메뉴 건너뛰기




Volumn 415, Issue 1, 2012, Pages 205-220

The evolution of cefotaximase activity in the TEM β-lactamase

Author keywords

catalytic activity; enzymatic evolution; MM GBSA; molecular dynamics; TEM lactamase

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; BETA LACTAMASE; BETA LACTAMASE TEM 1; CEFOTAXIME; LYSINE; MUTANT PROTEIN; SERINE;

EID: 84855254361     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.041     Document Type: Article
Times cited : (16)

References (61)
  • 2
    • 0035823272 scopus 로고    scopus 로고
    • Humans as the world's greatest evolutionary force
    • Palumbi, S. R. (2001). Humans as the world's greatest evolutionary force. Science, 293, 1786-1790.
    • (2001) Science , vol.293 , pp. 1786-1790
    • Palumbi, S.R.1
  • 3
    • 0034123845 scopus 로고    scopus 로고
    • Resisting resistance: New chemical strategies for battling superbugs
    • Wright, G. D. (2000). Resisting resistance: new chemical strategies for battling superbugs. Chem. Biol. 7, R127-R132.
    • (2000) Chem. Biol. , vol.7
    • Wright, G.D.1
  • 4
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to beta-lactam antibiotics: Compelling opportunism, compelling opportunity
    • DOI 10.1021/cr030102i
    • Fisher, J. F., Meroueh, S. O. & Mobashery, S. (2005). Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity. Chem. Rev. 105, 395-424. (Pubitemid 40351628)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 6
    • 0030292866 scopus 로고    scopus 로고
    • Molecular evolution of bacterial beta-lactam resistance
    • Knox, J. R., Moews, P. C. & Frere, J. M. (1996). Molecular evolution of bacterial [beta]-lactam resistance. Chem. Biol. 3, 937-947. (Pubitemid 27017092)
    • (1996) Chemistry and Biology , vol.3 , Issue.11 , pp. 937-947
    • Knox, J.R.1    Moews, P.C.2    Frere, J.-M.3
  • 7
    • 9144241152 scopus 로고    scopus 로고
    • Plasticity of class A beta-lactamases, an illustration with TEM and SHV enzymes
    • Labia, R. (2004). Plasticity of class A beta-lactamases, an illustration with TEM and SHV enzymes. Curr. Med. Chem. - Anti-Infect. Agents, 3, 251-266.
    • (2004) Curr. Med. Chem. - Anti-Infect. Agents , vol.3 , pp. 251-266
    • Labia, R.1
  • 8
    • 2942562249 scopus 로고    scopus 로고
    • Evolution of the serine beta-lactamases: Past, present and future
    • DOI 10.1016/j.drup.2004.02.003
    • Hall, B. G. & Barlow, M. (2004). Evolution of the serine beta-lactamases: past, present and future. Drug Resist. Updat. 7, 111-123. (Pubitemid 38736064)
    • (2004) Drug Resistance Updates , vol.7 , Issue.2 , pp. 111-123
    • Hall, B.G.1    Barlow, M.2
  • 9
    • 0029071785 scopus 로고
    • A functional classification scheme for beta-lactamases and its correlation with molecular structure
    • Bush, K., Jacoby, G. A. & Medeiros, A. A. (1995). A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39, 1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 12
    • 16244412269 scopus 로고    scopus 로고
    • Mechanisms of antibiotic resistance: QM/MM modeling of the acylation reaction of a class A beta-lactamase with benzylpenicillin
    • DOI 10.1021/ja044210d
    • Hermann, J. C., Hensen, C., Ridder, L., Mulholland, A. J. & Holtje, H. D. (2005). Mechanisms of antibiotic resistance: QM/MM modeling of the acylation reaction of a class A beta-lactamase with benzylpenicillin. J. Am. Chem. Soc. 127, 4454-4465. (Pubitemid 40463071)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.12 , pp. 4454-4465
    • Hermann, J.C.1    Hensen, C.2    Ridder, L.3    Mulholland, A.J.4    Holtje, H.-D.5
  • 13
    • 0025022490 scopus 로고
    • Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis
    • Oefner, C., D'Arcy, A., Daly, J. J., Gubernator, K., Charnas, R. L., Heinze, I. et al. (1990). Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. Nature, 343, 284-288.
