메뉴 건너뛰기




Volumn 45, Issue 50, 2006, Pages 15029-15038

GliP, a multimodular nonribosomal peptide synthetase in Aspergillus fumigatus, makes the diketopiperazine scaffold of gliotoxin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ESCHERICHIA COLI; METABOLITES; NITROGEN COMPOUNDS; REDOX REACTIONS; TOXIC MATERIALS;

EID: 33845592512     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061845b     Document Type: Article
Times cited : (128)

References (52)
  • 1
    • 17644412298 scopus 로고    scopus 로고
    • The epipolythiodioxopiperazine (ETP) class of fungal toxins: Distribution, mode of action, functions and biosynthesis
    • Gardiner, D. M., Waring, P., and Howlett, B. J. (2005) The epipolythiodioxopiperazine (ETP) class of fungal toxins: distribution, mode of action, functions and biosynthesis, Microbiology 151, 1021-1032.
    • (2005) Microbiology , vol.151 , pp. 1021-1032
    • Gardiner, D.M.1    Waring, P.2    Howlett, B.J.3
  • 2
    • 0030561529 scopus 로고    scopus 로고
    • Gliotoxin and related epipolythiodioxopiperazines
    • Waring, P., and Beaver, J. (1996) Gliotoxin and related epipolythiodioxopiperazines, Gen. Pharmacol. 27, 1311-1316.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 1311-1316
    • Waring, P.1    Beaver, J.2
  • 5
    • 0026583830 scopus 로고
    • Gliotoxin: Inhibitor of poliovirus RNA synthesis that blocks the viral RNA polymerase 3Dpol
    • Rodriguez, P. L., and Carrasco, L. (1992) Gliotoxin: inhibitor of poliovirus RNA synthesis that blocks the viral RNA polymerase 3Dpol, J. Virol. 66, 1971-1976.
    • (1992) J. Virol. , vol.66 , pp. 1971-1976
    • Rodriguez, P.L.1    Carrasco, L.2
  • 6
    • 0011925448 scopus 로고
    • Immunosuppression in vitro by a metabolite of a human pathogenic fungus
    • Mullbacher, A., and Eichner, R. D. (1984) Immunosuppression in vitro by a metabolite of a human pathogenic fungus, Proc. Natl. Acad. Sci. U.S.A. 81, 3835-3837.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3835-3837
    • Mullbacher, A.1    Eichner, R.D.2
  • 7
    • 0021825248 scopus 로고
    • Identification of an agent in cultures of Aspergillus fumigatus displaying anti-phagocytic and immunomodulating activity in vitro
    • Mullbacher, A., Waring, P., and Eichner, R. D. (1985) Identification of an agent in cultures of Aspergillus fumigatus displaying anti-phagocytic and immunomodulating activity in vitro, J. Gen. Microbiol. 131, 1251-1258.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1251-1258
    • Mullbacher, A.1    Waring, P.2    Eichner, R.D.3
  • 8
    • 0022658585 scopus 로고
    • Structural relationship of epipolythiodioxopiperazines and their immunomodulating activity
    • Mullbacher, A., Waring, P., Tiwari-Palni, U., and Eichner, R. D. (1986) Structural relationship of epipolythiodioxopiperazines and their immunomodulating activity, Mol. Immunol. 23, 231-235.
    • (1986) Mol. Immunol. , vol.23 , pp. 231-235
    • Mullbacher, A.1    Waring, P.2    Tiwari-Palni, U.3    Eichner, R.D.4
  • 9
    • 0028607248 scopus 로고
    • Lack of correlation between early intracellular calcium ion rises and the onset of apoptosis in thymocytes
    • Beaver, J. P., and Waring, P. (1994) Lack of correlation between early intracellular calcium ion rises and the onset of apoptosis in thymocytes, Immunol. Cell Biol. 72, 489-499.
