메뉴 건너뛰기




Volumn 93, Issue 2, 2007, Pages 645-654

Energy landscape of chelated uranyl: Antibody interactions by dynamic force spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID DERIVATIVE; LIGAND; METAL DERIVATIVE; MONOCLONAL ANTIBODY; PHENANTHROLINE DERIVATIVE; PROTEIN; UNCLASSIFIED DRUG; URANIUM DERIVATIVE; URANYL DICARBOXYPHENANTHROLINE;

EID: 34447299432     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.098129     Document Type: Article
Times cited : (44)

References (62)
  • 1
    • 0034085170 scopus 로고    scopus 로고
    • Transport of toxic heavy metals across cell membranes
    • Foulkes, E. C. 2000. Transport of toxic heavy metals across cell membranes. Proc. Soc. Exp. Biol. Med. 223:234-240.
    • (2000) Proc. Soc. Exp. Biol. Med , vol.223 , pp. 234-240
    • Foulkes, E.C.1
  • 4
    • 0037267492 scopus 로고    scopus 로고
    • Recent developments in computational actinide chemistry
    • Kaltsoyannis, N. 2003. Recent developments in computational actinide chemistry. Chem. Soc. Rev. 32:9-16.
    • (2003) Chem. Soc. Rev , vol.32 , pp. 9-16
    • Kaltsoyannis, N.1
  • 5
    • 4644364572 scopus 로고    scopus 로고
    • Novel monoclonal antibodies with specificity for chelated uranium(VI): Isolation and binding properties
    • Blake, I. R., A. R. Pavlov, M. Khosraviani, H. E. Ensley, G. E. Kiefer, H. Yu, X. Li, and D. A. Blake. 2004. Novel monoclonal antibodies with specificity for chelated uranium(VI): isolation and binding properties. Bioconjug. Chem. 15:1125-1136.
    • (2004) Bioconjug. Chem , vol.15 , pp. 1125-1136
    • Blake, I.R.1    Pavlov, A.R.2    Khosraviani, M.3    Ensley, H.E.4    Kiefer, G.E.5    Yu, H.6    Li, X.7    Blake, D.A.8
  • 7
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E. L., V. T. Moy, and H. E. Gaub. 1994. Adhesion forces between individual ligand-receptor pairs. Science. 264:415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 8
    • 0034948356 scopus 로고    scopus 로고
    • The rules are changing: Force measurements on single molecules and how they relate to bulk reaction kinetics and energies
    • Guthold, M., R. Superfine, and R. M. Taylor. 2001. The rules are changing: force measurements on single molecules and how they relate to bulk reaction kinetics and energies. Biomed. Microdev. 3:9-18.
    • (2001) Biomed. Microdev , vol.3 , pp. 9-18
    • Guthold, M.1    Superfine, R.2    Taylor, R.M.3
  • 9
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 10
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 11
    • 0037058902 scopus 로고    scopus 로고
    • The effect of force on thermodynamics and kinetics of single molecule reactions
    • Tinoco, I. Jr., and C. Bustamante. 2002. The effect of force on thermodynamics and kinetics of single molecule reactions. Biophys. Chem. 101-102:513-533.
    • (2002) Biophys. Chem , vol.101-102 , pp. 513-533
    • Tinoco Jr., I.1    Bustamante, C.2
  • 12
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R., P. Nassoy, A. Leung, K. Ritchie, and E. Evans. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature. 397:50-53.
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 13
    • 0032514687 scopus 로고    scopus 로고
    • Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy
    • Fritz, J., A. G. Katopodis, F. Kolbinger, and D. Anselmetti. 1998. Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy. Proc. Natl. Acad. Sci. USA. 95:12283-12288.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12283-12288
    • Fritz, J.1    Katopodis, A.G.2    Kolbinger, F.3    Anselmetti, D.4
  • 15
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • Yuan, C., A. Chen, P. Kolb, and V. T. Moy. 2000. Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochemistry. 39:10219-10223.
