메뉴 건너뛰기




Volumn 85, Issue 7, 2011, Pages 3677-3682

Differential sensitivities of retroviruses to integrase strand transfer inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ELVITEGRAVIR; RALTEGRAVIR; ZIDOVUDINE;

EID: 79952580956     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02541-10     Document Type: Article
Times cited : (34)

References (54)
  • 2
    • 0002075936 scopus 로고    scopus 로고
    • Retrotransposons, endogenous retroviruses, and the evolution of retroelements
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory Press, Plainview, NY
    • Boeke, J. D., and J. P. Stoye. 1997. Retrotransposons, endogenous retroviruses, and the evolution of retroelements p. 343-435. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, NY.
    • (1997) Retroviruses , pp. 343-435
    • Boeke, J.D.1    Stoye, J.P.2
  • 3
    • 67549145642 scopus 로고    scopus 로고
    • First Mariner Mos1 transposase inhibitors
    • Bouchet, N., et al. 2009. First Mariner Mos1 transposase inhibitors. Mini Rev. Med. Chem. 9:431-439.
    • (2009) Mini Rev. Med. Chem. , vol.9 , pp. 431-439
    • Bouchet, N.1
  • 4
    • 0034681278 scopus 로고    scopus 로고
    • X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293) - An initial glance of the viral DNA binding platform
    • Chen, Z., et al. 2000. X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293) - an initial glance of the viral DNA binding platform. J. Mol. Biol. 296:521-533.
    • (2000) J. Mol. Biol. , vol.296 , pp. 521-533
    • Chen, Z.1
  • 5
    • 47949114939 scopus 로고    scopus 로고
    • Subgroup and resistance analyses of raltegravir for resistant HIV-1 infection
    • Cooper, D. A., et al. 2008. Subgroup and resistance analyses of raltegravir for resistant HIV-1 infection. N. Engl. J. Med. 359:355-365.
    • (2008) N. Engl. J. Med. , vol.359 , pp. 355-365
    • Cooper, D.A.1
  • 6
    • 62149093020 scopus 로고    scopus 로고
    • The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation
    • Delelis, O., et al. 2009. The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation. Nucleic Acids Res. 37:1193-1201.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1193-1201
    • Delelis, O.1
  • 7
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F., et al. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266:1981-1986.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1
  • 8
    • 77958010223 scopus 로고    scopus 로고
    • Reverse transcription and integration
    • R. Kurth and N. Bannert (ed.), Caister Academic Press, Norfolk, United Kingdom
    • Engelman, A. 2010. Reverse transcription and integration, p. 129-159. In R. Kurth and N. Bannert (ed.), Retroviruses: molecular biology, genomics and pathogenesis. Caister Academic Press, Norfolk, United Kingdom.
    • (2010) Retroviruses: Molecular Biology, Genomics and Pathogenesis , pp. 129-159
    • Engelman, A.1
  • 9
    • 70350666377 scopus 로고    scopus 로고
    • Loss of raltegravir susceptibility by human immunodeficiency virus type 1 is conferred via multiple nonoverlapping genetic pathways
    • Fransen, S., et al. 2009. Loss of raltegravir susceptibility by human immunodeficiency virus type 1 is conferred via multiple nonoverlapping genetic pathways. J. Virol. 83:11440-11446.
    • (2009) J. Virol. , vol.83 , pp. 11440-11446
    • Fransen, S.1
  • 10
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S., S. S. Gupta, E. Valkov, A. Engelman, and P. Cherepanov. 2010. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464:232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 11
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance
    • Hare, S., et al. 2010. Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc. Natl. Acad. Sci. U. S. A. 107:20057-20062.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 20057-20062
    • Hare, S.1
  • 13
    • 34250701215 scopus 로고    scopus 로고
    • Retrotransposons influence the mouse transcriptome: Implication for the divergence of genetic traits
    • DOI 10.1534/genetics.107.071647
    • Horie, K., et al. 2007. Retrotransposons influence the mouse transcriptome: implication for the divergence of genetic traits. Genetics 176:815-827. (Pubitemid 46961087)
    • (2007) Genetics , vol.176 , Issue.2 , pp. 815-827
    • Horie, K.1    Saito, E.-S.2    Keng, V.W.3    Ikeda, R.4    Ishihara, H.5    Takeda, J.6
  • 14
    • 70349779189 scopus 로고    scopus 로고
    • Efficient stable gene transfer into human cells by the Sleeping Beauty transposon vectors
    • Izsvák, Z., M. K. Chuah, T. Vandendriessche, and Z. Ivics. 2009. Efficient stable gene transfer into human cells by the Sleeping Beauty transposon vectors. Methods 49:287-297.
