • 41
    • 77649337588 scopus 로고    scopus 로고
    • Protein-facilitated folding of group II intron ribozymes
    • Fedorova O., Solem A., and Pyle A.M. Protein-facilitated folding of group II intron ribozymes J. Mol. Biol. 397 2010 799 813
    • (2010) J. Mol. Biol. , vol.397 , pp. 799-813
    • Fedorova, O.1    Solem, A.2    Pyle, A.M.3
  • 42
    • 52949136970 scopus 로고    scopus 로고
    • A DExH/D-box protein coordinates the two steps of splicing in a group i intron
    • Bifano A.L., and Caprara M.G. A DExH/D-box protein coordinates the two steps of splicing in a group I intron J. Mol. Biol. 383 2008 667 682
    • (2008) J. Mol. Biol. , vol.383 , pp. 667-682
    • Bifano, A.L.1    Caprara, M.G.2
  • 43
    • 78751676793 scopus 로고    scopus 로고
    • Roles of DEAD-box proteins in RNA and RNP folding
    • Pan C., and Russell R. Roles of DEAD-box proteins in RNA and RNP folding RNA Biol. 7 2010 28 37
    • (2010) RNA Biol. , vol.7 , pp. 28-37
    • Pan, C.1    Russell, R.2
  • 44
    • 0032562221 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes
    • DOI 10.1021/bi9724319
    • Lorsch J.R., and Herschlag D. The DEAD box protein eIF4A: 2. A cycle of nucleotide and RNA-dependent conformational changes Biochemistry 37 1998 2194 2206 (Pubitemid 28119292)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 45
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • DOI 10.1021/bi972430g
    • Lorsch J.R., and Herschlag D. The DEAD box protein eIF4A: 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide Biochemistry 37 1998 2180 2193 (Pubitemid 28119291)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 46
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • DOI 10.1021/bi012062n
    • Polach K.J., and Uhlenbeck O.C. Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA Biochemistry 41 2002 3693 3702 (Pubitemid 34224682)
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2
  • 47
    • 71049181356 scopus 로고    scopus 로고
    • A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit
    • Sharpe Elles L.M., Sykes M.T., Williamson J.R., and Uhlenbeck O.C. A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit Nucleic Acids Res. 37 2009 6503 6514
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6503-6514
    • Sharpe Elles, L.M.1    Sykes, M.T.2    Williamson, J.R.3    Uhlenbeck, O.C.4
  • 48
    • 0027301893 scopus 로고
    • DbpA: A DEAD box protein specifically activated by 23S rRNA
    • Fuller-Pace F.V., Nicol S.M., Reid A.D., and Lane D.P. DbpA: a DEAD box protein specifically activated by 23S rRNA EMBO J. 12 1993 3619 3626 (Pubitemid 23256448)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3619-3626
    • Fuller-Space, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 49
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C., Barber J.D., and Barton G.J. The Jpred 3 secondary structure prediction server Nucleic Acids Res. 36 2008 W197 W201
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 50
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the yeast DEAD box protein Mss116p reveals two wedges that crimp RNA
    • Del Campo M., and Lambowitz A.M. Structure of the yeast DEAD box protein Mss116p reveals two wedges that crimp RNA Mol. Cell 35 2009 598 609
    • (2009) Mol. Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 51
    • 0033850082 scopus 로고    scopus 로고
    • ADP inhibition of myosin v ATPase activity
    • De La Cruz E.M., Sweeney H.L., and Ostap E.M. ADP inhibition of myosin V ATPase activity Biophys. J. 79 2000 1524 1529
    • (2000) Biophys. J. , vol.79 , pp. 1524-1529
    • De La Cruz, E.M.1    Sweeney, H.L.2    Ostap, E.M.3
  • 52
    • 28244468416 scopus 로고    scopus 로고
    • Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension
    • DOI 10.1074/jbc.M507667200
    • Henn A., and De La Cruz E.M. Vertebrate myosin VIIb is a high duty ratio motor adapted for generating and maintaining tension J. Biol. Chem. 280 2005 39665 39676 (Pubitemid 41713926)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39665-39676
    • Henn, A.1    De La Cruz, E.M.2
  • 54
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • Elbaum-Garfinkle S., Ramlall T., and Rhoades E. The role of the lipid bilayer in tau aggregation Biophys. J. 98 2010 2722 2730
    • (2010) Biophys. J. , vol.98 , pp. 2722-2730
    • Elbaum-Garfinkle, S.1    Ramlall, T.2    Rhoades, E.3


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