메뉴 건너뛰기




Volumn 55, Issue 7, 2012, Pages 3182-3192

Fragment-based design of symmetrical bis-benzimidazoles as selective inhibitors of the trimethoprim-resistant, type II R67 dihydrofolate reductase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BENZIMIDAZOLE DERIVATIVE; DIHYDROFOLATE REDUCTASE INHIBITOR; ENZYME VARIANT; TRIMETHOPRIM;

EID: 84859805882     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm201645r     Document Type: Article
Times cited : (27)

References (49)
  • 2
    • 0035370341 scopus 로고    scopus 로고
    • Resistance to trimethoprim-sulfamethoxazole
    • Huovinen, P. Resistance to trimethoprim-sulfamethoxazole Clin. Infect. Dis. 2001, 32 (11) 1608-1614
    • (2001) Clin. Infect. Dis. , vol.32 , Issue.11 , pp. 1608-1614
    • Huovinen, P.1
  • 4
    • 84859805991 scopus 로고    scopus 로고
    • (accessed November 29).
    • http://www.who.int/selection-medicines/committees/expert/18/applications/ Sulfamethoxazole-trimethoprim.pdf (accessed November 29, 2011).
    • (2011)
  • 5
    • 78651464871 scopus 로고    scopus 로고
    • Trimethoprim resistance in a porcine Pasteurella aerogenes isolate is based on a dfrA1 gene cassette located in a partially truncated class 2 integron
    • Kehrenberg, C.; Schwarz, S. Trimethoprim resistance in a porcine Pasteurella aerogenes isolate is based on a dfrA1 gene cassette located in a partially truncated class 2 integron J. Antimicrob. Chemother. 2011, 66 (2) 450-452
    • (2011) J. Antimicrob. Chemother. , vol.66 , Issue.2 , pp. 450-452
    • Kehrenberg, C.1    Schwarz, S.2
  • 6
    • 33745146852 scopus 로고    scopus 로고
    • Heavy use of prophylactic antibiotics in aquaculture: A growing problem for human and animal health and for the environment
    • Cabello, F. C. Heavy use of prophylactic antibiotics in aquaculture: A growing problem for human and animal health and for the environment Environ. Microbiol. 2006, 8 (7) 1137-1144
    • (2006) Environ. Microbiol. , vol.8 , Issue.7 , pp. 1137-1144
    • Cabello, F.C.1
  • 7
    • 26444496142 scopus 로고    scopus 로고
    • Antibiotic resistance in bacteria from shrimp farming in mangrove areas
    • Le, T. X.; Munekage, Y.; Kato, S. Antibiotic resistance in bacteria from shrimp farming in mangrove areas Sci. Total Environ. 2005, 349 (1-3) 95-105
    • (2005) Sci. Total Environ. , vol.349 , Issue.1-3 , pp. 95-105
    • Le, T.X.1    Munekage, Y.2    Kato, S.3
  • 8
    • 34047276658 scopus 로고    scopus 로고
    • Determination of six anti-infectives in wastewater using tandem solid-phase extraction and liquid chromatography-tandem mass spectrometry
    • Segura, P. A.; Garcia-Ac, A.; Lajeunesse, A.; Ghosh, D.; Gagnon, C.; Sauvé, S. Determination of six anti-infectives in wastewater using tandem solid-phase extraction and liquid chromatography-tandem mass spectrometry J. Environ. Monit. 2007, 9 (4) 307-313
    • (2007) J. Environ. Monit. , vol.9 , Issue.4 , pp. 307-313
    • Segura, P.A.1    Garcia-Ac, A.2    Lajeunesse, A.3    Ghosh, D.4    Gagnon, C.5    Sauvé, S.6
  • 9
    • 77955052630 scopus 로고    scopus 로고
    • Chemical use in salmon aquaculture: A review of current practices and possible environmental effects
    • Burridge, L.; Weis, J. S.; Cabello, F.; Pizarro, J.; Bostick, K. Chemical use in salmon aquaculture: A review of current practices and possible environmental effects Aquaculture 2010, 306 (1-4) 7-23
    • (2010) Aquaculture , vol.306 , Issue.1-4 , pp. 7-23
    • Burridge, L.1    Weis, J.S.2    Cabello, F.3    Pizarro, J.4    Bostick, K.5
  • 10
    • 78651501781 scopus 로고    scopus 로고
    • Phenotypic and Genotypic Characterization of Antimicrobial Resistance in Enterohemorrhagic Escherichia coli and Atypical Enteropathogenic E. coli Strains from Ruminants
