메뉴 건너뛰기




Volumn 24, Issue 1, 2011, Pages 25-36

Cell-penetrating peptides derived from viral capsid proteins

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; CELL PENETRATING PEPTIDE; GREEN FLUORESCENT PROTEIN; RECOMBINANT PROTEIN; VEGETABLE PROTEIN; VIRUS PROTEIN; VIRUS RNA;

EID: 78650635548     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-07-10-0147     Document Type: Article
Times cited : (21)

References (56)
  • 1
    • 13144271579 scopus 로고    scopus 로고
    • Deletion of highly conserved arginine-rich RNA binding motif in Cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints
    • Annamalai, P., Apte, S., Wilkens, S. and Rao, A. L. N. 2005. Deletion of highly conserved arginine-rich RNA binding motif in Cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints. J. Virol. 79:3277-3288.
    • (2005) J. Virol. , vol.79 , pp. 3277-3288
    • Annamalai, P.1    Apte, S.2    Wilkens, S.3    Rao, A.L.N.4
  • 2
    • 33751235599 scopus 로고    scopus 로고
    • Electrostatic origin of the genome packing in viruses
    • Belyi, V. A. and Muthukumar, M. 2006. Electrostatic origin of the genome packing in viruses. Proc. Natl. Acad. Sci. U.S.A. 103:17174-17178.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17174-17178
    • Belyi, V.A.1    Muthukumar, M.2
  • 3
    • 33847351351 scopus 로고    scopus 로고
    • Noncovalent protein transduction in plant cells by macropinocytosis
    • Chang, M., Chou, J.-C., Chen, C.-P., Liu, B. R. and Lee, H.-J. 2007. Noncovalent protein transduction in plant cells by macropinocytosis. New Phytol. 174:46-56.
    • (2007) New Phytol. , vol.174 , pp. 46-56
    • Chang, M.1    Chou, J.-C.2    Chen, C.-P.3    Liu, B.R.4    Lee, H.-J.5
  • 4
    • 67349259641 scopus 로고    scopus 로고
    • Translocation of cell-penetrating peptides and delivery of their cargoes in triticale microspores
    • Chugh, A., Amundsen, E., and Eudes, F. 2009. Translocation of cell-penetrating peptides and delivery of their cargoes in triticale microspores. Plant Cell Rep. 28:801-810.
    • (2009) Plant Cell Rep. , vol.28 , pp. 801-810
    • Chugh, A.1    Amundsen, E.2    Eudes, F.3
  • 5
    • 33847075874 scopus 로고    scopus 로고
    • Translocation and nuclear accumulation of monomer and dimer of HIV-1 Tat basic domain in triticale mesophyll protoplasts
    • Chugh, A., and Eudes, F. 2007. Translocation and nuclear accumulation of monomer and dimer of HIV-1 Tat basic domain in triticale mesophyll protoplasts. BBA-Biomembranes 1768:419-426.
    • (2007) BBA-Biomembranes , vol.1768 , pp. 419-426
    • Chugh, A.1    Eudes, F.2
  • 6
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. 1994. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269:10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 8
    • 0042232110 scopus 로고    scopus 로고
    • Studies on the internalization mechanism of cationic cell-penetrating peptides
    • Drin, G., Cottin, S., Blanc, E., Rees, A. R., and Temsamani, J. 2003. Studies on the internalization mechanism of cationic cell-penetrating peptides. J. Biol. Chem. 278:31192-31201.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31192-31201
    • Drin, G.1    Cottin, S.2    Blanc, E.3    Rees, A.R.4    Temsamani, J.5
  • 9
    • 0027369139 scopus 로고
    • Identification of domains in Brome mosaic virus RNA-1 and coat protein necessary for specific interaction and encapsidation
    • Duggal, R., and Hall, T. C. 1993. Identification of domains in Brome mosaic virus RNA-1 and coat protein necessary for specific interaction and encapsidation. J. Virol. 67:6406-6412.
    • (1993) J. Virol. , vol.67 , pp. 6406-6412
    • Duggal, R.1    Hall, T.C.2
  • 10
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherinderived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist, A., Lindgren, M., Bartfai, T., and Langel, Ü. 2001. VE-cadherinderived cell-penetrating peptide, pVEC, with carrier functions. Exp. Cell Res. 269:237-244.