    • (1990) Nature , vol.343 , pp. 284-288
    • Oefner, C.1    D'Arcy, A.2    Daly, J.J.3    Gubernator, K.4    Charnas, R.L.5    Heinze, I.6
  • 14
    • 0025270942 scopus 로고
    • Beta-Lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism
    • Christensen, H., Martin, M. T. & Waley, S. G. (1990). Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism. Biochem. J. 266, 853-861. (Pubitemid 20103722)
    • (1990) Biochemical Journal , vol.266 , Issue.3 , pp. 853-861
    • Christensen, H.1    Martin, M.T.2    Waley, S.G.3
  • 15
    • 0036721168 scopus 로고    scopus 로고
    • Predicting evolution by in vitro evolution requires determining evolutionary pathways
    • Hall, B. G. (2002). Predicting evolution by in vitro evolution requires determining evolutionary pathways. Antimicrob. Agents Chemother. 46, 3035-3038.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3035-3038
    • Hall, B.G.1
  • 16
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. C. (1994). Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 18
    • 0023794026 scopus 로고
    • A new revision of the sequence of plasmid pBR322
    • Watson, N. (1988). A new revision of the sequence of plasmid pBR322. Gene, 70, 399-403.
    • (1988) Gene , vol.70 , pp. 399-403
    • Watson, N.1
  • 19
    • 0035957080 scopus 로고    scopus 로고
    • Structures of the acyl-enzyme complexes of the Staphylococcus aureus beta-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine
    • DOI 10.1021/bi002277h
    • Chen, C. C. & Herzberg, O. (2001). Structures of the acylenzyme complexes of the Staphylococcus aureus beta-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine. Biochemistry, 40, 2351-2358. (Pubitemid 32171707)
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2351-2358
    • Chen, C.C.H.1    Herzberg, O.2
  • 20
    • 0034539018 scopus 로고    scopus 로고
    • Population structure and evolutionary dynamics of pathogenic bacteria
    • DOI 10.1002/1521-1878(200012)22:12<1115::AID-BIES9>3.0.CO;2-R
    • Smith, J. M., Feil, E. J. & Smith, N. H. (2000). Population structure and evolutionary dynamics of pathogenic bacteria. BioEssays, 22, 1115-1122. (Pubitemid 32010521)
    • (2000) BioEssays , vol.22 , Issue.12 , pp. 1115-1122
    • Smith, J.M.1    Feil, E.J.2    Smith, N.H.3
  • 21
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich, D. M., Delaney, N. F., DePristo, M. A. & Hartl, D. L. (2006). Darwinian evolution can follow only very few mutational paths to fitter proteins. Science, 312, 111-114.
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    DePristo, M.A.3    Hartl, D.L.4
  • 22
    • 33846551980 scopus 로고    scopus 로고
    • Empirical fitness landscapes reveal accessible evolutionary paths
    • DOI 10.1038/nature05451, PII NATURE05451
    • Poelwijk, F. J., Kiviet, D. J., Weinreich, D. M. & Tans, S. J. (2007). Empirical fitness landscapes reveal accessible evolutionary paths. Nature, 445, 383-386. (Pubitemid 46160901)
    • (2007) Nature , vol.445 , Issue.7126 , pp. 383-386
    • Poelwijk, F.J.1    Kiviet, D.J.2    Weinreich, D.M.3    Tans, S.J.4
  • 23
    • 0021136644 scopus 로고
    • m ratio of enzymatic modification of aminoglycosides by kanamycin acetyltransferase
    • m ratio of enzymatic modification of aminoglycosides by kanamycin acetyltransferase. Antimicrob. Agents Chemother. 25, 479-482.
