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Volumn 48, Issue 21, 2009, Pages 4548-4556

Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ARCHAEAL; BIOLOGICAL FUNCTIONS; CHEMICAL DYNAMICS; CHEMICAL EXCHANGE; COORDINATED MOTION; ENZYMATIC ACTIVITIES; ENZYMATIC FUNCTIONS; ENZYMATIC REACTION; HAHN ECHO; ISOTOPE EXCHANGE; LOOP INTERACTION; MODEL SYSTEM; MUTANT ENZYMES; PROTEIN SEQUENCES; SOLVENT EXCHANGES; SUBSTRATE BINDING; TEMPERATURE DEPENDENT; THERMAL STABILITY; TRIOSEPHOSPHATE ISOMERASE;

EID: 66349134420     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9002887     Document Type: Article
Times cited : (49)

References (47)
  • 1
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of surface loops
    • Hedstrom, L., Szilagyi, L., and Rutter, W. J. (1992) Converting trypsin to chymotrypsin: the role of surface loops. Science 255, 1249-1253.
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 2
    • 34247180580 scopus 로고    scopus 로고
    • Sequence-specific dynamics modulate recognition specificity in WW domains
    • Peng, T., Zintsmaster, J. S., Namanja, A. T., and Peng, J. W. (2007) Sequence-specific dynamics modulate recognition specificity in WW domains. Nat. Struct. Mol. Biol. 14, 325-331.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 325-331
    • Peng, T.1    Zintsmaster, J.S.2    Namanja, A.T.3    Peng, J.W.4
  • 3
    • 11144328151 scopus 로고    scopus 로고
    • Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle
    • DOI 10.1021/bi048119y
    • Venkitakrishnan, R. P., Zaborowski, E., McElheny, D., Benkovic, S. J., Dyson, H. J., and Wright, P. E. (2004) Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle. Biochemistry 43, 16046-16055. (Pubitemid 40041018)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16046-16055
    • Venkitakrishnan, R.P.1    Zaborowski, E.2    McElheny, D.3    Benkovic, S.J.4    Dyson, H.J.5    Wright, P.E.6
  • 6
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
    • Akke, M., Liu, J., Cavanagh, J., Erickson, H. P., and Palmer, A. G. (1998) Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat. Struct. Biol. 5, 55-59.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer, A.G.5
  • 7
    • 34848905895 scopus 로고    scopus 로고
    • Conformational dynamics in loop swap mutants of homologous fibronectin type III domains
    • DOI 10.1529/biophysj.106.100578
    • Siggers, K., Soto, C., and Palmer, A. G.3rd (2007) Conformational dynamics in loop swap mutants of homologous fibronectin type III domains. Biophys. J. 93, 2447-2456. (Pubitemid 47511145)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2447-2456
    • Siggers, K.1    Soto, C.2    Palmer III, A.G.3
  • 8
    • 33847771569 scopus 로고    scopus 로고
    • Substrate product equilibriumon a reversible enzyme, triosephosphate isomerase
    • Rozovsky, S., and McDermott, A. E. (2007) Substrate product equilibriumon a reversible enzyme, triosephosphate isomerase. Proc. Natl. Acad. Sci. U.S.A. 104, 2080-2085.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2080-2085
    • Rozovsky, S.1    McDermott, A.E.2
  • 9
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triosephosphate isomerase loop
    • Joseph, D., Petsko, G. A., and Karplus, M. (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
  • 10
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • Williams, J. C., and McDermott, A. E. (1995) Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34, 8309-8319.
