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Volumn 10, Issue 2, 2004, Pages 101-105

The actin-ADP-ribosylating Clostridium botulinum C2 toxin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE RIBOSE; BOTULINUM TOXIN; F ACTIN; G ACTIN; GELDANAMYCIN; NEUROTOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; RUBIDIUM;

EID: 1942454223     PISSN: 10759964     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.anaerobe.2003.10.003     Document Type: Short Survey
Times cited : (12)

References (56)
  • 1
    • 0023024730 scopus 로고
    • Purification and characterization of Clostridium perfringens iota toxin: Dependence on two nonlinked proteins for biological activity
    • Stiles B.G., Wilkens T.D. Purification and characterization of Clostridium perfringens iota toxin. dependence on two nonlinked proteins for biological activity Infect Immun. 54:1986;683-688.
    • (1986) Infect Immun , vol.54 , pp. 683-688
    • Stiles, B.G.1    Wilkens, T.D.2
  • 2
    • 0024339751 scopus 로고
    • Purification of the Clostridium spiroforme binary toxin and activity of the toxin on HEp2 cells
    • Popoff M.R., Milward F.W., Bancillon B., Boquet P. Purification of the Clostridium spiroforme binary toxin and activity of the toxin on HEp2 cells. Infect Immun. 57:1989;2462-2469.
    • (1989) Infect Immun , vol.57 , pp. 2462-2469
    • Popoff, M.R.1    Milward, F.W.2    Bancillon, B.3    Boquet, P.4
  • 3
    • 0031004306 scopus 로고    scopus 로고
    • Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196
    • Perelle S., Gibert M., bourlioux P., Corthier G., Popoff M.R. Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196. Infect Immun. 65:1997;1402-1407.
    • (1997) Infect Immun , vol.65 , pp. 1402-1407
    • Perelle, S.1    Gibert, M.2    Bourlioux, P.3    Corthier, G.4    Popoff, M.R.5
  • 4
    • 0034819726 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of the ADP- ribosyltransferase toxin CDTa from Clostridium difficile
    • Gülke I., Pfeifer G., Liese J., Fritz M., Hofmann F., Aktories K., Barth H. Characterization of the enzymatic component of the ADP- ribosyltransferase toxin CDTa from Clostridium difficile. Infect Immun. 69:2001;6004-6011.
    • (2001) Infect Immun , vol.69 , pp. 6004-6011
    • Gülke, I.1    Pfeifer, G.2    Liese, J.3    Fritz, M.4    Hofmann, F.5    Aktories, K.6    Barth, H.7
  • 5
    • 0032876380 scopus 로고    scopus 로고
    • Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex
    • Han S., Craig J.A., Putnam C.D., Carozzi N.B., Tainer J.A. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nat Struct Biol. 6:1999;932-936.
    • (1999) Nat Struct Biol , vol.6 , pp. 932-936
    • Han, S.1    Craig, J.A.2    Putnam, C.D.3    Carozzi, N.B.4    Tainer, J.A.5
  • 6
    • 0019158135 scopus 로고
    • Purification and characterization of two components of botulinum C2 toxin
    • Ohishi I., Iwasaki M., Sakaguchi G. Purification and characterization of two components of botulinum C2 toxin. Infect Immun. 30:1980;668-673.
    • (1980) Infect Immun , vol.30 , pp. 668-673
    • Ohishi, I.1    Iwasaki, M.2    Sakaguchi, G.3
  • 7
    • 0020672276 scopus 로고
    • Lethal and vascular permeability activities of botulinum C2 toxin induced by separate injections of the two toxin components
    • Ohishi I. Lethal and vascular permeability activities of botulinum C2 toxin induced by separate injections of the two toxin components. Infect Immun. 40:1983;336-339.
    • (1983) Infect Immun , vol.40 , pp. 336-339
    • Ohishi, I.1
  • 8
    • 0024846136 scopus 로고
    • The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects
    • Simpson L.L. The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects. J Pharmacol Exp Ther. 251:1989;1223-1228.
    • (1989) J Pharmacol Exp Ther , vol.251 , pp. 1223-1228
    • Simpson, L.L.1
  • 9
    • 0021216508 scopus 로고
    • Molecular basis for the pharmacological actions of Clostridium botulinum type C2 toxin
    • Simpson L.L. Molecular basis for the pharmacological actions of Clostridium botulinum type C2 toxin. J Pharmacol Exp Ther. 230:1984;665-669.
    • (1984) J Pharmacol Exp Ther , vol.230 , pp. 665-669
    • Simpson, L.L.1
  • 12
    • 0023708116 scopus 로고
    • ADP-ribosylated actin caps the barbed ends of actin filaments
    • Wegner A., Aktories K. ADP-ribosylated actin caps the barbed ends of actin filaments. J Biol Chem. 263:1988;13739-13742.
