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Volumn 312, Issue 1, 2003, Pages 223-228

Bacterial (CYP101) and mitochondrial P450 systems - How comparable are they?

Author keywords

Adrenodoxin; CYP101; CYP11A1; Protein protein interaction; Putidaredoxin

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME P450; FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; ISOENZYME; MITOCHONDRIAL PROTEIN; OXIDOREDUCTASE;

EID: 0345257882     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.214     Document Type: Article
Times cited : (22)

References (48)
  • 2
    • 0017295461 scopus 로고
    • Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam
    • Lipscomb J.D., Sligar S.G., Namtvedt M.J., Gunsalus I.C. Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. J. Biol. Chem. 251:1976;1116-1124.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1116-1124
    • Lipscomb, J.D.1    Sligar, S.G.2    Namtvedt, M.J.3    Gunsalus, I.C.4
  • 3
    • 0015523673 scopus 로고
    • The role of putidaredoxin and P450 cam in methylene hydroxylation
    • Tyson C.A., Lipscomb J.D., Gunsalus I.C. The role of putidaredoxin and P450 cam in methylene hydroxylation. J. Biol. Chem. 247:1972;5777-5784.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5777-5784
    • Tyson, C.A.1    Lipscomb, J.D.2    Gunsalus, I.C.3
  • 4
    • 0026760514 scopus 로고
    • Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors
    • Bernhardt R., Gunsalus I.C. Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors. Biochem. Biophys. Res. Commun. 187:1992;310-317.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 310-317
    • Bernhardt, R.1    Gunsalus, I.C.2
  • 5
    • 0344842411 scopus 로고
    • Heterologous reconstitution of cytochrome P-450LM2 activity with bacterial electron transfer systems. Cytochrome P-450
    • L. Vereczky, & K. Magyar. Budapest: Akademia Kiado
    • Bernhardt R., Gunsalus I.C. Heterologous reconstitution of cytochrome P-450LM2 activity with bacterial electron transfer systems. Cytochrome P-450. Vereczky L., Magyar K. Biochemistry, Biophysics and Induction. 1985;159-162 Akademia Kiado, Budapest.
    • (1985) Biochemistry, Biophysics and Induction , pp. 159-162
    • Bernhardt, R.1    Gunsalus, I.C.2
  • 6
    • 0005162541 scopus 로고
    • Redox dynamics in P450cam-Putidaredoxin complexes
    • V. Ullrich. Oxford: Pergamon Press
    • Pederson T.C., Austin R.H., Gunsalus I.C. Redox dynamics in P450cam-Putidaredoxin complexes. Ullrich V. Microsomes and Drug Oxidations. 1977;275-283 Pergamon Press, Oxford.
    • (1977) Microsomes and Drug Oxidations , pp. 275-283
    • Pederson, T.C.1    Austin, R.H.2    Gunsalus, I.C.3
  • 7
    • 0019877147 scopus 로고
    • The kinetics of reduction of cytochrome P-450cam by reduced putidaredoxin
    • Hintz M.J., Peterson J.A. The kinetics of reduction of cytochrome P-450cam by reduced putidaredoxin. J. Biol. Chem. 256:1981;6721-6728.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6721-6728
    • Hintz, M.J.1    Peterson, J.A.2
  • 8
    • 0022273753 scopus 로고
    • Cytochrome P-450scc-adrenodoxin interactions. Ionic effects on binding, and regulation of cytochrome reduction by bound steroid substrates
    • Lambeth J.D., Kriengsiri S. Cytochrome P-450scc-adrenodoxin interactions. Ionic effects on binding, and regulation of cytochrome reduction by bound steroid substrates. J. Biol. Chem. 260:1985;8810-8816.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8810-8816
    • Lambeth, J.D.1    Kriengsiri, S.2
  • 9
    • 0035965284 scopus 로고    scopus 로고
    • The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011beta). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin
    • Schiffler B., Kiefer M., Wilken A., Hannemann F., Adolph H.W., Bernhardt R. The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011beta). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin. J. Biol. Chem. 276:2001;36225-36232.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36225-36232
    • Schiffler, B.1    Kiefer, M.2    Wilken, A.3    Hannemann, F.4    Adolph, H.W.5    Bernhardt, R.6
  • 10
    • 0026496878 scopus 로고
    • Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands
    • Uhlmann H., Beckert V., Schwarz D., Bernhardt R. Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands. Biochem. Biophys. Res. Commun. 188:1992;1131-1138.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1131-1138
    • Uhlmann, H.1    Beckert, V.2    Schwarz, D.3    Bernhardt, R.4
