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Volumn 78, Issue 3, 2000, Pages 1541-1550

Induced fit in arginine kinase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE KINASE; CREATINE KINASE; GUANIDINE DERIVATIVE;

EID: 0034054987     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76706-3     Document Type: Article
Times cited : (42)

References (60)
  • 1
    • 0023498404 scopus 로고
    • Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: What can we learn and catalysis from a "simple" enzyme
    • Alber, T. C., R. C. Davenport, D. A. Giammona, E. Lolis, G. A. Petsko, and D. Ringe. 1987. Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn and catalysis from a "simple" enzyme. Cold Spring Harb. Symp. Quant. Biol. 52:603-613.
    • (1987) Cold Spring Harb. Symp. Quant. Biol. , vol.52 , pp. 603-613
    • Alber, T.C.1    Davenport, R.C.2    Giammona, D.A.3    Lolis, E.4    Petsko, G.A.5    Ringe, D.6
  • 2
    • 0018802524 scopus 로고
    • Space-filling models of kinase clefts and conformation changes
    • Anderson, C. M., F. H. Zucker, and T. A. Steitz. 1979. Space-Filling Models of Kinase Clefts and Conformation Changes. Science. 204: 375-380.
    • (1979) Science , vol.204 , pp. 375-380
    • Anderson, C.M.1    Zucker, F.H.2    Steitz, T.A.3
  • 4
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer
    • Bennett, W. S., Jr., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:211-230.
    • (1980) J. Mol. Biol. , vol.140 , pp. 211-230
    • Bennett W.S., Jr.1    Steitz, T.A.2
  • 5
    • 0015311105 scopus 로고
    • Kinetic properties of the arginine kinase isoenzymes of Limulus polyphemus
    • Blethen, S. L. 1972. Kinetic properties of the arginine kinase isoenzymes of Limulus polyphemus. Arch. Biochem. Biophys. 149:244-251.
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 244-251
    • Blethen, S.L.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N. 1994. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50:760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 8
    • 0021107965 scopus 로고
    • Solvent accessible surfaces of proteins and nucleic acids
    • Connolly, M. L. 1983. Solvent accessible surfaces of proteins and nucleic acids. Science. 221:709-713 .
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 10
    • 0027486802 scopus 로고
    • Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle
    • Dumas, C., and J. Camonis. 1993. Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle. J. Biol. Chem. 268: 21599-21606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21599-21606
    • Dumas, C.1    Camonis, J.2
  • 11
    • 0000219480 scopus 로고
    • Conformational changes in arginine kinase upon ligand binding seen by small-angle x-ray scattering
    • Dumas, C., and J. Janin. 1983. Conformational changes in arginine kinase upon ligand binding seen by small-angle x-ray scattering. FEBS Lett. 153:128-130.
    • (1983) FEBS Lett. , vol.153 , pp. 128-130
    • Dumas, C.1    Janin, J.2
  • 12
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D., and A. D. McLachlan. 1986. Solvation energy in protein folding and binding. Nature. 319:199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 14
    • 0030606976 scopus 로고    scopus 로고
    • Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering
    • Forstner, M., M. Kriechbaum, M. P. Laggner, and T. Wallimann. 1996. Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering. J. Mol. Struct. 383:217-227.
    • (1996) J. Mol. Struct. , vol.383 , pp. 217-227
    • Forstner, M.1    Kriechbaum, M.2    Laggner, M.P.3    Wallimann, T.4
  • 15
    • 0031848225 scopus 로고    scopus 로고
    • Structural changes of creatine kinase upon substrate binding
    • Forstner, M., K. Manfred. P. Laggner, and T. Wallimann. 1998. Structural changes of creatine kinase upon substrate binding. Biophys. J. 75: 1016-1023.
    • (1998) Biophys. J. , vol.75 , pp. 1016-1023
    • Forstner, M.1    Manfred, K.2    Laggner, P.3    Wallimann, T.4
  • 17
    • 0025777309 scopus 로고
    • Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase
    • Gerstein, M., and C. Chothia. 1991. Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase. J. Mol. Biol. 220:133-149.