    • (2009) Methods , vol.49 , pp. 287-297
    • Izsvák, Z.1    Chuah, M.K.2    Vandendriessche, T.3    Ivics, Z.4
  • 15
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins, T. M., D. Esposito, A. Engelman, and R. Craigie. 1997. Critical contacts between HIV-1 integrase and viral DNA identified by structurebased analysis and photo-crosslinking. EMBO J. 16:6849-6859. (Pubitemid 27503496)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 16
    • 53249087908 scopus 로고    scopus 로고
    • Selection of diverse and clinically relevant integrase inhibitor-resistant human immunodeficiency virus type 1 mutants
    • Kobayashi, M., et al. 2008. Selection of diverse and clinically relevant integrase inhibitor-resistant human immunodeficiency virus type 1 mutants. Antiviral Res. 80:213-222.
    • (2008) Antiviral Res. , vol.80 , pp. 213-222
    • Kobayashi, M.1
  • 17
    • 78650670855 scopus 로고    scopus 로고
    • Identification and characterization of persistent intracellular human immunodeficiency virus type 1 strand transfer inhibitor activity
    • Koh, Y., H. Haim, and A. Engelman. 2011. Identification and characterization of persistent intracellular human immunodeficiency virus type 1 strand transfer inhibitor activity. Antimicrob. Agents Chemother. 55:42-49.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 42-49
    • Koh, Y.1    Haim, H.2    Engelman, A.3
  • 18
    • 10744226241 scopus 로고    scopus 로고
    • Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro
    • Koh, Y., et al. 2003. Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro. Antimicrob. Agents Chemother. 47:3123-3129.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3123-3129
    • Koh, Y.1
  • 19
    • 77957670046 scopus 로고    scopus 로고
    • Structure-based modeling of the functional HIV-1 intasome and its inhibition
    • Krishnan, L., et al. 2010. Structure-based modeling of the functional HIV-1 intasome and its inhibition. Proc. Natl. Acad. Sci. U. S. A. 107:15910-15915.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15910-15915
    • Krishnan, L.1
  • 20
    • 72849130164 scopus 로고    scopus 로고
    • The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase
    • Krishnan, L., et al. 2010. The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase. J. Virol. 84:397-406.
    • (2010) J. Virol. , vol.84 , pp. 397-406
    • Krishnan, L.1
  • 21
    • 77951640265 scopus 로고    scopus 로고
    • Response of a simian immunodeficiency virus (SIVmac251) to raltegravir: A basis for a new treatment for simian AIDS and an animal model for studying lentiviral persistence during antiretroviral therapy
    • Lewis, M. G., et al. 2010. Response of a simian immunodeficiency virus (SIVmac251) to raltegravir: a basis for a new treatment for simian AIDS and an animal model for studying lentiviral persistence during antiretroviral therapy. Retrovirology 7:21.
    • (2010) Retrovirology , vol.7 , pp. 21
    • Lewis, M.G.1
  • 22
    • 8644226108 scopus 로고    scopus 로고
    • Class II integrase mutants with changes in putative nuclear localization signals are primarily blocked at a postnuclear entry step of human immunodeficiency virus type 1 replication
    • DOI 10.1128/JVI.78.23.12735-12746.2004
    • Lu, R., et al. 2004. Class II integrase mutants with changes in putative nuclear localization signals are primarily blocked at a postnuclear entry step of human immunodeficiency virus type 1 replication. J. Virol. 78:12735-12746. (Pubitemid 39507782)
    • (2004) Journal of Virology , vol.78 , Issue.23 , pp. 12735-12746
    • Lu, R.1    Limon, A.2    Devroe, E.3    Silver, P.A.4    Cherepanov, P.5    Engelman, A.6
  • 23
    • 67349250885 scopus 로고    scopus 로고
    • Molecular evolution of a novel hyperactive Sleeping Beauty transposase enables robust stable gene transfer in vertebrates
    • Mátés, L., et al. 2009. Molecular evolution of a novel hyperactive Sleeping Beauty transposase enables robust stable gene transfer in vertebrates. Nat. Genet. 41:753-761.
