메뉴 건너뛰기




Volumn 82, Issue 10, 2008, Pages 4774-4784

Mitochondrial dysfunction in lyssavirus-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 9; CYTOCHROME C OXIDASE; VIRUS PROTEIN;

EID: 43249084547     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02651-07     Document Type: Article
Times cited : (42)

References (60)
  • 2
    • 10044230387 scopus 로고    scopus 로고
    • On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
    • Antunes, F., A. Boveris, and E. Cadenas. 2004. On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide. Proc. Natl. Acad. Sci. USA 101:16774-16779.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16774-16779
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3
  • 3
    • 0035100866 scopus 로고    scopus 로고
    • Evidence of two Lyssavirus phylogroups with distinct pathogenicity and immunogenicity
    • Badrane, H., C. Bahloul, P. Perrin, and N. Tordo. 2001. Evidence of two Lyssavirus phylogroups with distinct pathogenicity and immunogenicity. J. Virol. 75:3268-3276.
    • (2001) J. Virol , vol.75 , pp. 3268-3276
    • Badrane, H.1    Bahloul, C.2    Perrin, P.3    Tordo, N.4
  • 4
    • 0036852215 scopus 로고    scopus 로고
    • To kill or be killed: Viral evasion of apoptosis
    • Benedict, C. A., P. S. Norris, and C. F. Ware. 2002. To kill or be killed: viral evasion of apoptosis. Nat. Immunol. 3:1013-1018.
    • (2002) Nat. Immunol , vol.3 , pp. 1013-1018
    • Benedict, C.A.1    Norris, P.S.2    Ware, C.F.3
  • 5
    • 0027237788 scopus 로고
    • Molecular diversity of the Lyssavirus genus
    • Bourhy, H., B. Kissi, and N. Tordo. 1993. Molecular diversity of the Lyssavirus genus. Virology 194:70-81.
    • (1993) Virology , vol.194 , pp. 70-81
    • Bourhy, H.1    Kissi, B.2    Tordo, N.3
  • 7
    • 0034711013 scopus 로고    scopus 로고
    • Identification of the structural subunits required for formation of the metal centers in subunit 1 of cytochrome c oxidase of Rhodobacter sphacroides
    • Bratton, M. R., L. Hiser, W. E. Antholine, C. Hoganson, and J. P. Hosler. 2000. Identification of the structural subunits required for formation of the metal centers in subunit 1 of cytochrome c oxidase of Rhodobacter sphacroides. Biochemistry 39:12989-12995.
    • (2000) Biochemistry , vol.39 , pp. 12989-12995
    • Bratton, M.R.1    Hiser, L.2    Antholine, W.E.3    Hoganson, C.4    Hosler, J.P.5
  • 8
    • 0034682695 scopus 로고    scopus 로고
    • Apoptosis. Mitochondria - the death signal integrators
    • Brenner, C., and G. Kroemer. 2000. Apoptosis. Mitochondria - the death signal integrators. Science 289:1150-1151.
    • (2000) Science , vol.289 , pp. 1150-1151
    • Brenner, C.1    Kroemer, G.2
  • 12
    • 0032894113 scopus 로고    scopus 로고
    • Apoptosis: An innate immune response to virus infection
    • Everett, H., and G. McFadden. 1999. Apoptosis: an innate immune response to virus infection. Trends Microbiol. 7:160-165.
    • (1999) Trends Microbiol , vol.7 , pp. 160-165
    • Everett, H.1    McFadden, G.2
  • 14
    • 0038314508 scopus 로고    scopus 로고
    • Rabies virus matrix protein regulates the balance of virus transcription and replication
    • Finke, S., R. Mueller-Waldeck, and K. K. Conzelmann. 2003. Rabies virus matrix protein regulates the balance of virus transcription and replication. J. Gen. Virol. 84:1613-1621.
    • (2003) J. Gen. Virol , vol.84 , pp. 1613-1621
    • Finke, S.1    Mueller-Waldeck, R.2    Conzelmann, K.K.3
  • 15
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine, M., J. C. Rain, and P. Legrain. 1997. Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet. 16:277-282.
