메뉴 건너뛰기




Volumn 367, Issue 1, 2007, Pages 147-155

The equine arteritis virus induces apoptosis via caspase-8 and mitochondria-dependent caspase-9 activation

Author keywords

Apoptosis; Bax; Bid; Caspases 8 and 9 activation pathways; Cytochrome c; Equine arteritis virus; Mitochondria

Indexed keywords

BENZYLOXYCARBONYLISOLEUCYLGLUTAMYLTHREONYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLLEUCYLGLUTAMYLHISTIDYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 8; CASPASE INHIBITOR; CYTOCHROME C; PROTEIN BID;

EID: 34548676391     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2007.05.023     Document Type: Article
Times cited : (24)

References (54)
  • 1
    • 0034129674 scopus 로고    scopus 로고
    • Induction of apoptosis by equine arteritis virus infection
    • Archambault D., and St-Laurent G. Induction of apoptosis by equine arteritis virus infection. Virus Genes 20 (2000) 143-147
    • (2000) Virus Genes , vol.20 , pp. 143-147
    • Archambault, D.1    St-Laurent, G.2
  • 4
    • 0030634897 scopus 로고    scopus 로고
    • Nidovirales: a new order comprising Coronaviridae and Arteriviridae
    • Cavanagh D. Nidovirales: a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 142 (1997) 629-633
    • (1997) Arch. Virol. , vol.142 , pp. 629-633
    • Cavanagh, D.1
  • 5
    • 33846794626 scopus 로고    scopus 로고
    • The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function
    • Chabaud S., Sasseville A.M., Elahi S.M., Caron A., Dufour F., Massie B., and Langelier Y. The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function. J. Gen. Virol. 88 (2007) 384-394
    • (2007) J. Gen. Virol. , vol.88 , pp. 384-394
    • Chabaud, S.1    Sasseville, A.M.2    Elahi, S.M.3    Caron, A.4    Dufour, F.5    Massie, B.6    Langelier, Y.7
  • 6
    • 33747877119 scopus 로고    scopus 로고
    • Ultraviolet-inactivated human cytomegalovirus induces placental syncytiotrophoblast apoptosis in a Toll-like receptor-2 and tumor necrosis factor-α dependent manner
    • Chan G., and Guilbert L.J. Ultraviolet-inactivated human cytomegalovirus induces placental syncytiotrophoblast apoptosis in a Toll-like receptor-2 and tumor necrosis factor-α dependent manner. J. Pathol. 210 (2006) 111-120
    • (2006) J. Pathol. , vol.210 , pp. 111-120
    • Chan, G.1    Guilbert, L.J.2
  • 7
    • 11044236739 scopus 로고    scopus 로고
    • Mitochondrial membrane potential change induced by Hoechst 33342 in myelogenous leukemia cell line HL-60
    • Chen J.C., Zhang X., Singleton T.P., and Kiechle F.L. Mitochondrial membrane potential change induced by Hoechst 33342 in myelogenous leukemia cell line HL-60. Ann. Clin. Lab. Sci. 34 (2004) 458-466
    • (2004) Ann. Clin. Lab. Sci. , vol.34 , pp. 458-466
    • Chen, J.C.1    Zhang, X.2    Singleton, T.P.3    Kiechle, F.L.4
  • 8
    • 33646061035 scopus 로고    scopus 로고
    • Caspase-3 and -7 mediate apoptosis of human Chang's conjunctival cells induced by enterovirus 70
    • Chen D., Texada D.E., Duggan C., Deng Y., Redens T.B., and Langford M.P. Caspase-3 and -7 mediate apoptosis of human Chang's conjunctival cells induced by enterovirus 70. Virology 47 (2006) 307-322
    • (2006) Virology , vol.47 , pp. 307-322
    • Chen, D.1    Texada, D.E.2    Duggan, C.3    Deng, Y.4    Redens, T.B.5    Langford, M.P.6
  • 9
    • 33144469269 scopus 로고    scopus 로고
    • Recognition of vaccinia virus-infected cells by human natural killer cells depends on natural cytotoxicity receptors
    • Chisholm S.E., and Reyburn H.T. Recognition of vaccinia virus-infected cells by human natural killer cells depends on natural cytotoxicity receptors. J. Virol. 80 (2006) 2225-2233
    • (2006) J. Virol. , vol.80 , pp. 2225-2233
    • Chisholm, S.E.1    Reyburn, H.T.2
  • 10
