메뉴 건너뛰기




Volumn 423, Issue 6939, 2003, Pages 512-518

Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; DNA; GENES; GENETIC ENGINEERING; MOLECULAR STRUCTURE; PROTEINS; TUMORS; VIRUSES; X RAY ANALYSIS;

EID: 0038700763     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01691     Document Type: Article
Times cited : (262)

References (50)
  • 1
    • 0026692874 scopus 로고
    • Common and unique features of T antigens encoded by the polyomavirus group
    • Pipas, J. M. Common and unique features of T antigens encoded by the polyomavirus group. J. Virol. 66, 3979-3985 (1992).
    • (1992) J. Virol. , vol.66 , pp. 3979-3985
    • Pipas, J.M.1
  • 2
    • 0034573640 scopus 로고    scopus 로고
    • SV40 large T antigen functions in DNA replication and transformation
    • Simmons, D. T. SV40 large T antigen functions in DNA replication and transformation. Adv. Virus Res. 55, 75-134 (2000).
    • (2000) Adv. Virus Res. , vol.55 , pp. 75-134
    • Simmons, D.T.1
  • 3
    • 0027936237 scopus 로고
    • Smart machines at the DNA replication fork
    • Stillman, B. Smart machines at the DNA replication fork. Cell 78, 725-728 (1994).
    • (1994) Cell , vol.78 , pp. 725-728
    • Stillman, B.1
  • 4
    • 0031405599 scopus 로고    scopus 로고
    • The initiation of simian virus 40 DNA replication in vitro
    • Bullock, P. A. The initiation of simian virus 40 DNA replication in vitro. Crit. Rev. Biochem. Mol. Biol. 32, 503-568 (1997).
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 503-568
    • Bullock, P.A.1
  • 5
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 Tantigen at the viral origin of DNA replication
    • Mastrangelo, I. A. et al. ATP-dependent assembly of double hexamers of SV40 Tantigen at the viral origin of DNA replication. Nature 338, 658-662 (1989).
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1
  • 6
    • 0024095899 scopus 로고
    • Localized melting and structural changes in the SV40 origin of replication induced by T-antigen
    • Borowiec, J. A. & Hurwitz, J. Localized melting and structural changes in the SV40 origin of replication induced by T-antigen. EMBO J. 7, 3149-3158 (1988).
    • (1988) EMBO J. , vol.7 , pp. 3149-3158
    • Borowiec, J.A.1    Hurwitz, J.2
  • 7
    • 0031893217 scopus 로고    scopus 로고
    • Assembly of T-antigen double hexamers on the simian virus 40 core origin requires only a subset of the available binding sites
    • Joo, W. S., Kim, H. Y., Purviance, J. D., Sreekumar, K. R. & Bullock, P. A. Assembly of T-antigen double hexamers on the simian virus 40 core origin requires only a subset of the available binding sites. Mol. Cell. Biol. 18, 2677-2687 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2677-2687
    • Joo, W.S.1    Kim, H.Y.2    Purviance, J.D.3    Sreekumar, K.R.4    Bullock, P.A.5
  • 8
    • 0009607249 scopus 로고
    • Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication
    • Dean, F. B. et al. Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication. Proc. Natl Acad. Sci. USA 84, 16-20 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 16-20
    • Dean, F.B.1
  • 9
    • 0342564930 scopus 로고
    • Initiation of simian virus 40 DNA replication in vitro: Large-tumor-antigen- and origin-dependent unwinding of the template
    • Wold, M. S., Li, J. J. & Kelly, T. J. Initiation of simian virus 40 DNA replication in vitro: Large-tumor-antigen- and origin-dependent unwinding of the template. Proc. Natl Acad. Sci. USA 84, 3643-3647 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3643-3647
    • Wold, M.S.1    Li, J.J.2    Kelly, T.J.3
  • 10
    • 0031663234 scopus 로고    scopus 로고
    • Synthetic DNA replication bubbles bound and unwound with twofold symmetry by a simian virus 40 T-antigen double hexamer
    • Smelkova, N. V. & Borowiec, J. A. Synthetic DNA replication bubbles bound and unwound with twofold symmetry by a simian virus 40 T-antigen double hexamer. J. Virol. 72, 8676-8681 (1998).
