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Volumn 414, Issue 2, 2011, Pages 217-230

Functional implications of the conformational switch in AICD peptide upon binding to Grb2-SH2 domain

Author keywords

Alzheimer's disease; conformational switch; Grb2; phosphorylated tyrosine; SH2

Indexed keywords

AMYLOID BETA PROTEIN; BINDING PROTEIN; GROWTH FACTOR RECEPTOR BINDING PROTEIN 2; PROTEIN SH2; UNCLASSIFIED DRUG;

EID: 81355127252     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.046     Document Type: Article
Times cited : (20)

References (53)
  • 1
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • DOI 10.1038/nature02621
    • Mattson M.P. Pathways towards and away from Alzheimer's disease Nature 430 2004 631 639 (Pubitemid 39061671)
    • (2004) Nature , vol.430 , Issue.7000 , pp. 631-639
    • Mattson, M.P.1
  • 2
    • 0029792928 scopus 로고    scopus 로고
    • New clues to Alzheimer's disease: Unraveling the roles of amyloid and tau
    • DOI 10.1038/nm0896-850
    • Yankner B.A. New clues to Alzheimer's disease: unraveling the roles of amyloid and tau Nat. Med. 2 1996 850 852 (Pubitemid 26296747)
    • (1996) Nature Medicine , vol.2 , Issue.8 , pp. 850-852
    • Yankner, B.A.1
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 0035997231 scopus 로고    scopus 로고
    • Biogenesis and metabolism of Alzheimer's disease Aβ amyloid peptides
    • DOI 10.1016/S0196-9781(02)00063-3, PII S0196978102000633
    • Evin G., and Weidemann A. Biogenesis and metabolism of Alzheimer's disease Abeta amyloid peptides Peptides 23 2002 1285 1297 (Pubitemid 34786707)
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1285-1297
    • Evin, G.1    Weidemann, A.2
  • 6
    • 33845324145 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression
    • Kim H.S., Kim E.M., Lee J.P., Park C.H., Kim S., and Seo J.H. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression FASEB J. 17 2003 1951 1953
    • (2003) FASEB J. , vol.17 , pp. 1951-1953
    • Kim, H.S.1    Kim, E.M.2    Lee, J.P.3    Park, C.H.4    Kim, S.5    Seo, J.H.6
  • 7
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein
    • DOI 10.1016/S0092-8674(02)00809-7
    • Baek S.H., Ohgi K.A., Rose D.W., Koo E.H., Glass C.K., and Rosenfeld M.G. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein Cell 110 2002 55 67 (Pubitemid 34874606)
    • (2002) Cell , vol.110 , Issue.1 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 8
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • DOI 10.1242/jcs.01323
    • von Rotz R.C., Kohli B.M., Bosset J., Meier M., Suzuki T., Nitsch R.M., and Konietzko U. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor J. Cell Sci. 117 2004 4435 4448 (Pubitemid 39360070)
    • (2004) Journal of Cell Science , vol.117 , Issue.19 , pp. 4435-4448
    • Von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 9
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • DOI 10.1038/sj.embor.7400704, PII 7400704
    • Hebert S.S., Serneels L., Tolia A., Craessaerts K., Derks C., and Filippov M.A. Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes EMBO Rep. 7 2006 739 745 (Pubitemid 43986273)
    • (2006) EMBO Reports , vol.7 , Issue.7 , pp. 739-745
    • Hebert, S.S.1    Serneels, L.2    Tolia, A.3    Craessaerts, K.4    Derks, C.5    Filippov, M.A.6    Muller, U.7    De Strooper, B.8
  • 11
    • 78049267204 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP
    • Li H., Wang B., Wang Z., Guo Q., Tabuchi K., and Hammer R.E. Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP Proc. Natl Acad. Sci. USA 107 2010 17362 17367
