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Volumn 49, Issue 16, 2010, Pages 3412-3419

P450cam visits an open conformation in the absence of substrate

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CONFORMATIONAL CHANGE; FREE STRUCTURES; OPEN CONFORMATION; PSEUDOMONAS PUTIDA; SOAKING CRYSTALS; X-RAY STRUCTURE;

EID: 77951247090     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100183g     Document Type: Article
Times cited : (119)

References (59)
  • 2
    • 73249132581 scopus 로고    scopus 로고
    • The cytochrome p450 homepage
    • Nelson, D. R. (2009) The cytochrome p450 homepage Hum. Genomics 4, 59-65
    • (2009) Hum. Genomics , vol.4 , pp. 59-65
    • Nelson, D.R.1
  • 3
    • 0022273620 scopus 로고
    • The 2.6-⋯ crystal structure of Pseudomonas putida cytochrome P-450
    • Poulos, T. L., Finzel, B. C., Gunsalus, I. C., Wagner, G. C., and Kraut, J. (1985) The 2.6-⋯ crystal structure of Pseudomonas putida cytochrome P-450 J. Biol. Chem. 260, 16122-16130
    • (1985) J. Biol. Chem. , vol.260 , pp. 16122-16130
    • Poulos, T.L.1    Finzel, B.C.2    Gunsalus, I.C.3    Wagner, G.C.4    Kraut, J.5
  • 4
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T. L., Finzel, B. C., and Howard, A. J. (1987) High-resolution crystal structure of cytochrome P450cam J. Mol. Biol. 195, 687-700
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 5
    • 3943081412 scopus 로고    scopus 로고
    • Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s
    • Pylypenko, O. and Schlichting, I. (2004) Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s Annu. Rev. Biochem. 73, 991-1018
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 991-1018
    • Pylypenko, O.1    Schlichting, I.2
  • 6
    • 27544516024 scopus 로고    scopus 로고
    • Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases
    • Johnson, E. F. and Stout, C. D. (2005) Structural diversity of human xenobiotic-metabolizing cytochrome P450 monooxygenases Biochem. Biophys. Res. Commun. 338, 331-336
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 331-336
    • Johnson, E.F.1    Stout, C.D.2
  • 7
    • 77449094112 scopus 로고    scopus 로고
    • The crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism
    • Annalora, A. J., Goodin, D. B., Hong, W., Zhang, Q., Johnson, E. F., and Stout, C. D. (2009) The crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism J. Mol. Biol. 396, 441-451
    • (2009) J. Mol. Biol. , vol.396 , pp. 441-451
    • Annalora, A.J.1    Goodin, D.B.2    Hong, W.3    Zhang, Q.4    Johnson, E.F.5    Stout, C.D.6
  • 8
    • 70350353089 scopus 로고    scopus 로고
    • Investigating the structural plasticity of a cytochrome P450: Three dimensional structures of P450 EryK and binding to its physiological substrate
    • Savino, C., Montemiglio, L. C., Sciara, G., Miele, A. E., Kendrew, S. G., Jemth, P., Gianni, S., and Vallone, B. (2009) Investigating the structural plasticity of a cytochrome P450: Three dimensional structures of P450 EryK and binding to its physiological substrate J. Biol. Chem. 284, 29170-29179
    • (2009) J. Biol. Chem. , vol.284 , pp. 29170-29179
    • Savino, C.1    Montemiglio, L.C.2    Sciara, G.3    Miele, A.E.4    Kendrew, S.G.5    Jemth, P.6    Gianni, S.7    Vallone, B.8
  • 9
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • Sherman, D. H., Li, S., Yermalitskaya, L. V., Kim, Y., Smith, J. A., Waterman, M. R., and Podust, L. M. (2006) The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae J. Biol. Chem. 281, 26289-26297
    • (2006) J. Biol. Chem. , vol.281 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, L.M.7
  • 10
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H. and Poulos, T. L. (1997) The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid Nat. Struct. Biol. 4, 140-146
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 12
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structure and functional properties
    • Park, S. Y., Yamane, K., Adachi, S., Shiro, Y., Weiss, K. E., Maves, S. A., and Sligar, S. G. (2002) Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structure and functional properties J. Inorg. Biochem. 91, 491-501
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3    Shiro, Y.4    Weiss, K.E.5    Maves, S.A.6    Sligar, S.G.7
  • 13
    • 60849125093 scopus 로고    scopus 로고
    • Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: Conformational flexibility and histidine ligation state
    • Xu, L. H., Fushinobu, S., Ikeda, H., Wakagi, T., and Shoun, H. (2009) Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: Conformational flexibility and histidine ligation state J. Bacteriol. 191, 1211-1219
    • (2009) J. Bacteriol. , vol.191 , pp. 1211-1219
    • Xu, L.H.1    Fushinobu, S.2    Ikeda, H.3    Wakagi, T.4    Shoun, H.5
  • 14