    • (1994) Immunol. Cell Biol. , vol.72 , pp. 489-499
    • Beaver, J.P.1    Waring, P.2
  • 11
    • 0013537645 scopus 로고
    • Biosynthesis of gliotoxin. II. Further studies on the incorporation of carbon-14 and tritium-labeled precursors
    • Winstead, J. A., and Suhadolnik, R. J. (1960) Biosynthesis of gliotoxin. II. Further studies on the incorporation of carbon-14 and tritium-labeled precursors, J. Am. Chem. Soc. 82, 1644-1647.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 1644-1647
    • Winstead, J.A.1    Suhadolnik, R.J.2
  • 13
    • 0004725406 scopus 로고
    • cyclo-(L-Phenylalanyl-L-seryl) as an intermediate in the biosynthesis of gliotoxin
    • Kirby, G. W., Graham, P. L., and Robins, D. J. (1978) cyclo-(L-Phenylalanyl-L-seryl) as an intermediate in the biosynthesis of gliotoxin, J. Chem. Soc., Perkin Trans. 1 11, 1336-1338.
    • (1978) J. Chem. Soc., Perkin Trans. 1 , vol.11 , pp. 1336-1338
    • Kirby, G.W.1    Graham, P.L.2    Robins, D.J.3
  • 14
    • 0018813869 scopus 로고
    • Formation of phenylalanylserine and cyclo-phenylalanylseryl by protoplasts of Gliocladium virens
    • Behling, R. A., and Fischer, A. G. (1980) Formation of phenylalanylserine and cyclo-phenylalanylseryl by protoplasts of Gliocladium virens, Int. J. Biochem. 11, 457-458.
    • (1980) Int. J. Biochem. , vol.11 , pp. 457-458
    • Behling, R.A.1    Fischer, A.G.2
  • 15
    • 0016670325 scopus 로고
    • Biosynthesis of gliotoxin and mycelianamide
    • Macdonald, J. C., and Slater, G. P. (1975) Biosynthesis of gliotoxin and mycelianamide, Can. J. Biochem. 53, 475-478.
    • (1975) Can. J. Biochem. , vol.53 , pp. 475-478
    • Macdonald, J.C.1    Slater, G.P.2
  • 18
    • 0036727255 scopus 로고    scopus 로고
    • Lactobacillus plantarum MiLAB 393 produces the antifungal cyclic dipeptides cyclo(L-Phe-L-Pro) and cyclo(L-Phe-trans-4-OH-L-Pro) and 3-phenyllactic acid
    • Strom, K., Sjogren, J., Broberg, A., and Schnurer, J. (2002) Lactobacillus plantarum MiLAB 393 produces the antifungal cyclic dipeptides cyclo(L-Phe-L-Pro) and cyclo(L-Phe-trans-4-OH-L-Pro) and 3-phenyllactic acid, Appl. Environ. Microbiol. 68, 4322-4327.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4322-4327
    • Strom, K.1    Sjogren, J.2    Broberg, A.3    Schnurer, J.4
  • 19
    • 0242321129 scopus 로고    scopus 로고
    • dd-diketopiperazines: Antibiotics active against Vibrio anguillarum isolated from marine bacteria associated with cultures of Pecten maximus
    • Fdhila, F., Vazquez, V., Sanchez, J. L., and Riguera, R. (2003) dd-diketopiperazines: antibiotics active against Vibrio anguillarum isolated from marine bacteria associated with cultures of Pecten maximus, J. Nat. Prod. 66, 1299-1301.
    • (2003) J. Nat. Prod. , vol.66 , pp. 1299-1301
    • Fdhila, F.1    Vazquez, V.2    Sanchez, J.L.3    Riguera, R.4
  • 20
    • 21744453939 scopus 로고    scopus 로고
    • Bioinformatic and expression analysis of the putative gliotoxin biosynthetic gene cluster of Aspergillus fumigatus
    • Gardiner, D. M., and Hewlett, B. J. (2005) Bioinformatic and expression analysis of the putative gliotoxin biosynthetic gene cluster of Aspergillus fumigatus, FEMS Microbiol. Lett. 248, 241-248.