    • (1998) J. Virol. , vol.72 , pp. 8676-8681
    • Smelkova, N.V.1    Borowiec, J.A.2
  • 11
    • 0025328320 scopus 로고
    • Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin
    • Tsurimoto, T., Melendy, T. & Stillman, B. Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin. Nature 346, 534-539 (1990).
    • (1990) Nature , vol.346 , pp. 534-539
    • Tsurimoto, T.1    Melendy, T.2    Stillman, B.3
  • 12
    • 0025967720 scopus 로고
    • Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase α and δ during initiation of leading and lagging strand synthesis
    • Tsurimoto, T. & Stillman, B. Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase α and δ during initiation of leading and lagging strand synthesis. J. Biol. Chem. 266, 1961-1968 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 1961-1968
    • Tsurimoto, T.1    Stillman, B.2
  • 13
    • 0025271051 scopus 로고
    • Mapping of helicase and helicase substrate-binding domains on simian virus 40 large T antigen
    • Wun-Kim, K. & Simmons, D. T. Mapping of helicase and helicase substrate-binding domains on simian virus 40 large T antigen. J. Virol. 64, 2014-2020 (1990).
    • (1990) J. Virol. , vol.64 , pp. 2014-2020
    • Wun-Kim, K.1    Simmons, D.T.2
  • 14
    • 0035123455 scopus 로고    scopus 로고
    • Role of single-stranded DNA binding activity of T antigen in simian virus 40 DNA replication
    • Wu, C., Roy, R. & Simmons, D. T. Role of single-stranded DNA binding activity of T antigen in simian virus 40 DNA replication. J. Virol. 75, 2839-2847 (2001).
    • (2001) J. Virol. , vol.75 , pp. 2839-2847
    • Wu, C.1    Roy, R.2    Simmons, D.T.3
  • 15
    • 0025019702 scopus 로고
    • Binding and unwinding-how T antigen engages the SV40 origin of DNA replication
    • Borowiec, J. A., Dean, F. B., Bullock, P. A. & Hurwitz, J. Binding and unwinding-how T antigen engages the SV40 origin of DNA replication. Cell 60, 181-184 (1990).
    • (1990) Cell , vol.60 , pp. 181-184
    • Borowiec, J.A.1    Dean, F.B.2    Bullock, P.A.3    Hurwitz, J.4
  • 16
    • 0026724311 scopus 로고
    • Structure and function of simian virus 40 large tumor antigen
    • Fanning, E. & Knippers, R. Structure and function of simian virus 40 large tumor antigen. Annu. Rev. Biochem. 61, 55-85 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 55-85
    • Fanning, E.1    Knippers, R.2
  • 17
    • 0027267908 scopus 로고
    • A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
    • Koonin, E. V. A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res. 21, 2541-2547 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2541-2547
    • Koonin, E.V.1
  • 18
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L. & Koonin, E. V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 19
    • 0036121096 scopus 로고    scopus 로고
    • Regions and activities of simian virus 40 T antigen that cooperate with an activated ras oncogene in transforming primary rat embryo fibroblasts
    • Beachy, T. M., Cole, S. L., Cavender, J. F. & Tevethia, M. J. Regions and activities of simian virus 40 T antigen that cooperate with an activated ras oncogene in transforming primary rat embryo fibroblasts. J. Virol. 76, 3145-3157 (2002).
    • (2002) J. Virol. , vol.76 , pp. 3145-3157
    • Beachy, T.M.1    Cole, S.L.2    Cavender, J.F.3    Tevethia, M.J.4
  • 20
    • 0028811976 scopus 로고
    • Simian virus 40 large T antigen contains two independent activities that cooperate with a ras oncogene to transform rat embryo fibroblasts
    • Cavender, J. F., Conn, A., Epler, M., Lacko, H. & Tevethia, M. J. Simian virus 40 large T antigen contains two independent activities that cooperate with a ras oncogene to transform rat embryo fibroblasts. J. Virol. 69, 923-934 (1995).