    • (2009) Nat. Genet. , vol.41 , pp. 753-761
    • Mátés, L.1
  • 24
    • 73549123203 scopus 로고    scopus 로고
    • Strand transfer inhibitors of HIV-1 integrase: Bringing in a new era of antiretroviral therapy
    • McColl, D. J., and X. Chen. 2010. Strand transfer inhibitors of HIV-1 integrase: bringing IN a new era of antiretroviral therapy. Antiviral Res. 85:101-118.
    • (2010) Antiviral Res. , vol.85 , pp. 101-118
    • McColl, D.J.1    Chen, X.2
  • 25
    • 0037039347 scopus 로고    scopus 로고
    • Effect of HIV integrase inhibitors on the RAG1/2 recombinase
    • Melek, M., et al. 2002. Effect of HIV integrase inhibitors on the RAG1/2 recombinase. Proc. Natl. Acad. Sci. U. S. A. 99:134-137.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 134-137
    • Melek, M.1
  • 26
    • 77951677904 scopus 로고    scopus 로고
    • Biochemical and pharmacological analyses of HIV-1 integrase flexible loop mutants resistant to raltegravir
    • Métifiot, M., et al. 2010. Biochemical and pharmacological analyses of HIV-1 integrase flexible loop mutants resistant to raltegravir. Biochemistry 49:3715-3722.
    • (2010) Biochemistry , vol.49 , pp. 3715-3722
    • Métifiot, M.1
  • 28
    • 0001707601 scopus 로고
    • 3′-Azido-3′-deoxythymidine (BW A509U): An antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type III/lymphadenopathy-associated virus in vitro
    • Mitsuya, H., et al. 1985. 3′-Azido-3′-deoxythymidine (BW A509U): an antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type III/lymphadenopathy-associated virus in vitro. Proc. Natl. Acad. Sci. U. S. A. 82:7096-7100.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7096-7100
    • Mitsuya, H.1
  • 30
    • 34250840762 scopus 로고    scopus 로고
    • Balancing selection and the evolution of functional polymorphism in Old World monkey TRIM5alpha
    • Newman, R. M., et al. 2006. Balancing selection and the evolution of functional polymorphism in Old World monkey TRIM5alpha. Proc. Natl. Acad. Sci. U. S. A. 103:19134-19139.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 19134-19139
    • Newman, R.M.1
  • 31
    • 0024332802 scopus 로고
    • Feline immunodeficiency virus, a model for reverse transcriptase-targeted chemotherapy for acquired immune deficiency syndrome
    • North, T. W., G. L. North, and N. C. Pedersen. 1989. Feline immunodeficiency virus, a model for reverse transcriptase-targeted chemotherapy for acquired immune deficiency syndrome. Antimicrob. Agents Chemother. 33:915-919.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 915-919
    • North, T.W.1    North, G.L.2    Pedersen, N.C.3
  • 32
    • 59649101866 scopus 로고    scopus 로고
    • Retroviral integrase superfamily: The structural perspective
    • Nowotny, M. 2009. Retroviral integrase superfamily: the structural perspective. EMBO Rep. 10:144-151.
    • (2009) EMBO Rep. , vol.10 , pp. 144-151
    • Nowotny, M.1
  • 34
    • 77951996954 scopus 로고    scopus 로고
    • Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs
    • Paprotka, T., et al. 2010. Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs. J. Virol. 84:5719-5729.
    • (2010) J. Virol. , vol.84 , pp. 5719-5729
    • Paprotka, T.1
  • 36
    • 85158041860 scopus 로고    scopus 로고
    • The Tc1/mariner family of transposable elements
    • N. L. Craig, R. Craigie, M. Gellert, and A. M. Lambowitz (ed.), ASM Press, Washington, DC
    • Plasterk, R. H., and H. G. van Luenen. 2002. The Tc1/mariner family of transposable elements, p. 519-532. In N. L. Craig, R. Craigie, M. Gellert, and A. M. Lambowitz (ed.), Mobile DNA II. ASM Press, Washington, DC.