    • (1997) Nat. Genet , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 16
    • 16244400495 scopus 로고    scopus 로고
    • Neuronal dysfunction and death in rabies virus infection
    • Fu, Z. F., and A. C. Jackson. 2005. Neuronal dysfunction and death in rabies virus infection. J. Neurovirol. 11:101-106.
    • (2005) J. Neurovirol , vol.11 , pp. 101-106
    • Fu, Z.F.1    Jackson, A.C.2
  • 17
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 18
    • 11144300814 scopus 로고    scopus 로고
    • Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria
    • Gizatullina, Z. Z., Y. Chen, S. Zierz, and F. N. Gellerich. 2005. Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria. Biochim. Biophys. Acta 1706:98-104.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 98-104
    • Gizatullina, Z.Z.1    Chen, Y.2    Zierz, S.3    Gellerich, F.N.4
  • 19
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D. R., and G. Kroemer. 2004. The pathophysiology of mitochondrial cell death. Science 305:626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 20
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D. R., and J. C. Reed. 1998. Mitochondria and apoptosis. Science 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 22
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty, R. N., J. Paragas, M. Sudol, and P. Palese. 1999. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J. Virol. 73:2921-2929.
    • (1999) J. Virol , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 23
    • 3042737429 scopus 로고    scopus 로고
    • Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inactivation of NF-kappa B and inhibition of Bcl-xl expression
    • Huerta-Yepez, S., M. Vega, A. Jazirehi, H. Garban, F. Hongo, G. Cheng, and B. Bonavida. 2004. Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inactivation of NF-kappa B and inhibition of Bcl-xl expression. Oncogene 23:4993-5003.
    • (2004) Oncogene , vol.23 , pp. 4993-5003
    • Huerta-Yepez, S.1    Vega, M.2    Jazirehi, A.3    Garban, H.4    Hongo, F.5    Cheng, G.6    Bonavida, B.7
  • 24
    • 3142751325 scopus 로고    scopus 로고
    • Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein
    • Irie, T., J. M. Licata, H. R. Jayakar, M. A. Whitt, P. Bell, and R. N. Harty. 2004. Functional analysis of late-budding domain activity associated with the PSAP motif within the vesicular stomatitis virus M protein. J. Virol. 78:7823-7827.
    • (2004) J. Virol , vol.78 , pp. 7823-7827
    • Irie, T.1    Licata, J.M.2    Jayakar, H.R.3    Whitt, M.A.4    Bell, P.5    Harty, R.N.6
  • 25
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 26
    • 0030994226 scopus 로고    scopus 로고
    • Apoptosis plays an important role in experimental rabies virus infection
    • Jackson, A. C., and J. P. Rossiter. 1997. Apoptosis plays an important role in experimental rabies virus infection. J. Virol. 71:5603-5607.
    • (1997) J. Virol , vol.71 , pp. 5603-5607
    • Jackson, A.C.1    Rossiter, J.P.2
  • 28
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus, K., C. Barrett, and R. Hughey. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14:846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 29
    • 2642566701 scopus 로고    scopus 로고
    • Lyssavirus matrix protein induces apoptosis by a TRAIL-dependent mechanism involving caspase-8 activation
    • Kassis, R., F. Larrous, J. Estaquier, and H. Bourhy. 2004. Lyssavirus matrix protein induces apoptosis by a TRAIL-dependent mechanism involving caspase-8 activation. J. Virol. 78:6543-6555.
    • (2004) J. Virol , vol.78 , pp. 6543-6555
    • Kassis, R.1    Larrous, F.2    Estaquier, J.3    Bourhy, H.4
  • 31
    • 0037383430 scopus 로고    scopus 로고
    • Contrasting effects of matrix protein on apoptosis in HeLa and BHK cells infected with vesicular stomatitis virus are due to inhibition of host gene expression
    • Kopecky, S. A., and D. S. Lyles. 2003. Contrasting effects of matrix protein on apoptosis in HeLa and BHK cells infected with vesicular stomatitis virus are due to inhibition of host gene expression. J. Virol. 77:4658-4669.