    • (1988) J Biol Chem , vol.263 , pp. 13739-13742
    • Wegner, A.1    Aktories, K.2
  • 13
    • 0024543962 scopus 로고
    • Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments
    • Weigt C., Just I., Wegner A., Aktories K. Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments. FEBS Lett. 246:1989;181-184.
    • (1989) FEBS Lett , vol.246 , pp. 181-184
    • Weigt, C.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 14
    • 0026584952 scopus 로고
    • ADP-ribosylation of the gelsolin-actin complex by clostridial toxins
    • Wille M., Just I., Wegner A., Aktories K. ADP-ribosylation of the gelsolin-actin complex by clostridial toxins. J Biol Chem. 267:1992;50-55.
    • (1992) J Biol Chem , vol.267 , pp. 50-55
    • Wille, M.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 15
    • 0023144930 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells
    • Reuner K.H., Presek P., Boschek C.B., Aktories K. Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells. Eur J Cell Biol. 43:1987;134-140.
    • (1987) Eur J Cell Biol , vol.43 , pp. 134-140
    • Reuner, K.H.1    Presek, P.2    Boschek, C.B.3    Aktories, K.4
  • 16
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin
    • Schering B., Bärmann M., Chhatwal G.S., Geipel U., Aktories K. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur J Biochem. 171:1988;225-229.
    • (1988) Eur J Biochem , vol.171 , pp. 225-229
    • Schering, B.1    Bärmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 17
    • 0025242426 scopus 로고
    • ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin
    • Mauss S., Chaponnier C., Just I., Aktories K., Gabbiani G. ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Eur J Biochem. 194:1990;237-241.
    • (1990) Eur J Biochem , vol.194 , pp. 237-241
    • Mauss, S.1    Chaponnier, C.2    Just, I.3    Aktories, K.4    Gabbiani, G.5
  • 18
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • Sotiropoulos A., Gineitis D., Copeland J., Treisman R. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell. 98:1999;159-169.
    • (1999) Cell , vol.98 , pp. 159-169
    • Sotiropoulos, A.1    Gineitis, D.2    Copeland, J.3    Treisman, R.4
  • 19
    • 0020539980 scopus 로고
    • Response of mouse intestinal loop to botulinum C2 toxin: Enterotoxic activity induced by cooperation of nonlinked protein components
    • Ohishi I. Response of mouse intestinal loop to botulinum C2 toxin. enterotoxic activity induced by cooperation of nonlinked protein components Infect Immun. 40:1983;691-695.
    • (1983) Infect Immun , vol.40 , pp. 691-695
    • Ohishi, I.1
  • 20
    • 0021358479 scopus 로고
    • Histopathological effect of Botulinum C2 toxin on mouse intestines
    • Ohishi I., Odagiri Y. Histopathological effect of Botulinum C2 toxin on mouse intestines. Infect Immun. 43:1984;54-58.
    • (1984) Infect Immun , vol.43 , pp. 54-58
    • Ohishi, I.1    Odagiri, Y.2
  • 21
    • 0025913370 scopus 로고
    • Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity
    • Considine R.V., Simpson L.L. Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. Toxicon. 29:1991;913-936.
    • (1991) Toxicon , vol.29 , pp. 913-936
    • Considine, R.V.1    Simpson, L.L.2
  • 22
    • 0023779031 scopus 로고
    • Functional modification of a 21-Kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin E.J., Gill D.M., Boquet P., Popoff M.R. Functional modification of a 21-Kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol Cell Biol. 8:1988;418-426.
    • (1988) Mol Cell Biol , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 24
    • 0032036388 scopus 로고    scopus 로고
    • The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin
    • Barth H., Hofmann F., Olenik C., Just I., Aktories K. The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin. Infect Immun. 66:1998;1364-1369.
    • (1998) Infect Immun , vol.66 , pp. 1364-1369
    • Barth, H.1    Hofmann, F.2    Olenik, C.3    Just, I.4    Aktories, K.5
  • 25
    • 0037085473 scopus 로고    scopus 로고
    • The binary Clostridium botulinum C2 toxin as a protein delivery system
    • Barth H., Roebling R., Fritz M., Aktories K. The binary Clostridium botulinum C2 toxin as a protein delivery system. J Biol Chem. 277:2002;5074-5081.
    • (2002) J Biol Chem , vol.277 , pp. 5074-5081
    • Barth, H.1    Roebling, R.2    Fritz, M.3    Aktories, K.4
  • 26
    • 0038208865 scopus 로고    scopus 로고
    • The C-terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding
    • Blöcker D., Barth H., Maier E., Benz R., Barbieri J.T., Aktories K. The C-terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding. Infect Immun. 68:2000;4566-4573.