    • Medina, A.; Horcajo, P.; Jurado, S.; De La Fuente, R.; Ruiz-Santa-Quiteria, J. A.; Domínguez-Bernal, G.; Orden, J. A. Phenotypic and Genotypic Characterization of Antimicrobial Resistance in Enterohemorrhagic Escherichia coli and Atypical Enteropathogenic E. coli Strains from Ruminants J. Vet. Diagn. Invest. 2011, 23 (1) 91-95
    • (2011) J. Vet. Diagn. Invest. , vol.23 , Issue.1 , pp. 91-95
    • Medina, A.1    Horcajo, P.2    Jurado, S.3    De La Fuente, R.4    Ruiz-Santa-Quiteria, J.A.5    Domínguez-Bernal, G.6    Orden, J.A.7
  • 11
    • 1442300139 scopus 로고    scopus 로고
    • Isolation and characterization of integron-containing bacteria without antibiotic selection
    • Barlow, R. S.; Pemberton, J. M.; Desmarchelier, P. M.; Gobius, K. S. Isolation and characterization of integron-containing bacteria without antibiotic selection Antimicrob. Agents Chemother. 2004, 48 (3) 838-842
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.3 , pp. 838-842
    • Barlow, R.S.1    Pemberton, J.M.2    Desmarchelier, P.M.3    Gobius, K.S.4
  • 12
    • 80555155634 scopus 로고    scopus 로고
    • Characterization of integrons in multiple antimicrobial resistant Escherichia coli isolates from bovine endometritis
    • Zhao, H. X.; Shen, J. Z.; An, X. P.; Fan, H. L.; Cao, J. S.; Li, P. F. Characterization of integrons in multiple antimicrobial resistant Escherichia coli isolates from bovine endometritis Res. Vet. Sci. 2011, 91 (3) 412-414
    • (2011) Res. Vet. Sci. , vol.91 , Issue.3 , pp. 412-414
    • Zhao, H.X.1    Shen, J.Z.2    An, X.P.3    Fan, H.L.4    Cao, J.S.5    Li, P.F.6
  • 13
    • 62949106183 scopus 로고    scopus 로고
    • Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: Sequence and structural comparison
    • Volpato, J. P.; Pelletier, J. N. Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: Sequence and structural comparison Drug Resist. Updates 2009, 12 (1-2) 28-41
    • (2009) Drug Resist. Updates , vol.12 , Issue.1-2 , pp. 28-41
    • Volpato, J.P.1    Pelletier, J.N.2
  • 14
    • 1542283603 scopus 로고    scopus 로고
    • Sustained clinical efficacy of sulfadoxine-pyrimethamine for uncomplicated falciparum malaria in Malawi after 10 years as first line treatment: Five year prospective study
    • Plowe, C. V.; Kublin, J. G.; Dzinjalamala, F. K.; Kamwendo, D. S.; Mukadam, R. A.; Chimpeni, P.; Molyneux, M. E.; Taylor, T. E. Sustained clinical efficacy of sulfadoxine-pyrimethamine for uncomplicated falciparum malaria in Malawi after 10 years as first line treatment: five year prospective study BMJ 2004, 328 (7439) 545
    • (2004) BMJ , vol.328 , Issue.7439 , pp. 545
    • Plowe, C.V.1    Kublin, J.G.2    Dzinjalamala, F.K.3    Kamwendo, D.S.4    Mukadam, R.A.5    Chimpeni, P.6    Molyneux, M.E.7    Taylor, T.E.8
  • 15
    • 30344439521 scopus 로고    scopus 로고
    • Apparent absence of atovaquone/proguanil resistance in 477 Plasmodium falciparum isolates from untreated French travellers
    • Musset, L.; Pradines, B.; Parzy, D.; Durand, R.; Bigot, P.; Le Bras, J. Apparent absence of atovaquone/proguanil resistance in 477 Plasmodium falciparum isolates from untreated French travellers J. Antimicrob. Chemother. 2006, 57 (1) 110-115
    • (2006) J. Antimicrob. Chemother. , vol.57 , Issue.1 , pp. 110-115
    • Musset, L.1    Pradines, B.2    Parzy, D.3    Durand, R.4    Bigot, P.5    Le Bras, J.6
  • 16
    • 0023730578 scopus 로고
    • Kinetics of the formation and isomerization of methotrexate complexes of recombinant human dihydrofolate reductase
