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Volumn 326, Issue 2, 2003, Pages 493-502

Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4

Author keywords

Ebola virus; Matrix protein; Nedd4, filovirus; Tsg101; VP40

Indexed keywords

CELL PROTEIN; ENZYME; MATRIX PROTEIN; OLIGOMER; PROTEIN VP40; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 0037436346     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01406-7     Document Type: Article
Times cited : (177)

References (59)
  • 2
    • 0000995139 scopus 로고    scopus 로고
    • Filoviridae: Marburg and Ebola viruses
    • Fields B.N. 3rd edit. Philadelphia: Lippincott-Raven
    • Peters C.J., Sanchez A., Rollin P.E., Ksiazek T.G., Murphy F.A. Filoviridae: Marburg and Ebola viruses. Fields B.N. 3rd edit. Fields Virology. vol. 1:1996;1161-1176 Lippincott-Raven, Philadelphia.
    • (1996) Fields Virology , vol.1 , pp. 1161-1176
    • Peters, C.J.1    Sanchez, A.2    Rollin, P.E.3    Ksiazek, T.G.4    Murphy, F.A.5
  • 3
    • 0036150019 scopus 로고    scopus 로고
    • VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment
    • Kolesnikova L., Bugany H., Klenk H.D., Becker S. VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment. J. Virol. 76:2002;1825-1838.
    • (2002) J. Virol. , vol.76 , pp. 1825-1838
    • Kolesnikova, L.1    Bugany, H.2    Klenk, H.D.3    Becker, S.4
  • 4
    • 0029591306 scopus 로고
    • Differentiation of filoviruses by electron microscopy
    • Geisbert T.W., Jahrling P.B. Differentiation of filoviruses by electron microscopy. Virus Res. 39:1995;129-150.
    • (1995) Virus Res. , vol.39 , pp. 129-150
    • Geisbert, T.W.1    Jahrling, P.B.2
  • 5
    • 0034733392 scopus 로고    scopus 로고
    • Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus
    • Ruigrok R.W., Schoehn G., Dessen A., Forest E., Volchkov V., Dolnik O., et al. Structural characterization and membrane binding properties of the matrix protein VP40 of Ebola virus. J. Mol. Biol. 300:2000;103-112.
    • (2000) J. Mol. Biol. , vol.300 , pp. 103-112
    • Ruigrok, R.W.1    Schoehn, G.2    Dessen, A.3    Forest, E.4    Volchkov, V.5    Dolnik, O.6
  • 7
    • 0037018099 scopus 로고    scopus 로고
    • Lipid raft microdomains: A gateway for compartmentalized trafficking of ebola and marburg viruses
    • Bavari S., Bosio C.M., Wiegand E., Ruthel G., Will A.B., Geisbert T.W., et al. Lipid raft microdomains: a gateway for compartmentalized trafficking of ebola and marburg viruses. J. Expt. Med. 195:2002;593-602.
    • (2002) J. Expt. Med. , vol.195 , pp. 593-602
    • Bavari, S.1    Bosio, C.M.2    Wiegand, E.3    Ruthel, G.4    Will, A.B.5    Geisbert, T.W.6
  • 8
    • 0036235725 scopus 로고    scopus 로고
    • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP
    • Noda T., Sagara H., Suzuki E., Takada A., Kida H., Kawaoka Y. Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. J. Virol. 76:2002;4855-4865.
    • (2002) J. Virol. , vol.76 , pp. 4855-4865
    • Noda, T.1    Sagara, H.2    Suzuki, E.3    Takada, A.4    Kida, H.5    Kawaoka, Y.6
  • 9
    • 0034663762 scopus 로고    scopus 로고
    • Crystal structure of the matrix protein VP40 from Ebola virus
    • Dessen A., Volchkov V., Dolnik O., Klenk H.D., Weissenhorn W. Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J. 19:2000;4228-4236.
    • (2000) EMBO J. , vol.19 , pp. 4228-4236
    • Dessen, A.1    Volchkov, V.2    Dolnik, O.3    Klenk, H.D.4    Weissenhorn, W.5
  • 11
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky L.D., Neumann G., Lukashevich I., Kawaoka Y. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75:2001;5205-5214.
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukashevich, I.3    Kawaoka, Y.4
  • 12
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Göttlinger H.G., Dorfman T., Sodroski J.G., Haseltine W.A. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc. Natl Acad. Sci. USA. 88:1991;3195-3199.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3195-3199
    • Göttlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 14
    • 0031968983 scopus 로고    scopus 로고
    • A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release
    • Yasuda J., Hunter E. A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release. J. Virol. 72:1998;4095-4103.
    • (1998) J. Virol. , vol.72 , pp. 4095-4103
    • Yasuda, J.1    Hunter, E.2
  • 15