    • (1984) Antimicrob. Agents Chemother. , vol.25 , pp. 479-482
    • Radika, K.1    Northrop, D.B.2
  • 24
    • 0032500512 scopus 로고    scopus 로고
    • The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics
    • Cantu, C., 3rd & Palzkill, T. (1998). The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics. J. Biol. Chem. 273, 26603-26609.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26603-26609
    • Cantu III, C.1    Palzkill, T.2
  • 25
    • 0027408874 scopus 로고
    • Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling
    • Huletsky, A., Knox, J. R. & Levesque, R. C. (1993). Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling. J. Biol. Chem. 268, 3690-3697. (Pubitemid 23071015)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.5 , pp. 3690-3697
    • Huletsky, A.1    Knox, J.R.2    Levesque, R.C.3
  • 26
    • 0029090979 scopus 로고
    • Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by beta-lactamase TEM-1 and the G238S mutant
    • Saves, I., Burlet-Schiltz, O., Maveyraud, L., Samama, J. P., Prome, J. C. & Masson, J. M. (1995). Mass spectral kinetic study of acylation and deacylation during the hydrolysis of penicillins and cefotaxime by beta-lactamase TEM-1 and the G238S mutant. Biochemistry, 34, 11660-11667.
    • (1995) Biochemistry , vol.34 , pp. 11660-11667
    • Saves, I.1    Burlet-Schiltz, O.2    Maveyraud, L.3    Samama, J.P.4    Prome, J.C.5    Masson, J.M.6
  • 27
    • 0037460169 scopus 로고    scopus 로고
    • Insights into the acylation mechanism of class A beta-lactamases from molecular dynamics simulations of the TEM-1 enzyme complexed with benzylpenicillin
    • DOI 10.1021/ja027704o
    • Diaz, N., Sordo, T. L., Merz, K. M. & Suarez, D. (2003). Insights into the acylation mechanism of class A beta-lactamases from molecular dynamics simulations of the TEM-1 enzyme complexed with benzylpenicillin. J. Am. Chem. Soc. 125, 672-684. (Pubitemid 36109929)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.3 , pp. 672-684
    • Diaz, N.1    Sordo, T.L.2    Merz Jr., K.M.3    Suarez, D.4
  • 28
    • 13444302257 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the TEM-1 beta-lactamase complexed with cephalothin
    • DOI 10.1021/jm0493663
    • Diaz, N., Suarez, D., Merz, K. M. & Sordo, T. L. (2005). Molecular dynamics simulations of the TEM-1 beta-lactamase complexed with cephalothin. J. Med. Chem. 48, 780-791. (Pubitemid 40209100)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.3 , pp. 780-791
    • Diaz, N.1    Suarez, D.2    Merz Jr., K.M.3    Sordo, T.L.4
  • 31
    • 0000916046 scopus 로고
    • Theoretical calculations of [beta]-lactam antibiotics: Part 2. AM1, MNDO and MINDO/3 calculations of some cephalosporins
    • Fraua, J., Donoso, J., Muñoz, F. & Blanco, F. G. (1991). Theoretical calculations of [beta]-lactam antibiotics: Part 2. AM1, MNDO and MINDO/3 calculations of some cephalosporins. J. Mol. Struct.: THEOCHEM. 251, 205-218.
    • (1991) J. Mol. Struct.: THEOCHEM. , vol.251 , pp. 205-218
    • Fraua, J.1    Donoso, J.2    Muñoz, F.3    Blanco, F.G.4
  • 32
    • 37349021516 scopus 로고    scopus 로고
    • Evolution of extended-spectrum beta-lactamases by mutation
    • Gniadkowski, M. (2008). Evolution of extended-spectrum beta-lactamases by mutation. Clin. Microbiol. Infect. 14, 11-32.