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17362-17367
    • Li, H.1    Wang, B.2    Wang, Z.3    Guo, Q.4    Tabuchi, K.5    Hammer, R.E.6
  • 12
    • 70450235497 scopus 로고    scopus 로고
    • Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain
    • Ghosal K., Vogt D.L., Liang M., Shen Y., Lamb B.T., and Pimplikar S.W. Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain Proc. Natl Acad. Sci. USA 106 2009 18367 18372
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18367-18372
    • Ghosal, K.1    Vogt, D.L.2    Liang, M.3    Shen, Y.4    Lamb, B.T.5    Pimplikar, S.W.6
  • 13
    • 77955408755 scopus 로고    scopus 로고
    • Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce Alzheimer's disease-like traits in vivo
    • Giliberto L., d'Abramo C., Acker C.M., Davies P., and D'Adamio L. Transgenic expression of the amyloid-beta precursor protein-intracellular domain does not induce Alzheimer's disease-like traits in vivo PLoS One 5 2010 e11609
    • (2010) PLoS One , vol.5 , pp. 11609
    • Giliberto, L.1    D'Abramo, C.2    Acker, C.M.3    Davies, P.4    D'Adamio, L.5
  • 14
    • 77955637621 scopus 로고    scopus 로고
    • APP intracellular domain impairs adult neurogenesis in transgenic mice by inducing neuroinflammation
    • Ghosal K., Stathopoulos A., and Pimplikar S.W. APP intracellular domain impairs adult neurogenesis in transgenic mice by inducing neuroinflammation PLoS One 5 2010 e11866
    • (2010) PLoS One , vol.5 , pp. 11866
    • Ghosal, K.1    Stathopoulos, A.2    Pimplikar, S.W.3
  • 15
    • 77955640059 scopus 로고    scopus 로고
    • Aging and excitotoxic stress exacerbate neural circuit reorganization in amyloid precursor protein intracellular domain transgenic mice
    • Ghosal K., and Pimplikar S.W. Aging and excitotoxic stress exacerbate neural circuit reorganization in amyloid precursor protein intracellular domain transgenic mice Neurobiol. Aging 2010
    • (2010) Neurobiol. Aging
    • Ghosal, K.1    Pimplikar, S.W.2
  • 17
    • 17844399784 scopus 로고    scopus 로고
    • The amyloid precursor protein and its network of interacting proteins: Physiological and pathological implications
    • DOI 10.1016/j.brainresrev.2004.12.016, Glial-Neuron Crosstalk in Neuroinflamation, Neurodegeneration and Neuroprotection
    • Russo C., Venezia V., Repetto E., Nizzari M., Violani E., Carlo P., and Schettini G. The amyloid precursor protein and its network of interacting proteins: physiological and pathological implications Brain Res. Rev. 48 2005 257 264 (Pubitemid 40585757)
    • (2005) Brain Research Reviews , vol.48 , Issue.2 , pp. 257-264
    • Russo, C.1    Venezia, V.2    Repetto, E.3    Nizzari, M.4    Violani, E.5    Carlo, P.6    Schettini, G.7
  • 19
    • 60349103104 scopus 로고    scopus 로고
    • Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling
    • Zhou D., Zambrano N., Russo T., and D'Adamio L. Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling J. Alzheimers. Dis. 16 2009 301 307
    • (2009) J. Alzheimers. Dis. , vol.16 , pp. 301-307
    • Zhou, D.1    Zambrano, N.2    Russo, T.3    D'Adamio, L.4
  • 20
    • 79952952445 scopus 로고    scopus 로고
    • The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function
    • Barbagallo A.P., Wang Z., Zheng H., and D'Adamio L. The intracellular threonine of amyloid precursor protein that is essential for docking of Pin1 is dispensable for developmental function PLoS One 6 2011 e18006
    • (2011) PLoS One , vol.6 , pp. 18006
    • Barbagallo, A.P.1    Wang, Z.2    Zheng, H.3    D'Adamio, L.4
  • 21
    • 69049118186 scopus 로고    scopus 로고
    • The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains
    • Tamayev R., Zhou D., and D'Adamio L. The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains Mol. Neurodegener. 4 2009 28
    • (2009) Mol. Neurodegener. , vol.4 , pp. 28
    • Tamayev, R.1    Zhou, D.2    D'Adamio, L.3
  • 22
    • 79952903577 scopus 로고    scopus 로고
    • A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function
    • Barbagallo A.P., Wang Z., Zheng H., and D'Adamio L. A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function J. Biol. Chem. 286 2011 8717 8721
    • (2011) J. Biol. Chem. , vol.286 , pp. 8717-8721
    • Barbagallo, A.P.1    Wang, Z.2    Zheng, H.3    D'Adamio, L.4
  • 23
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • DOI 10.1074/jbc.M110286200
    • Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., and D'Adamio L. Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc J. Biol. Chem. 277 2002 16798 16804 (Pubitemid 34967702)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16798-16804
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'Adamio, L.5
  • 24
    • 2942586693 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 2 interaction with the tyrosine-phosphorylated tail of amyloid β precursor protein is mediated by its Src homology 2 domain
    • DOI 10.1074/jbc.M400488200
    • Zhou D., Noviello C., D'Ambrosio C., Scaloni A., and D'Adamio L. Growth factor receptor-bound protein 2 interaction with the tyrosine-phosphorylated tail of amyloid beta precursor protein is mediated by its Src homology 2 domain J. Biol. Chem. 279 2004 25374 25380 (Pubitemid 38756794)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25374-25380
    • Zhou, D.1    Noviello, C.2    D'Ambrosio, C.3    Scaloni, A.4    D'Adamio, L.5
  • 25
    • 0037144497 scopus 로고    scopus 로고
    • Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain
    • Russo C., Dolcini V., Salis S., Venezia V., Zambrano N., Russo T., and Schettini G. Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain J. Biol. Chem. 277 2002 35282 35288
    • (2002) J. Biol. Chem. , vol.277 , pp. 35282-35288
    • Russo, C.1    Dolcini, V.2    Salis, S.3    Venezia, V.4    Zambrano, N.5    Russo, T.6    Schettini, G.7
  • 26
    • 77954517945 scopus 로고    scopus 로고
    • Grb2-mediated alteration in the trafficking of AbetaPP: Insights from Grb2-AICD interaction
    • Raychaudhuri M., and Mukhopadhyay D. Grb2-mediated alteration in the trafficking of AbetaPP: insights from Grb2-AICD interaction J. Alzheimers Dis. 20 2010 275 292
    • (2010) J. Alzheimers Dis. , vol.20 , pp. 275-292
    • Raychaudhuri, M.1    Mukhopadhyay, D.2
  • 27
    • 79959621499 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and neurodegenerative diseases: Conformational promiscuity at its best
    • Das S., and Mukhopadhyay D. Intrinsically unstructured proteins and neurodegenerative diseases: conformational promiscuity at its best IUBMB Life 63 2011 478 488
    • (2011) IUBMB Life , vol.63 , pp. 478-488
    • Das, S.1    Mukhopadhyay, D.2
  • 28
    • 0035827587 scopus 로고    scopus 로고
    • The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene
    • Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., and Russo C. The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene J. Biol. Chem. 276 2001 19787 19792
    • (2001) J. Biol. Chem. , vol.276 , pp. 19787-19792
    • Zambrano, N.1    Bruni, P.2    Minopoli, G.3    Mosca, R.4    Molino, D.5    Russo, C.6
  • 30
    • 4544302611 scopus 로고    scopus 로고
    • Apoptotic cell death influences the signaling activity of the amyloid precursor protein through ShcA and Grb2 adaptor proteins in neuroblastoma SH-SY5Y cells