    • (2003) J. Virol , vol.77 , pp. 4658-4669
    • Kopecky, S.A.1    Lyles, D.S.2
  • 32
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • Kroemer, G. 2003. Mitochondrial control of apoptosis: an introduction. Biochem. Biophys. Res. Commun. 304:433-435.
    • (2003) Biochem. Biophys. Res. Commun , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 33
    • 4644359695 scopus 로고    scopus 로고
    • Cytochrome C oxidase III interacts with hepatitis B virus X protein in vivo by yeast two-hybrid system
    • Li, D., X. Z. Wang, J. P. Yu, Z. X. Chen, Y. H. Huang, and Q. M. Tao. 2004. Cytochrome C oxidase III interacts with hepatitis B virus X protein in vivo by yeast two-hybrid system. World J. Gastroenterol. 10:2805-2808.
    • (2004) World J. Gastroenterol , vol.10 , pp. 2805-2808
    • Li, D.1    Wang, X.Z.2    Yu, J.P.3    Chen, Z.X.4    Huang, Y.H.5    Tao, Q.M.6
  • 34
    • 22544462822 scopus 로고    scopus 로고
    • Degeneration of neuronal processes after infection with pathogenic, but not attenuated, rabies viruses
    • Li, X. Q., L. Sarmento, and Z. F. Fu. 2005. Degeneration of neuronal processes after infection with pathogenic, but not attenuated, rabies viruses. J. Virol. 79:10063-10068.
    • (2005) J. Virol , vol.79 , pp. 10063-10068
    • Li, X.Q.1    Sarmento, L.2    Fu, Z.F.3
  • 35
    • 33750231542 scopus 로고    scopus 로고
    • Matrix protein of vesicular stomatitis virus harbours a cryptic mitochondrial- targeting motif
    • Lichty, B. D., H. McBride, S. Hanson, and J. C. Bell. 2006. Matrix protein of vesicular stomatitis virus harbours a cryptic mitochondrial- targeting motif. J. Gen. Virol. 87:3379-3384.
    • (2006) J. Gen. Virol , vol.87 , pp. 3379-3384
    • Lichty, B.D.1    McBride, H.2    Hanson, S.3    Bell, J.C.4
  • 36
    • 0032889562 scopus 로고    scopus 로고
    • Matrix protein of rabies virus is responsible for the assembly and budding of bullet-shaped particles and interacts with the transmembrane spike glycoprotein G
    • Mebatsion, T., F. Weiland, and K. K. Conzelmann. 1999. Matrix protein of rabies virus is responsible for the assembly and budding of bullet-shaped particles and interacts with the transmembrane spike glycoprotein G. J. Virol. 73:242-250.
    • (1999) J. Virol , vol.73 , pp. 242-250
    • Mebatsion, T.1    Weiland, F.2    Conzelmann, K.K.3
  • 38
    • 0033822780 scopus 로고    scopus 로고
    • Reinvestigation of the role of the rabies virus glycoprotein in viral pathogenesis using a reverse genetics approach
    • Morimoto, K., H. D. Foley, J. P. McGettigan, M. J. Schnell, and B. Dietzschold. 2000. Reinvestigation of the role of the rabies virus glycoprotein in viral pathogenesis using a reverse genetics approach. J. Neurovirol. 6:373-381.
    • (2000) J. Neurovirol , vol.6 , pp. 373-381
    • Morimoto, K.1    Foley, H.D.2    McGettigan, J.P.3    Schnell, M.J.4    Dietzschold, B.5
  • 39
    • 17344368263 scopus 로고    scopus 로고
    • Pathogenicity of different rabies virus variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron cultures
    • Morimoto, K., D. C. Hooper, S. Spitsin, H. Koprowski, and B. Dietzschold. 1999. Pathogenicity of different rabies virus variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron cultures. J. Virol. 73:510-518.