    • 41949110521 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis CYP130: Crystal structure, biophysical characterization, and interactions with antifungal azole drugs
    • Ouellet, H., Podust, L. M., and de Montellano, P. R. O. (2008) Mycobacterium tuberculosis CYP130: Crystal structure, biophysical characterization, and interactions with antifungal azole drugs J. Biol. Chem. 283, 5069-5080
    • (2008) J. Biol. Chem. , vol.283 , pp. 5069-5080
    • Ouellet, H.1    Podust, L.M.2    De Montellano, P.R.O.3
  • 18
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • Poulos, T. L., Finzel, B. C., and Howard, A. J. (1986) Crystal structure of substrate-free Pseudomonas putida cytochrome P-450 Biochemistry 25, 5314-5322
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 19
    • 0021111804 scopus 로고
    • Structural studies of cytochrome P-450 using small angle x-ray scattering
    • Lewis, B. A. and Sligar, S. G. (1983) Structural studies of cytochrome P-450 using small angle x-ray scattering J. Biol. Chem. 258, 3599-3601
    • (1983) J. Biol. Chem. , vol.258 , pp. 3599-3601
    • Lewis, B.A.1    Sligar, S.G.2
  • 20
    • 0028950935 scopus 로고
    • Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450cam spin transition
    • Di Primo, C., Deprez, E., Hoa, G. H., and Douzou, P. (1995) Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450cam spin transition Biophys. J. 68, 2056-2061
    • (1995) Biophys. J. , vol.68 , pp. 2056-2061
    • Di Primo, C.1    Deprez, E.2    Hoa, G.H.3    Douzou, P.4
  • 21
    • 0021832318 scopus 로고
    • High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria
    • Fisher, M. T., Scarlata, S. F., and Sligar, S. G. (1985) High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria Arch. Biochem. Biophys. 240, 456-463
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 456-463
    • Fisher, M.T.1    Scarlata, S.F.2    Sligar, S.G.3
  • 22
    • 0020485740 scopus 로고
    • The pressure-dependence of the spin equilibrium in camphor-bound ferric cytochrome-P-450
    • Hui Bin Hoa, G. and Marden, M. C. (1982) The pressure-dependence of the spin equilibrium in camphor-bound ferric cytochrome-P-450 Eur. J. Biochem. 124, 311-315
    • (1982) Eur. J. Biochem. , vol.124 , pp. 311-315
    • Hui Bin Hoa, G.1    Marden, M.C.2
  • 25
    • 7444264562 scopus 로고    scopus 로고
    • Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires
    • Hays, A. M. A., Dunn, A. R., Chiu, R., Gray, H. B., Stout, C. D., and Goodin, D. B. (2004) Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires J. Mol. Biol. 344, 455-469
    • (2004) J. Mol. Biol. , vol.344 , pp. 455-469
    • Hays, A.M.A.1    Dunn, A.R.2    Chiu, R.3    Gray, H.B.4    Stout, C.D.5    Goodin, D.B.6
  • 26
    • 0031404684 scopus 로고    scopus 로고
    • The dimerization of Pseudomonas putida cytochrome P450cam: Practical consequences and engineering of a monomeric enzyme
    • Nickerson, D. P. and Wong, L. L. (1997) The dimerization of Pseudomonas putida cytochrome P450cam: Practical consequences and engineering of a monomeric enzyme Protein Eng. 10, 1357-1361
    • (1997) Protein Eng. , vol.10 , pp. 1357-1361
    • Nickerson, D.P.1    Wong, L.L.2
  • 28
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: An automated program for molecular replacement J. Appl. Crystallogr. 30, 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr., Sect. D 60, 2126-2132
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D 53, 240-255
    • (1997) Acta Crystallogr., Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0000243829 scopus 로고
    • Procheck-A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck-A program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr., Sect. D 55, 191-205
    • (1999) Acta Crystallogr., Sect. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 36
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism
    • Nagano, S. and Poulos, T. L. (2005) Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism J. Biol. Chem. 280, 31659-31663
    • (2005) J. Biol. Chem. , vol.280 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 37
    • 5644282610 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding
    • Nagano, S., Tosha, T., Ishimori, K., Morishima, I., and Poulos, T. L. (2004) Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding J. Biol. Chem. 279, 42844-42849
    • (2004) J. Biol. Chem. , vol.279 , pp. 42844-42849
    • Nagano, S.1    Tosha, T.2    Ishimori, K.3    Morishima, I.4    Poulos, T.L.5
  • 39
    • 77951240144 scopus 로고    scopus 로고
    • 2D NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates
    • (in press)
    • Lampe, J. N., Brandman, R., Sivaramakrishnan, S., and Ortiz de Montellano, P. R. (2010) 2D NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates, J. Biol. Chem. (in press).
