메뉴 건너뛰기




Volumn 15, Issue 3, 2004, Pages 1356-1363

Mitochondrial Localization of the Mevalonate Pathway Enzyme 3-Hydroxy-3-methyl-glutaryl-CoA Reductase in the Trypanosomatidae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIGITONIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVALONIC ACID;

EID: 1542373737     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-10-0720     Document Type: Article
Times cited : (40)

References (50)
  • 1
    • 0023506415 scopus 로고
    • Identifying mutations in duplicated functions in Saccharomyces cerevisiae: Recessive mutations in HMG-CoA reductase genes
    • Basson, M.E., Moore, R.L., O'Rear, J., and Rine, J. (1987). Identifying mutations in duplicated functions in Saccharomyces cerevisiae: recessive mutations in HMG-CoA reductase genes. Genetics 117, 645-655.
    • (1987) Genetics , vol.117 , pp. 645-655
    • Basson, M.E.1    Moore, R.L.2    O'Rear, J.3    Rine, J.4
  • 2
    • 1442283623 scopus 로고
    • Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl Coenzyme A reductase
    • Basson, M.E., Thorsness, M., and Rine, J. (1986). Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl Coenzyme A reductase. Proc. Natl. Acad. Sci. USA 83, 5563-5567.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5563-5567
    • Basson, M.E.1    Thorsness, M.2    Rine, J.3
  • 3
    • 0025850305 scopus 로고
    • The YDp plasmids: A uniform set of vectors bearing versatile gene disruption cassettes for Saccharomyces cerevisiae
    • Berben, G., Dumont, J., Gilliquet, V., Bolle, P.A., and Hilger, F. (1991). The YDp plasmids: a uniform set of vectors bearing versatile gene disruption cassettes for Saccharomyces cerevisiae. Yeast 7, 475-477.
    • (1991) Yeast , vol.7 , pp. 475-477
    • Berben, G.1    Dumont, J.2    Gilliquet, V.3    Bolle, P.A.4    Hilger, F.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 131, 499-503.
    • (1976) Anal. Biochem. , vol.131 , pp. 499-503
    • Bradford, M.M.1
  • 5
    • 0028999123 scopus 로고
    • Characterization of two nuclear-encoded protein components of mitochondrial ribonucleoprotein complexes from Leishmania tarentolae
    • Bringaud, F., Peris, M., Zen, K.H., and Simpson, L. (1995). Characterization of two nuclear-encoded protein components of mitochondrial ribonucleoprotein complexes from Leishmania tarentolae. Mol. Biochem. Parasitol. 71, 65-69.
    • (1995) Mol. Biochem. Parasitol. , vol.71 , pp. 65-69
    • Bringaud, F.1    Peris, M.2    Zen, K.H.3    Simpson, L.4
  • 6
    • 0025806193 scopus 로고
    • Characterization of pyruvate kinase of Trypanosoma brucei and its role in the regulation of carbohydrate metabolism
    • Callens, M., Kuntz, D.A., and Opperdoes, F.R. (1991). Characterization of pyruvate kinase of Trypanosoma brucei and its role in the regulation of carbohydrate metabolism. Mol. Biochem. Parasitol. 47, 19-29.
    • (1991) Mol. Biochem. Parasitol. , vol.47 , pp. 19-29
    • Callens, M.1    Kuntz, D.A.2    Opperdoes, F.R.3
  • 7
    • 0021287730 scopus 로고
    • Glycosomal and mitochondrial malate dehydrogenases in epimastigotes of Trypanosoma cruzi
    • Cannata, J.J.B., and Cazzulo, J.J. (1984). Glycosomal and mitochondrial malate dehydrogenases in epimastigotes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 11, 37-49.
    • (1984) Mol. Biochem. Parasitol. , vol.11 , pp. 37-49
    • Cannata, J.J.B.1    Cazzulo, J.J.2
  • 8
    • 0029166451 scopus 로고
    • Protein trafficking in kineto-plastid protozoa
    • Clayton, C., Häusler T., and Blattner, J. (1995). Protein trafficking in kineto-plastid protozoa. Microbiol. Rev. 59, 325-344.