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V., and Yuan J. Proteases to die for. Genes Dev. 12 (1998) 1551-1570
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 11
    • 0030861788 scopus 로고    scopus 로고
    • The genome organization of the Nidovirales: similarities and differences between Arteri-, Toro-, and Coronaviruses
    • De Vries A.A.F., Horzinek M.C., Rottier P.J.M., and de Groot J.R. The genome organization of the Nidovirales: similarities and differences between Arteri-, Toro-, and Coronaviruses. Semin. Virol. 8 (1997) 33-47
    • (1997) Semin. Virol. , vol.8 , pp. 33-47
    • De Vries, A.A.F.1    Horzinek, M.C.2    Rottier, P.J.M.3    de Groot, J.R.4
  • 12
    • 0037176728 scopus 로고    scopus 로고
    • Characterization of regions in the GP5 protein of porcine reproductive and respiratory syndrome virus required to induce apoptotic cell death
    • Fernandez A., Suarez P., Castro J.M., Tabares E., and Diaz-Guerra M. Characterization of regions in the GP5 protein of porcine reproductive and respiratory syndrome virus required to induce apoptotic cell death. Virus Res. 83 (2002) 103-118
    • (2002) Virus Res. , vol.83 , pp. 103-118
    • Fernandez, A.1    Suarez, P.2    Castro, J.M.3    Tabares, E.4    Diaz-Guerra, M.5
  • 13
    • 0037718355 scopus 로고    scopus 로고
    • Adenoviral-expressed GP5 of porcine respiratory and reproductive syndrome virus differs in its cellular maturation from the authentic viral protein but maintains known biological functions
    • Gagnon C.A., Lachapelle G., Langelier Y., Massie B., and Dea S. Adenoviral-expressed GP5 of porcine respiratory and reproductive syndrome virus differs in its cellular maturation from the authentic viral protein but maintains known biological functions. Arch. Virol. 148 (2003) 951-972
    • (2003) Arch. Virol. , vol.148 , pp. 951-972
    • Gagnon, C.A.1    Lachapelle, G.2    Langelier, Y.3    Massie, B.4    Dea, S.5
  • 14
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., and Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13 (1999) 1899-1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 16
    • 0036289047 scopus 로고    scopus 로고
    • A time to kill: viral manipulation of the cell death program
    • Hay S., and Kannourakis G. A time to kill: viral manipulation of the cell death program. J. Gen. Virol. 83 (2002) 1547-1564
    • (2002) J. Gen. Virol. , vol.83 , pp. 1547-1564
    • Hay, S.1    Kannourakis, G.2
  • 17
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen K.M., Bhat M.B., Wang H.W., Ma J., and Nieminen A.L. Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274 (1999) 5654-5658
    • (1999) J. Biol. Chem. , vol.274 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.4    Nieminen, A.L.5
  • 19
    • 0037086661 scopus 로고    scopus 로고
    • Heat-shock protein 70 attenuates nitric oxide-induced apoptosis in RAW macrophages by preventing cytochrome c release
    • Klein S.D., and Brüne B. Heat-shock protein 70 attenuates nitric oxide-induced apoptosis in RAW macrophages by preventing cytochrome c release. Biochem. J. 362 (2002) 635-641
    • (2002) Biochem. J. , vol.362 , pp. 635-641
    • Klein, S.D.1    Brüne, B.2
  • 20
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer S.J., Wei M.C., Saito M., Weiler S., Oh K.J., and Schlesinger P.H. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 12 (2000) 1166-1173
    • (2000) Cell Death Differ. , vol.12 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 21
    • 0038787758 scopus 로고    scopus 로고
    • Apoptosis in the lungs of pigs infected with porcine reproductive and respiratory syndrome virus and associations with the production of apoptogenic cytokines
    • Labarque G., Van Gucht S., Nauwynck H., Van Reeth K., and Pensaert M. Apoptosis in the lungs of pigs infected with porcine reproductive and respiratory syndrome virus and associations with the production of apoptogenic cytokines. Vet. Res. 34 (2003) 249-260