    • Appleman, J. R.; Prendergast, N.; Delcamp, T. J.; Freisheim, J. H.; Blakley, R. L. Kinetics of the formation and isomerization of methotrexate complexes of recombinant human dihydrofolate reductase J. Biol. Chem. 1988, 263 (21) 10304-10313
    • (1988) J. Biol. Chem. , vol.263 , Issue.21 , pp. 10304-10313
    • Appleman, J.R.1    Prendergast, N.2    Delcamp, T.J.3    Freisheim, J.H.4    Blakley, R.L.5
  • 17
    • 0343337173 scopus 로고    scopus 로고
    • Resistance to trimethoprim and sulfonamides
    • Sköld, O. Resistance to trimethoprim and sulfonamides Vet. Res. 2001, 32 (3-4) 261-273
    • (2001) Vet. Res. , vol.32 , Issue.3-4 , pp. 261-273
    • Sköld, O.1
  • 18
    • 0020397035 scopus 로고
    • Monitoring of plasmid-encoded, trimethoprim-resistant dihydrofolate reductase genes: Detection of a new resistant enzyme
    • Fling, M. E.; Walton, L.; Elwell, L. P. Monitoring of plasmid-encoded, trimethoprim-resistant dihydrofolate reductase genes: Detection of a new resistant enzyme Antimicrob. Agents Chemother. 1982, 22 (5) 882-888
    • (1982) Antimicrob. Agents Chemother. , vol.22 , Issue.5 , pp. 882-888
    • Fling, M.E.1    Walton, L.2    Elwell, L.P.3
  • 19
    • 0018638966 scopus 로고
    • The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67
    • Stone, D.; Smith, S. L. The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67 J. Biol. Chem. 1979, 254 (21) 10857-10861
    • (1979) J. Biol. Chem. , vol.254 , Issue.21 , pp. 10857-10861
    • Stone, D.1    Smith, S.L.2
  • 20
    • 33745879777 scopus 로고    scopus 로고
    • Integron-sequestered dihydrofolate reductase: A recently redeployed enzyme
    • Alonso, H.; Gready, J. E. Integron-sequestered dihydrofolate reductase: A recently redeployed enzyme Trends Microbiol. 2006, 14 (5) 236-242
    • (2006) Trends Microbiol. , vol.14 , Issue.5 , pp. 236-242
    • Alonso, H.1    Gready, J.E.2
  • 22
  • 23
    • 21044452600 scopus 로고    scopus 로고
    • Searching sequence space: Two different approaches to dihydrofolate reductase catalysis
    • Howell, E. E. Searching sequence space: two different approaches to dihydrofolate reductase catalysis ChemBioChem 2005, 6 (4) 590-600
    • (2005) ChemBioChem , vol.6 , Issue.4 , pp. 590-600
    • Howell, E.E.1
  • 24
    • 14644433770 scopus 로고    scopus 로고
    • Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: Creating alternative functional configurations
    • Schmitzer, A. R.; Lépine, F.; Pelletier, J. N. Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: Creating alternative functional configurations Protein Eng. Des. Sel. 2004, 17 (11) 809-819
    • (2004) Protein Eng. Des. Sel. , vol.17 , Issue.11 , pp. 809-819
    • Schmitzer, A.R.1    Lépine, F.2    Pelletier, J.N.3
  • 25
    • 37349009656 scopus 로고    scopus 로고
    • Crystal structure of a type II dihydrofolate reductase catalytic ternary complex
    • Krahn, J. M.; Jackson, M. R.; DeRose, E. F.; Howell, E. E.; London, R. E. Crystal structure of a type II dihydrofolate reductase catalytic ternary complex Biochemistry 2007, 46 (51) 14878-14888
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14878-14888
    • Krahn, J.M.1    Jackson, M.R.2    Derose, E.F.3    Howell, E.E.4    London, R.E.5
  • 26
    • 22544488422 scopus 로고    scopus 로고
    • Fragonomics: Fragment-based drug discovery [Review]
    • Zartler, E. R.; Shapiro, M. J. Fragonomics: Fragment-based drug discovery [Review] Curr. Opin. Chem. Biol. 2005, 9 (4) 366-370
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.4 , pp. 366-370
    • Zartler, E.R.1    Shapiro, M.J.2
  • 27
    • 67649494337 scopus 로고    scopus 로고
    • Transforming fragments into candidates: Small becomes big in medicinal chemistry
    • de Kloe, G. E.; Bailey, D.; Leurs, R.; de Esch, I. J. Transforming fragments into candidates: Small becomes big in medicinal chemistry Drug Discovery Today 2009, 14 (13-14) 630-646