    • (1995) Microbiol. Rev. , vol.59 , pp. 325-344
    • Clayton, C.1    Häusler, T.2    Blattner, J.3
  • 10
    • 0032052932 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methyl-glutaryl-CoA reductase in Trypanosoma (Schizotrypanum) cruzi: Subcellular localization and kinetic properties
    • Concepción, J.L., González-Pacanowska, D., and Urbina, J.A. (1998). 3-Hydroxy-3-methyl-glutaryl-CoA reductase in Trypanosoma (Schizotrypanum) cruzi: subcellular localization and kinetic properties. Arch. Biochem. Biophys. 352, 114-120.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 114-120
    • Concepción, J.L.1    González-Pacanowska, D.2    Urbina, J.A.3
  • 11
    • 0028795713 scopus 로고
    • Activity, pharmacological inhibition and biological regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Trypanosoma brucei
    • Coppens, I., Bastin, P., Levade, T., and Courtoy, P.J. (1995). Activity, pharmacological inhibition and biological regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Trypanosoma brucei. Mol. Biochem. Parasitol. 69, 29-40.
    • (1995) Mol. Biochem. Parasitol. , vol.69 , pp. 29-40
    • Coppens, I.1    Bastin, P.2    Levade, T.3    Courtoy, P.J.4
  • 12
    • 0002360092 scopus 로고    scopus 로고
    • Chemotherapy of human Leishmaniasis and Trypanosomiasis
    • ed. G. Hide, J.C. Mottram, G.H. Coombs, and P.H. Holmes. Wallingford, United Kingdom: CAB International
    • Croft, S.L., Urbina, J.A., and Brun, R. (1997). Chemotherapy of human Leishmaniasis and Trypanosomiasis. In: Trypanosomiasis and Leishmaniasis; Biology and Control, ed. G. Hide, J.C. Mottram, G.H. Coombs, and P.H. Holmes. Wallingford, United Kingdom: CAB International, 245-258.
    • (1997) Trypanosomiasis and Leishmaniasis; Biology and Control , pp. 245-258
    • Croft, S.L.1    Urbina, J.A.2    Brun, R.3
  • 13
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast
    • Daum, G., Bohni, P.C., and Schatz, G. (1982). Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 14
    • 0021315215 scopus 로고
    • Cell biology of Trypanosoma cruzi
    • De Souza, W. (1984). Cell biology of Trypanosoma cruzi. Int. Rev. Cytol. 86, 197-282.
    • (1984) Int. Rev. Cytol. , vol.86 , pp. 197-282
    • De Souza, W.1
  • 15
    • 0033256023 scopus 로고    scopus 로고
    • A short review on the morphology of Trypanosoma cruzi: From 1909 to 1999
    • De Souza, W. (1999). "A short review on the morphology of Trypanosoma cruzi: from 1909 to 1999." Mem. Inst. Oswaldo Cruz. 94, 17-36.
    • (1999) Mem. Inst. Oswaldo Cruz , vol.94 , pp. 17-36
    • De Souza, W.1
  • 16
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • Edwards, P.A., and Ericsson, J. (1999). Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway. Annu. Rev. Biochem. 68, 157-185.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 17
    • 0024415802 scopus 로고
    • Multiple drug resistance and conservative amplification of the H region in Leishmania major
    • Ellenberg, T.E., and Beverley, S.M. (1989). Multiple drug resistance and conservative amplification of the H region in Leishmania major. J. Biol. Chem. 264, 15094-15103.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15094-15103
    • Ellenberg, T.E.1    Beverley, S.M.2
  • 19
    • 0027755498 scopus 로고
    • HMG-CoA reductase inhibitors
    • Endo, A., and Hasumi, K. (1993). HMG-CoA reductase inhibitors. Nat. Prod. Rep. 10, 541-50.
    • (1993) Nat. Prod. Rep. , vol.10 , pp. 541-550
    • Endo, A.1    Hasumi, K.2
  • 20
    • 0022458573 scopus 로고
    • Stable amplified DNA in drug-resistant Leishmania exists as extrachromosomal circles
    • Garvey, E.P., and Santi, D.V. (1986). Stable amplified DNA in drug-resistant Leishmania exists as extrachromosomal circles. Science 233, 535-540.