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 11
    • 34249071321 scopus 로고    scopus 로고
    • Value of a hydrogen bond in triosephosphate isomerase loop motion
    • DOI 10.1021/bi700344v
    • Berlow, R. B., Igumenova, T. I., and Loria, J. P. (2007) Value of a hydrogen bond in triosephosphate isomerase loop motion. Biochemistry 46, 6001-6010. (Pubitemid 46799162)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 6001-6010
    • Berlow, R.B.1    Igumenova, T.I.2    Loria, J.P.3
  • 12
    • 0345894320 scopus 로고    scopus 로고
    • Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation
    • DOI 10.1021/bi026994i
    • Desamero, R., Rozovsky, S., Zhadin, N., McDermott, A., and Callender, R. (2003) Active site loop motion in triosephosphate isomerase: T-Jump relaxation spectroscopy of thermal activation. Biochemistry 42, 2941-2951. (Pubitemid 36331538)
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2941-2951
    • Desamero, R.1    Rozovsky, S.2    Zhadin, N.3    McDermott, A.4    Callender, R.5
  • 13
    • 33748511877 scopus 로고    scopus 로고
    • Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase
    • DOI 10.1021/bi060764c
    • Massi, F., Wang, C., and Palmer, A. G.3rd (2006) Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry 45, 10787-10794. (Pubitemid 44360148)
    • (2006) Biochemistry , vol.45 , Issue.36 , pp. 10787-10794
    • Massi, F.1    Wang, C.2    Palmer III, A.G.3
  • 14
    • 0035967856 scopus 로고    scopus 로고
    • Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
    • Rozovsky, S., Jogl, G., Tong, L., and McDermott, A. E. (2001) Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310, 271-280.
    • (2001) J. Mol. Biol. , vol.310 , pp. 271-280
    • Rozovsky, S.1    Jogl, G.2    Tong, L.3    McDermott, A.E.4
  • 15
    • 0035967901 scopus 로고    scopus 로고
    • The time scale of the catalytic loop motion in triosephosphate isomerase
    • Rozovsky, S., and McDermott, A. E. (2001) The time scale of the catalytic loop motion in triosephosphate isomerase. J. Mol. Biol. 310, 259-270.
    • (2001) J. Mol. Biol. , vol.310 , pp. 259-270
    • Rozovsky, S.1    McDermott, A.E.2
  • 16
    • 0026782489 scopus 로고
    • Segmental motion in catalysis: Investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase
    • Sampson, N. S., and Knowles, J. R. (1992) Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry 31, 8488-8494.
    • (1992) Biochemistry , vol.31 , pp. 8488-8494
    • Sampson, N.S.1    Knowles, J.R.2
  • 17
    • 0025276041 scopus 로고
    • Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase
    • Pompliano, D. L., Peyman, A., and Knowles, J. R. (1990) Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry 29, 3186-3194. (Pubitemid 20131455)
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3186-3194
    • Pompliano, D.L.1    Peyman, A.2    Knowles, J.R.3
  • 18
    • 0026779802 scopus 로고
    • Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase
    • Sampson, N. S., and Knowles, J. R. (1992) Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. Biochemistry 21, 8482-8487.
    • (1992) Biochemistry , vol.21 , pp. 8482-8487
    • Sampson, N.S.1    Knowles, J.R.2
  • 20
    • 0031820040 scopus 로고    scopus 로고
    • Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase
    • Sun, J., and Sampson, N. S. (1998) Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase. Protein Sci. 7, 1495-1505. (Pubitemid 28331268)
    • (1998) Protein Science , vol.7 , Issue.7 , pp. 1495-1505
    • Sun, J.1    Sampson, N.S.2
  • 21
    • 0033621030 scopus 로고    scopus 로고
    • Understanding protein lids: Kinetic analysis of active hinge mutants in triosephosphate isomerase
    • Sun, J., and Sampson, N. S. (1999) Understanding protein lids: Kinetic analysis of active hinge mutants in triosephosphate isomerase. Biochemistry 38, 11474-11481. (Pubitemid 129516725)
    • (1999) Biochemistry , vol.38 , Issue.35 , pp. 11474-11481
    • Sun, J.1    Sampson, N.S.2
  • 22
    • 0035815109 scopus 로고    scopus 로고
    • The importance of hinge sequences for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase
    • Xiang, J., Sun, J., and Sampson, N. S. (2001) The importance of hinge sequences for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase. J. Mol. Biol. 307, 1103-1112.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1103-1112
    • Xiang, J.1    Sun, J.2    Sampson, N.S.3
  • 23
    • 4444321214 scopus 로고    scopus 로고
    • Entropy effects on protein hinges: The reaction catalyzed by triosephosphate isomerase
    • DOI 10.1021/bi049208d
    • Xiang, J. Y., Jung, J. Y., and Sampson, N. S. (2004) Entropy effects on protein hinges: The reaction catalyzed by triosephosphate isomerase. Biochemistry 43, 11436-11445. (Pubitemid 39186965)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11436-11445