    • (1991) J. Mol. Biol. , vol.220 , pp. 133-149
    • Gerstein, M.1    Chothia, C.2
  • 18
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • Gerstein, M., and M. Krebs. 1998. A database of macromolecular motions. Nucleic Acids Res. 26:4280-4290.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4280-4290
    • Gerstein, M.1    Krebs, M.2
  • 19
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., A. M. Lesk, and C. Chothia. 1994. Structural mechanisms for domain movements in proteins. Biochemistry. 33:6739-49.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 20
    • 0028246759 scopus 로고
    • The tryptophan residues of mitochondrial creatine kinase: Roles of Trp-223, Trp-206, and Trp-264 in active-site and quaternary structure formation
    • Gross, M., E. M. Furter-Graves, T. Wallimann, H. M. Eppenberger, and R. Furter. 1994. The tryptophan residues of mitochondrial creatine kinase: roles of Trp-223, Trp-206, and Trp-264 in active-site and quaternary structure formation. Protein Sci. 3:1058-1068.
    • (1994) Protein Sci. , vol.3 , pp. 1058-1068
    • Gross, M.1    Furter-Graves, E.M.2    Wallimann, T.3    Eppenberger, H.M.4    Furter, R.5
  • 21
    • 0029008061 scopus 로고
    • Dimer-dimer interaction in octameric mitochondrial creatine kinase
    • Gross, M., and T. Wallimann. 1995. Dimer-dimer interaction in octameric mitochondrial creatine kinase. Biochemistry. 34:6660-6667.
    • (1995) Biochemistry , vol.34 , pp. 6660-6667
    • Gross, M.1    Wallimann, T.2
  • 22
    • 0019888151 scopus 로고
    • The stereochemical course of the reaction catalyzed by creatine kinase
    • Hansen, D. E., and J. R. Knowles. 1981. The stereochemical course of the reaction catalyzed by creatine kinase. J. Biol. Chem. 256:5967-5969.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5967-5969
    • Hansen, D.E.1    Knowles, J.R.2
  • 23
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA. 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 24
    • 0016378955 scopus 로고
    • "Orbital steering," entropy and rate accelerations
    • Jencks, W. P., and M. I. Mage. 1974. "Orbital steering," entropy and rate accelerations. Biochem. Biophys. Res. Commun. 57:887-892.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 887-892
    • Jencks, W.P.1    Mage, M.I.2
  • 25
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones, T. A., and M. Kjeldgaard. 1997. Electron-density map interpretation. Methods Enzymol. 277:173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 26
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • Joseph, D., G. A. Petsko, and M. Karplus. 1990. Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science. 249:1425-1428.
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 27
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. 1976. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A. 32:922-923.
    • (1976) Acta Crystallogr. A. , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 28
    • 0031469493 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase - A square protein
    • Kabsch, W., and K. Fritz-Wolf. 1997. Mitochondrial creatine kinase - a square protein. Curr. Opin. Struct. Biol. 7:811-818.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 811-818
    • Kabsch, W.1    Fritz-Wolf, K.2
  • 29
    • 0020654939 scopus 로고
    • Creatine kinase: Structure-activity relationships
    • Kenyon, G. L., and G. H. Reed. 1983. Creatine kinase: structure-activity relationships. Adv. Enzymol. 54:367-426.
    • (1983) Adv. Enzymol. , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 30
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E. J. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA. 44:98-104.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.J.1
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 32
    • 0013866009 scopus 로고
    • Cooperative effects of substrates and substrate analogs on the conformation of creatine phosphokinase
    • Lui, N. S. T., and L. Cunningham. 1966. Cooperative effects of substrates and substrate analogs on the conformation of creatine phosphokinase. Biochemistry. 5:144-149.
    • (1966) Biochemistry , vol.5 , pp. 144-149
    • Lui, N.S.T.1    Cunningham, L.2
  • 33
    • 0018798888 scopus 로고
    • Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose 6-phosphate
    • McDonald, R. C., T. A. Steitz, and D. M. Engelman. 1979. Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose 6-phosphate. Biochemistry. 18:338-342.