    • (2002) Mobile DNA II , pp. 519-532
    • Plasterk, R.H.1    Van Luenen, H.G.2
  • 37
    • 70149109999 scopus 로고    scopus 로고
    • Molecular architecture of the Mos1 paired-end complex: The structural basis of DNA transposition in a eukaryote
    • Richardson, J. M., S. D. Colloms, D. J. Finnegan, and M. D. Walkinshaw. 2009. Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote. Cell 138:1096-1108.
    • (2009) Cell , vol.138 , pp. 1096-1108
    • Richardson, J.M.1    Colloms, S.D.2    Finnegan, D.J.3    Walkinshaw, M.D.4
  • 38
    • 54549099338 scopus 로고    scopus 로고
    • HIV-2 integrase gene polymorphism and phenotypic susceptibility of HIV-2 clinical isolates to the integrase inhibitors raltegravir and elvitegravir in vitro
    • Roquebert, B., et al. 2008. HIV-2 integrase gene polymorphism and phenotypic susceptibility of HIV-2 clinical isolates to the integrase inhibitors raltegravir and elvitegravir in vitro. J. Antimicrob. Chemother. 62:914-920.
    • (2008) J. Antimicrob. Chemother. , vol.62 , pp. 914-920
    • Roquebert, B.1
  • 39
    • 0022500371 scopus 로고
    • Suppression of mouse viraemia and retroviral disease by 3'-azido-3'-deoxythymidine
    • Ruprecht, R. M., L. G. O'Brien, L. D. Rossoni, and S. Nusinoff-Lehrman. 1986. Suppression of mouse viraemia and retroviral disease by 3′-azido-3′-deoxythymidine. Nature 323:467-469. (Pubitemid 16026279)
    • (1986) Nature , vol.323 , Issue.6087 , pp. 467-469
    • Ruprecht, R.M.1    O'Brien, L.G.2    Rossoni, L.D.3    Nusinoff-Lehrman, S.4
  • 40
    • 37849002059 scopus 로고    scopus 로고
    • Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137)
    • Shimura, K., et al. 2008. Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137). J. Virol. 82:764-774.
    • (2008) J. Virol. , vol.82 , pp. 764-774
    • Shimura, K.1
  • 41
    • 70449411340 scopus 로고    scopus 로고
    • Elvitegravir: A new HIV integrase inhibitor
    • Shimura, K., and E. N. Kodama. 2009. Elvitegravir: a new HIV integrase inhibitor. Antivir. Chem. Chemother. 20:79-85.
    • (2009) Antivir. Chem. Chemother. , vol.20 , pp. 79-85
    • Shimura, K.1    Kodama, E.N.2
  • 42
    • 77953308545 scopus 로고    scopus 로고
    • Raltegravir is a potent inhibitor of XMRV, a virus implicated in prostate cancer and chronic fatigue syndrome
    • Singh, I. R., J. E. Gorzynski, D. Drobysheva, L. Bassit, and R. F. Schinazi. 2010. Raltegravir is a potent inhibitor of XMRV, a virus implicated in prostate cancer and chronic fatigue syndrome. PLoS One 5:e9948.
    • (2010) PLoS One , vol.5
    • Singh, I.R.1    Gorzynski, J.E.2    Drobysheva, D.3    Bassit, L.4    Schinazi, R.F.5
  • 43
    • 77956484577 scopus 로고    scopus 로고
    • Susceptibility of the human retrovirus XMRV to antiretroviral inhibitors
    • Smith, R. A., G. S. Gottlieb, and A. D. Miller. 2010. Susceptibility of the human retrovirus XMRV to antiretroviral inhibitors. Retrovirology 7:70.
    • (2010) Retrovirology , vol.7 , pp. 70
    • Smith, R.A.1    Gottlieb, G.S.2    Miller, A.D.3
  • 44
    • 49549100511 scopus 로고    scopus 로고
    • Trex1 prevents cell-intrinsic initiation of autoimmunity
    • Stetson, D. B., J. S. Ko, T. Heidmann, and R. Medzhitov. 2008. Trex1 prevents cell-intrinsic initiation of autoimmunity. Cell 134:587-598.