    • (2009) Drug Discovery Today , vol.14 , Issue.13-14 , pp. 630-646
    • De Kloe, G.E.1    Bailey, D.2    Leurs, R.3    De Esch, I.J.4
  • 28
    • 77953530689 scopus 로고    scopus 로고
    • Contributions of computational chemistry and biophysical techniques to fragment-based drug discovery
    • Gozalbes, R.; Carbajo, R. J.; Pineda-Lucena, A. Contributions of computational chemistry and biophysical techniques to fragment-based drug discovery Curr. Med. Chem. 2010, 17 (17) 1769-1794
    • (2010) Curr. Med. Chem. , vol.17 , Issue.17 , pp. 1769-1794
    • Gozalbes, R.1    Carbajo, R.J.2    Pineda-Lucena, A.3
  • 29
    • 67849113794 scopus 로고    scopus 로고
    • The rise of fragment-based drug discovery
    • Murray, C. W.; Rees, D. C. The rise of fragment-based drug discovery Nat. Chem. 2009, 1 (3) 187-192
    • (2009) Nat. Chem. , vol.1 , Issue.3 , pp. 187-192
    • Murray, C.W.1    Rees, D.C.2
  • 30
    • 36949079198 scopus 로고
    • Crystalline Dihydropteroylglutamic Acid
    • Blakley, R. L. Crystalline Dihydropteroylglutamic Acid Nature 1960, 188, 231-232
    • (1960) Nature , vol.188 , pp. 231-232
    • Blakley, R.L.1
  • 32
    • 0000669055 scopus 로고
    • Synthesis of Potential Rickettsiostatic Agents.1a I. 4,4′- Dicarboxy-α,I-diphenoxyalkanes1b
    • Donahoe, H. B.; Benjamin, L. E.; Fennoy, L. V.; Greiff, D. Synthesis of Potential Rickettsiostatic Agents.1a I. 4,4′-Dicarboxy-α,I- diphenoxyalkanes1b J. Org. Chem. 1961, 26 (2) 474-476
    • (1961) J. Org. Chem. , vol.26 , Issue.2 , pp. 474-476
    • Donahoe, H.B.1    Benjamin, L.E.2    Fennoy, L.V.3    Greiff, D.4
  • 34
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H.; von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 1987, 166 (2) 368-379
    • (1987) Anal. Biochem. , vol.166 , Issue.2 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 35
    • 67749106478 scopus 로고    scopus 로고
    • Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance
    • Volpato, J. P.; Yachnin, B. J.; Blanchet, J.; Guerrero, V.; Poulin, L.; Fossati, E.; Berghuis, A. M.; Pelletier, J. N. Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance J. Biol. Chem. 2009, 284 (30) 20079-20089
    • (2009) J. Biol. Chem. , vol.284 , Issue.30 , pp. 20079-20089
    • Volpato, J.P.1    Yachnin, B.J.2    Blanchet, J.3    Guerrero, V.4    Poulin, L.5    Fossati, E.6    Berghuis, A.M.7    Pelletier, J.N.8
  • 36
    • 0031018009 scopus 로고    scopus 로고
    • Mechanistic studies of R67 dihydrofolate reductase - Effects of pH and an H62C mutation
    • Park, H. Y.; Zhuang, P.; Nichols, R.; Howell, E. E. Mechanistic studies of R67 dihydrofolate reductase-Effects of pH and an H62C mutation J. Biol. Chem. 1997, 272 (4) 2252-2258
    • (1997) J. Biol. Chem. , vol.272 , Issue.4 , pp. 2252-2258
    • Park, H.Y.1    Zhuang, P.2    Nichols, R.3    Howell, E.E.4
  • 37
    • 41949105752 scopus 로고    scopus 로고
    • A Balancing Act between Net Uptake of Water during Dihydrofolate Binding and Net Release of Water upon NADPH Binding in R67 Dihydrofolate Reductase
    • Chopra, S.; Dooling, R. M.; Horner, C. G.; Howell, E. E. A Balancing Act between Net Uptake of Water during Dihydrofolate Binding and Net Release of Water upon NADPH Binding in R67 Dihydrofolate Reductase J. Biol. Chem. 2008, 283 (8) 4690-4698
    • (2008) J. Biol. Chem. , vol.283 , Issue.8 , pp. 4690-4698
    • Chopra, S.1    Dooling, R.M.2    Horner, C.G.3    Howell, E.E.4
  • 38
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction
    • Cheng, Y.; Prusoff, W. H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction Biochem. Pharmacol. 1973, 22 (23) 3099-3108
