메뉴 건너뛰기




Volumn 35, Issue 2, 2008, Pages 107-112

Functional diversity of mammalian type 2C protein phosphatase isoforms: New tales from an old family

Author keywords

Human disease; Protein phosphatase; Signal transduction; Type 2C protein phosphatase (PP2C) isoforms

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE; PROTEIN PP 2 C; UNCLASSIFIED DRUG;

EID: 38149011286     PISSN: 03051870     EISSN: 14401681     Source Type: Journal    
DOI: 10.1111/j.1440-1681.2007.04843.x     Document Type: Short Survey
Times cited : (69)

References (56)
  • 2
    • 17044391680 scopus 로고    scopus 로고
    • Overview of protein serine/threonine phosphatases
    • In: Arino, J., Alexander, D.R. (eds). Vol. 5. Springer, Heidelberg.
    • Cohen PCT. Overview of protein serine/threonine phosphatases. In: Arino J, Alexander DR (eds). Topics in Current Genetics, Vol. 5. Springer, Heidelberg. 2004 1 20.
    • (2004) Topics in Current Genetics , pp. 1-20
    • Cohen, P.C.T.1
  • 3
    • 0001574833 scopus 로고
    • Nomenclature and chromosomal localization of human protein serine/threonine phosphatase genes
    • Cohen PTW. Nomenclature and chromosomal localization of human protein serine/threonine phosphatase genes. Adv. Protein Phosphatases 1994 8: 371 6.
    • (1994) Adv. Protein Phosphatases , vol.8 , pp. 371-6
    • Cohen, P.T.W.1
  • 4
    • 33845881426 scopus 로고    scopus 로고
    • Evolution of the metazoan protein phosphatase 2C superfamily
    • Stern A, Privman E, Rasis M, Lavi S, Pupko T. Evolution of the metazoan protein phosphatase 2C superfamily. J. Mol. Evol. 2007 64: 61 70.
    • (2007) J. Mol. Evol. , vol.64 , pp. 61-70
    • Stern, A.1    Privman, E.2    Rasis, M.3    Lavi, S.4    Pupko, T.5
  • 5
    • 34147129534 scopus 로고    scopus 로고
    • A novel mitochondrial matrix serine/threonine protein phosphatase regulates the mitochondria permeability transition pore and is essential for cellular survival and development
    • Lu G, Ren S, Korge P et al. A novel mitochondrial matrix serine/threonine protein phosphatase regulates the mitochondria permeability transition pore and is essential for cellular survival and development. Genes Dev. 2007 21: 784 96.
    • (2007) Genes Dev. , vol.21 , pp. 784-96
    • Lu, G.1    Ren, S.2    Korge, P.3
  • 6
    • 0032035043 scopus 로고    scopus 로고
    • Signal transduction by MAP kinase cascades in budding yeast
    • Posas F, Takekawa M, Saito H. Signal transduction by MAP kinase cascades in budding yeast. Curr. Opin. Microbiol. 1998 1: 175 82.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 175-82
    • Posas, F.1    Takekawa, M.2    Saito, H.3
  • 7
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman M, Chen W, Cobb MH. Differential regulation and properties of MAPKs. Oncogene 2007 26: 3100 12.
    • (2007) Oncogene , vol.26 , pp. 3100-12
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 8
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb MH, Goldsmith EJ. How MAP kinases are regulated. J. Biol. Chem. 1995 270: 14 843 6.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-6
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 9
    • 0032541227 scopus 로고    scopus 로고
    • Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways
    • Takekawa M, Maeda T, Saito H. Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J. 1998 17: 4744 52.
    • (1998) EMBO J. , vol.17 , pp. 4744-52
    • Takekawa, M.1    Maeda, T.2    Saito, H.3
  • 10
    • 0032561413 scopus 로고    scopus 로고
    • Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells
    • Hanada M, Kobayashi T, Ohnishi M et al. Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells. FEBS Lett. 1998 437: 172 6.