    • (2005) FEMS Microbiol. Lett. , vol.248 , pp. 241-248
    • Gardiner, D.M.1    Hewlett, B.J.2
  • 21
    • 4444376010 scopus 로고    scopus 로고
    • The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus Leptosphaeria maculans
    • Gardiner, D. M., Cozijnsen, A. J., Wilson, L. M., Pedras, M. S., and Hewlett, B. J. (2004) The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus Leptosphaeria maculans, Mol. Microbiol. 53, 1307-1318.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1307-1318
    • Gardiner, D.M.1    Cozijnsen, A.J.2    Wilson, L.M.3    Pedras, M.S.4    Hewlett, B.J.5
  • 23
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
    • Cane, D. E., and Walsh, C. T. (1999) The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases, Chem. Biol. 6, R319-R325.
    • (1999) Chem. Biol. , vol.6
    • Cane, D.E.1    Walsh, C.T.2
  • 24
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D. E., Walsh, C. T., and Khosla, C. (1998) Harnessing the biosynthetic code: combinations, permutations, and mutations, Science 282, 63-68.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 25
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel, M. A., Stachelhaus, T., and Mootz, H. D. (1997) Modular peptide synthetases involved in nonribosomal peptide synthesis, Chem. Rev. 97, 2651-2674.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 26
    • 0035023450 scopus 로고    scopus 로고
    • Multimodular biocatalysts for natural product assembly
    • Schwarzer, D., and Marahiel, M. A. (2001) Multimodular biocatalysts for natural product assembly, Naturwissenschaften 88, 93-101.
    • (2001) Naturwissenschaften , vol.88 , pp. 93-101
    • Schwarzer, D.1    Marahiel, M.A.2
  • 28
    • 0035156443 scopus 로고    scopus 로고
    • Exploring the domain structure of modular nonribosomal peptide synthetases
    • Weber, T., and Marahiel, M. A. (2001) Exploring the domain structure of modular nonribosomal peptide synthetases, Structure 9, R3-R9.
    • (2001) Structure , vol.9
    • Weber, T.1    Marahiel, M.A.2
  • 29
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S
    • Conti, E., Stachelhaus, T., Marahiel, M. A., and Brick, P. (1997) Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S, EMBO J. 16, 4174-4183.
    • (1997) EMBO J. , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 30
    • 0030292865 scopus 로고    scopus 로고
    • Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases
    • Stachelhaus, T., Huser, A., and Marahiel, M. A. (1996) Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases, Chem. Biol. 3, 913-921.
    • (1996) Chem. Biol. , vol.3 , pp. 913-921
    • Stachelhaus, T.1    Huser, A.2    Marahiel, M.A.3
  • 31
    • 0034656331 scopus 로고    scopus 로고
    • Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases
    • Weber, T., Baumgartner, R., Renner, C., Marahiel, M. A., and Holak, T. A. (2000) Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases, Structure 8, 407-418.
    • (2000) Structure , vol.8 , pp. 407-418
    • Weber, T.1    Baumgartner, R.2    Renner, C.3    Marahiel, M.A.4    Holak, T.A.5
  • 32
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • Belshaw, P. J., Walsh, C. T., and Stachelhaus, T. (1999) Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis, Science 284, 486-489.
    • (1999) Science , vol.284 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3
  • 33
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain
    • Stachelhaus, T., Mootz, H. D., Bergendahl, V., and Marahiel, M. A. (1998) Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain, J. Biol. Chem. 273, 22773-22781.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 35
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri, L. E., Weinreb, P. H., Lei, M., Nakano, M. M., Zuber, P., and Walsh, C. T. (1998) Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases, Biochemistry 37, 1585-1595.
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 36
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 37
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus, T., Mootz, H. D., and Marahiel, M. A. (1999) The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases, Chem. Biol. 6, 493-505.