  • 11
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H., Kraft R., Bernhardt R. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J. Biol. Chem. 269:1994;22557-22564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 12
    • 0029560248 scopus 로고
    • The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function
    • Uhlmann H., Bernhardt R. The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function. J. Biol. Chem. 270:1995;29959-29966.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29959-29966
    • Uhlmann, H.1    Bernhardt, R.2
  • 13
    • 0030864409 scopus 로고    scopus 로고
    • Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the protein
    • Uhlmann H., Iametti S., Vecchio G., Bonomi F., Bernhardt R. Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the protein. Eur. J. Biochem. 248:1997;897-902.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 897-902
    • Uhlmann, H.1    Iametti, S.2    Vecchio, G.3    Bonomi, F.4    Bernhardt, R.5
  • 14
    • 0027980825 scopus 로고
    • Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer
    • Beckert V., Dettmer R., Bernhardt R. Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer. J. Biol. Chem. 269:1994;2568-2573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2568-2573
    • Beckert, V.1    Dettmer, R.2    Bernhardt, R.3
  • 15
    • 0031053908 scopus 로고    scopus 로고
    • Specific aspects of electron transfer from adrenodoxin to cytochromes P450scc and P45011beta
    • Beckert V., Bernhardt R. Specific aspects of electron transfer from adrenodoxin to cytochromes P450scc and P45011beta. J. Biol. Chem. 272:1997;4883-4888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4883-4888
    • Beckert, V.1    Bernhardt, R.2
  • 16
    • 0025049895 scopus 로고
    • Putidaredoxin reduction of cytochrome P450cam dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid
    • Davies M.D., Quin L., Beck J.L., Suslick K.S., Koga H., Horiuchi T., Sligar S.G. Putidaredoxin reduction of cytochrome P450cam dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid. J. Am. Chem. Soc. 112:1990;7396-7398.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7396-7398
    • Davies, M.D.1    Quin, L.2    Beck, J.L.3    Suslick, K.S.4    Koga, H.5    Horiuchi, T.6    Sligar, S.G.7
  • 17
    • 0026442895 scopus 로고
    • Genetic variants in the putidaredoxin-cytochrome P-450cam electron-transfer complex: Identification of the residue responsible for redox-state-dependent conformers
    • Davies M.D., Sligar S.G. Genetic variants in the putidaredoxin- cytochrome P-450cam electron-transfer complex: identification of the residue responsible for redox-state-dependent conformers. Biochemistry. 31:1992;11383-11389.
    • (1992) Biochemistry , vol.31 , pp. 11383-11389
    • Davies, M.D.1    Sligar, S.G.2
  • 18
    • 0028307538 scopus 로고
    • An NMR-derived model for the solution structure of oxidized putidaredoxin, a [2Fe-2S] ferredoxin from Pseudomonas putida
    • Pochapsky T.C., Ye X.M., Ratnaswamy G., Lyons T.A. An NMR-derived model for the solution structure of oxidized putidaredoxin, a [2Fe-2S] ferredoxin from Pseudomonas putida. Biochemistry. 33:1994;6424-6432.
    • (1994) Biochemistry , vol.33 , pp. 6424-6432
    • Pochapsky, T.C.1    Ye, X.M.2    Ratnaswamy, G.3    Lyons, T.A.4
  • 19
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
    • Müller A., Müller J.J., Müller Y.A., Uhlmann H., Bernhardt R., Heinemann U. New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure. 6:1998;269-280.
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.J.2    Müller, Y.A.3    Uhlmann, H.4    Bernhardt, R.5    Heinemann, U.6
  • 20
    • 0037172776 scopus 로고    scopus 로고
    • A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of Adrenodoxin
    • Beilke D., Weiß R., Löhr F., Pristovsek P., Hannemann F., Bernhardt R., Rüterjans H. A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of Adrenodoxin. Biochemistry. 41:2002;7969-7978.
    • (2002) Biochemistry , vol.41 , pp. 7969-7978
    • Beilke, D.1    Weiß, R.2    Löhr, F.3    Pristovsek, P.4    Hannemann, F.5    Bernhardt, R.6    Rüterjans, H.7
  • 21
    • 0033979988 scopus 로고    scopus 로고
    • The tertiary structure of full-length bovine adrenodoxin suggests functional dimers
    • Pikuleva I.A., Tesh K., Waterman M.R., Kim Y. The tertiary structure of full-length bovine adrenodoxin suggests functional dimers. Arch. Biochem. Biophys. 373:2000;44-55.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 44-55