    • (1998) FEBS Lett. , vol.437 , pp. 172-6
    • Hanada, M.1    Kobayashi, T.2    Ohnishi, M.3
  • 11
    • 0035937111 scopus 로고    scopus 로고
    • Regulation of the TAK1 signaling pathway by protein phosphatase 2C
    • Hanada M, Ninomiya-Tsuji J, Komaki K et al. Regulation of the TAK1 signaling pathway by protein phosphatase 2C. J. Biol. Chem. 2001 276: 5753 9.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5753-9
    • Hanada, M.1    Ninomiya-Tsuji, J.2    Komaki, K.3
  • 12
    • 34547413496 scopus 로고    scopus 로고
    • Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cepsilon
    • Saito JI, Toriumi S, Awano K et al. Regulation of apoptosis signal-regulating kinase 1 by protein phosphatase 2Cepsilon. Biochem. J. 2007 405: 591 6.
    • (2007) Biochem. J. , vol.405 , pp. 591-6
    • Saito, J.I.1    Toriumi, S.2    Awano, K.3
  • 13
    • 0037809234 scopus 로고    scopus 로고
    • Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon)
    • Li MG, Katsura K, Nomiyama H et al. Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). J. Biol. Chem. 2003 278: 12 013 21.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12013-21
    • Li, M.G.1    Katsura, K.2    Nomiyama, H.3
  • 14
    • 33847038271 scopus 로고    scopus 로고
    • P38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity
    • Vahebi S, Ota A, Li M et al. p38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity. Circ. Res. 2007 100: 408 15.
    • (2007) Circ. Res. , vol.100 , pp. 408-15
    • Vahebi, S.1    Ota, A.2    Li, M.3
  • 16
    • 9144253936 scopus 로고    scopus 로고
    • The ASK1-MAP kinase cascades in mammalian stress response
    • Matsukawa J, Matsuzawa A, Takeda K, Ichijo H. The ASK1-MAP kinase cascades in mammalian stress response. J. Biochem. 2004 136: 261 5.
    • (2004) J. Biochem. , vol.136 , pp. 261-5
    • Matsukawa, J.1    Matsuzawa, A.2    Takeda, K.3    Ichijo, H.4
  • 17
    • 33745955405 scopus 로고    scopus 로고
    • PP2C family members play key roles in regulation of cell survival and apoptosis
    • Tamura S, Toriumi S, Saito J, Awano K, Kudo TA, Kobayashi T. PP2C family members play key roles in regulation of cell survival and apoptosis. Cancer Sci. 2006 97: 563 7.
    • (2006) Cancer Sci. , vol.97 , pp. 563-7
    • Tamura, S.1    Toriumi, S.2    Saito, J.3    Awano, K.4    Kudo, T.A.5    Kobayashi, T.6
  • 19
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: A hard Akt to follow
    • Brazil DP, Hemmings BA. Ten years of protein kinase B signalling: A hard Akt to follow. Trends Biochem. Sci. 2001 26: 657 64.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 657-64
    • Brazil, D.P.1    Hemmings, B.A.2
  • 20
    • 33947243276 scopus 로고    scopus 로고
    • PHLPPing it off: Phosphatases get in the Akt
    • Mendoza MC, Blenis J. PHLPPing it off: Phosphatases get in the Akt. Mol. Cell 2007 25: 798 800.
    • (2007) Mol. Cell , vol.25 , pp. 798-800
    • Mendoza, M.C.1    Blenis, J.2
  • 21
    • 1642499409 scopus 로고    scopus 로고
    • Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo
    • Foukas LC, Beeton CA, Jensen J, Phillips WA, Shepherd PR. Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo. Mol. Cell. Biol. 2004 24: 966 75.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 966-75
    • Foukas, L.C.1    Beeton, C.A.2    Jensen, J.3    Phillips, W.A.4    Shepherd, P.R.5
  • 22
    • 0027953284 scopus 로고
    • PI 3-kinase is a dual specificity enzyme: Autoregulation by an intrinsic protein-serine kinase activity
    • Dhand R, Hiles I, Panayotou G et al. PI 3-kinase is a dual specificity enzyme: Autoregulation by an intrinsic protein-serine kinase activity. EMBO J. 1994 13: 522 33.