    • (2010) J. Biol. Chem.
    • Lampe, J.N.1    Brandman, R.2    Sivaramakrishnan, S.3    Ortiz De Montellano, P.R.4
  • 40
    • 57149092138 scopus 로고    scopus 로고
    • Ligand-induced conformational heterogeneity of cytochrome P450 CYP119 identified by 2D NMR spectroscopy with the unnatural amino acid (13)C-p-methoxyphenylalanine
    • Lampe, J. N., Floor, S. N., Gross, J. D., Nishida, C. R., Jiang, Y., Trnka, M. J., and Ortiz de Montellano, P. R. (2008) Ligand-induced conformational heterogeneity of cytochrome P450 CYP119 identified by 2D NMR spectroscopy with the unnatural amino acid (13)C-p-methoxyphenylalanine J. Am. Chem. Soc. 130, 16168-16169
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16168-16169
    • Lampe, J.N.1    Floor, S.N.2    Gross, J.D.3    Nishida, C.R.4    Jiang, Y.5    Trnka, M.J.6    Ortiz De Montellano, P.R.7
  • 41
    • 0025264366 scopus 로고
    • Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation
    • Di Primo, C., Hui Bon Hoa, G., Douzou, P., and Sligar, S. (1990) Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation J. Biol. Chem. 265, 5361-5363
    • (1990) J. Biol. Chem. , vol.265 , pp. 5361-5363
    • Di Primo, C.1    Hui Bon Hoa, G.2    Douzou, P.3    Sligar, S.4
  • 42
    • 41949088824 scopus 로고    scopus 로고
    • Reversible inactivation of cytochrome P450 by alkaline earth metal ions: Auxiliary metal ion induced conformation change and formation of inactive P420 species in CYP101
    • Manna, S. K. and Mazumdar, S. (2008) Reversible inactivation of cytochrome P450 by alkaline earth metal ions: Auxiliary metal ion induced conformation change and formation of inactive P420 species in CYP101 J. Inorg. Biochem. 102, 1312-1321
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1312-1321
    • Manna, S.K.1    Mazumdar, S.2
  • 43
    • 33845252049 scopus 로고    scopus 로고
    • Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam
    • OuYang, B., Pochapsky, S. S., Pagani, G. M., and Pochapsky, T. C. (2006) Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam Biochemistry 45, 14379-14388
    • (2006) Biochemistry , vol.45 , pp. 14379-14388
    • Ouyang, B.1    Pochapsky, S.S.2    Pagani, G.M.3    Pochapsky, T.C.4
  • 44
    • 0141925683 scopus 로고    scopus 로고
    • NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes
    • Tosha, T., Yoshioka, S., Takahashi, S., Ishimori, K., Shimada, H., and Morishima, I. (2003) NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes J. Biol. Chem. 278, 39809-39821
    • (2003) J. Biol. Chem. , vol.278 , pp. 39809-39821
    • Tosha, T.1    Yoshioka, S.2    Takahashi, S.3    Ishimori, K.4    Shimada, H.5    Morishima, I.6
  • 45
    • 5644272669 scopus 로고    scopus 로고
    • L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: The structural changes trigger electron transfer to oxy-P450cam from electron donors
    • Tosha, T., Yoshioka, S., Ishimori, K., and Morishima, I. (2004) L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: The structural changes trigger electron transfer to oxy-P450cam from electron donors J. Biol. Chem. 279, 42836-42843
    • (2004) J. Biol. Chem. , vol.279 , pp. 42836-42843
    • Tosha, T.1    Yoshioka, S.2    Ishimori, K.3    Morishima, I.4
  • 46
    • 0019330820 scopus 로고
    • Electron paramagnetic resonance detectable states of cytochrome P-450cam
    • Lipscomb, J. D. (1980) Electron paramagnetic resonance detectable states of cytochrome P-450cam Biochemistry 19, 3590-3599