    • (2003) Vet. Res. , vol.34 , pp. 249-260
    • Labarque, G.1    Van Gucht, S.2    Nauwynck, H.3    Van Reeth, K.4    Pensaert, M.5
  • 22
    • 0034717139 scopus 로고    scopus 로고
    • Caspase inhibitor P35 and inhibitor of apoptosis Op-IAP block in vivo proteolytic activation of an effector caspase at different steps
    • LaCount D.J., Hanson S.F., Schneider C.L., and Friesen P.D. Caspase inhibitor P35 and inhibitor of apoptosis Op-IAP block in vivo proteolytic activation of an effector caspase at different steps. J. Biol. Chem. 275 (2000) 15657-15664
    • (2000) J. Biol. Chem. , vol.275 , pp. 15657-15664
    • LaCount, D.J.1    Hanson, S.F.2    Schneider, C.L.3    Friesen, P.D.4
  • 23
    • 0036843525 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation
    • Langelier Y., Bergeron S., Chabaud S., Lippens J., Guilbault C., Sasseville A.M., Denis S., Mosser D.D., and Massie B. The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation. J. Gen. Virol. 83 (2002) 2779-2789
    • (2002) J. Gen. Virol. , vol.83 , pp. 2779-2789
    • Langelier, Y.1    Bergeron, S.2    Chabaud, S.3    Lippens, J.4    Guilbault, C.5    Sasseville, A.M.6    Denis, S.7    Mosser, D.D.8    Massie, B.9
  • 24
    • 34547684476 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus induces apoptosis through a mitochondria-mediated pathway
    • (Epub ahead of print)
    • Lee S.-M., and Kleiboeker S.B. Porcine reproductive and respiratory syndrome virus induces apoptosis through a mitochondria-mediated pathway. Virology (2007) (Epub ahead of print)
    • (2007) Virology
    • Lee, S.-M.1    Kleiboeker, S.B.2
  • 25
    • 7044231025 scopus 로고    scopus 로고
    • Differential host cell gene expression regulated by the porcine reproductive and respiratory syndrome virus GP4 and GP5 glycoproteins
    • Lee C., Bachand A., Murthaugh M.P., and Yoo D. Differential host cell gene expression regulated by the porcine reproductive and respiratory syndrome virus GP4 and GP5 glycoproteins. Vet. Immunol. Immunopathol. 102 (2004) 189-198
    • (2004) Vet. Immunol. Immunopathol. , vol.102 , pp. 189-198
    • Lee, C.1    Bachand, A.2    Murthaugh, M.P.3    Yoo, D.4
  • 26
    • 2642543931 scopus 로고    scopus 로고
    • Characterization of the porcine reproductive and respiratory syndrome virus glycoprotein 5 (GP5) in stably expressing cells
    • Lee C., Rogan D., Erickson L., Zhang J., and Yoo D. Characterization of the porcine reproductive and respiratory syndrome virus glycoprotein 5 (GP5) in stably expressing cells. Virus Res. 104 (2004) 33-38
    • (2004) Virus Res. , vol.104 , pp. 33-38
    • Lee, C.1    Rogan, D.2    Erickson, L.3    Zhang, J.4    Yoo, D.5
  • 27
    • 0029860897 scopus 로고    scopus 로고
    • Comparison of nucleic and amino acid sequences and phylogenetic analysis of the GS protein of various equine arteritis virus isolates
    • Lepage N., St-Laurent G., Carman S., and Archambault D. Comparison of nucleic and amino acid sequences and phylogenetic analysis of the GS protein of various equine arteritis virus isolates. Virus Genes 13 (1996) 87-91
    • (1996) Virus Genes , vol.13 , pp. 87-91
    • Lepage, N.1    St-Laurent, G.2    Carman, S.3    Archambault, D.4
  • 28
    • 0242331747 scopus 로고    scopus 로고
    • Induction of caspase-dependent apoptosis in cultured rat oligodendrocytes by murine coronavirus is mediated during cell entry and does not require virus replication
    • Liu Y., Cai Y., and Zhang X. Induction of caspase-dependent apoptosis in cultured rat oligodendrocytes by murine coronavirus is mediated during cell entry and does not require virus replication. J. Virol. 77 (2003) 11952-11963