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias M.J., Hyvonen M., Baraldi E., Schultz J., Sudol M., Saraste M., Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382:1996;646-649.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 16
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias M.J., Wiesner S., Sudol M. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Letters. 513:2002;30-37.
    • (2002) FEBS Letters , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 17
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells
    • Kikonyogo A., Bouamr F., Vana M.L., Xiang Y., Aiyar A., Carter C., Leis J. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl Acad. Sci. USA. 98:2001;11199-11204.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11199-11204
    • Kikonyogo, A.1    Bouamr, F.2    Vana, M.L.3    Xiang, Y.4    Aiyar, A.5    Carter, C.6    Leis, J.7
  • 18
    • 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., Paragas J., Sudol M., Palese P. 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. 73:1999;2921-2929.
    • (1999) J. Virol. , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 19
  • 20
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • Harty R.N., Brown M.E., Wang G., Huibregtse J., Hayes F.P. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding. Proc. Natl Acad. Sci. USA. 97:2000;13871-13876.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 21
    • 0025351117 scopus 로고
    • Ubiquitin in avian leukosis virus particles
    • Putterman D., Pepinsky R.B., Vogt V.M. Ubiquitin in avian leukosis virus particles. Virology. 176:1990;633-637.
    • (1990) Virology , vol.176 , pp. 633-637
    • Putterman, D.1    Pepinsky, R.B.2    Vogt, V.M.3
  • 22
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott D.E., Coren L.V., Copeland T.D., Kane B.P., Johnson D.G., Sowder R.C. II, et al. Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J. Virol. 72:1998;2962-2968.
    • (1998) J. Virol. , vol.72 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder R.C. II6
  • 23
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A., Chau V., Wills J.W. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl Acad. Sci. USA. 97:2000;13069-13074.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 25
    • 0034700088 scopus 로고    scopus 로고
    • Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2
    • Schubert U., Ott D.E., Chertova E.N., Welker R., Tessmer U., Princiotta M.F., et al. Proteasome inhibition interferes with gag polyprotein processing, release, and maturation of HIV-1 and HIV-2. Proc. Natl Acad. Sci. USA. 97:2000;13057-13062.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13057-13062
    • Schubert, U.1    Ott, D.E.2    Chertova, E.N.3    Welker, R.4    Tessmer, U.5    Princiotta, M.F.6
  • 26
    • 0028901720 scopus 로고
    • Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells
    • Sasaki H., Nakamura M., Ohno T., Matsuda Y., Yuda Y., Nonomura Y. Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells. Proc. Natl Acad. Sci. USA. 92:1995;2026-2030.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2026-2030
    • Sasaki, H.1    Nakamura, M.2    Ohno, T.3    Matsuda, Y.4    Yuda, Y.5    Nonomura, Y.6
  • 29
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov D.G., Ono A., Orenstein J.M., Freed E.O. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl Acad. Sci. USA. 99:2002;955-960.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 30
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J., Zang T., Bieniasz P.D. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nature Med. 7:2001;1313-1319.
    • (2001) Nature Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 32
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O., Alam S.L., Davis D.R., Sundquist W.I. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nature Struct. Biol. 9:2002;812-817.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 33
    • 0035853688 scopus 로고    scopus 로고
    • TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes
    • Bishop N., Woodman P. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. J. Biol. Chem. 276:2001;11735-11742.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11735-11742
    • Bishop, N.1    Woodman, P.2
  • 34
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann D.J., Babst M., Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:2001;145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 36