    • (2008) Clin. Microbiol. Infect. , vol.14 , pp. 11-32
    • Gniadkowski, M.1
  • 33
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O. & Tawfik, D. (2010). Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.2
  • 34
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki, N. & Tawfik, D. S. (2009). Protein dynamism and evolvability. Science, 324, 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 35
    • 24344494387 scopus 로고    scopus 로고
    • 8-barrels: In vitro enhancement of a "new" reaction in the enolase superfamily
    • DOI 10.1021/bi050963g
    • Vick, J. E., Schmidt, D. M. & Gerlt, J. A. (2005). Evolutionary potential of (beta/alpha)8-barrels: in vitro enhancement of a "new" reaction in the enolase superfamily. Biochemistry, 44, 11722-11729. (Pubitemid 41262706)
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11722-11729
    • Vick, J.E.1    Schmidt, D.M.Z.2    Gerlt, J.A.3
  • 36
    • 51649110669 scopus 로고    scopus 로고
    • A compromise required by gene sharing enables survival: Implications for evolution of new enzyme activities
    • McLoughlin, S. Y. & Copley, S. D. (2008). A compromise required by gene sharing enables survival: implications for evolution of new enzyme activities. Proc. Natl Acad. Sci. USA, 105, 13497-13502.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13497-13502
    • McLoughlin, S.Y.1    Copley, S.D.2
  • 37
    • 52049112316 scopus 로고    scopus 로고
    • Increased folding stability of TEM-1 beta-lactamase by in vitro selection
    • Kather, I., Jakob, R. P., Dobbek, H. & Schmid, F. X. (2008). Increased folding stability of TEM-1 beta-lactamase by in vitro selection. J. Mol. Biol. 383, 238-251.
    • (2008) J. Mol. Biol. , vol.383 , pp. 238-251
    • Kather, I.1    Jakob, R.P.2    Dobbek, H.3    Schmid, F.X.4
  • 38
    • 77952783129 scopus 로고    scopus 로고
    • Thermodynamic database for proteins: Features and applications
    • Gromiha, M. M. & Sarai, A. (2010). Thermodynamic database for proteins: features and applications. Methods Mol. Biol. 609, 97-112.
    • (2010) Methods Mol. Biol. , vol.609 , pp. 97-112
    • Gromiha, M.M.1    Sarai, A.2
  • 40
  • 42
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • DOI 10.1016/j.jmgm.2005.12.005, PII S1093326305001737
    • Wang, J., Wang, W., Kollman., P. A. & Case, D. A. (2006). Automatic atom type and bond type perception in molecular mechanical calculations. J. Mol. Graphics Modell. 25, 247-260. (Pubitemid 44363172)
    • (2006) Journal of Molecular Graphics and Modelling , vol.25 , Issue.2 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 43
    • 77954566051 scopus 로고    scopus 로고
    • The R.E.D. tools: Advances in RESP and ESP charge derivation and force field library building
    • Dupradeau, F. Y., Pigache, A., Zaffran, T., Savineau, C., Lelong, R., Grivel, N. et al. (2010). The R.E.D. tools: advances in RESP and ESP charge derivation and force field library building. Phys. Chem. Chem. Phys. 12, 7821-7839.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 7821-7839
    • Dupradeau, F.Y.1    Pigache, A.2    Zaffran, T.3    Savineau, C.4    Lelong, R.5    Grivel, N.6
  • 45
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C., Cieplak, P., Cornell, W. & Kollman, P. (1993). A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. J. Phys. Chem. 97, 10269-10280.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.1    Cieplak, P.2    Cornell, W.3    Kollman, P.4
  • 46
    • 34548426131 scopus 로고    scopus 로고
    • Modeling mutations in protein structures
    • DOI 10.1110/ps.072855507
    • Feyfant, E., Sali, A. & Fiser, A. (2007). Modeling mutations in protein structures. Protein Sci. 16, 2030-2041. (Pubitemid 47367126)
    • (2007) Protein Science , vol.16 , Issue.9 , pp. 2030-2041
    • Feyfant, E.1    Sali, A.2    Fiser, A.3
  • 51
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren, W. F. & Berendsen, H. J. C. (1977). Algorithms for macromolecular dynamics and constraint dynamics. Mol. Phys. 34, 1311-1327.