    • (2000) Infect Immun , vol.68 , pp. 4566-4573
    • Blöcker, D.1    Barth, H.2    Maier, E.3    Benz, R.4    Barbieri, J.T.5    Aktories, K.6
  • 28
    • 0030015488 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Pseudomonas exotoxin a complexed with a nicotinamide adenine dinucleotide analog: Implications for the activation process and for ADP ribosylation
    • Li M., Dyda F., Benhar I., Pastan I., Davies D.R. Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog. implications for the activation process and for ADP ribosylation Proc Natl Acad Sci USA. 93:1996;6902-6906.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6902-6906
    • Li, M.1    Dyda, F.2    Benhar, I.3    Pastan, I.4    Davies, D.R.5
  • 31
    • 0021280847 scopus 로고
    • NAD binding site of diphtheria toxin: Identification of a residue within the nicotinamide subsite by photochemical modification with NAD
    • Carroll S.F., Collier R.J. NAD binding site of diphtheria toxin. identification of a residue within the nicotinamide subsite by photochemical modification with NAD Proc Natl Acad Sci USA. 81:1984;3307-3311.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3307-3311
    • Carroll, S.F.1    Collier, R.J.2
  • 32
    • 0027519408 scopus 로고
    • NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum
    • Jung M., Just I., van Damme J., Vandekerckhove J., Aktories K. NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum. J Biol Chem. 268:1993;23215-23218.
    • (1993) J Biol Chem , vol.268 , pp. 23215-23218
    • Jung, M.1    Just, I.2    Van Damme, J.3    Vandekerckhove, J.4    Aktories, K.5
  • 33
    • 0028938731 scopus 로고
    • Conservation of a common motif in enzymes catalyzing ADP-ribose transfer
    • Takada T., Iida K., Moss J. Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. J Biol Chem. 270:1995;541-544.
    • (1995) J Biol Chem , vol.270 , pp. 541-544
    • Takada, T.1    Iida, K.2    Moss, J.3
  • 34
    • 0032491480 scopus 로고    scopus 로고
    • Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis
    • Barth H., Preiss J.C., Hofmann F., Aktories K. Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis. J Biol Chem. 273:1998;29506-29511.
    • (1998) J Biol Chem , vol.273 , pp. 29506-29511
    • Barth, H.1    Preiss, J.C.2    Hofmann, F.3    Aktories, K.4
  • 36
    • 0345830908 scopus 로고    scopus 로고
    • Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization
    • Marvaud J.C., Stiles B.G., Chenal A., Gillet D., Gibert M., Smith L.A., Popoff M.R. Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization. J Biol Chem. 277:2002;43659-43666.
    • (2002) J Biol Chem , vol.277 , pp. 43659-43666
    • Marvaud, J.C.1    Stiles, B.G.2    Chenal, A.3    Gillet, D.4    Gibert, M.5    Smith, L.A.6    Popoff, M.R.7
  • 37
    • 0023161694 scopus 로고
    • Activation of botulinum C2 toxin by trypsin
    • Ohishi I. Activation of botulinum C2 toxin by trypsin. Infect Immun. 55:1987;1461-1465.
    • (1987) Infect Immun , vol.55 , pp. 1461-1465
    • Ohishi, I.1
  • 41
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • Miller C.J., Elliott J.L., Collier R.J. Anthrax protective antigen. prepore-to-pore conversion Biochemistry. 38:1999;10432-10441.
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 43
    • 0032506245 scopus 로고    scopus 로고
    • Characterization of membrane translocation by anthrax protective antigen
    • Wesche J., Elliott J.L., Falnes P.O., Olsnes S., Collier R.J. Characterization of membrane translocation by anthrax protective antigen. Biochemistry. 37:1998;15737-15746.
    • (1998) Biochemistry , vol.37 , pp. 15737-15746
    • Wesche, J.1    Elliott, J.L.2    Falnes, P.O.3    Olsnes, S.4    Collier, R.J.5
  • 45
    • 0028286786 scopus 로고
    • Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes: Formation of cation-selective channels and inhibition of channel function by chloroquine and peptides
    • Schmid A., Benz R., Just I., Aktories K. Interaction of Clostridium botulinum C2 toxin with lipid bilayer membranes. formation of cation-selective channels and inhibition of channel function by chloroquine and peptides J Biol Chem. 269(24):1994;16706-16711.