    • (2008) Cell , vol.134 , pp. 587-598
    • Stetson, D.B.1    Ko, J.S.2    Heidmann, T.3    Medzhitov, R.4
  • 45
    • 52449097240 scopus 로고    scopus 로고
    • Discovery of raltegravir, a potent, selective orally bioavailable HIV-integrase inhibitor for the treatment of HIV-AIDS infection
    • Summa, V., et al. 2008. Discovery of raltegravir, a potent, selective orally bioavailable HIV-integrase inhibitor for the treatment of HIV-AIDS infection. J. Med. Chem. 51:5843-5855.
    • (2008) J. Med. Chem. , vol.51 , pp. 5843-5855
    • Summa, V.1
  • 46
    • 0030273010 scopus 로고    scopus 로고
    • Inhibition of bovine immunodeficiency virus by anti-HIV-1 compounds in a cell culture-based assay
    • Tobin, G. J., W. H. Ennis, D. J. Clanton, and M. A. Gonda. 1996. Inhibition of bovine immunodeficiency virus by anti-HIV-1 compounds in a cell culture-based assay. Antiviral Res. 33:21-31.
    • (1996) Antiviral Res. , vol.33 , pp. 21-31
    • Tobin, G.J.1    Ennis, W.H.2    Clanton, D.J.3    Gonda, M.A.4
  • 47
    • 0028791836 scopus 로고
    • Prevention of SIV infection in macaques by (R)-9-(2- phosphonylmethoxypropyl)adenine
    • Tsai, C. C., et al. 1995. Prevention of SIV infection in macaques by (R)-9-(2-phosphonylmethoxypropyl)adenine. Science 270:1197-1199.
    • (1995) Science , vol.270 , pp. 1197-1199
    • Tsai, C.C.1
  • 48
    • 58549092798 scopus 로고    scopus 로고
    • Functional and structural characterization of the integrase from the prototype foamy virus
    • Valkov, E., et al. 2009. Functional and structural characterization of the integrase from the prototype foamy virus. Nucleic Acids Res. 37:243-255.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 243-255
    • Valkov, E.1
  • 49
    • 2942531259 scopus 로고    scopus 로고
    • Crystal structure of the targeting endonuclease of the human LINE-1 retrotransposon
    • DOI 10.1016/j.str.2004.04.011, PII S0969212604001534
    • Weichenrieder, O., K. Repanas, and A. Perrakis. 2004. Crystal structure of the targeting endonuclease of the human LINE-1 retrotransposon. Structure 12:975-986. (Pubitemid 38748770)
    • (2004) Structure , vol.12 , Issue.6 , pp. 975-986
    • Weichenrieder, O.1    Repanas, K.2    Perrakis, A.3
  • 52
    • 0034681303 scopus 로고    scopus 로고
    • Crystal structure of an active two-domain derivative of Rous sarcoma virus integrase
    • Yang, Z.-N., T. C. Mueser, F. D. Bushman, and C. C. Hyde. 2000. Crystal structure of an active two-domain derivative of Rous sarcoma virus integrase. J. Mol. Biol. 296:535-548.
    • (2000) J. Mol. Biol. , vol.296 , pp. 535-548
    • Yang, Z.-N.1    Mueser, T.C.2    Bushman, F.D.3    Hyde, C.C.4
  • 53
    • 67649603896 scopus 로고    scopus 로고
    • Transgenesis in Xenopus using the Sleeping Beauty transposon system
    • Yergeau, D. A., et al. 2009. Transgenesis in Xenopus using the Sleeping Beauty transposon system. Dev. Dyn. 238:1727-1743.
    • (2009) Dev. Dyn. , vol.238 , pp. 1727-1743
    • Yergeau, D.A.1
  • 54
    • 33748701449 scopus 로고    scopus 로고
    • Antiretroviral potential of human tripartite motif-5 and related proteins
    • Zhang, F., T. Hatziioannou, D. Perez-Caballero, D. Derse, and P. D. Bieniasz. 2006. Antiretroviral potential of human tripartite motif-5 and related proteins. Virology 353:396-409.
    • (2006) Virology , vol.353 , pp. 396-409
    • Zhang, F.1    Hatziioannou, T.2    Perez-Caballero, D.3    Derse, D.4    Bieniasz, P.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.