    • (1977) Mol. Phys. , vol.34 , pp. 1311-1327
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 52
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • Gilson, M., Given, J., Bush, B. & McCammon, J. (1997). The statistical-thermodynamic basis for computation of binding affinities: a critical review. Biophys. J. 72, 1047-1069. (Pubitemid 27113632)
    • (1997) Biophysical Journal , vol.72 , Issue.3 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 55
    • 76249112547 scopus 로고    scopus 로고
    • Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA
    • Rastelli, G., Del Rio, A., Degliesposti, G. & Sgobba, M. (2010). Fast and accurate predictions of binding free energies using MM-PBSA and MM-GBSA. J. Comput. Chem. 31, 797-810.
    • (2010) J. Comput. Chem. , vol.31 , pp. 797-810
    • Rastelli, G.1    Del Rio, A.2    Degliesposti, G.3    Sgobba, M.4
  • 56
    • 0034084991 scopus 로고    scopus 로고
    • Combined molecular mechanical and continuum solvent approach (MM- PBSA/GBSA) to predict ligand binding
    • DOI 10.1023/A:1008763014207
    • Massova, I. & Kollman, P. (2000). Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding. Perspect. Drug Discovery Des. 18, 113-135. (Pubitemid 30191024)
    • (2000) Perspectives in Drug Discovery and Design , vol.18 , pp. 113-135
    • Massova, I.1    Kollman, P.A.2
  • 57
    • 33745407153 scopus 로고    scopus 로고
    • Computational simulations of HIV-1 proteases-multi-drug resistance due to nonactive site mutation L90M
    • DOI 10.1021/ja060682b
    • Ode, H., Neya, S., Hata, M., Sugiura, W. & Hoshino, T. (2006). Computational simulations of HIV-1 proteases - multi-drug resistance due to nonactive site mutation L90M. J. Am. Chem. Soc. 128, 7887-7895. (Pubitemid 43945729)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.24 , pp. 7887-7895
    • Ode, H.1    Neya, S.2    Hata, M.3    Sugiura, W.4    Hoshino, T.5
  • 58
    • 72249091122 scopus 로고    scopus 로고
    • Multiple molecular dynamics simulations of TEM beta-lactamase: Dynamics and water binding of the omega-loop
    • Bos, F. & Pleiss, J. (2009). Multiple molecular dynamics simulations of TEM beta-lactamase: dynamics and water binding of the omega-loop. Biophys. J. 97, 2550-2558.
    • (2009) Biophys. J. , vol.97 , pp. 2550-2558
    • Bos, F.1    Pleiss, J.2
  • 59
    • 70349755625 scopus 로고    scopus 로고
    • Importance of ligand reorganization free energy in protein-ligand binding-affinity prediction
    • Yang, C. Y., Sun, H., Chen, J., Nikolovska-Coleska, Z. & Wang, S. (2009). Importance of ligand reorganization free energy in protein-ligand binding-affinity prediction. J. Am. Chem. Soc. 131, 13709-13721.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13709-13721
    • Yang, C.Y.1    Sun, H.2    Chen, J.3    Nikolovska-Coleska, Z.4    Wang, S.5
  • 60
    • 42449147045 scopus 로고    scopus 로고
    • Evaluating the potency of HIV-1 protease drugs to combat resistance
    • DOI 10.1002/prot.21808
    • Hou, T., McLaughlin, W. A. & Wang, W. (2008). Evaluating the potency of HIV-1 protease drugs to combat resistance. Proteins, 71, 1163-1174. (Pubitemid 351564043)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1163-1174
    • Hou, T.1    McLaughlin, W.A.2    Wang, W.3
  • 61
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke, H., Kiel, C. & Case, D. A. (2003). Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J. Mol. Biol. 330, 891-913.
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.