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Volumn 11, Issue 10, 2010, Pages 912-919

Caspase-12 controls West Nile virus infection via the viral RNA receptor RIG-I

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 12; INTERFERON; PATTERN RECOGNITION RECEPTOR; PATTERN RECOGNITION RECEPTOR RIG I; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRUS RNA; CASP12 PROTEIN, MOUSE; DDX58 PROTEIN, MOUSE; DEAD BOX PROTEIN; DNA BINDING PROTEIN; TRANSCRIPTION FACTOR; TRIM25 PROTEIN, MOUSE; UBIQUITIN PROTEIN LIGASE; VIRUS RECEPTOR;

EID: 77956947459     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.1933     Document Type: Article
Times cited : (82)

References (50)
  • 2
    • 33845478357 scopus 로고    scopus 로고
    • The inflammatory caspases: Guardians against infections and sepsis
    • Scott, A.M. & Saleh, M. The inflammatory caspases: guardians against infections and sepsis. Cell Death Differ. 14, 23-31 (2007).
    • (2007) Cell Death Differ. , vol.14 , pp. 23-31
    • Scott, A.M.1    Saleh, M.2
  • 3
    • 2342457148 scopus 로고    scopus 로고
    • Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms
    • Saleh, M. et al. Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms. Nature 429, 75-79 (2004).
    • (2004) Nature , vol.429 , pp. 75-79
    • Saleh, M.1
  • 4
    • 33646175602 scopus 로고    scopus 로고
    • Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice
    • Saleh, M. et al. Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature 440, 1064-1068 (2006).
    • (2006) Nature , vol.440 , pp. 1064-1068
    • Saleh, M.1
  • 5
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: A caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • Franchi, L., Eigenbrod, T., Munoz-Planillo, R. & Nunez, G. The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat. Immunol. 10, 241-247 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Munoz-Planillo, R.3    Nunez, G.4
  • 6
    • 60549112774 scopus 로고    scopus 로고
    • Inflammasome recognition of influenza virus is essential for adaptive immune responses
    • Ichinohe, T., Lee, H.K., Ogura, Y., Flavell, R. & Iwasaki, A. Inflammasome recognition of influenza virus is essential for adaptive immune responses. J. Exp. Med. 206, 79-87 (2009).
    • (2009) J. Exp. Med. , vol.206 , pp. 79-87
    • Ichinohe, T.1    Lee, H.K.2    Ogura, Y.3    Flavell, R.4    Iwasaki, A.5
  • 7
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • Allen, I.C. et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 30, 556-565 (2009).
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1
  • 8
    • 64049096334 scopus 로고    scopus 로고
    • The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1
    • Thomas, P.G. et al. The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1. Immunity 30, 566-575 (2009).
    • (2009) Immunity , vol.30 , pp. 566-575
    • Thomas, P.G.1
  • 9
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production
    • Poeck, H. et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production. Nat. Immunol. 11, 63-69 (2009).
    • (2009) Nat. Immunol. , vol.11 , pp. 63-69
    • Poeck, H.1
  • 10
    • 41949115934 scopus 로고    scopus 로고
    • Confinement of caspase-12 proteolytic activity to autoprocessing
    • Roy, S. et al. Confinement of caspase-12 proteolytic activity to autoprocessing. Proc. Natl. Acad. Sci. USA 105, 4133-4138 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4133-4138
    • Roy, S.1
  • 11
    • 40149084641 scopus 로고    scopus 로고
    • Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity
    • LeBlanc, P.M. et al. Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity. Cell Host Microbe 3, 146-157 (2008).
    • (2008) Cell Host Microbe , vol.3 , pp. 146-157
    • Leblanc, P.M.1
  • 12
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta;
    • Nakagawa, T. et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta;. Nature 403, 98-103 (2000).