    • Xiang, J.1    Jung, J.-Y.2    Sampson, N.S.3
  • 25
    • 0025358007 scopus 로고
    • Structure of yeast triosephosphate isomerase at 1.9-A ° resolution
    • DOI 10.1021/bi00480a009
    • Lolis, E., Alber, T., Davenport, R. C., Rose, D., Hartman, F. C., and Petsko, G. A. (1990) Structure of yeast triosephosphate isomerase at 1.9-A ° resolution. Biochemistry 29, 6609-6618. (Pubitemid 20223555)
    • (1990) Biochemistry , vol.29 , Issue.28 , pp. 6609-6618
    • Lolis, E.1    Alber, T.2    Davenport, R.C.3    Rose, D.4    Hartman, F.C.5    Petsko, G.A.6
  • 26
    • 0025331920 scopus 로고
    • Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A° resolution: Implications for catalysis
    • DOI 10.1021/bi00480a010
    • Lolis, E., and Petsko, G. A. (1990) Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A ° resolution: implications for catalysis. Biochemistry 29, 6619-6625. (Pubitemid 20223556)
    • (1990) Biochemistry , vol.29 , Issue.28 , pp. 6619-6625
    • Lolis, E.1    Petsko, G.A.2
  • 27
    • 0028209049 scopus 로고
    • Crystal structure of recombinant chicken triosephosphate isomerase- Phosphoglycolohydroxamate complex at 1.8-Angstrom resolution
    • Zhang, Z., Sugio, S., Komives, E. A., Liu, K. D., Knowles, J. R., Petsko, G. A., and Ringe, D. (1994) Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-Angstrom resolution. Biochemistry 33, 2830-2837. (Pubitemid 24103341)
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 2830-2837
    • Zhang, Z.1    Sugio, S.2    Komives, E.A.3    Liu, K.D.4    Knowles, J.R.5    Petsko, G.A.6    Ringe, D.7
  • 28
    • 0015394088 scopus 로고
    • H-dependence of the triose phosphate isomerase reaction
    • Plaut, B., and Knowles, J. R. (1972) pH-dependence of the triose phosphate isomerase reaction. Biochem. J. 129, 311-320.
    • (1972) Biochem. J. , vol.129 , pp. 311-320
    • Plaut, B.1    Knowles, J.R.2
  • 29
    • 14044268187 scopus 로고    scopus 로고
    • Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of (R)-glyceraldehyde 3-phosphate in D2O
    • O'Donoghue, A. C., Amyes, T. L., and Richard, J. P. (2005) Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of (R)-glyceraldehyde 3-phosphate in D2O. Biochemistry 44, 2610-2621.
    • (2005) Biochemistry , vol.44 , pp. 2610-2621
    • O'Donoghue, A.C.1    Amyes, T.L.2    Richard, J.P.3
  • 30
    • 0033226859 scopus 로고    scopus 로고
    • Transverse-relaxation- optimized (TROSY) gradient-enhnaced triple-resonance NMR spectroscopy
    • Loria, J. P., Rance, M., and Palmer, A. G. (1999) Transverse-relaxation- optimized (TROSY) gradient-enhnaced triple-resonance NMR spectroscopy. J. Magn. Reson. 141, 180-184.
    • (1999) J. Magn. Reson. , vol.141 , pp. 180-184
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.3
  • 31
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 32
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind, M., and Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson., Ser. B 101, 201-205.
    • (1993) J. Magn. Reson., Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiak, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiak, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Goddard, T., and Kneller, D. G. SPARKY 3, University of California, San Francisco, CA.
    • SPARKY 3
    • Goddard, T.1    Kneller, D.G.2
  • 35
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease a
    • DOI 10.1021/bi025655m
    • Cole, R., and Loria, J. P. (2002) Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072-6081. (Pubitemid 34498913)
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 6072-6081
    • Cole, R.1    Loria, J.P.2
  • 37
    • 33745642439 scopus 로고    scopus 로고
    • Off-resonance TROSY-selected R 1rho experiment with improved sensitivity for medium- and high-molecular-weight proteins
    • Igumenova, T. I., and Palmer, A. G.III (2006) Off-resonance TROSY-selected R 1rho experiment with improved sensitivity for medium- and high-molecular-weight proteins. J. Am. Chem. Soc. 128, 8110-8111.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8110-8111
    • Igumenova, T.I.1    Palmer III, A.G.2
  • 38
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • Palmer, A. G., Kroenke, C. D., and Loria, J. P. (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339 (Part B), 204-238. (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 39
    • 4644273901 scopus 로고    scopus 로고
    • Measurement of Intermediate Exchange Phenomena
    • Downing,A. K., Ed. Humana Press, Totowa, NJ
    • Kempf, J. G., and Loria, J. P. (2004) Measurement of Intermediate Exchange Phenomena, in Protein NMR Techniques (Downing,A. K., Ed.) pp 185-231, Humana Press, Totowa, NJ..