    • (2003) J. Virol. , vol.77 , pp. 11952-11963
    • Liu, Y.1    Cai, Y.2    Zhang, X.3
  • 29
    • 0031888264 scopus 로고    scopus 로고
    • Inducible overexpression of a toxic protein by an adenovirus vector with a tetracycline-regulatable expression cassette
    • Massie B., Couture F., Lamoureux L., Mosser D.D., Guilbault C., Jolicoeur P., Bélanger F., and Langelier Y. Inducible overexpression of a toxic protein by an adenovirus vector with a tetracycline-regulatable expression cassette. J. Virol. 72 (1998) 2289-2298
    • (1998) J. Virol. , vol.72 , pp. 2289-2298
    • Massie, B.1    Couture, F.2    Lamoureux, L.3    Mosser, D.D.4    Guilbault, C.5    Jolicoeur, P.6    Bélanger, F.7    Langelier, Y.8
  • 33
    • 7044264364 scopus 로고    scopus 로고
    • Apoptosis and porcine reproductive and respiratory syndrome virus
    • Miller L.C., and Fox J.M. Apoptosis and porcine reproductive and respiratory syndrome virus. Vet. Immunol. Immunopathol. 102 (2004) 131-142
    • (2004) Vet. Immunol. Immunopathol. , vol.102 , pp. 131-142
    • Miller, L.C.1    Fox, J.M.2
  • 34
    • 0036302456 scopus 로고    scopus 로고
    • Growth characteristics of a highly virulent, a moderately virulent, and an avirulent strain of equine arteritis virus in primary equine endothelial cells are predictive of their virulence to horses
    • Moore B.D., Balasuriya U.B.R., Hedges J.F., and MacLachlan N.J. Growth characteristics of a highly virulent, a moderately virulent, and an avirulent strain of equine arteritis virus in primary equine endothelial cells are predictive of their virulence to horses. Virology 298 (2002) 39-44
    • (2002) Virology , vol.298 , pp. 39-44
    • Moore, B.D.1    Balasuriya, U.B.R.2    Hedges, J.F.3    MacLachlan, N.J.4
  • 36
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., and Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 98-103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 37
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6 (1999) 1028-1042
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 39
    • 2342510973 scopus 로고    scopus 로고
    • Use of multiple assay endpoints to investigate the effects of incubation time, dose of toxin, and plating density in cell-based cytotoxicity assays
    • Riss T.L., and Moravec R.A. Use of multiple assay endpoints to investigate the effects of incubation time, dose of toxin, and plating density in cell-based cytotoxicity assays. Assay Drug Dev. Technol. 2 (2004) 51-62
    • (2004) Assay Drug Dev. Technol. , vol.2 , pp. 51-62
    • Riss, T.L.1    Moravec, R.A.2
  • 40
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • Roucou X., Montessuit S., Antonssonã B., and Martinou J.C. Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein. Biochem. J. 368 (2002) 915-921
    • (2002) Biochem. J. , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonssonã, B.3    Martinou, J.C.4
  • 41
    • 0032873283 scopus 로고    scopus 로고
    • Isolation and analysis of components of CD95 (APO-1/Fas) death-inducing signaling complex
    • Scaffidi C., Krammer P.H., and Peter M.E. Isolation and analysis of components of CD95 (APO-1/Fas) death-inducing signaling complex. Methods 17 (1999) 287-291
    • (1999) Methods , vol.17 , pp. 287-291
    • Scaffidi, C.1    Krammer, P.H.2    Peter, M.E.3
  • 43
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9 (2002) 459-470
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 44
    • 0032408195 scopus 로고    scopus 로고
    • A pneumo-virulent United States isolate of porcine reproductive and respiratory syndrome virus induces apoptosis in bystander cells both in vitro and in vivo
    • Sirinarumitr T., Zhang Y., Kluge J.P., Halbur P.G., and Paul P.S. A pneumo-virulent United States isolate of porcine reproductive and respiratory syndrome virus induces apoptosis in bystander cells both in vitro and in vivo. J. Gen. Virol. 79 (1998) 2989-2995