    • (1994) EMBO J. , vol.13 , pp. 522-33
    • Dhand, R.1    Hiles, I.2    Panayotou, G.3
  • 23
    • 2542475897 scopus 로고    scopus 로고
    • Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes
    • Yoshizaki T, Maegawa H, Egawa K et al. Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes. J. Biol. Chem. 2004 279: 22 715 26.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22715-26
    • Yoshizaki, T.1    Maegawa, H.2    Egawa, K.3
  • 24
    • 15244344356 scopus 로고    scopus 로고
    • A portrait of AKT kinases: Human cancer and animal models depict a family with strong individualities
    • Bellacosa A, Testa JR, Moore R, Larue L. A portrait of AKT kinases: Human cancer and animal models depict a family with strong individualities. Cancer Biol. Ther. 2004 3: 268 75.
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 268-75
    • Bellacosa, A.1    Testa, J.R.2    Moore, R.3    Larue, L.4
  • 25
    • 33947203621 scopus 로고    scopus 로고
    • PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms
    • Brognard J, Sierecki E, Gao T, Newton AC. PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. Mol. Cell 2007 25: 917 31.
    • (2007) Mol. Cell , vol.25 , pp. 917-31
    • Brognard, J.1    Sierecki, E.2    Gao, T.3    Newton, A.C.4
  • 26
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP. a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • Gao T, Furnari F, Newton AC. PHLPP. A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol. Cell 2005 18: 13 24.
    • (2005) Mol. Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 28
    • 33747889727 scopus 로고    scopus 로고
    • Functional distinctions of protein kinase B/Akt isoforms defined by their influence on cell migration
    • Stambolic V, Woodgett JR. Functional distinctions of protein kinase B/Akt isoforms defined by their influence on cell migration. Trends Cell Biol. 2006 16: 461 6.
    • (2006) Trends Cell Biol. , vol.16 , pp. 461-6
    • Stambolic, V.1    Woodgett, J.R.2
  • 29
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • Jacinto E, Facchinetti V, Liu D et al. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 2006 127: 125 37.
    • (2006) Cell , vol.127 , pp. 125-37
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3
  • 30
    • 33751079895 scopus 로고    scopus 로고
    • Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity
    • Yang Q, Inoki K, Ikenoue T, Guan KL. Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev. 2006 20: 2820 32.
    • (2006) Genes Dev. , vol.20 , pp. 2820-32
    • Yang, Q.1    Inoki, K.2    Ikenoue, T.3    Guan, K.L.4
  • 31
    • 0038690163 scopus 로고    scopus 로고
    • Suprachiasmatic nucleus circadian oscillatory protein, a novel binding partner of K-Ras in the membrane rafts, negatively regulates MAPK pathway
    • Shimizu K, Okada M, Nagai K, Fukada Y. Suprachiasmatic nucleus circadian oscillatory protein, a novel binding partner of K-Ras in the membrane rafts, negatively regulates MAPK pathway. J. Biol. Chem. 2003 278: 14 920 5.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14920-5
    • Shimizu, K.1    Okada, M.2    Nagai, K.3    Fukada, Y.4
  • 32
    • 0035895375 scopus 로고    scopus 로고
    • New responsibilities for the PI3K regulatory subunit p85 alpha
    • Okkenhaug K, Vanhaesebroeck B. New responsibilities for the PI3K regulatory subunit p85 alpha. Sci. STKE 2001 2001: PE1.
    • (2001) Sci. STKE , vol.2001
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 33
    • 33751419716 scopus 로고    scopus 로고
    • Surviving the breakup: The DNA damage checkpoint
    • Harrison JC, Haber JE. Surviving the breakup: The DNA damage checkpoint. Annu. Rev. Genet. 2006 40: 209 35.