    • (2000) Biochemistry , vol.39 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 16
    • 0035970109 scopus 로고    scopus 로고
    • Selectin receptor-ligand bonds: Formation limited by shear rate and dissociation governed by the Bell model
    • Chen, S., and T. A. Springer. 2001. Selectin receptor-ligand bonds: formation limited by shear rate and dissociation governed by the Bell model. Proc. Natl. Acad. Sci. USA. 98:950-955.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 950-955
    • Chen, S.1    Springer, T.A.2
  • 17
    • 0038354493 scopus 로고    scopus 로고
    • Cooperative adhesion of ligand-receptor bonds
    • Zhang, X., and V. T. Moy. 2003. Cooperative adhesion of ligand-receptor bonds. Biophys. Chem. 104:271-278.
    • (2003) Biophys. Chem , vol.104 , pp. 271-278
    • Zhang, X.1    Moy, V.T.2
  • 18
    • 0037306230 scopus 로고    scopus 로고
    • Force measurements of the alpha5beta1 integrin-fibronectin interaction
    • Li, F., S. D. Redick, H. P. Erickson, and V. T. Moy. 2003. Force measurements of the alpha5beta1 integrin-fibronectin interaction. Biophys. J. 84:1252-1262.
    • (2003) Biophys. J , vol.84 , pp. 1252-1262
    • Li, F.1    Redick, S.D.2    Erickson, H.P.3    Moy, V.T.4
  • 20
    • 14744290539 scopus 로고    scopus 로고
    • Single molecule studies of antibody-antigen interaction strength versus intramolecular antigen stability
    • Kienberger, F., G. Kada, H. Mueller, and P. Hinterdorfer. 2005. Single molecule studies of antibody-antigen interaction strength versus intramolecular antigen stability. J. Mol. Biol. 347:597-606.
    • (2005) J. Mol. Biol , vol.347 , pp. 597-606
    • Kienberger, F.1    Kada, G.2    Mueller, H.3    Hinterdorfer, P.4
  • 23
    • 1642387872 scopus 로고    scopus 로고
    • Identification of functionally important residues in proteins using comparative models
    • Chen, S.-w. W., and J. L. Pellequer. 2004. Identification of functionally important residues in proteins using comparative models. Curr. Med. Chem. 11:595-605.
    • (2004) Curr. Med. Chem , vol.11 , pp. 595-605
    • Chen, S.-W.W.1    Pellequer, J.L.2
  • 24
    • 8344267604 scopus 로고    scopus 로고
    • Influence of surfactants and antibody immobilization strategy on reducing nonspecific protein interactions for molecular recognition force microscopy
    • Brogan, K. L., J. H. Shin, and M. H. Schoenfisch. 2004. Influence of surfactants and antibody immobilization strategy on reducing nonspecific protein interactions for molecular recognition force microscopy. Langmuir. 20:9729-9735.
    • (2004) Langmuir , vol.20 , pp. 9729-9735
    • Brogan, K.L.1    Shin, J.H.2    Schoenfisch, M.H.3
  • 26
    • 0030952393 scopus 로고    scopus 로고
    • Detection of antigen-antibody binding events with the atomic force microscope
    • Allen, S. 1997. Detection of antigen-antibody binding events with the atomic force microscope. Biochemistry. 36:7457-7463.
    • (1997) Biochemistry , vol.36 , pp. 7457-7463
    • Allen, S.1
  • 27
    • 0034054531 scopus 로고    scopus 로고
    • High-resolution imaging of antibodies by tapping-mode atomic force microscopy: Attractive and repulsive tip-sample interaction regimes
    • San Paulo, A., and R. Garcia. 2000. High-resolution imaging of antibodies by tapping-mode atomic force microscopy: attractive and repulsive tip-sample interaction regimes. Biophys. J. 78:1599-1605.