    • (2001) Exp. Cell Res. , vol.269 , pp. 237-244
    • Elmquist, A.1    Lindgren, M.2    Bartfai, T.3    Langel, Ü.4
  • 12
    • 0035137639 scopus 로고    scopus 로고
    • Protein transduction: An alternative to genetic intervention?
    • Ford, K. G., Souberbielle, B. E., Darling, D., and Farzaneh, F. 2001. Protein transduction: An alternative to genetic intervention? Gene Ther. 8:1-4.
    • (2001) Gene Ther. , vol.8 , pp. 1-4
    • Ford, K.G.1    Souberbielle, B.E.2    Darling, D.3    Farzaneh, F.4
  • 13
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and Pabo, C. O. 1988. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55:1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 14
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane- permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S., Suzuki, T., Ohashi, W., Yagami, T., Tanaka, S., Ueda, K., and Sugiura, Y. 2001. Arginine-rich peptides. An abundant source of membrane- permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:5836-5840.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 15
    • 34147103472 scopus 로고    scopus 로고
    • First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodelling
    • Gerbal-Chaloin, S., Gondeau, C., Aldrian-Herrada, G., Heitz, F., Gauthier- Rouvière, C., and Divita, G. 2007. First step of the cell-penetrating peptide mechanism involves Rac1 GTPase-dependent actin-network remodelling. Biol. Cell 99:223-238.
    • (2007) Biol Cell , vol.99 , pp. 223-238
    • Gerbal-Chaloin, S.1    Gondeau, C.2    Aldrian-Herrada, G.3    Heitz, F.4    Gauthier-Rouvière, C.5    Divita, G.6
  • 16
    • 27644451296 scopus 로고    scopus 로고
    • Interaction between Brome mosaic virus proteins and RNAs: Effects on RNA replication, protein expression, and RNA stability
    • Gopinath, K., Dragnea, B., and Kao, C. 2005. Interaction between Brome mosaic virus proteins and RNAs: Effects on RNA replication, protein expression, and RNA stability. J. Virol. 79:14222-14234.
    • (2005) J. Virol. , vol.79 , pp. 14222-14234
    • Gopinath, K.1    Dragnea, B.2    Kao, C.3
  • 17
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat transactivator protein
    • Green, M., and Loewenstein, P. M. 1988. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat transactivator protein. Cell 55:1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 18
    • 0345742595 scopus 로고    scopus 로고
    • Template sequence near the initiation nucleotide can modulate Brome mosaic virus RNA accumulation in plant protoplasts
    • Hema, M., and Kao, C. C. 2004. Template sequence near the initiation nucleotide can modulate Brome mosaic virus RNA accumulation in plant protoplasts. J. Virol. 78:1169-1180.
    • (2004) J. Virol. , vol.78 , pp. 1169-1180
    • Hema, M.1    Kao, C.C.2
  • 21
    • 0036112232 scopus 로고    scopus 로고
    • Barley stripe mosaic virus-induced gene silencing in a monocot plant
    • Holzberg, S., Brosio, P., Gross, C., and Pogue, G. P. 2002. Barley stripe mosaic virus-induced gene silencing in a monocot plant. Plant J. 30:315-327.
    • (2002) Plant J. , vol.30 , pp. 315-327
    • Holzberg, S.1    Brosio, P.2    Gross, C.3    Pogue, G.P.4
  • 22
    • 0027469808 scopus 로고
    • RNA-dependent replication, transcription, and persistence of brome mosaic virus RNA replicons in S. cerevisiae
    • Janda, M., and Ahlquist, P. 1993. RNA-dependent replication, transcription, and persistence of brome mosaic virus RNA replicons in S. cerevisiae. Cell 72:961-970.
    • (1993) Cell , vol.72 , pp. 961-970
    • Janda, M.1    Ahlquist, P.2
  • 23
    • 0023273613 scopus 로고
    • High efficiency T7 polymerase synthesis of infectious rna from cloned brome mosaic virus cdna and effects of 5′ extensions on transcript infectivity
    • Janda, M., French, R., and Ahlquist, P. 1987. High efficiency T7 polymerase synthesis of infectious rna from cloned brome mosaic virus cdna and effects of 5′ extensions on transcript infectivity. Virology 158:259-262.