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 13
    • 33744918550 scopus 로고    scopus 로고
    • Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis
    • Tan, Y. et al. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J. Biol. Chem. 281, 16016-16024 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 16016-16024
    • Tan, Y.1
  • 14
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda, T. et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J. Biol. Chem. 276, 13935-13940 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1
  • 15
    • 0035823579 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation
    • Rao, R.V. et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J. Biol. Chem. 276, 33869-33874 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 33869-33874
    • Rao, R.V.1
  • 16
    • 23644436847 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control and apoptosis
    • Groenendyk, J. & Michalak, M. Endoplasmic reticulum quality control and apoptosis. Acta Biochim. Pol. 52, 381-395 (2005). (Pubitemid 41133773)
    • (2005) Acta Biochimica Polonica , vol.52 , Issue.2 , pp. 381-395
    • Groenendyk, J.1    Michalak, M.2
  • 17
    • 0037077254 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway
    • Rao, R.V. et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway. J. Biol. Chem. 277, 21836-21842 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21836-21842
    • Rao, R.V.1
  • 18
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • Obeng, E.A. & Boise, L.H. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J. Biol. Chem. 280, 29578-29587 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 19
    • 33645124763 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism
    • Di Sano, F. et al. Endoplasmic reticulum stress induces apoptosis by an apoptosome-dependent but caspase 12-independent mechanism. J. Biol. Chem. 281, 2693-2700 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 2693-2700
    • Di Sano, F.1
  • 20
    • 33845497181 scopus 로고    scopus 로고
    • Inflammatory caspases and inflammasomes: Master switches of inflammation
    • Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 14, 10-22 (2007).
    • (2007) Cell Death Differ. , vol.14 , pp. 10-22
    • Martinon, F.1    Tschopp, J.2
  • 21
    • 0038731144 scopus 로고    scopus 로고
    • Linking Toll-like receptors to IFN-α/beta; Expression
    • Barton, G.M. & Medzhitov, R. Linking Toll-like receptors to IFN-α/beta; expression. Nat. Immunol. 4, 432-433 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 432-433
    • Barton, G.M.1    Medzhitov, R.2
  • 22
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama, M. et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5, 730-737 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 730-737
    • Yoneyama, M.1
  • 23
    • 23844438864 scopus 로고    scopus 로고
    • Shared and unique functions of the DExD/H-box helicases RIG-I MDA5 and LGP2 in antiviral innate immunity
    • Yoneyama, M. et al. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J. Immunol. 175, 2851-2858 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 2851-2858
    • Yoneyama, M.1
  • 24
    • 11144273976 scopus 로고    scopus 로고
    • Toll-like receptor 3 mediates West Nile virus entry into the brain causing lethal encephalitis
    • Wang, T. et al. Toll-like receptor 3 mediates West Nile virus entry into the brain causing lethal encephalitis. Nat. Med. 10, 1366-1373 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 1366-1373
    • Wang, T.1
  • 25
    • 55249084240 scopus 로고    scopus 로고
    • Toll-like receptor 3 has a protective role against West Nile virus infection
    • Daffis, S., Samuel, M.A., Suthar, M.S., Gale, M. Jr & Diamond, M.S. Toll-like receptor 3 has a protective role against West Nile virus infection. J. Virol. 82, 10349-10358 (2008).
    • (2008) J. Virol. , vol.82 , pp. 10349-10358
    • Daffis, S.1    Samuel, M.A.2    Suthar, M.S.3    Gale Jr., M.4    Diamond, M.S.5
  • 26
    • 60149109538 scopus 로고    scopus 로고
    • Toll-like receptor 7 mitigates lethal West Nile encephalitis via interleukin 23-dependent immune cell infiltration and homing
    • Town, T. et al. Toll-like receptor 7 mitigates lethal West Nile encephalitis via interleukin 23-dependent immune cell infiltration and homing. Immunity 30, 242-253 (2009).
    • (2009) Immunity , vol.30 , pp. 242-253
    • Town, T.1
  • 27
    • 37849045856 scopus 로고    scopus 로고
    • Establishment and maintenance of the innate antiviral response to West Nile Virus involves both RIG-I and MDA5 signaling through IPS-1
    • Fredericksen, B.L., Keller, B.C., Fornek, J., Katze, M.G. & Gale, M. Jr. Establishment and maintenance of the innate antiviral response to West Nile Virus involves both RIG-I and MDA5 signaling through IPS-1. J. Virol. 82, 609-616 (2008).