    • (1995) J. Virol. , vol.69 , pp. 923-934
    • Cavender, J.F.1    Conn, A.2    Epler, M.3    Lacko, H.4    Tevethia, M.J.5
  • 21
    • 0033988190 scopus 로고    scopus 로고
    • Large T-antigen double hexamers imaged at the simian virus 40 origin of replication
    • Valle, M., Gruss, C., Halmer, L., Carazo, J. M. & Donate, L. E. Large T-antigen double hexamers imaged at the simian virus 40 origin of replication. Mol. Cell. Biol. 20, 34-41 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 34-41
    • Valle, M.1    Gruss, C.2    Halmer, L.3    Carazo, J.M.4    Donate, L.E.5
  • 22
    • 0030443808 scopus 로고    scopus 로고
    • Solution structure of the origin DNA-binding domain of SV40 T-antigen
    • Luo, X., Sanford, D. G., Bullock, P. A. & Bachovchin, W. W. Solution structure of the origin DNA-binding domain of SV40 T-antigen. Nature Struct. Biol. 3, 1034-1039 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1034-1039
    • Luo, X.1    Sanford, D.G.2    Bullock, P.A.3    Bachovchin, W.W.4
  • 23
    • 0037336323 scopus 로고    scopus 로고
    • The structure and function of MCM dodecamer from Archaeal M. thermoautotrophicum
    • Fletcher, R., Bishop, B., Sclafani, R., Ogata, G. & Chen, X. The structure and function of MCM dodecamer from Archaeal M. thermoautotrophicum. Nature Struct. Biol. 10, 160-167 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 160-167
    • Fletcher, R.1    Bishop, B.2    Sclafani, R.3    Ogata, G.4    Chen, X.5
  • 24
    • 0037031834 scopus 로고    scopus 로고
    • MCM2-7 complexes bind chromatin in a distributed pattern surrounding ORC in Xenopus egg extracts
    • Edwards, M. C. et al. MCM2-7 complexes bind chromatin in a distributed pattern surrounding ORC in Xenopus egg extracts. J. Biol. Chem. 277, 33049-33059 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33049-33059
    • Edwards, M.C.1
  • 25
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C. U., Steinmann, D., Whiteheart, S. W. & Weis, W. I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 26
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HsUV protease-chaperone complex
    • Sousa, M. C. et al. Crystal and solution structures of an HsUV protease-chaperone complex. Cell 103, 633-643 (2000).
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1
  • 27
    • 0034677361 scopus 로고    scopus 로고
    • The structures of HsIU and the ATP-dependent protease HsIU-HsIV
    • Bochtler, M. et al. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature 403, 800-805 (2000).
    • (2000) Nature , vol.403 , pp. 800-805
    • Bochtler, M.1
  • 28
    • 0035839032 scopus 로고    scopus 로고
    • Structure and mechanism of the RuvB Holliday junction branch migration motor
    • Putnam, C. D. et al. Structure and mechanism of the RuvB Holliday junction branch migration motor. J. Mol. Biol. 311, 297-310 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 297-310
    • Putnam, C.D.1
  • 29
    • 0024597678 scopus 로고
    • The zinc finger region of simian virus 40 large T antigen
    • Loeber, G., Parsons, R. & Tegtmeyer, P. The zinc finger region of simian virus 40 large T antigen. J. Virol. 63, 94-100 (1989).
    • (1989) J. Virol. , vol.63 , pp. 94-100
    • Loeber, G.1    Parsons, R.2    Tegtmeyer, P.3
  • 30
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya, M. R., Guo, S., Tabor, S., Richardson, C. C. & Ellenberger, T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell 99, 167-177 (1999).
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 31
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton, M. R., Sawaya, M. R., Ellenberger, T. & Wigley, D. B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589-600 (2000).
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 32
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338 (1997).
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1
  • 33
    • 0023147631 scopus 로고
    • Trans-dominant defective mutants of simian virus 40 T antigen
    • Farber, J. M., Peden, K. W. & Nathans, D. Trans-dominant defective mutants of simian virus 40 T antigen. J. Virol. 61, 436-445 (1987).
    • (1987) J. Virol. , vol.61 , pp. 436-445
    • Farber, J.M.1    Peden, K.W.2    Nathans, D.3
  • 34
    • 0024450988 scopus 로고
    • Temperature-sensitive mutants identify crucial structural regions of simian virus 40 large T antigen
    • Loeber, G., Tevethia, M. J., Schwedes, J. F. & Tegtmeyer, P. Temperature-sensitive mutants identify crucial structural regions of simian virus 40 large T antigen. J. Virol. 63, 4426-4430 (1989).
    • (1989) J. Virol. , vol.63 , pp. 4426-4430
    • Loeber, G.1    Tevethia, M.J.2    Schwedes, J.F.3    Tegtmeyer, P.4
  • 35
    • 0026705907 scopus 로고
    • Functional characterization of temperature-sensitive mutants of simian virus 40 large T antigen
    • Ray, S., Anderson, M. E., Loeber, G., McVey, D. & Tegtmeyer, P. Functional characterization of temperature-sensitive mutants of simian virus 40 large T antigen. J. Virol. 66, 6509-6516 (1992).