    • (1986) Science , vol.233 , pp. 535-540
    • Garvey, E.P.1    Santi, D.V.2
  • 21
    • 0027751894 scopus 로고
    • The in-vitro anti-leishmanial activity of inhibitors of ergosterol biosynthesis
    • Gebre-Hiwot, A., and Frommel, D. (1993). The in-vitro anti-leishmanial activity of inhibitors of ergosterol biosynthesis. J. Antimicrob. Chemother. 32, 873-842.
    • (1993) J. Antimicrob. Chemother. , vol.32 , pp. 873-842
    • Gebre-Hiwot, A.1    Frommel, D.2
  • 23
    • 0034111424 scopus 로고    scopus 로고
    • Utilization of leucine and acetate as carbon sources for sterol and fatty acid biosynthesis by Old and New World Leishmania species, Endotrypanum monterogeii and Trypanosoma cruzi
    • Ginger, M.L., Prescott, M.C., Reynolds, D.G., Chance, M.L., and Goad, L.J. (2000). Utilization of leucine and acetate as carbon sources for sterol and fatty acid biosynthesis by Old and New World Leishmania species, Endotrypanum monterogeii and Trypanosoma cruzi. Eur. J. Biochem. 267, 2555-2566.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2555-2566
    • Ginger, M.L.1    Prescott, M.C.2    Reynolds, D.G.3    Chance, M.L.4    Goad, L.J.5
  • 24
    • 0033199769 scopus 로고    scopus 로고
    • Elucidation of carbon sources used for the biosynthesis of fatty acids and sterol in the trypanosomatid Leishmania mexicana
    • Ginger, M. L., Chance, M.L., and Goad, L.J. (1999). Elucidation of carbon sources used for the biosynthesis of fatty acids and sterol in the trypanosomatid Leishmania mexicana. Biochem. J. 342, 397-405.
    • (1999) Biochem. J. , vol.342 , pp. 397-405
    • Ginger, M.L.1    Chance, M.L.2    Goad, L.J.3
  • 25
    • 0035853715 scopus 로고    scopus 로고
    • The biosynthetic incorporation of the intact leucine skeleton into sterol by the trypanosomatid Leishmania mexicana
    • Ginger, M.L., Chance, M.L., Sadler, I.H., and Goad, L.J. (2001). The biosynthetic incorporation of the intact leucine skeleton into sterol by the trypanosomatid Leishmania mexicana. J. Biol. Chem. 276, 11674-82.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11674-11682
    • Ginger, M.L.1    Chance, M.L.2    Sadler, I.H.3    Goad, L.J.4
  • 26
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J.L. and Brown, M.S. (1990). Regulation of the mevalonate pathway. Nature 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 27
    • 0029917248 scopus 로고    scopus 로고
    • The biology of HMG-CoA reductase: The pros of contra-regulation
    • Hampton, R., Dimster-Denk, D., and Rine, J. (1996). The biology of HMG-CoA reductase: the pros of contra-regulation. Trends Biochem. Sci. 21, 140-145.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 140-145
    • Hampton, R.1    Dimster-Denk, D.2    Rine, J.3
  • 28
    • 0030063301 scopus 로고    scopus 로고
    • In vitro import of proteins into mitochondria of Trypanosoma brucei and Leishmanía tarentolae
    • Hauser, R., Pypaert, M., Häusler, T., Horn, E.K., and Schneider, A. (1996). In vitro import of proteins into mitochondria of Trypanosoma brucei and Leishmanía tarentolae. J. Cell Sci. 109, 517-523.