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • Kumar S., Tomooka Y., Noda M. Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem. Biophys. Res. Commun. 185:1992;1155-1161.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 1155-1161
    • Kumar, S.1    Tomooka, Y.2    Noda, M.3
  • 37
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl Acad. Sci. USA. 95:1998;5857-5864.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 39
    • 0035658016 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus: The getaway driver nabbed
    • Luban J. HIV-1 and Ebola virus: the getaway driver nabbed. Nature Med. 7:2001;1278-1280.
    • (2001) Nature Med. , vol.7 , pp. 1278-1280
    • Luban, J.1
  • 40
    • 0034704216 scopus 로고    scopus 로고
    • NeW wrinkles for an old domain
    • Sudol M., Hunter T. NeW wrinkles for an old domain. Cell. 103:2000;1001-1004.
    • (2000) Cell , vol.103 , pp. 1001-1004
    • Sudol, M.1    Hunter, T.2
  • 41
    • 0034717801 scopus 로고    scopus 로고
    • Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb
    • Plant P.J., Lafont F., Lecat S., Verkade P., Simons K., Rotin D. Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb. J. Cell Biol. 149:2000;1473-1484.
    • (2000) J. Cell Biol. , vol.149 , pp. 1473-1484
    • Plant, P.J.1    Lafont, F.2    Lecat, S.3    Verkade, P.4    Simons, K.5    Rotin, D.6
  • 42
    • 0035853045 scopus 로고    scopus 로고
    • Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE- triggered cell signaling
    • Lafont F., Simons K. Raft-partitioning of the ubiquitin ligases Cbl and Nedd4 upon IgE- triggered cell signaling. Proc. Natl Acad. Sci. USA. 98:2001;3180-3184.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3180-3184
    • Lafont, F.1    Simons, K.2
  • 43
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke L. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell. Biol. 9:1999;107-112.
    • (1999) Trends Cell. Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 44
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke L. Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11:1997;1215-1226.
    • (1997) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 45
    • 0033054154 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and endocytosis
    • Strous G.J., Govers R. The ubiquitin-proteasome system and endocytosis. J. Cell Sci. 112:1999;1417-1423.
    • (1999) J. Cell Sci. , vol.112 , pp. 1417-1423
    • Strous, G.J.1    Govers, R.2
  • 46
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast
    • Beck T., Schmidt A., Hall M.N. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell Biol. 146:1999;1227-1238.
    • (1999) J. Cell Biol. , vol.146 , pp. 1227-1238
    • Beck, T.1    Schmidt, A.2    Hall, M.N.3
  • 47
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nature Rev. Mol. Cell. Biol. 2:2001;195-201.
    • (2001) Nature Rev. Mol. Cell. Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 48
    • 0031688699 scopus 로고    scopus 로고
    • A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever
    • Bray M., Davis K., Geisbert T., Schmaljohn C., Huggins J. A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever. J. Infect. Dis. 178:1998;651-661.
    • (1998) J. Infect. Dis. , vol.178 , pp. 651-661
    • Bray, M.1    Davis, K.2    Geisbert, T.3    Schmaljohn, C.4    Huggins, J.5
  • 50
    • 0035027506 scopus 로고    scopus 로고
    • Solution structure of a Nedd4 WW domain-ENaC peptide complex
    • Kanelis V., Rotin D., Forman-Kay J.D. Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nature Struct. Biol. 8:2001;407-412.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 407-412
    • Kanelis, V.1    Rotin, D.2    Forman-Kay, J.D.3
  • 52
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann U., Mattes R.E., Buckel P. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene. 85:1989;109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 54
    • 0014301425 scopus 로고
    • Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli
    • Valentine R.C., Shapiro B.M., Stadtman E.R. Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli. Biochemistry. 7:1968;2143-2152.
    • (1968) Biochemistry , vol.7 , pp. 2143-2152
    • Valentine, R.C.1    Shapiro, B.M.2    Stadtman, E.R.3
  • 56
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:1996;190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 57
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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