    • (1987) Virology , vol.158 , pp. 259-262
    • Janda, M.1    French, R.2    Ahlquist, P.3
  • 25
  • 26
    • 4644225722 scopus 로고    scopus 로고
    • Heterologous RNA encapsidated in Pariacoto virus-like particles forms a dodecahedral cage similar to genomic RNA in wild-type virions
    • Johnson, K. N., Tang, L., Johnson, J. E., and Ball, L. A. 2004. Heterologous RNA encapsidated in Pariacoto virus-like particles forms a dodecahedral cage similar to genomic RNA in wild-type virions. J. Virol. 78:11371-11378.
    • (2004) J. Virol. , vol.78 , pp. 11371-11378
    • Johnson, K.N.1    Tang, L.2    Johnson, J.E.3    Ball, L.A.4
  • 27
    • 34548172649 scopus 로고    scopus 로고
    • Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides
    • Jones, A. T. 2007. Macropinocytosis: Searching for an endocytic identity and role in the uptake of cell penetrating peptides. J. Cell Mol. Med. 11:670-684.
    • (2007) J. Cell Mol. Med. , vol.11 , pp. 670-684
    • Jones, A.T.1
  • 28
    • 0347966546 scopus 로고    scopus 로고
    • Brome mosaic virus, good for an RNA virologist's basic needs
    • Kao, C. C., and Sivakumaran, K. 2000. Brome mosaic virus, good for an RNA virologist's basic needs. Mol. Plant Path. 1:91-97.
    • (2000) Mol. Plant Path. , vol.1 , pp. 91-97
    • Kao, C.C.1    Sivakumaran, K.2
  • 29
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr, M. C., and Teasdale, R. D. 2009. Defining macropinocytosis. Traffic 10:364-371.
    • (2009) Traffic , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 31
    • 0025251611 scopus 로고
    • Analysis of the role of brome mosaic virus 1a protein domains in RNA replication, using linker insertion mutagenesis
    • Kroner, P. A., Young, B. M., and Ahlquist, P. 1990. Analysis of the role of brome mosaic virus 1a protein domains in RNA replication, using linker insertion mutagenesis. J. Virol. 64:6110-6120.
    • (1990) J. Virol. , vol.64 , pp. 6110-6120
    • Kroner, P.A.1    Young, B.M.2    Ahlquist, P.3
  • 33
    • 0036294226 scopus 로고    scopus 로고
    • The crystallographic structure of brome mosaic virus
    • Lucas, R. W., Larson, S. B., and McPherson, A. 2002. The crystallographic structure of brome mosaic virus. J. Mol. Biol. 317:95-108.
    • (2002) J. Mol. Biol. , vol.317 , pp. 95-108
    • Lucas, R.W.1    Larson, S.B.2    McPherson, A.3
  • 35
    • 25144520907 scopus 로고    scopus 로고
    • On the mechanisms of the internalization of S4(13)-PV cellpenetrating peptide
    • Mano, M., Teodosio, C., Paiva, A., Simoes, S., and Pedroso de Lima, M. C. 2005. On the mechanisms of the internalization of S4(13)-PV cellpenetrating peptide. Biochem. J. 390:603-612.
    • (2005) Biochem. J. , vol.390 , pp. 603-612
    • Mano, M.1    Teodosio, C.2    Paiva, A.3    Simoes, S.4    Pedroso De Lima, M.C.5
  • 36
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer, J., and Helenius, A. 2008. Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320:531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 37
    • 70449120118 scopus 로고    scopus 로고
    • Cell-surface accumulation of Flock house virusderived peptide leads to efficient internalization via macropinocytosis
    • Nakase, I., Hirose, H., Tanaka, G., Tadokoro, A., Kobayashi, S., Takeuchi, T., and Futaki, S. 2009. Cell-surface accumulation of Flock house virusderived peptide leads to efficient internalization via macropinocytosis. Mol. Ther. 17:1868-1876.