    • (2008) J. Virol. , vol.82 , pp. 609-616
    • Fredericksen, B.L.1    Keller, B.C.2    Fornek, J.3    Katze, M.G.4    Gale Jr., M.5
  • 28
    • 37349052379 scopus 로고    scopus 로고
    • Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity
    • Loo, Y.M. et al. Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity. J. Virol. 82, 335-345 (2008).
    • (2008) J. Virol. , vol.82 , pp. 335-345
    • Loo, Y.M.1
  • 29
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack, M.U. et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 446, 916-920 (2007).
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1
  • 30
    • 34250632829 scopus 로고    scopus 로고
    • Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125
    • Arimoto, K. et al. Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125. Proc. Natl. Acad. Sci. USA 104, 7500-7505 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7500-7505
    • Arimoto, K.1
  • 31
    • 35348921764 scopus 로고    scopus 로고
    • The Atg5 Atg12 conjugate associates with innate antiviral immune responses
    • Jounai, N. et al. The Atg5 Atg12 conjugate associates with innate antiviral immune responses. Proc. Natl. Acad. Sci. USA 104, 14050-14055 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14050-14055
    • Jounai, N.1
  • 32
    • 33846307026 scopus 로고    scopus 로고
    • Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2
    • Saito, T. et al. Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc. Natl. Acad. Sci. USA 104, 582-587 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 582-587
    • Saito, T.1
  • 33
    • 76549109497 scopus 로고    scopus 로고
    • LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses
    • Satoh, T. et al. LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses. Proc. Natl. Acad. Sci. USA 107, 1512-1517 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1512-1517
    • Satoh, T.1
  • 34
    • 1442324707 scopus 로고    scopus 로고
    • Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia
    • Simon, D. et al. Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia. J. Neurosci. 24, 1987-1995 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 1987-1995
    • Simon, D.1
  • 35
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato, H. et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441, 101-105 (2006).
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1
  • 36
    • 34447560071 scopus 로고    scopus 로고
    • Function of RIG-I-like receptors in antiviral innate immunity
    • Yoneyama, M. & Fujita, T. Function of RIG-I-like receptors in antiviral innate immunity. J. Biol. Chem. 282, 15315-15318 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 15315-15318
    • Yoneyama, M.1    Fujita, T.2
  • 37
    • 33947383048 scopus 로고    scopus 로고
    • P53-independent endoplasmic reticulum stress-mediated cytotoxicity of a Newcastle disease virus strain in tumor cell lines
    • Fabian, Z., Csatary, C.M., Szeberenyi, J. & Csatary, L.K. p53-independent endoplasmic reticulum stress-mediated cytotoxicity of a Newcastle disease virus strain in tumor cell lines. J. Virol. 81, 2817-2830 (2007).
    • (2007) J. Virol. , vol.81 , pp. 2817-2830
    • Fabian, Z.1    Csatary, C.M.2    Szeberenyi, J.3    Csatary, L.K.4
  • 38
    • 13544263363 scopus 로고    scopus 로고
    • Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells
    • Li, X.D., Lankinen, H., Putkuri, N., Vapalahti, O. & Vaheri, A. Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells. Virology 333, 180-189 (2005).
    • (2005) Virology , vol.333 , pp. 180-189
    • Li, X.D.1    Lankinen, H.2    Putkuri, N.3    Vapalahti, O.4    Vaheri, A.5
  • 39
    • 0036776317 scopus 로고    scopus 로고
    • Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells
    • Jordan, R., Wang, L., Graczyk, T.M., Block, T.M. & Romano, P.R. Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells. J. Virol. 76, 9588-9599 (2002).
    • (2002) J. Virol. , vol.76 , pp. 9588-9599
    • Jordan, R.1    Wang, L.2    Graczyk, T.M.3    Block, T.M.4    Romano, P.R.5
  • 40
    • 0034476896 scopus 로고    scopus 로고
    • An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus
    • Bitko, V. & Barik, S. An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus. J. Cell. Biochem. 80, 441-454 (2001).