    • (1999) J. Virol , vol.73 , pp. 510-518
    • Morimoto, K.1    Hooper, D.C.2    Spitsin, S.3    Koprowski, H.4    Dietzschold, B.5
  • 40
    • 4143064737 scopus 로고    scopus 로고
    • Rabies virus stimulates nitric oxide production and CXC chemokine ligand 10 expression in macrophages through activation of extracellular signal-regulated kinases 1 and 2
    • Nakamichi, K., S. Inoue, T. Takasaki, K. Morimoto, and I. Kurane. 2004. Rabies virus stimulates nitric oxide production and CXC chemokine ligand 10 expression in macrophages through activation of extracellular signal-regulated kinases 1 and 2. J. Virol. 78:9376-9388.
    • (2004) J. Virol , vol.78 , pp. 9376-9388
    • Nakamichi, K.1    Inoue, S.2    Takasaki, T.3    Morimoto, K.4    Kurane, I.5
  • 41
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali, M., and R. D. King. 2000. Cascaded multiple classifiers for secondary structure prediction. Protein Sci. 9:1162-1176.
    • (2000) Protein Sci , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 42
    • 0032509105 scopus 로고    scopus 로고
    • Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods
    • Park, J., K. Karplus, C. Barrett, R. Hughey, D. Haussler, T. Hubbard, and C. Chothia. 1998. Sequence comparisons using multiple sequences detect three times as many remote homologues as pairwise methods. J. Mol. Biol. 284:1201-1210.
    • (1998) J. Mol. Biol , vol.284 , pp. 1201-1210
    • Park, J.1    Karplus, K.2    Barrett, C.3    Hughey, R.4    Haussler, D.5    Hubbard, T.6    Chothia, C.7
  • 43
    • 0037318902 scopus 로고    scopus 로고
    • Mitochondria, AIF and caspases - rivaling for cell death execution
    • Penninger, J. M., and G. Kroemer. 2003. Mitochondria, AIF and caspases - rivaling for cell death execution. Nat. Cell Biol. 5:97-99.
    • (2003) Nat. Cell Biol , vol.5 , pp. 97-99
    • Penninger, J.M.1    Kroemer, G.2
  • 44
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N., and A. Geissler. 2001. Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol. 2:339-349.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 45
    • 0242568964 scopus 로고    scopus 로고
    • Glycoprotein of nonpathogenic rabies viruses is a key determinant of human cell apoptosis
    • Prehaud, C., S. Lay, B. Dietzschold, and M. Lafon. 2003. Glycoprotein of nonpathogenic rabies viruses is a key determinant of human cell apoptosis. J. Virol. 77:10537-10547.
    • (2003) J. Virol , vol.77 , pp. 10537-10547
    • Prehaud, C.1    Lay, S.2    Dietzschold, B.3    Lafon, M.4
  • 46
    • 0034766467 scopus 로고    scopus 로고
    • Overexpression of cytochrome c by a recombinant rabies virus attenuates pathogenicity and enhances antiviral immunity
    • Pulmanausahakul, R., M. Faber, K. Morimoto, S. Spitsin, E. Weihe, D. C. Hooper, M. J. Schnell, and B. Dietzschold. 2001. Overexpression of cytochrome c by a recombinant rabies virus attenuates pathogenicity and enhances antiviral immunity. J. Virol. 75:10800-10807.
    • (2001) J. Virol , vol.75 , pp. 10800-10807
    • Pulmanausahakul, R.1    Faber, M.2    Morimoto, K.3    Spitsin, S.4    Weihe, E.5    Hooper, D.C.6    Schnell, M.J.7    Dietzschold, B.8
  • 47
    • 0002478233 scopus 로고    scopus 로고
    • Immunogold labeling of ultrathin cryosections: Application in immunology
    • D. M. Weir, L. A. Herzenberg, and C. Blackwell ed, Blackwell Science, Cambridge, MA
    • Raposo, G., M. J. Kleijmeer, G. Posthuma, J. W. Slot, and H. J. Geuze. 1996. Immunogold labeling of ultrathin cryosections: application in immunology, p. 1-11. In D. M. Weir, L. A. Herzenberg, and C. Blackwell (ed.), Weir's handbook of experimental immunology in four volumes, vol. 4. Blackwell Science, Cambridge, MA.