    • (1979) Biochemistry , vol.18 , pp. 338-342
    • McDonald, R.C.1    Steitz, T.A.2    Engelman, D.M.3
  • 34
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and D. J. Bacon. 1997. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:505-525.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-525
    • Merritt, E.A.1    Bacon, D.J.2
  • 37
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page, M. I., and W. P. Jencks. 1971. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc. Natl. Acad. Sci. USA. 68:1678-1683.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 38
    • 0017381166 scopus 로고
    • Substrate positions and induced-fit in crystalline adenylate kinase
    • Pai, E. F., W. Sachsenheimer, R. H. Schirmer, and G. E. Schulz. 1977. Substrate positions and induced-fit in crystalline adenylate kinase. J. Mol. Biol. 114:37-45.
    • (1977) J. Mol. Biol. , vol.114 , pp. 37-45
    • Pai, E.F.1    Sachsenheimer, W.2    Schirmer, R.H.3    Schulz, G.E.4
  • 39
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao, J. K., G. Bujacz, and A. Wlodawer. 1998. Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 439:133-137.
    • (1998) FEBS Lett. , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3
  • 41
    • 0015523053 scopus 로고
    • Structural changes induced by substrates and anions at the active site of creatine kinase
    • Reed, G. H., and M. Cohn. 1972. Structural changes induced by substrates and anions at the active site of creatine kinase. J. Biol. Chem. 247: 3073-3081.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3073-3081
    • Reed, G.H.1    Cohn, M.2
  • 42
    • 0030800147 scopus 로고    scopus 로고
    • Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes
    • Rhee, S., K. D. Parris, C. C. Hyde, S. A. Ahmed, E. W. Miles, and D. R. Davies. 1997. Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes. Biochemistry. 36:7664-7680.
    • (1997) Biochemistry , vol.36 , pp. 7664-7680
    • Rhee, S.1    Parris, K.D.2    Hyde, C.C.3    Ahmed, S.A.4    Miles, E.W.5    Davies, D.R.6
  • 43
    • 0026431776 scopus 로고
    • Mitochondrial creatine kinase mediates contact formation between mitochondrial membranes
    • Rojo, M., R. Hovius, R. A. Demel, K. Nicolay, and T. Wallimann. 1991. Mitochondrial creatine kinase mediates contact formation between mitochondrial membranes. J. Biol. Chem. 266:20290-20295.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20290-20295
    • Rojo, M.1    Hovius, R.2    Demel, R.A.3    Nicolay, K.4    Wallimann, T.5
  • 44
    • 0027371878 scopus 로고
    • Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form
    • Schreuder, H. A., S. Knight, P. Curmi, I. Andersson, D. Cascio, C.-I. Brändén, and D. S. Eisenberg. 1993. Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form. Proc. Natl. Acad. Sci. USA. 90:9968-9972.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9968-9972
    • Schreuder, H.A.1    Knight, S.2    Curmi, P.3    Andersson, I.4    Cascio, D.5    Brändén, C.-I.6    Eisenberg, D.S.7
  • 45
    • 0029091493 scopus 로고
    • A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase
    • Schubert, H. L., E. B. Fauman, J. A. Stuckey, J. E. Dixon, and M. A. Saper. 1995. A ligand-induced conformational change in the Yersinia protein tyrosine phosphatase. Protein Sci. 4:1904-1913.