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 209-35
    • Harrison, J.C.1    Haber, J.E.2
  • 34
    • 0842287638 scopus 로고    scopus 로고
    • DNA damage tumor suppressor genes and genomic instability
    • Motoyama N, Naka K. DNA damage tumor suppressor genes and genomic instability. Curr. Opin. Genet. Dev. 2004 14: 11 16.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 11-16
    • Motoyama, N.1    Naka, K.2
  • 35
    • 0344643062 scopus 로고    scopus 로고
    • PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break
    • Leroy C, Lee SE, Vaze MB et al. PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break. Mol. Cell 2003 11: 827 35.
    • (2003) Mol. Cell , vol.11 , pp. 827-35
    • Leroy, C.1    Lee, S.E.2    Vaze, M.B.3
  • 36
    • 33748150967 scopus 로고    scopus 로고
    • Wip1 phosphatase modulates ATM-dependent signaling pathways
    • Shreeram S, Demidov ON, Hee WK et al. Wip1 phosphatase modulates ATM-dependent signaling pathways. Mol. Cell 2006 23: 757 64.
    • (2006) Mol. Cell , vol.23 , pp. 757-64
    • Shreeram, S.1    Demidov, O.N.2    Hee, W.K.3
  • 37
    • 18844405191 scopus 로고    scopus 로고
    • PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints
    • Lu X, Nannenga B, Donehower LA. PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints. Genes Dev. 2005 19: 1162 74.
    • (2005) Genes Dev. , vol.19 , pp. 1162-74
    • Lu, X.1    Nannenga, B.2    Donehower, L.A.3
  • 38
    • 33745206498 scopus 로고    scopus 로고
    • Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1 phosphatase
    • Fujimoto H, Onishi N, Kato N et al. Regulation of the antioncogenic Chk2 kinase by the oncogenic Wip1 phosphatase. Cell Death Differ. 2006 13: 1170 80.
    • (2006) Cell Death Differ. , vol.13 , pp. 1170-80
    • Fujimoto, H.1    Onishi, N.2    Kato, N.3
  • 39
    • 33847382384 scopus 로고    scopus 로고
    • The Wip1 phosphatase (PPM1D) antagonizes activation of the Chk2 tumour suppressor kinase
    • Oliva-Trastoy M, Berthonaud V, Chevalier A et al. The Wip1 phosphatase (PPM1D) antagonizes activation of the Chk2 tumour suppressor kinase. Oncogene 2007 26: 1449 58.
    • (2007) Oncogene , vol.26 , pp. 1449-58
    • Oliva-Trastoy, M.1    Berthonaud, V.2    Chevalier, A.3
  • 40
    • 0034383398 scopus 로고    scopus 로고
    • P53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation
    • Takekawa M, Adachi M, Nakahata A et al. p53-inducible wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation. EMBO J. 2000 19: 6517 26.
    • (2000) EMBO J. , vol.19 , pp. 6517-26
    • Takekawa, M.1    Adachi, M.2    Nakahata, A.3
  • 41
    • 4344560876 scopus 로고    scopus 로고
    • The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
    • Lu X, Bocangel D, Nannenga B, Yamaguchi H, Appella E, Donehower LA. The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair. Mol. Cell 2004 15: 621 34.
    • (2004) Mol. Cell , vol.15 , pp. 621-34
    • Lu, X.1    Bocangel, D.2    Nannenga, B.3    Yamaguchi, H.4    Appella, E.5    Donehower, L.A.6
  • 42
    • 0030925222 scopus 로고    scopus 로고
    • Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner
    • Fiscella M, Zhang H, Fan S et al. Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner. Proc. Natl Acad. Sci. USA 1997 94: 6048 53.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6048-53
    • Fiscella, M.1    Zhang, H.2    Fan, S.3
  • 43
    • 0036613212 scopus 로고    scopus 로고
    • Amplification of PPM1D in human tumors abrogates p53 tumor-suppressor activity
    • Bulavin DV, Demidov ON, Saito S et al. Amplification of PPM1D in human tumors abrogates p53 tumor-suppressor activity. Nat. Genet. 2002 31: 210 15.