    • (2000) Biophys. J , vol.78 , pp. 1599-1605
    • San Paulo, A.1    Garcia, R.2
  • 28
    • 0033861876 scopus 로고    scopus 로고
    • Model energy landscapes and the force-induced dissociation of ligand-receptor bonds
    • Strunz, T., K. Oroszlan, I. Schumakovitch, H. Guntherodt, and M. Hegner. 2000. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys. J. 79:1206-1212.
    • (2000) Biophys. J , vol.79 , pp. 1206-1212
    • Strunz, T.1    Oroszlan, K.2    Schumakovitch, I.3    Guntherodt, H.4    Hegner, M.5
  • 29
    • 0037621477 scopus 로고    scopus 로고
    • Dynamic single-molecule force spectroscopy: Bond rupture analysis with variable spacer length
    • Friedsam, C., A. K. Wehle, F. Kühner, and H. Gaub. 2003. Dynamic single-molecule force spectroscopy: bond rupture analysis with variable spacer length. J. Phys. Cond. Mat. 15:1709-1723.
    • (2003) J. Phys. Cond. Mat , vol.15 , pp. 1709-1723
    • Friedsam, C.1    Wehle, A.K.2    Kühner, F.3    Gaub, H.4
  • 32
    • 23044516621 scopus 로고    scopus 로고
    • Structural basis for preferential binding of non-ortho-substituted polychlorinated biphenyls by the monoclonal antibody S2B1
    • Pellequer, J.-L., S.-w. W. Chen, Y.-s. Keum, A. E. Karu, Q. X. Li, and V. A. Roberts. 2005. Structural basis for preferential binding of non-ortho-substituted polychlorinated biphenyls by the monoclonal antibody S2B1. J. Mol. Recogn. 18:282-294.
    • (2005) J. Mol. Recogn , vol.18 , pp. 282-294
    • Pellequer, J.-L.1    Chen, S.-W.W.2    Keum, Y.-S.3    Karu, A.E.4    Li, Q.X.5    Roberts, V.A.6
  • 34
    • 0028013654 scopus 로고
    • Catalytic antibody model and mutagenesis implicate arginine in transitionstate stabilization
    • Roberts, V. A., J. Stewart, S. J. Benkovic, and E. D. Getzoff. 1994. Catalytic antibody model and mutagenesis implicate arginine in transitionstate stabilization. J. Mol. Biol. 235:1098-1116.
    • (1994) J. Mol. Biol , vol.235 , pp. 1098-1116
    • Roberts, V.A.1    Stewart, J.2    Benkovic, S.J.3    Getzoff, E.D.4
  • 35
    • 85030521343 scopus 로고    scopus 로고
    • Brünger, A. T. 1992. X-PLOR, version 3.1. A system for x-ray crystallography and NMR. Yale University Press, New Haven, CT
    • Brünger, A. T. 1992. X-PLOR, version 3.1. A system for x-ray crystallography and NMR. Yale University Press, New Haven, CT.
  • 36
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack Jr., J. D. Evanseck, M. J. Field, S. Fisher, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher III, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack Jr., J. D. Evanseck, M. J. Field, S. Fisher, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher III, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 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
  • 38
    • 17844371706 scopus 로고    scopus 로고
    • The synthesis and structure of the NiII complex of 1,10-phenanthroline-2,9-dicarboxylate: A three-dimensional network via hydrogen bonding interactions
    • Xie, Y.-B., J.-R. Li, and X.-H. Bu. 2005. The synthesis and structure of the NiII complex of 1,10-phenanthroline-2,9-dicarboxylate: a three-dimensional network via hydrogen bonding interactions. J. Mol. Struct. 741:249-253.
    • (2005) J. Mol. Struct , vol.741 , pp. 249-253
    • Xie, Y.-B.1    Li, J.-R.2    Bu, X.-H.3
  • 39
    • 33750976430 scopus 로고    scopus 로고
    • Structural insights into protein-uranyl interaction: Towards an in-silico detection method
    • Pible, O., P. Guilbaud, J.-L. Pellequer, C. Vidaud, and E. Quéméneur. 2006. Structural insights into protein-uranyl interaction: towards an in-silico detection method. Biochimie. 88:1631-1638.