    • (1980) Biochemistry , vol.19 , pp. 3590-3599
    • Lipscomb, J.D.1
  • 49
    • 0035918265 scopus 로고    scopus 로고
    • The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study
    • Furukawa, Y. and Morishima, I. (2001) The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study J. Biol. Chem. 276, 12983-12990
    • (2001) J. Biol. Chem. , vol.276 , pp. 12983-12990
    • Furukawa, Y.1    Morishima, I.2
  • 50
    • 0037614992 scopus 로고    scopus 로고
    • A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450(cam)-putidaredoxin couple
    • Pochapsky, S. S., Pochapsky, T. C., and Wei, J. W. (2003) A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450(cam)-putidaredoxin couple Biochemistry 42, 5649-5656
    • (2003) Biochemistry , vol.42 , pp. 5649-5656
    • Pochapsky, S.S.1    Pochapsky, T.C.2    Wei, J.W.3
  • 51
    • 44649083646 scopus 로고    scopus 로고
    • A functional proline switch in cytochrome P450cam
    • OuYang, B., Pochapsky, S. S., Dang, M., and Pochapsky, T. C. (2008) A functional proline switch in cytochrome P450cam Structure 16, 916-923
    • (2008) Structure , vol.16 , pp. 916-923
    • Ouyang, B.1    Pochapsky, S.S.2    Dang, M.3    Pochapsky, T.C.4
  • 52
    • 0033547829 scopus 로고    scopus 로고
    • Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: Comparison with P450cam and P450 2B4
    • Davydov, D. R., Hui Bon Hoa, G., and Peterson, J. A. (1999) Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4 Biochemistry 38, 751-761
    • (1999) Biochemistry , vol.38 , pp. 751-761
    • Davydov, D.R.1    Hui Bon Hoa, G.2    Peterson, J.A.3
  • 53
    • 0034823445 scopus 로고    scopus 로고
    • Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants
    • Tschirret-Guth, R. A., Koo, L. S., Hoa, G. H., and Ortiz de Montellano, P. R. (2001) Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants J. Am. Chem. Soc. 123, 3412-3417
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3412-3417
    • Tschirret-Guth, R.A.1    Koo, L.S.2    Hoa, G.H.3    Ortiz De Montellano, P.R.4
  • 57
    • 0008698783 scopus 로고
    • Quantum chemical explanation of the hyper spectrum of the carbon-monoxide complex of cytochrome-P-450
    • Jung, C. (1985) Quantum chemical explanation of the hyper spectrum of the carbon-monoxide complex of cytochrome-P-450 Chem. Phys. Lett. 113, 589-596
    • (1985) Chem. Phys. Lett. , vol.113 , pp. 589-596
    • Jung, C.1
  • 58
    • 0037390012 scopus 로고    scopus 로고
    • Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction
    • Perera, R., Sono, M., Sigman, J. A., Pfister, T. D., Lu, Y., and Dawson, J. H. (2003) Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction Proc. Natl. Acad. Sci. U.S.A. 100, 3641-3646
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3641-3646
    • Perera, R.1    Sono, M.2    Sigman, J.A.3    Pfister, T.D.4    Lu, Y.5    Dawson, J.H.6
  • 59
    • 34548309047 scopus 로고    scopus 로고
    • Structural evidence for a functionally relevant second camphor binding site in P450cam: Model for substrate entry into a P450 active site
    • Yao, H., McCullough, C. R., Costache, A. D., Pullela, P. K., and Sem, D. S. (2007) Structural evidence for a functionally relevant second camphor binding site in P450cam: Model for substrate entry into a P450 active site Proteins 69, 125-138
    • (2007) Proteins , vol.69 , pp. 125-138
    • Yao, H.1    McCullough, C.R.2    Costache, A.D.3    Pullela, P.K.4    Sem, D.S.5


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