    • (2002) Nat. Genet. , vol.31 , pp. 210-15
    • Bulavin, D.V.1    Demidov, O.N.2    Saito, S.3
  • 44
    • 18544385947 scopus 로고    scopus 로고
    • Oncogenic properties of PPM1D located within a breast cancer amplification epicenter at 17q23
    • Li J, Yang Y, Peng Y et al. Oncogenic properties of PPM1D located within a breast cancer amplification epicenter at 17q23. Nat. Genet. 2002 31: 133 4.
    • (2002) Nat. Genet. , vol.31 , pp. 133-4
    • Li, J.1    Yang, Y.2    Peng, Y.3
  • 45
    • 1842483852 scopus 로고    scopus 로고
    • Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK-mediated activation of the p16 (Ink4a)-p19 (Arf) pathway
    • Bulavin DV, Phillips C, Nannenga B et al. Inactivation of the Wip1 phosphatase inhibits mammary tumorigenesis through p38 MAPK-mediated activation of the p16 (Ink4a)-p19 (Arf) pathway. Nat. Genet. 2004 36: 343 50.
    • (2004) Nat. Genet. , vol.36 , pp. 343-50
    • Bulavin, D.V.1    Phillips, C.2    Nannenga, B.3
  • 48
  • 50
    • 28444483130 scopus 로고    scopus 로고
    • Gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair
    • Chowdhury D, Keogh MC, Ishii H, Peterson CL, Buratowski S, Lieberman J. gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair. Mol. Cell 2005 20: 801 9.
    • (2005) Mol. Cell , vol.20 , pp. 801-9
    • Chowdhury, D.1    Keogh, M.C.2    Ishii, H.3    Peterson, C.L.4    Buratowski, S.5    Lieberman, J.6
  • 51
    • 0032901297 scopus 로고    scopus 로고
    • The type 2C Ser/Thr phosphatase PP2Cgamma is a pre-mRNA splicing factor
    • Murray MV, Kobayashi R, Krainer AR. The type 2C Ser/Thr phosphatase PP2Cgamma is a pre-mRNA splicing factor. Genes Dev 1999 13: 87 97.
    • (1999) Genes Dev , vol.13 , pp. 87-97
    • Murray, M.V.1    Kobayashi, R.2    Krainer, A.R.3
  • 52
    • 33750715383 scopus 로고    scopus 로고
    • A novel histone exchange factor, protein phosphatase 2Cgamma, mediates the exchange and dephosphorylation of H2A-H2B
    • Kimura H, Takizawa N, Allemand E et al. A novel histone exchange factor, protein phosphatase 2Cgamma, mediates the exchange and dephosphorylation of H2A-H2B. J. Cell Biol. 2006 175: 389 400.
    • (2006) J. Cell Biol. , vol.175 , pp. 389-400
    • Kimura, H.1    Takizawa, N.2    Allemand, E.3
  • 53
    • 10344242925 scopus 로고    scopus 로고
    • Kinase signaling cascades in the mitochondrion: A matter of life or death
    • Horbinski C, Chu CT. Kinase signaling cascades in the mitochondrion: A matter of life or death. Free Radic. Biol. Med. 2005 38: 2 11.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 2-11
    • Horbinski, C.1    Chu, C.T.2
  • 54
    • 32544448056 scopus 로고    scopus 로고
    • Role of mitochondria as the gardens of cell death
    • Kim R, Emi M, Tanabe K. Role of mitochondria as the gardens of cell death. Cancer Chemother. Pharmacol. 2006 57: 545 53.
    • (2006) Cancer Chemother. Pharmacol. , vol.57 , pp. 545-53
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 55
  • 56
    • 34248670864 scopus 로고    scopus 로고
    • Protein phosphatases types 2Calpha and 2Cbeta in apoptosis
    • Klumpp S, Thissen MC, Krieglstein J. Protein phosphatases types 2Calpha and 2Cbeta in apoptosis. Biochem. Soc. Trans. 2006 34: 1370 5.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1370-5
    • Klumpp, S.1    Thissen, M.C.2    Krieglstein, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.