    • (2009) Mol. Ther. , vol.17 , pp. 1868-1876
    • Nakase, I.1    Hirose, H.2    Tanaka, G.3    Tadokoro, A.4    Kobayashi, S.5    Takeuchi, T.6    Futaki, S.7
  • 38
    • 33846223900 scopus 로고    scopus 로고
    • Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis
    • Nakase, I., Tadokoro, A., Kawabata, N., Takeuchi, T., Katoh, H., Hiramoto, K., Negishi, M., Nomizu, M., Sugiura, Y., and Futaki, S. 2007. Interaction of arginine-rich peptides with membrane-associated proteoglycans is crucial for induction of actin organization and macropinocytosis. Biochem. 46:492-501.
    • (2007) Biochem. , vol.46 , pp. 492-501
    • Nakase, I.1    Tadokoro, A.2    Kawabata, N.3    Takeuchi, T.4    Katoh, H.5    Hiramoto, K.6    Negishi, M.7    Nomizu, M.8    Sugiura, Y.9    Futaki, S.10
  • 39
    • 0031944983 scopus 로고    scopus 로고
    • Proton gradientdriven nickel uptake by vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Nishimura, K., Igarashi, K., and Kakinuma, Y. 1998. Proton gradientdriven nickel uptake by vacuolar membrane vesicles of Saccharomyces cerevisiae. J. Bacteriol. 180:1962-1964.
    • (1998) J. Bacteriol. , vol.180 , pp. 1962-1964
    • Nishimura, K.1    Igarashi, K.2    Kakinuma, Y.3
  • 40
    • 0242406997 scopus 로고    scopus 로고
    • Brome mosaic virus RNA replication: Revealing the role of the host in RNA virus replication
    • Noueiry, A. O., and Ahlquist, P. 2003. Brome mosaic virus RNA replication: Revealing the role of the host in RNA virus replication. Ann. Rev.Phytopath. 41:77-98.
    • (2003) Ann. Rev.Phytopath. , vol.41 , pp. 77-98
    • Noueiry, A.O.1    Ahlquist, P.2
  • 41
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • Oehlke, J., Scheller, A., Wiesner, B., Krause, E., Beyermann, M., Klauschenz, E., Melzig, M., and Bienert, M. 1998. Cellular uptake of an α-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. BBA-Biomembranes 1414:127-139.
    • (1998) BBA-Biomembranes , vol.1414 , pp. 127-139
    • Oehlke, J.1    Scheller, A.2    Wiesner, B.3    Krause, E.4    Beyermann, M.5    Klauschenz, E.6    Melzig, M.7    Bienert, M.8
  • 42
    • 0025895141 scopus 로고
    • Use of bromovirus RNA3 hybrids to study template specificity in viral RNA amplication
    • Pacha, R. F., and Ahlquist, P. 1991. use of bromovirus RNA3 hybrids to study template specificity in viral RNA amplication. J. Virol. 65:3693-3703.
    • (1991) J. Virol. , vol.65 , pp. 3693-3703
    • Pacha, R.F.1    Ahlquist, P.2
  • 44
    • 0031014704 scopus 로고    scopus 로고
    • Encapsidation of turnip crinkle virus is defined by a specific packaging signal and RNA size
    • Qu, F., and Morris, T. 1997. Encapsidation of turnip crinkle virus is defined by a specific packaging signal and RNA size. J. Virol., 71:1428-1435.
    • (1997) J. Virol. , vol.71 , pp. 1428-1435
    • Qu, F.1    Morris, T.2
  • 45
    • 0024759051 scopus 로고
    • Effects of deletions in the N-terminal basic arm of brome mosaic virus coat protein on RNA packaging and systemic infection
    • Sacher, R., and Ahlquist, P. 1989. Effects of deletions in the N-terminal basic arm of brome mosaic virus coat protein on RNA packaging and systemic infection. J. Virol. 63:4545-4552.
    • (1989) J. Virol. , vol.63 , pp. 4545-4552
    • Sacher, R.1    Ahlquist, P.2
  • 46
    • 0036919078 scopus 로고    scopus 로고
    • Tip-growing cells of the moss Ceratodon purpureus are gravitropic in high-density media
    • Schwuchow, J. M., Kern, V. D., and Sack, F. D. 2002. Tip-growing cells of the moss Ceratodon purpureus are gravitropic in high-density media. Plant Physiol. 130:2095-2100.