    • (2001) J. Cell. Biochem. , vol.80 , pp. 441-454
    • Bitko, V.1    Barik, S.2
  • 41
    • 33947415733 scopus 로고    scopus 로고
    • Caspase 3-dependent cell death of neurons contributes to the pathogenesis of West Nile virus encephalitis
    • Samuel, M.A., Morrey, J.D. & Diamond, M.S. Caspase 3-dependent cell death of neurons contributes to the pathogenesis of West Nile virus encephalitis. J. Virol. 81, 2614-2623 (2007).
    • (2007) J. Virol. , vol.81 , pp. 2614-2623
    • Samuel, M.A.1    Morrey, J.D.2    Diamond, M.S.3
  • 42
    • 0344736838 scopus 로고    scopus 로고
    • Infection and injury of neurons by West Nile encephalitis virus
    • Shrestha, B., Gottlieb, D. & Diamond, M.S. Infection and injury of neurons by West Nile encephalitis virus. J. Virol. 77, 13203-13213 (2003).
    • (2003) J. Virol. , vol.77 , pp. 13203-13213
    • Shrestha, B.1    Gottlieb, D.2    Diamond, M.S.3
  • 43
    • 70350464626 scopus 로고    scopus 로고
    • Neurocognitive and functional outcomes in persons recovering from West Nile virus illness
    • Sejvar, J.J. et al. Neurocognitive and functional outcomes in persons recovering from West Nile virus illness. J. Neuropsychol. 2, 477-499 (2008).
    • (2008) J. Neuropsychol. , vol.2 , pp. 477-499
    • Sejvar, J.J.1
  • 44
    • 0037075551 scopus 로고    scopus 로고
    • RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
    • Kobayashi, K. et al. RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature 416, 194-199 (2002).
    • (2002) Nature , vol.416 , pp. 194-199
    • Kobayashi, K.1
  • 45
    • 33645786318 scopus 로고    scopus 로고
    • Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA
    • Takahashi, K. et al. Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA. J. Immunol. 176, 4520-4524 (2006).
    • (2006) J. Immunol. , vol.176 , pp. 4520-4524
    • Takahashi, K.1
  • 46
    • 58149185720 scopus 로고    scopus 로고
    • Active caspase-1-mediated secretion of retinoic acid inducible gene-I
    • Kim, M.J. & Yoo, J.Y. Active caspase-1-mediated secretion of retinoic acid inducible gene-I. J. Immunol. 181, 7324-7331 (2008).
    • (2008) J. Immunol. , vol.181 , pp. 7324-7331
    • Kim, M.J.1    Yoo, J.Y.2
  • 47
    • 0034292338 scopus 로고    scopus 로고
    • IL-1 beta attenuates IFN-αβ-induced antiviral activity and STAT1 activation in the liver: Involvement of proteasome-dependent pathway
    • Tian, Z., Shen, X., Feng, H. & Gao, B. IL-1 beta attenuates IFN-αβ-induced antiviral activity and STAT1 activation in the liver: involvement of proteasome-dependent pathway. J. Immunol. 165, 3959-3965 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 3959-3965
    • Tian, Z.1    Shen, X.2    Feng, H.3    Gao, B.4
  • 48
    • 67049158196 scopus 로고    scopus 로고
    • Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection
    • Yeretssian, G. et al. Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection. Proc. Natl. Acad. Sci. USA 106, 9016-9020 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9016-9020
    • Yeretssian, G.1
  • 49
    • 58149378449 scopus 로고    scopus 로고
    • Estrogen inhibits dendritic cell maturation to RNA viruses
    • Escribese, M.M. et al. Estrogen inhibits dendritic cell maturation to RNA viruses. Blood 112, 4574-4584 (2008).
    • (2008) Blood , vol.112 , pp. 4574-4584
    • Escribese, M.M.1
  • 50
    • 0030864463 scopus 로고    scopus 로고
    • Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations
    • Clark, H.B. et al. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations. J. Neurosci. 17, 7385-7395 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 7385-7395
    • Clark, H.B.1


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