    • (1998) J. Gen. Virol. , vol.79 , pp. 2989-2995
    • Sirinarumitr, T.1    Zhang, Y.2    Kluge, J.P.3    Halbur, P.G.4    Paul, P.S.5
  • 45
    • 0031925071 scopus 로고    scopus 로고
    • The molecular biology of arteriviruses
    • Snijder E.J., and Meulenberg J.M. The molecular biology of arteriviruses. J. Gen. Virol. 79 (1998) 961-979
    • (1998) J. Gen. Virol. , vol.79 , pp. 961-979
    • Snijder, E.J.1    Meulenberg, J.M.2
  • 47
    • 0027955176 scopus 로고
    • Detection of equine arteritis virus following amplification of structural and nonstructural viral genes by reverse transcription-PCR
    • St-Laurent G., Morin G., and Archambault D. Detection of equine arteritis virus following amplification of structural and nonstructural viral genes by reverse transcription-PCR. J. Clin. Microbiol. 32 (1994) 658-665
    • (1994) J. Clin. Microbiol. , vol.32 , pp. 658-665
    • St-Laurent, G.1    Morin, G.2    Archambault, D.3
  • 48
    • 14844346931 scopus 로고    scopus 로고
    • The bovine viral diarrhea virus NS3 protein, when expressed alone in mammalian cells, induces apoptosis which correlates with caspase-8 and caspase-9 activation
    • St-Louis M.-C., Massie B., and Archambault D. The bovine viral diarrhea virus NS3 protein, when expressed alone in mammalian cells, induces apoptosis which correlates with caspase-8 and caspase-9 activation. Vet. Res. 36 (2005) 213-227
    • (2005) Vet. Res. , vol.36 , pp. 213-227
    • St-Louis, M.-C.1    Massie, B.2    Archambault, D.3
  • 49
    • 0029937848 scopus 로고    scopus 로고
    • Open reading frame 5 of porcine reproductive and respiratory syndrome virus as a cause of virus-induced apoptosis
    • Suárez P., Díaz-Guerra M., Prieto C., Esteban M., Castro J.M., Nieto A., and Ortín J. Open reading frame 5 of porcine reproductive and respiratory syndrome virus as a cause of virus-induced apoptosis. J. Virol. 70 (1996) 2876-2882
    • (1996) J. Virol. , vol.70 , pp. 2876-2882
    • Suárez, P.1    Díaz-Guerra, M.2    Prieto, C.3    Esteban, M.4    Castro, J.M.5    Nieto, A.6    Ortín, J.7
  • 52
    • 0032558412 scopus 로고    scopus 로고
    • Cyclosporin A inhibits apoptosis of human endothelial cells by preventing release of cytochrome c from mitochondria
    • Walter D.H., Haendeler J., Galle J., Zeiher A.M., and Dimmeler S. Cyclosporin A inhibits apoptosis of human endothelial cells by preventing release of cytochrome c from mitochondria. Circulation 98 (1998) 1153-1157
    • (1998) Circulation , vol.98 , pp. 1153-1157
    • Walter, D.H.1    Haendeler, J.2    Galle, J.3    Zeiher, A.M.4    Dimmeler, S.5
  • 53
    • 33846414395 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus productively infects monocyte-derived dentritic cells and compromises their antigen-presenting ability
    • Wang X., Eaton M., Mayer M., Li H., He D., Nelson E., and Christopher-Hennings J. Porcine reproductive and respiratory syndrome virus productively infects monocyte-derived dentritic cells and compromises their antigen-presenting ability. Arch. Virol. 152 (2007) 289-303
    • (2007) Arch. Virol. , vol.152 , pp. 289-303
    • Wang, X.1    Eaton, M.2    Mayer, M.3    Li, H.4    He, D.5    Nelson, E.6    Christopher-Hennings, J.7
  • 54
    • 0029983059 scopus 로고    scopus 로고
    • Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis
    • Zamzami N., Marchetti P., Castedo M., Hirsch T., Susin S.A., Masse B., and Kroemer G. Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis. FEBS Lett. 384 (1996) 53-57
    • (1996) FEBS Lett. , vol.384 , pp. 53-57
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Hirsch, T.4    Susin, S.A.5    Masse, B.6    Kroemer, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.