    • (1973) Biochem. Pharmacol. , vol.22 , Issue.23 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 39
    • 33744826819 scopus 로고    scopus 로고
    • MolDock: A new technique for high-accuracy molecular docking
    • Thomsen, R.; Christensen, M. H. MolDock: a new technique for high-accuracy molecular docking J. Med. Chem. 2006, 49 (11) 3315-3321
    • (2006) J. Med. Chem. , vol.49 , Issue.11 , pp. 3315-3321
    • Thomsen, R.1    Christensen, M.H.2
  • 40
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O.; Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J. Comput. Chem. 2010, 31 (2) 455-461
    • (2010) J. Comput. Chem. , vol.31 , Issue.2 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 41
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays J. Immunol. Methods 1983, 65 (1-2) 55-63
    • (1983) J. Immunol. Methods , vol.65 , Issue.1-2 , pp. 55-63
    • Mosmann, T.1
  • 42
    • 0042318979 scopus 로고    scopus 로고
    • Role of ionic interactions in ligand binding and catalysis of R67 dihydrofolate reductase
    • Hicks, S. N.; Smiley, R. D.; Hamilton, J. B.; Howell, E. E. Role of ionic interactions in ligand binding and catalysis of R67 dihydrofolate reductase Biochemistry 2003, 42 (36) 10569-10578
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10569-10578
    • Hicks, S.N.1    Smiley, R.D.2    Hamilton, J.B.3    Howell, E.E.4
  • 43
    • 0032586721 scopus 로고    scopus 로고
    • Estimation of Ki in a competitive enzyme-inhibition model: Comparisons among three methods of data analysis
    • Kakkar, T.; Boxenbaum, H.; Mayersohn, M. Estimation of Ki in a competitive enzyme-inhibition model: Comparisons among three methods of data analysis Drug Metab. Dispos. 1999, 27 (6) 756-762
    • (1999) Drug Metab. Dispos. , vol.27 , Issue.6 , pp. 756-762
    • Kakkar, T.1    Boxenbaum, H.2    Mayersohn, M.3
  • 44
    • 0037207139 scopus 로고    scopus 로고
    • Breaking symmetry: Mutations engineered into R67 dihydrofolate reductase, a D2 symmetric homotetramer possessing a single active site pore
    • Smiley, R. D.; Stinnett, L. G.; Saxton, A. M.; Howell, E. E. Breaking symmetry: mutations engineered into R67 dihydrofolate reductase, a D2 symmetric homotetramer possessing a single active site pore Biochemistry 2002, 41 (52) 15664-15675
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15664-15675
    • Smiley, R.D.1    Stinnett, L.G.2    Saxton, A.M.3    Howell, E.E.4
  • 45
    • 0029738545 scopus 로고    scopus 로고
    • Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein
    • Bradrick, T. D.; Beechem, J. M.; Howell, E. E. Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein Biochemistry 1996, 35 (35) 11414-11424
    • (1996) Biochemistry , vol.35 , Issue.35 , pp. 11414-11424
    • Bradrick, T.D.1    Beechem, J.M.2    Howell, E.E.3
  • 47
    • 0035732844 scopus 로고    scopus 로고
    • One site fits both: A model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme
    • Howell, E. E.; Shukla, U.; Hicks, S. N.; Smiley, R. D.; Kuhn, L. A.; Zavodszky, M. I. One site fits both: A model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme J. Comput.-Aided Mol. Des. 2001, 15 (11) 1035-1052
    • (2001) J. Comput.-Aided Mol. Des. , vol.15 , Issue.11 , pp. 1035-1052
    • Howell, E.E.1    Shukla, U.2    Hicks, S.N.3    Smiley, R.D.4    Kuhn, L.A.5    Zavodszky, M.I.6
  • 49
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C.; D'Arcy, A.; Winkler, F. K. Crystal structure of human dihydrofolate reductase complexed with folate Eur. J. Biochem. 1988, 174 (2) 377-385
    • (1988) Eur. J. Biochem. , vol.174 , Issue.2 , pp. 377-385
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.