    • Pikuleva, I.A.1    Tesh, K.2    Waterman, M.R.3    Kim, Y.4
  • 22
    • 0033057396 scopus 로고    scopus 로고
    • The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis
    • Ziegler G.A., Vonrhein C., Hanukoglu I., Schulz G.E. The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. J. Mol. Biol. 289:1999;981-990.
    • (1999) J. Mol. Biol. , vol.289 , pp. 981-990
    • Ziegler, G.A.1    Vonrhein, C.2    Hanukoglu, I.3    Schulz, G.E.4
  • 23
    • 0034641677 scopus 로고    scopus 로고
    • Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family
    • Ziegler G.A., Schulz G.E. Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family. Biochemistry. 39:2000;10986-10995.
    • (2000) Biochemistry , vol.39 , pp. 10986-10995
    • Ziegler, G.A.1    Schulz, G.E.2
  • 24
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis
    • Muller J.J., Lapko A., Bourenkov G., Ruckpaul K., Heinemann U. Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. J. Biol. Chem. 276:2001;2786-2789.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2786-2789
    • Muller, J.J.1    Lapko, A.2    Bourenkov, G.3    Ruckpaul, K.4    Heinemann, U.5
  • 25
    • 85030949441 scopus 로고    scopus 로고
    • Putidaredoxin and putidaredoxin reductase: Finally crystal clear
    • University of California, Los Angeles, USA, August 20-25
    • I.F. Sevrioukova, T.L. Poulos, Putidaredoxin and putidaredoxin reductase: finally crystal clear, in: Sixth International Symposium on Cytochrome P450 Biodiversity, University of California, Los Angeles, USA, August 20-25, 2002.
    • (2002) Sixth International Symposium on Cytochrome P450 Biodiversity
    • Sevrioukova, I.F.1    Poulos, T.L.2
  • 27
  • 28
    • 0035893679 scopus 로고    scopus 로고
    • Modelling of three-dimensional structures of cytochromes P450 11B1 and 11B2
    • Belkina N.V., Lisurek M., Ivanov A.S., Bernhardt R. Modelling of three-dimensional structures of cytochromes P450 11B1 and 11B2. J. Inorg. Biochem. 87:2001;197-207.
    • (2001) J. Inorg. Biochem. , vol.87 , pp. 197-207
    • Belkina, N.V.1    Lisurek, M.2    Ivanov, A.S.3    Bernhardt, R.4
  • 29
    • 0033630119 scopus 로고    scopus 로고
    • Molecular modeling of mammalian cytochromes P450: Application to study enzyme function
    • Szklarz G.D., Graham S.E., Paulsen M.D. Molecular modeling of mammalian cytochromes P450: application to study enzyme function. Vitam. Horm. 58:2000;53-87.
    • (2000) Vitam. Horm. , vol.58 , pp. 53-87
    • Szklarz, G.D.1    Graham, S.E.2    Paulsen, M.D.3
  • 30
    • 0017847807 scopus 로고
    • Two univalent electron transfers from putidaredoxin to bacterial cytochrome P450 at subzero temperature
    • Hoa G.H., Begard E., Debey P., Gunsalus I.C. Two univalent electron transfers from putidaredoxin to bacterial cytochrome P450 at subzero temperature. Biochemistry. 17:1978;2835-2839.
    • (1978) Biochemistry , vol.17 , pp. 2835-2839
    • Hoa, G.H.1    Begard, E.2    Debey, P.3    Gunsalus, I.C.4
  • 31
    • 0018803839 scopus 로고
    • Proton coupling in the cytochrome P-450 spin and redox equilibria
    • Sligar S.G., Gunsalus I.C. Proton coupling in the cytochrome P-450 spin and redox equilibria. Biochemistry. 18:1979;2290-2295.
    • (1979) Biochemistry , vol.18 , pp. 2290-2295
    • Sligar, S.G.1    Gunsalus, I.C.2
  • 32
    • 0345705424 scopus 로고
    • Molecular recognition by cytochrome P450cam: Substrate specificity, catalysis and electron transfer
    • K. Ruckpaul, & H. Rein. Berlin: Akademie-Verlag
    • Martinis S.A., Ropp J.D., Sligar S.G., Gunsalus I.C. Molecular recognition by cytochrome P450cam: substrate specificity, catalysis and electron transfer. Ruckpaul K., Rein H. Frontiers in Biotransformation. 1990;54-86 Akademie-Verlag, Berlin.
    • (1990) Frontiers in Biotransformation , pp. 54-86
    • Martinis, S.A.1    Ropp, J.D.2    Sligar, S.G.3    Gunsalus, I.C.4
  • 33
    • 0018291970 scopus 로고
    • Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle
    • Lambeth J.D., Seybert D.W., Kamin H. Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. J. Biol. Chem. 254:1979;7255-7264.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7255-7264
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 34
    • 0030457189 scopus 로고    scopus 로고
    • A structure-based model for cytochrome P450cam-putidaredoxin interactions