    • (1996) J. Cell Sci. , vol.109 , pp. 517-523
    • Hauser, R.1    Pypaert, M.2    Häusler, T.3    Horn, E.K.4    Schneider, A.5
  • 29
    • 0030612496 scopus 로고    scopus 로고
    • Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma, and Trichomonas
    • Häusler, T., Stierhof, Y.D., Blattner, J., and Clayton, C. (1997). Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma, and Trichomonas. Eur. J. Cell Biol. 73, 240-251.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 240-251
    • Häusler, T.1    Stierhof, Y.D.2    Blattner, J.3    Clayton, C.4
  • 30
    • 0033949781 scopus 로고    scopus 로고
    • Localisation of a 3-hydroxy-3-methylglutaryl-Coenzyme A reductase in the mitochondrial matrix of Trypanosoma brucei procyclics
    • Heise, H., and Opperdoes, F.R. (2000). Localisation of a 3-hydroxy-3-methylglutaryl-Coenzyme A reductase in the mitochondrial matrix of Trypanosoma brucei procyclics. Z. Naturforsch. 55, 473-477.
    • (2000) Z. Naturforsch. , vol.55 , pp. 473-477
    • Heise, H.1    Opperdoes, F.R.2
  • 31
    • 0242659786 scopus 로고    scopus 로고
    • Mitochondrial targeting and import
    • ed. D. A. Phoenix, London: Portland Press Ltd.
    • Hovius, R. (1998). Mitochondrial targeting and import. In: Protein Targeting and Translocation, ed. D. A. Phoenix, London: Portland Press Ltd., XII: 231-244.
    • (1998) Protein Targeting and Translocation , vol.12 , pp. 231-244
    • Hovius, R.1
  • 32
    • 0023030829 scopus 로고
    • 3-hydroxy-3-methylglutaryl-coenzyme A reductase localization in rat liver peroxisomes and microsomes of control and cholestyramine-treated animals: Quantitative biochemical and inmunoelectron microscopical analyses
    • Keller, G.A., Pazirandeh, M., and Krisans, S. (1986). 3-hydroxy-3-methylglutaryl-coenzyme A reductase localization in rat liver peroxisomes and microsomes of control and cholestyramine-treated animals: quantitative biochemical and inmunoelectron microscopical analyses. J. Cell Biol. 103, 875-886.
    • (1986) J. Cell Biol. , vol.103 , pp. 875-886
    • Keller, G.A.1    Pazirandeh, M.2    Krisans, S.3
  • 33
    • 0027274006 scopus 로고
    • Experimental chemotherapy with combinations of ergosterol biosynthesis inhibitors in murine models of Chagas' disease
    • Maldonado, R.A., Molina, J., Payares, G., and Urbina, J.A. (1993). Experimental chemotherapy with combinations of ergosterol biosynthesis inhibitors in murine models of Chagas' disease. Antimicrob. Agents Chemother. 37, 1353-1359.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1353-1359
    • Maldonado, R.A.1    Molina, J.2    Payares, G.3    Urbina, J.A.4
  • 34
    • 0343416375 scopus 로고    scopus 로고
    • pRIBOTEX expression vector: A pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants
    • Martínez-Calvillo, S., Lopez, I., and Hernandez, R. (1997). pRIBOTEX expression vector: a pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants. Gene 199, 71-76.
    • (1997) Gene , vol.199 , pp. 71-76
    • Martínez-Calvillo, S.1    Lopez, I.2    Hernandez, R.3
  • 35
  • 36
    • 0027453012 scopus 로고
    • Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth in glucose
    • Navas, M.A., Cerdán, S., and Gancedo, J.M. (1993). Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth in glucose. Proc. Natl. Acad. Sci. USA 90, 1290-1294.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1290-1294
    • Navas, M.A.1    Cerdán, S.2    Gancedo, J.M.3
  • 37
    • 0034672695 scopus 로고    scopus 로고
    • Peroxisomal protein targeting and identification of peroxisomal targeting signals in cholesterol biosynthesis enzymes
    • Olivier, L.M., and Krisans, S.K. (2000). Peroxisomal protein targeting and identification of peroxisomal targeting signals in cholesterol biosynthesis enzymes. Biochim. Biophys. Acta 1529, 89-102.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 89-102
    • Olivier, L.M.1    Krisans, S.K.2
  • 38
    • 0028070305 scopus 로고
    • Autonomous replication of bacterial DNA plasmid oligomers in Leishmania
    • Papadopoulou, B., Roy, G., and Ouellette, M. (1994). Autonomous replication of bacterial DNA plasmid oligomers in Leishmania. Mol. Biochem. Parasitol. 65, 39-49.