    • (1995) Protein Sci. , vol.4 , pp. 1904-1913
    • Schubert, H.L.1    Fauman, E.B.2    Stuckey, J.A.3    Dixon, J.E.4    Saper, M.A.5
  • 46
    • 0029742013 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop
    • Schumacher, M. A., D. Carter, D. S. Roos, B. Ullman, and R. G. Brennan. 1996. Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop. Nature Struct. Biol. 3:881-887.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 881-887
    • Schumacher, M.A.1    Carter, D.2    Roos, D.S.3    Ullman, B.4    Brennan, R.G.5
  • 47
    • 0025263879 scopus 로고
    • A cloned ATP:Guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure
    • Stein, H. D., D. A. Ham, and J. R. David. 1990. A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure. J. Biol. Chem. 265:6582-6588.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6582-6588
    • Stein, H.D.1    Ham, D.A.2    David, J.R.3
  • 49
    • 0027133018 scopus 로고
    • Horseshoe crab sperm contain a unique isoform of arginine kinase that is present in midpiece and flagellum
    • Strong, S. J., and W. R. Ellington. 1993. Horseshoe crab sperm contain a unique isoform of arginine kinase that is present in midpiece and flagellum. J. Exp. Zool. 267:563-571.
    • (1993) J. Exp. Zool. , vol.267 , pp. 563-571
    • Strong, S.J.1    Ellington, W.R.2
  • 50
    • 0028858939 scopus 로고
    • Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into catalytically important residues
    • Strong, S. J., and W. R. Ellington. 1995. Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues. Biochim. Biophys. Acta. 1246:197-200.
    • (1995) Biochim. Biophys. Acta. , vol.1246 , pp. 197-200
    • Strong, S.J.1    Ellington, W.R.2
  • 51
    • 0029992890 scopus 로고    scopus 로고
    • Balancing ATP in the cell
    • Stroud, R. M. 1996. Balancing ATP in the cell. Nature Struct. Biol. 3:567-569.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 567-569
    • Stroud, R.M.1
  • 52
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase: Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki, T., and T. Furukohri. 1994. Evolution of phosphagen kinase: primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237:353-357.
    • (1994) J. Mol. Biol. , vol.237 , pp. 353-357
    • Suzuki, T.1    Furukohri, T.2
  • 53
    • 0030671447 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus
    • Suzuki, T., Y. Kawasaki, and T. Furukohri. 1997a. Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus. Biochem. J. 328:301-306.
    • (1997) Biochem. J. , vol.328 , pp. 301-306
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3
  • 54
    • 0031555335 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase and the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
    • Suzuki, T., Y. Kawasaki, T. Furukohri, and W. R. Ellington. 1997b. Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase and the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site. Biochim. Biophys. Acta. 1343: 152-159.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 152-159
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3    Ellington, W.R.4
  • 55
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes: The "phospho-creatine circuit" for cellular energy homeostasis
    • Wallimann, T., M. Wyss, D. Brdiczka, K. Nicolay, and H. M. Eppenberger. 1992. Intracellular compartmentation, structure and function of creatine kinase isoenzymes: the "phospho-creatine circuit" for cellular energy homeostasis. Biochem. J. 281:21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 56
    • 0025287976 scopus 로고
    • The phosphocreatine shuttle of sea urchin sperm: Flagellar creatine kinase resulted from a gene triplication
    • Wothe, D. D., H. Charbonneau, and B. M. Shapiro. 1990. The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication. Proc Natl. Acad. Sci. USA. 87:5203-5207.
    • (1990) Proc Natl. Acad. Sci. USA , vol.87 , pp. 5203-5207
    • Wothe, D.D.1    Charbonneau, H.2    Shapiro, B.M.3
  • 57
    • 4243764970 scopus 로고
    • Mitochondrial creatine kinase: Localization, structure and function, and clinical aspects
    • Wyss, M., J. Smeitink, R. A. Wevers, and T. Wallimann. 1992. Mitochondrial creatine kinase: localization, structure and function, and clinical aspects. Biochim. Biophys. Acta. 288:771-775.
    • (1992) Biochim. Biophys. Acta , vol.288 , pp. 771-775
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 58
    • 0030573015 scopus 로고    scopus 로고
    • Canine parvovirus capsid structure, analyzed at 2.9 Å resolution
    • Xie, Q., and M. S. Chapman. 1996. Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol. 264:497-520.
    • (1996) J. Mol. Biol. , vol.264 , pp. 497-520
    • Xie, Q.1    Chapman, M.S.2


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