    • (1999) Chem. Biol. , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 38
    • 14044264103 scopus 로고    scopus 로고
    • In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family
    • Di Vincenzo, L., Grgurina, I., and Pascarella, S. (2005) In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family, FEBS J. 272, 929-941.
    • (2005) FEBS J. , vol.272 , pp. 929-941
    • Di Vincenzo, L.1    Grgurina, I.2    Pascarella, S.3
  • 39
    • 0032829915 scopus 로고    scopus 로고
    • Initiation, elongation, and termination strategies in polyketide and polypeptide antibiotic biosynthesis
    • Keating, T. A., and Walsh, C. T. (1999) Initiation, elongation, and termination strategies in polyketide and polypeptide antibiotic biosynthesis, Curr. Opin. Chem. Biol. 3, 598-606.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 598-606
    • Keating, T.A.1    Walsh, C.T.2
  • 40
    • 0036161991 scopus 로고    scopus 로고
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis
    • Bergendahl, V., Linne, U., and Marahiel, M. A. (2002) Mutational analysis of the C-domain in nonribosomal peptide synthesis, Eur. J. Biochem. 269, 620-629.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 620-629
    • Bergendahl, V.1    Linne, U.2    Marahiel, M.A.3
  • 41
    • 0037423499 scopus 로고    scopus 로고
    • Enzymology of acyl chain macrocyclization in natural product biosynthesis
    • Kohli, R. M., and Walsh, C. T. (2003) Enzymology of acyl chain macrocyclization in natural product biosynthesis, Chem. Commun. (Cambridge), 297-307.
    • (2003) Chem. Commun. (Cambridge) , pp. 297-307
    • Kohli, R.M.1    Walsh, C.T.2
  • 42
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus, T., and Walsh, C. T. (2000) Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase, Biochemistry 39, 5775-5787.
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2
  • 43
    • 22144479730 scopus 로고    scopus 로고
    • Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus
    • Grundmann, A., and Li, S. M. (2005) Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus, Microbiology 151, 2199-2207.
    • (2005) Microbiology , vol.151 , pp. 2199-2207
    • Grundmann, A.1    Li, S.M.2
  • 44
    • 33645781037 scopus 로고    scopus 로고
    • Identification of the cytochrome P450 monooxygenase that bridges the clavine and ergoline alkaloid pathways
    • Haarmann, T., Ortel, I., Tudzynski, P., and Keller, U. (2006) Identification of the cytochrome P450 monooxygenase that bridges the clavine and ergoline alkaloid pathways, ChemBioChem 7, 645-652.
    • (2006) ChemBioChem , vol.7 , pp. 645-652
    • Haarmann, T.1    Ortel, I.2    Tudzynski, P.3    Keller, U.4
  • 45
    • 20444414907 scopus 로고    scopus 로고
    • The ergot alkaloid gene cluster in Claviceps purpurea: Extension of the cluster sequence and intra species evolution
    • Haarmann, T., Machado, C., Lubbe, Y., Correia, T., Schardl, C. L., Panaccione, D. G., and Tudzynski, P. (2005) The ergot alkaloid gene cluster in Claviceps purpurea: extension of the cluster sequence and intra species evolution, Phytochemistry 66, 1312-1320.
    • (2005) Phytochemistry , vol.66 , pp. 1312-1320
    • Haarmann, T.1    Machado, C.2    Lubbe, Y.3    Correia, T.4    Schardl, C.L.5    Panaccione, D.G.6    Tudzynski, P.7
  • 46
    • 0033636188 scopus 로고    scopus 로고
    • The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin a production and pathogenicity
    • Healy, F. G., Wach, M., Krasnoff, S. B., Gibson, D. M., and Loria, R. (2000) The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin A production and pathogenicity, Mol. Microbiol. 38, 794-804.