    • (2006) Biochimie , vol.88 , pp. 1631-1638
    • Pible, O.1    Guilbaud, P.2    Pellequer, J.-L.3    Vidaud, C.4    Quéméneur, E.5
  • 40
    • 0037304678 scopus 로고    scopus 로고
    • Relating single-molecule measurements to thermodynamics
    • Keller, D., D. Swigon, and C. Bustamante. 2003. Relating single-molecule measurements to thermodynamics. Biophys. J. 84:733-738.
    • (2003) Biophys. J , vol.84 , pp. 733-738
    • Keller, D.1    Swigon, D.2    Bustamante, C.3
  • 41
    • 0242385306 scopus 로고    scopus 로고
    • On the precise meaning of extension in the interpretation of polymer-chain stretching experiments
    • Neumann, R. M. 2003. On the precise meaning of extension in the interpretation of polymer-chain stretching experiments. Biophys. J. 85:3418-3420.
    • (2003) Biophys. J , vol.85 , pp. 3418-3420
    • Neumann, R.M.1
  • 42
    • 28444492383 scopus 로고    scopus 로고
    • The solution to the streptavidin-biotin paradox: The influence of history on the strength of single molecular bonds
    • Pincet, F., and J. Husson. 2005. The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds. Biophys. J. 89:4374-4381.
    • (2005) Biophys. J , vol.89 , pp. 4374-4381
    • Pincet, F.1    Husson, J.2
  • 43
    • 33645767959 scopus 로고    scopus 로고
    • Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape
    • Schlierf, M., and M. Rief. 2006. Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape. Biophys. J. 90:L33-L35.
    • (2006) Biophys. J , vol.90
    • Schlierf, M.1    Rief, M.2
  • 44
    • 0026829635 scopus 로고
    • Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays
    • Azimzadeh, A., J. L. Pellequer, and M. H. V. Van Regenmortel. 1992. Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays. J. Mol. Recogn. 5:9-18.
    • (1992) J. Mol. Recogn , vol.5 , pp. 9-18
    • Azimzadeh, A.1    Pellequer, J.L.2    Van Regenmortel, M.H.V.3
  • 45
    • 0029883621 scopus 로고    scopus 로고
    • Detection and localization of individual antibodyantigen recognition events by atomic force microscopy
    • Hinterdorfer, P., W. Baumgartner, H. J. Gruber, K. Schilcher, and H. Schindler. 1996. Detection and localization of individual antibodyantigen recognition events by atomic force microscopy. Proc. Natl. Acad. Sci. USA. 93:3477-3481.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3477-3481
    • Hinterdorfer, P.1    Baumgartner, W.2    Gruber, H.J.3    Schilcher, K.4    Schindler, H.5
  • 48
    • 0034093896 scopus 로고    scopus 로고
    • A metalchelating microscopy tip as a new toolbox for single-molecule experiments by atomic force microscopy
    • Schmitt, L., M. Ludwig, H. E. Gaub, and R. Tampe. 2000. A metalchelating microscopy tip as a new toolbox for single-molecule experiments by atomic force microscopy. Biophys. J. 78:3275-3285.
    • (2000) Biophys. J , vol.78 , pp. 3275-3285
    • Schmitt, L.1    Ludwig, M.2    Gaub, H.E.3    Tampe, R.4
  • 49
    • 0037420289 scopus 로고    scopus 로고
    • Analytical descriptions of dynamic force spectroscopy: Behaviour of multiple connections
    • Williams, P. M. 2003. Analytical descriptions of dynamic force spectroscopy: behaviour of multiple connections. Anal. Chim. Acta. 479:107-115.