    • Pochapsky T.C., Lyons T.A., Kazanis S., Arakaki T., Ratnaswamy G. A structure-based model for cytochrome P450cam-putidaredoxin interactions. Biochimie. 78:1996;723-733.
    • (1996) Biochimie , vol.78 , pp. 723-733
    • Pochapsky, T.C.1    Lyons, T.A.2    Kazanis, S.3    Arakaki, T.4    Ratnaswamy, G.5
  • 35
    • 0030869074 scopus 로고    scopus 로고
    • Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues
    • Holden M., Mayhew M., Bunk D., Roitberg A., Vilker V. Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues. J. Biol. Chem. 272:1997;21720-21725.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21720-21725
    • Holden, M.1    Mayhew, M.2    Bunk, D.3    Roitberg, A.4    Vilker, V.5
  • 37
    • 0027284228 scopus 로고
    • Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations
    • Brandt M.E., Vickery L.E. Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations. J. Biol. Chem. 268:1993;17126-17130.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17126-17130
    • Brandt, M.E.1    Vickery, L.E.2
  • 38
    • 0031022337 scopus 로고    scopus 로고
    • Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems
    • Vickery L.E. Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems. Steroids. 62:1997;124-127.
    • (1997) Steroids , vol.62 , pp. 124-127
    • Vickery, L.E.1
  • 39
    • 0021135839 scopus 로고
    • Adrenodoxin interaction with adrenodoxin reductase and cytochrome P- 450scc. Cross-linking of protein complexes and effects of adrenodoxin modification by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
    • Lambeth J.D., Geren L.M., Millett F. Adrenodoxin interaction with adrenodoxin reductase and cytochrome P- 450scc. Cross-linking of protein complexes and effects of adrenodoxin modification by 1-ethyl-3-(3- dimethylaminopropyl)carbodiimide. J. Biol. Chem. 259:1984;10025-10029.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10025-10029
    • Lambeth, J.D.1    Geren, L.M.2    Millett, F.3
  • 40
    • 0021351056 scopus 로고
    • Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase
    • Geren L.M., O'Brien P., Stonehuerner J., Millett F. Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase. J. Biol. Chem. 259:1984;2155-2160.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2155-2160
    • Geren, L.M.1    O'brien, P.2    Stonehuerner, J.3    Millett, F.4
  • 41
    • 0026488375 scopus 로고
    • Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
    • Wada A., Waterman M.R. Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J. Biol. Chem. 267:1992;22877-22882.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22877-22882
    • Wada, A.1    Waterman, M.R.2
  • 42
    • 0029073959 scopus 로고
    • Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications
    • Beckert V., Schrauber H., Bernhardt R., Van Dijk A.A., Kakoschke C., Wray V. Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications. Eur. J. Biochem. 231:1995;226-235.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 226-235
    • Beckert, V.1    Schrauber, H.2    Bernhardt, R.3    Van Dijk, A.A.4    Kakoschke, C.5    Wray, V.6
  • 43
    • 0037489446 scopus 로고    scopus 로고
    • A conserved histidine in vertebrate-type ferredoxin is critical for redox-dependent dynamics
    • Kostic M., Bernhardt R., Pochapsky T.C. A conserved histidine in vertebrate-type ferredoxin is critical for redox-dependent dynamics. Biochemistry. 42:2003;8171-8182.
    • (2003) Biochemistry , vol.42 , pp. 8171-8182
    • Kostic, M.1    Bernhardt, R.2    Pochapsky, T.C.3
  • 45
    • 0035846906 scopus 로고    scopus 로고
    • The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners
    • Hannemann F., Rottmann M., Schiffler B., Zapp J., Bernhardt R. The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners. J. Biol. Chem. 276:2001;1369-1375.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1369-1375
    • Hannemann, F.1    Rottmann, M.2    Schiffler, B.3    Zapp, J.4    Bernhardt, R.5
  • 47
    • 0032500339 scopus 로고    scopus 로고
    • Binding and electron transfer between putidaredoxin and cytochrome P450cam. Theory and experiments
    • Roitberg A., Holden M., Mayhew M., Kurnikov I.V., Beratan D.N., Vilker V. Binding and electron transfer between putidaredoxin and cytochrome P450cam. Theory and experiments. J. Am. Chem. Soc. 120:1998;8927-8932.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8927-8932
    • Roitberg, A.1    Holden, M.2    Mayhew, M.3    Kurnikov, I.V.4    Beratan, D.N.5    Vilker, V.6


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