    • (2002) Plant Physiol. , vol.130 , pp. 2095-2100
    • Schwuchow, J.M.1    Kern, V.D.2    Sack, F.D.3
  • 47
    • 0023039977 scopus 로고
    • Identification of regions of Brome mosaic virus coat protein chemically cross-linked in situ to viral RNA
    • Sgro J.-Y., Jacrot, B., and Chroboczek, J. 1986. Identification of regions of Brome mosaic virus coat protein chemically cross-linked in situ to viral RNA. Eur. J. Biochem. 154:69-76.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 69-76
    • Sgro, J.-Y.1    Jacrot, B.2    Chroboczek, J.3
  • 48
    • 0038371349 scopus 로고    scopus 로고
    • Brome mosaic virus RNA syntheses in vitro and in barley protoplasts
    • Sivakumaran, K., Hema, M., and Kao, C. C. 2003. Brome mosaic virus RNA syntheses in vitro and in barley protoplasts. J. Virol. 77:5703-5711.
    • (2003) J. Virol. , vol.77 , pp. 5703-5711
    • Sivakumaran, K.1    Hema, M.2    Kao, C.C.3
  • 49
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith, A. E., and Helenius, A. 2004. How viruses enter animal cells. Science 304:237-242.
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 50
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia, J. S., Stan, R. V., and Dowdy, S. F. 2004. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10:310-315.
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 51
    • 35548933794 scopus 로고    scopus 로고
    • Arabidopsis TANGLED identifies the division plane throughout mitosis and cytokinesis
    • Walker, K. L., Müller, S., Moss, D., Ehrhardt, D. W., and Smith, L. G. 2007. Arabidopsis TANGLED identifies the division plane throughout mitosis and cytokinesis. Curr. Biol. 17:1827-1836.
    • (2007) Curr. Biol. , vol.17 , pp. 1827-1836
    • Walker, K.L.1    Müller, S.2    Moss, D.3    Ehrhardt, D.W.4    Smith, L.G.5
  • 52
    • 34447252122 scopus 로고    scopus 로고
    • Entry of Rice dwarf virus into cultured cells of its insect vector involves clathrin-mediated endocytosis
    • Wei, T., Chen, H., Ichiki-Uehara, T., Hibino, H., and Omura, T. 2007. Entry of Rice dwarf virus into cultured cells of its insect vector involves clathrin-mediated endocytosis. J. Virol. 81:7811-7815.
    • (2007) J. Virol. , vol.81 , pp. 7811-7815
    • Wei, T.1    Chen, H.2    Ichiki-Uehara, T.3    Hibino, H.4    Omura, T.5
  • 53
    • 40149105692 scopus 로고    scopus 로고
    • Cis- and trans-acting functions of Brome mosaic virus protein 1a in genomic RNA1 replication
    • Yi, G., and Kao, C. 2008. Cis- and trans-acting functions of Brome mosaic virus protein 1a in genomic RNA1 replication. J. Virol., 82:3045-3053.
    • (2008) J. Virol. , vol.82 , pp. 3045-3053
    • Yi, G.1    Kao, C.2
  • 54
    • 67650700208 scopus 로고    scopus 로고
    • RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation
    • Yi, G., Vaughan, R. C., Yarbrough, I., Dharmaiah, S., and Kao, C. C. 2009. RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation. J. Mol. Biol. 391:314-326.
    • (2009) J. Mol. Biol. , vol.391 , pp. 314-326
    • Yi, G.1    Vaughan, R.C.2    Yarbrough, I.3    Dharmaiah, S.4    Kao, C.C.5
  • 55
    • 37649002522 scopus 로고    scopus 로고
    • The P2 capsid protein of the nonenveloped rice dwarf phytoreovirus induces membrane fusion in insect host cells
    • Zhou, F., Pu, Y., Wei, T., Liu, H., Deng, W., Wei, C., Ding, B., Omura, T., and Li, Y. 2007. The P2 capsid protein of the nonenveloped rice dwarf phytoreovirus induces membrane fusion in insect host cells. Proc. Natl. Acad. Sci U.S.A. 104:19547-19552.
    • (2007) Proc. Natl. Acad. Sci U.S.A. , vol.104 , pp. 19547-19552
    • Zhou, F.1    Pu, Y.2    Wei, T.3    Liu, H.4    Deng, W.5    Wei, C.6    Ding, B.7    Omura, T.8    Li, Y.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.