    • (2000) Mol. Microbiol. , vol.38 , pp. 794-804
    • Healy, F.G.1    Wach, M.2    Krasnoff, S.B.3    Gibson, D.M.4    Loria, R.5
  • 47
    • 0025364218 scopus 로고
    • Kinetics and mechanism of the facile cyclization of histidyl-prolineamide to cyclo(His-Pro) in aqueous solution and the competitive influence of human plasma
    • Moss, J., and Bundgaard, H. (1990) Kinetics and mechanism of the facile cyclization of histidyl-prolineamide to cyclo(His-Pro) in aqueous solution and the competitive influence of human plasma, J. Pharm. Pharmacol. 42, 7-12.
    • (1990) J. Pharm. Pharmacol. , vol.42 , pp. 7-12
    • Moss, J.1    Bundgaard, H.2
  • 48
    • 0036914164 scopus 로고    scopus 로고
    • The albonoursin gene cluster of S noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases
    • Lautru, S., Gondry, M., Genet, R., and Pernodet, J. L. (2002) The albonoursin gene cluster of S noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases, Chem. Biol. 9, 1355-1364.
    • (2002) Chem. Biol. , vol.9 , pp. 1355-1364
    • Lautru, S.1    Gondry, M.2    Genet, R.3    Pernodet, J.L.4
  • 49
    • 0036037587 scopus 로고    scopus 로고
    • Enniatin synthetase is a monomer with extended structure: Evidence for an intramolecular reaction mechanism
    • Glinski, M., Urbanke, C., Hornbogen, T., and Zocher, R. (2002) Enniatin synthetase is a monomer with extended structure: evidence for an intramolecular reaction mechanism, Arch. Microbiol. 178, 267-273.
    • (2002) Arch. Microbiol. , vol.178 , pp. 267-273
    • Glinski, M.1    Urbanke, C.2    Hornbogen, T.3    Zocher, R.4
  • 50
    • 0344739821 scopus 로고    scopus 로고
    • A nonribosomal peptide synthetase involved in the biosynthesis of ampullosporins in Sepedonium ampullosporum
    • Reiber, K., Neuhof, T., Ozegowski, J. H., von Dohrend, H., and Schwecke, T. (2003) A nonribosomal peptide synthetase involved in the biosynthesis of ampullosporins in Sepedonium ampullosporum, J. Pept. Sci. 9, 701-713.
    • (2003) J. Pept. Sci. , vol.9 , pp. 701-713
    • Reiber, K.1    Neuhof, T.2    Ozegowski, J.H.3    Von Dohrend, H.4    Schwecke, T.5
  • 51
    • 33644527914 scopus 로고    scopus 로고
    • A bidomain nonribosomal peptide synthetase encoded by FUM14 catalyzes the formation of tricarballylic esters in the biosynthesis of fumonisins
    • Zaleta-Rivera, K., Xu, C., Yu, F., Butchko, R. A., Proctor, R. H., Hidalgo-Lara, M. E., Raza, A., Dussault, P. H., and Du, L. (2006) A bidomain nonribosomal peptide synthetase encoded by FUM14 catalyzes the formation of tricarballylic esters in the biosynthesis of fumonisins, Biochemistry 45, 2561-2569.
    • (2006) Biochemistry , vol.45 , pp. 2561-2569
    • Zaleta-Rivera, K.1    Xu, C.2    Yu, F.3    Butchko, R.A.4    Proctor, R.H.5    Hidalgo-Lara, M.E.6    Raza, A.7    Dussault, P.H.8    Du, L.9
  • 52
    • 33745905309 scopus 로고    scopus 로고
    • The fumitremorgin gene cluster of Aspergillus fumigatus: Identification of a gene encoding brevianamide F synthetase
    • in press
    • Maiya, S., Grundmann, A., Li, S. M., and Turner, G. (2006) The fumitremorgin gene cluster of Aspergillus fumigatus: identification of a gene encoding brevianamide F synthetase, ChemBioChem (in press).
    • (2006) ChemBioChem
    • Maiya, S.1    Grundmann, A.2    Li, S.M.3    Turner, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.