    • (2003) Anal. Chim. Acta , vol.479 , pp. 107-115
    • Williams, P.M.1
  • 50
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P., and Y. F. Dufrene. 2006. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods. 3:347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 52
    • 0027522084 scopus 로고
    • How the anti-(metal chelate) antibody CHA255 is specific for the metal ion of its antigen: X-ray structures for two Fab'/hapten complexes with different metals in the chelate
    • Love, R. A., J. E. Villafranca, R. M. Aust, K. K. Nakamura, R. A. Jue, J. G. Major Jr., R. Radhakrishnan, and W. F. Butler. 1993. How the anti-(metal chelate) antibody CHA255 is specific for the metal ion of its antigen: x-ray structures for two Fab'/hapten complexes with different metals in the chelate. Biochemistry. 32:10950-10959.
    • (1993) Biochemistry , vol.32 , pp. 10950-10959
    • Love, R.A.1    Villafranca, J.E.2    Aust, R.M.3    Nakamura, K.K.4    Jue, R.A.5    Major Jr., J.G.6    Radhakrishnan, R.7    Butler, W.F.8
  • 53
    • 0025461296 scopus 로고
    • Kinetics of the dissociation of indium-(p-substituted-benzyl)ethylenediaminetetraacetic acid hapten analogues from the monoclonal antihapten antibody CHA255
    • Meyer, D. L., M. Fineman, B. W. Unger, and J. M. Frincke. 1990. Kinetics of the dissociation of indium-(p-substituted-benzyl)ethylenediaminetetraacetic acid hapten analogues from the monoclonal antihapten antibody CHA255. Bioconjug. Chem. 1:278-284.
    • (1990) Bioconjug. Chem , vol.1 , pp. 278-284
    • Meyer, D.L.1    Fineman, M.2    Unger, B.W.3    Frincke, J.M.4
  • 54
    • 0036789541 scopus 로고    scopus 로고
    • Force spectroscopy of the leukocyte function-associated antigen-1/intercellular adhesion molecule-1 interaction
    • Zhang, X., E. Wojcikiewicz, and V. T. Moy. 2002. Force spectroscopy of the leukocyte function-associated antigen-1/intercellular adhesion molecule-1 interaction. Biophys. J. 83:2270-2279.
    • (2002) Biophys. J , vol.83 , pp. 2270-2279
    • Zhang, X.1    Wojcikiewicz, E.2    Moy, V.T.3
  • 55
    • 1542375742 scopus 로고    scopus 로고
    • Effects of intermediate bound states in dynamic force spectroscopy
    • Derenyi, I., D. Bartolo, and A. Ajdari. 2004. Effects of intermediate bound states in dynamic force spectroscopy. Biophys. J. 86:1263-1269.
    • (2004) Biophys. J , vol.86 , pp. 1263-1269
    • Derenyi, I.1    Bartolo, D.2    Ajdari, A.3
  • 57
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • Neuert, G., C. Albrecht, E. Pamir, and H. E. Gaub. 2006. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580:505-509.
    • (2006) FEBS Lett , vol.580 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 58
    • 0027422957 scopus 로고
    • Measurement of kinetic binding constants of viral antibodies using a new biosensor technology
    • Pellequer, J.-L., and M. H. V. Van Regenmortel. 1993. Measurement of kinetic binding constants of viral antibodies using a new biosensor technology. J Immunol. Meth. 166:133-143.
    • (1993) J Immunol. Meth , vol.166 , pp. 133-143
    • Pellequer, J.-L.1    Van Regenmortel, M.H.V.2
  • 60
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 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.J.1
  • 61
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and D. J. Bacon. 1997. Raster3D: photorealistic molecular graphics. Meth. Enzymol. 277:505-524.
    • (1997) Meth. Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 62
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M. F. 1999. Python: a programming language for software integration and development. J. Mol. Graph. Model. 17:57-61.
    • (1999) J. Mol. Graph. Model , vol.17 , pp. 57-61
    • Sanner, M.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.