    • (1994) J Biol Chem , vol.269 , Issue.24 , pp. 16706-16711
    • Schmid, A.1    Benz, R.2    Just, I.3    Aktories, K.4
  • 46
    • 0037155268 scopus 로고    scopus 로고
    • Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes: Demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia
    • Knapp O., Benz R., Gibert M., Marvaud J.C., Popoff M.R. Interaction of the binding component of Clostridium perfringens iota-toxin with lipid bilayer membranes. demonstration of channel formation by the activated binding component Ib and channel block by the enzyme component Ia J Biol Chem. 277:2002;6143-6152.
    • (2002) J Biol Chem , vol.277 , pp. 6143-6152
    • Knapp, O.1    Benz, R.2    Gibert, M.3    Marvaud, J.C.4    Popoff, M.R.5
  • 47
    • 0035063194 scopus 로고    scopus 로고
    • Cellular uptake of the binary Clostridium perfringens iota-toxin
    • Blöcker D., Behlke J., Aktories K., Barth H. Cellular uptake of the binary Clostridium perfringens iota-toxin. Infect Immun. 69:2001;2980-2987.
    • (2001) Infect Immun , vol.69 , pp. 2980-2987
    • Blöcker, D.1    Behlke, J.2    Aktories, K.3    Barth, H.4
  • 48
    • 0033934871 scopus 로고    scopus 로고
    • Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity
    • Gibert M., Petit L., Raffestin S., Okabe A., Popoff M. Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity. Infect Immun. 68:2000;3848-3853.
    • (2000) Infect Immun , vol.68 , pp. 3848-3853
    • Gibert, M.1    Petit, L.2    Raffestin, S.3    Okabe, A.4    Popoff, M.5
  • 49
    • 0036130586 scopus 로고    scopus 로고
    • Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells
    • Nagahama M., Nagayasu K., Kobayashi K., Sakurai J. Binding component of Clostridium perfringens iota-toxin induces endocytosis in Vero cells. Infect Immun. 70:2002;1909-1914.
    • (2002) Infect Immun , vol.70 , pp. 1909-1914
    • Nagahama, M.1    Nagayasu, K.2    Kobayashi, K.3    Sakurai, J.4
  • 50
    • 0034723205 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates
    • Eckhardt M., Barth H., Blöcker D., Aktories K. Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates. J Biol Chem. 275:2000;2328-2334.
    • (2000) J Biol Chem , vol.275 , pp. 2328-2334
    • Eckhardt, M.1    Barth, H.2    Blöcker, D.3    Aktories, K.4
  • 51
    • 0029071726 scopus 로고
    • Isolation and characterization of a Clostridium botulinum C2 toxin-resistant cell line: Evidence for possible involvement of the cellular C2II receptor in growth regulation
    • Fritz G., Schroeder P., Aktories K. Isolation and characterization of a Clostridium botulinum C2 toxin-resistant cell line. evidence for possible involvement of the cellular C2II receptor in growth regulation Infect Immun. 63:1995;2334-2340.
    • (1995) Infect Immun , vol.63 , pp. 2334-2340
    • Fritz, G.1    Schroeder, P.2    Aktories, K.3
  • 52
    • 0036445526 scopus 로고    scopus 로고
    • The uptake machinery of clostridial actin ADP-ribosylating toxins - A cell delivery system for fusion proteins and polypeptide drugs
    • Barth H., Blöcker D., Aktories K. The uptake machinery of clostridial actin ADP-ribosylating toxins - a cell delivery system for fusion proteins and polypeptide drugs. Naunyn-Schmiedeberg's Arch Pharmacol. 366:2002;501-512.
    • (2002) Naunyn-Schmiedeberg's Arch Pharmacol , vol.366 , pp. 501-512
    • Barth, H.1    Blöcker, D.2    Aktories, K.3
  • 53
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem. 42:1999;260-266.
    • (1999) J Med Chem , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 54
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young J.C., Moarefi I., Hartl F.U. Hsp90. a specialized but essential protein-folding tool J Cell Biol. 154:2001;267-273.
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 55
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts R., Zeng H., Berg E.A., Blue C., McComb M.E., Costello C.E., Vanderspek J.C., Murphy J.R. The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex. J Cell Biol. 160:2003;1139-1150.
    • (2003) J Cell Biol , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6    Vanderspek, J.C.7    Murphy, J.R.8
  • 56
    • 0041856090 scopus 로고    scopus 로고
    • The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol
    • Haug G., Leemhuis J., Tiemann D., Meyer D.K., Aktories K., Barth H. The host cell chaperone Hsp90 is essential for translocation of the binary Clostridium botulinum C2 toxin into the cytosol. J Biol Chem. 278:2003;32266-32274.
    • (2003) J Biol Chem , vol.278 , pp. 32266-32274
    • Haug, G.1    Leemhuis, J.2    Tiemann, D.3    Meyer, D.K.4    Aktories, K.5    Barth, H.6


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