    • (2004) Protein NMR Techniques , pp. 185-231
    • Kempf, J.G.1    Loria, J.P.2
  • 40
    • 0001230743 scopus 로고
    • Optimization of modulation functions to improve insensitivity of adiabatic pulses to variations in B1 magnitude
    • Ugurbil, K., Garwood, M., and Rath, A. R. (1988) Optimization of modulation functions to improve insensitivity of adiabatic pulses to variations in B1 magnitude. J. Magn. Reson. 80, 448-469.
    • (1988) J. Magn. Reson. , vol.80 , pp. 448-469
    • Ugurbil, K.1    Garwood, M.2    Rath, A.R.3
  • 41
    • 44949273876 scopus 로고
    • Symmetric pulses to induce arbitrary flip angles with compensation of RF inhomogeneity and resonance offsets
    • Garwood, M., and Ke, Y. (1991) Symmetric pulses to induce arbitrary flip angles with compensation of RF inhomogeneity and resonance offsets. J. Magn. Reson. 94, 511-525.
    • (1991) J. Magn. Reson. , vol.94 , pp. 511-525
    • Garwood, M.1    Ke, Y.2
  • 42
    • 0000987483 scopus 로고    scopus 로고
    • An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations
    • Mulder, F.A. A., de Graaf, R. A., Kaptein, R., and Boelens, R. (1998) An off-resonance rotating frame relaxation experiment for the investigation of macromolecular dynamics using adiabatic rotations J. Magn. Reson. 131, 351-357.
    • (1998) J. Magn. Reson. , vol.131 , pp. 351-357
    • Mulder, F.A.A.1    De Graaf, R.A.2    Kaptein, R.3    Boelens, R.4
  • 43
    • 0041866694 scopus 로고    scopus 로고
    • Mapping chemical exchange in proteins with MW > 50 kD
    • Wang, C., Rance, M., and Palmer, A. G. (2003) Mapping chemical exchange in proteins with MW > 50 kD. J. Am. Chem. Soc. 125, 8968-8969.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8968-8969
    • Wang, C.1    Rance, M.2    Palmer, A.G.3
  • 44
    • 2542487312 scopus 로고    scopus 로고
    • Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes
    • Butterwick, J. A., Loria, J. P., Astrof, N. S., Kroenke, C. D., Cole, R., Rance, M., and Palmer, A. G.3rd (2004) Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes. J. Mol. Biol. 339, 855-871.
    • (2004) J. Mol. Biol. , vol.339 , pp. 855-871
    • Butterwick, J.A.1    Loria, J.P.2    Astrof, N.S.3    Kroenke, C.D.4    Cole, R.5    Rance, M.6    Palmer III, A.G.7
  • 45
    • 0033546403 scopus 로고    scopus 로고
    • Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations
    • Evenas, J., Forsen, S., Malmendal, A., and Akke, M. (1999) Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. J. Mol. Biol. 289, 603-617.
    • (1999) J. Mol. Biol. , vol.289 , pp. 603-617
    • Evenas, J.1    Forsen, S.2    Malmendal, A.3    Akke, M.4
  • 46
    • 0030445011 scopus 로고    scopus 로고
    • Dynamics of ribonuclease H: Temperature dependence of motions on multiple time scales
    • DOI 10.1021/bi962089k
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1996) Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales. Biochemistry 35, 16009-16023. (Pubitemid 27045735)
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16009-16023
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 47
    • 14044276979 scopus 로고    scopus 로고
    • Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of dihydroxyacetone phosphate in D2O
    • O'Donoghue, A. C., Amyes, T. L., and Richard, J. P. (2005) Hydron transfer catalyzed by triosephosphate isomerase. Products of isomerization of dihydroxyacetone phosphate in D2O. Biochemistry 44, 2622-2631.
    • (2005) Biochemistry , vol.44 , pp. 2622-2631
    • O'Donoghue, A.C.1    Amyes, T.L.2    Richard, J.P.3


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