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 39-49
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 39
    • 0028864187 scopus 로고
    • Identification of the sequences in HMG-CoA reductase required for karmellae assembly
    • Parrish, M.L., Sengstag, C., Rine, J.D., and Wright, R.L. (1995). Identification of the sequences in HMG-CoA reductase required for karmellae assembly. Mol. Biol. Cell 6, 1535-1547.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1535-1547
    • Parrish, M.L.1    Sengstag, C.2    Rine, J.D.3    Wright, R.L.4
  • 41
    • 0029077985 scopus 로고
    • The significance of the cholesterol biosynthetic pathway in cell growth and carcinogenesis
    • Rao, K.N. (1995). The significance of the cholesterol biosynthetic pathway in cell growth and carcinogenesis. Anticancer Res. 15, 309-314.
    • (1995) Anticancer Res. , vol.15 , pp. 309-314
    • Rao, K.N.1
  • 42
    • 0034806092 scopus 로고    scopus 로고
    • The sterol composition of Trypanosoma cruzi changes after growth in different culture media and results in different sensitivity to digitonin-permeabilization
    • Rodrigues, C.O., Catisti, R., Uyemura, S.A., Vercesi, A.E., Lira, R., Rodriguez, C., Urbina, J.A., and Docampo, R. (2001). The sterol composition of Trypanosoma cruzi changes after growth in different culture media and results in different sensitivity to digitonin-permeabilization. J. Eukaryot. Microbiol. 48, 588-594.
    • (2001) J. Eukaryot. Microbiol. , vol.48 , pp. 588-594
    • Rodrigues, C.O.1    Catisti, R.2    Uyemura, S.A.3    Vercesi, A.E.4    Lira, R.5    Rodriguez, C.6    Urbina, J.A.7    Docampo, R.8
  • 43
    • 0027319703 scopus 로고
    • Testis and ovary express the gene for ketogenic mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase
    • Royo, T., Pedragosa, M.J., Ayte, J., Gil-Gomez, G., Vilaro, S., and Hegardt, F.G. (1993). Testis and ovary express the gene for ketogenic mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. J. Lipid Res. 34, 867-874.
    • (1993) J. Lipid Res. , vol.34 , pp. 867-874
    • Royo, T.1    Pedragosa, M.J.2    Ayte, J.3    Gil-Gomez, G.4    Vilaro, S.5    Hegardt, F.G.6
  • 44
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini, J.C., and Poulter, C.D. (1997). Creating isoprenoid diversity. Science 277, 1788-1789.
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 45
    • 0027267007 scopus 로고
    • Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major
    • Searle, S., McCrossan, M.V., and Smith, D.F. (1993). Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major. J. Cell Sci. 104, 1091-1000.
    • (1993) J. Cell Sci. , vol.104 , pp. 1091-1000
    • Searle, S.1    McCrossan, M.V.2    Smith, D.F.3
  • 47
    • 0030921232 scopus 로고    scopus 로고
    • Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites
    • Urbina, J.A. (1997). Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites. Parasitology 114, 91-99.
    • (1997) Parasitology , vol.114 , pp. 91-99
    • Urbina, J.A.1
  • 48
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R., and Philippsenm, P. (1994). New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsenm, P.4
  • 49
    • 0024388570 scopus 로고
    • Transmission electron microscopy and inmmunocytochemicaI studies of yeast: Analysis of HMG-CoA reductase overproduction by electron microscopy
    • Wright, R., and Rine, J. (1989). Transmission electron microscopy and inmmunocytochemicaI studies of yeast: analysis of HMG-CoA reductase overproduction by electron microscopy. Methods Cell Biol. 31, 473-512.
    • (1989) Methods Cell Biol. , vol.31 , pp. 473-512
    • Wright, R.1    Rine, J.2
  • 50
    • 0027499503 scopus 로고
    • Isolation of proteins associated with kinetoplast DNA networks in vivo
    • Xu, C., and Ray, D.S. (1993). Isolation of proteins associated with kinetoplast DNA networks in vivo. Proc. Natl. Acad. Sci. 90, 1786-1789.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 1786-1789
    • Xu, C.1    Ray, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.