    • (1992) J. Virol. , vol.66 , pp. 6509-6516
    • Ray, S.1    Anderson, M.E.2    Loeber, G.3    McVey, D.4    Tegtmeyer, P.5
  • 36
    • 0025830174 scopus 로고
    • The ability of large T antigen to complex with p53 is necessary for the increased life span and partial transformation of human cells by simian virus 40
    • Lin, J. Y. & Simmons, D. T. The ability of large T antigen to complex with p53 is necessary for the increased life span and partial transformation of human cells by simian virus 40. J. Virol. 65, 6447-6453 (1991).
    • (1991) J. Virol. , vol.65 , pp. 6447-6453
    • Lin, J.Y.1    Simmons, D.T.2
  • 37
    • 0025977777 scopus 로고
    • Stable T-p 53 complexes are not required for replication of simian virus 40 in culture or for enhanced phosphorylation of T antigen and p53
    • Lin, J. Y. & Simmons, D. T. Stable T-p53 complexes are not required for replication of simian virus 40 in culture or for enhanced phosphorylation of T antigen and p53. J. Virol. 65, 2066-2072 (1991).
    • (1991) J. Virol. , vol.65 , pp. 2066-2072
    • Lin, J.Y.1    Simmons, D.T.2
  • 38
    • 0027535098 scopus 로고
    • Association of p53 binding and immortalization of primary C57BL/6 mouse embryo fibroblasts by using simian virus 40 T-antigen mutants bearing internal overlapping deletion mutations
    • Kierstead, T. D. & Tevethia, M. J. Association of p53 binding and immortalization of primary C57BL/6 mouse embryo fibroblasts by using simian virus 40 T-antigen mutants bearing internal overlapping deletion mutations. J. Virol. 67, 1817-1829 (1993).
    • (1993) J. Virol. , vol.67 , pp. 1817-1829
    • Kierstead, T.D.1    Tevethia, M.J.2
  • 39
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P. D. & Pavletich, N. P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265, 346-355 (1994).
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 40
    • 0024558618 scopus 로고
    • Mutants with changes within or near a hydrophobic region of simian virus 40 large tumor antigen are defective for binding cellular protein p53
    • Peden, K. W., Srinivasan, A., Farber, J. M. & Pipas, J. M. Mutants with changes within or near a hydrophobic region of simian virus 40 large tumor antigen are defective for binding cellular protein p53. Virology 168, 13-21 (1989).
    • (1989) Virology , vol.168 , pp. 13-21
    • Peden, K.W.1    Srinivasan, A.2    Farber, J.M.3    Pipas, J.M.4
  • 41
    • 0031743611 scopus 로고    scopus 로고
    • The origin DNA-binding and single-stranded DNA-binding domains of simian virus 40 large T antigen are distinct
    • Wu, C., Edgil, D. & Simmons, D. T. The origin DNA-binding and single-stranded DNA-binding domains of simian virus 40 large T antigen are distinct. J. Virol. 72, 10256-10259 (1998).
    • (1998) J. Virol. , vol.72 , pp. 10256-10259
    • Wu, C.1    Edgil, D.2    Simmons, D.T.3
  • 42
    • 18744414494 scopus 로고    scopus 로고
    • Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
    • Rouiller, I. et al. Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle. Nature Struct. Biol. 9, 950-957 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 950-957
    • Rouiller, I.1
  • 43
    • 0026501124 scopus 로고
    • Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication
    • Wessel, R., Schweizer, J. & Stahl, H. Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication. J. Virol. 66, 804-815 (1992).
    • (1992) J. Virol. , vol.66 , pp. 804-815
    • Wessel, R.1    Schweizer, J.2    Stahl, H.3
  • 44
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • Cook, P. R. The organization of replication and transcription. Science 284, 1790-1795 (1999).
    • (1999) Science , vol.284 , pp. 1790-1795
    • Cook, P.R.1
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-325 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T. C. & Berendzen, J. Automated structure solution for MIR and MAD. Acta Crystallogr. D 55, 849-861 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 47
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 48
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 49
    • 0026244229 scopus 로고
    • MOLSCRIPT a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. E. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.E.1
  • 50
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.