    • (1996) Weir's handbook of experimental immunology in four volumes , vol.4 , pp. 1-11
    • Raposo, G.1    Kleijmeer, M.J.2    Posthuma, G.3    Slot, J.W.4    Geuze, H.J.5
  • 49
    • 0026675014 scopus 로고
    • Identification of heat shock protein 70 in the rabies virion
    • Sagara, J., and A. Kawai. 1992. Identification of heat shock protein 70 in the rabies virion. Virology 190:845-848.
    • (1992) Virology , vol.190 , pp. 845-848
    • Sagara, J.1    Kawai, A.2
  • 50
    • 0041168570 scopus 로고    scopus 로고
    • NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: Molecular insights into its biological functions
    • Schuler, W., K. Wecker, H. de Rocquigny, Y. Baudat, J. Sire, and B. P. Roques. 1999. NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions. J. Mol. Biol. 285:2105-2117.
    • (1999) J. Mol. Biol , vol.285 , pp. 2105-2117
    • Schuler, W.1    Wecker, K.2    de Rocquigny, H.3    Baudat, Y.4    Sire, J.5    Roques, B.P.6
  • 52
    • 0038158319 scopus 로고    scopus 로고
    • Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential
    • Shirakata, Y., and K. Koike. 2003. Hepatitis B virus X protein induces cell death by causing loss of mitochondrial membrane potential. J. Biol. Chem. 278:22071-22078.
    • (2003) J. Biol. Chem , vol.278 , pp. 22071-22078
    • Shirakata, Y.1    Koike, K.2
  • 55
    • 0141758307 scopus 로고    scopus 로고
    • High level of Bcl-2 counteracts apoptosis mediated by a live rabies virus vaccine strain and induces long-term infection
    • Thoulouze, M. I., M. Lafage, V. J. Yuste, L. Baloul, L. Edelman, G. Kroemer, N. Israel, S. A. Susin, and M. Lafon. 2003. High level of Bcl-2 counteracts apoptosis mediated by a live rabies virus vaccine strain and induces long-term infection. Virology 314:549-561.
    • (2003) Virology , vol.314 , pp. 549-561
    • Thoulouze, M.I.1    Lafage, M.2    Yuste, V.J.3    Baloul, L.4    Edelman, L.5    Kroemer, G.6    Israel, N.7    Susin, S.A.8    Lafon, M.9
  • 57
    • 0035116548 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase inhibition delays death of rabies virus-infected mice
    • Ubol, S., C. Sukwattanapan, and Y. Maneerat. 2001. Inducible nitric oxide synthase inhibition delays death of rabies virus-infected mice. J. Med. Microbiol. 50:238-242.
    • (2001) J. Med. Microbiol , vol.50 , pp. 238-242
    • Ubol, S.1    Sukwattanapan, C.2    Maneerat, Y.3
  • 58
    • 0035283084 scopus 로고    scopus 로고
    • The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria
    • Wiedemann, N., N. Pfanner, and M. T. Ryan. 2001. The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria. EMBO J. 20:951-960.
    • (2001) EMBO J , vol.20 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 59
    • 0035064503 scopus 로고    scopus 로고
    • Multiple viral strategies of HTLV-1 for dysregulation of cell growth control
    • Yoshida, M. 2001. Multiple viral strategies of HTLV-1 for dysregulation of cell growth control. Annu. Rev. Immunol. 19:475-496.
    • (2001) Annu. Rev. Immunol , vol.19 , pp. 475-496
    • Yoshida, M.1
  • 60
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young, J. C., N. J. Hoogenraad, and F. U. Hartl. 2003. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112:41-50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.