    • DOI 10.1111/j.1471-4159.2004.02618.x
    • Venezia V., Russo C., Repetto E., Salis S., Dolcini V., and Genova F. Apoptotic cell death influences the signaling activity of the amyloid precursor protein through ShcA and Grb2 adaptor proteins in neuroblastoma SH-SY5Y cells J. Neurochem. 90 2004 1359 1370 (Pubitemid 39223640)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.6 , pp. 1359-1370
    • Venezia, V.1    Russo, C.2    Repetto, E.3    Salis, S.4    Dolcini, V.5    Genova, F.6    Nizzari, M.7    Mueller, U.8    Schettini, G.9
  • 32
    • 0034646447 scopus 로고    scopus 로고
    • Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors
    • DOI 10.1021/bi992580m
    • Ramelot T.A., Gentile L.N., and Nicholson L.K. Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors Biochemistry 39 2000 2714 2725 (Pubitemid 30148926)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2714-2725
    • Ramelot, T.A.1    Gentile, L.N.2    Nicholson, L.K.3
  • 33
    • 0035970301 scopus 로고    scopus 로고
    • Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR
    • DOI 10.1006/jmbi.2001.4535
    • Ramelot T.A., and Nicholson L.K. Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR J. Mol. Biol. 307 2001 871 884 (Pubitemid 33027665)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.3 , pp. 871-884
    • Ramelot, T.A.1    Nicholson, L.K.2
  • 34
    • 0030723614 scopus 로고    scopus 로고
    • Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain
    • DOI 10.1093/emboj/16.20.6141
    • Zhang Z., Lee C.H., Mandiyan V., Borg J.P., Margolis B., Schlessinger J., and Kuriyan J. Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain EMBO J. 16 1997 6141 6150 (Pubitemid 27458334)
    • (1997) EMBO Journal , vol.16 , Issue.20 , pp. 6141-6150
    • Zhang, Z.1    Lee, C.-H.2    Mandiyan, V.3    Borg, J.-P.4    Margolis, B.5    Schlessinger, J.6    Kuriyan, J.7
  • 35
    • 55549113149 scopus 로고    scopus 로고
    • Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2
    • Radzimanowski J., Simon B., Sattler M., Beyreuther K., Sinning I., and Wild K. Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2 EMBO Rep. 9 2008 1134 1140
    • (2008) EMBO Rep. , vol.9 , pp. 1134-1140
    • Radzimanowski, J.1    Simon, B.2    Sattler, M.3    Beyreuther, K.4    Sinning, I.5    Wild, K.6
  • 38
    • 0029811093 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain
    • DOI 10.1021/bi952615s
    • Thornton K.H., Mueller W.T., McConnell P., Zhu G., Saltiel A.R., and Thanabal V. Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain Biochemistry 35 1996 11852 11864 (Pubitemid 26303705)
    • (1996) Biochemistry , vol.35 , Issue.36 , pp. 11852-11864
    • Thornton, K.H.1    Mueller, W.T.2    McConnell, P.3    Zhu, G.4    Saltiel, A.R.5    Thanabal, V.6
  • 42
    • 25144517155 scopus 로고    scopus 로고
    • Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain
    • DOI 10.1016/j.jmb.2005.08.037, PII S0022283605009745
    • Phan J., Shi Z.D., Burke T.R. Jr. , and Waugh D.S. Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain J. Mol. Biol. 353 2005 104 115 (Pubitemid 41338843)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.1 , pp. 104-115
    • Phan, J.1    Shi, Z.-D.2    Burke Jr., T.R.3    Waugh, D.S.4
  • 44
    • 0028337397 scopus 로고
    • Structure of the regulatory domains of the Src-family tyrosine kinase Lck
    • DOI 10.1038/368764a0
    • Eck M.J., Atwell S.K., Shoelson S.E., and Harrison S.C. Structure of the regulatory domains of the Src-family tyrosine kinase Lck Nature 368 1994 764 769 (Pubitemid 24153420)
    • (1994) Nature , vol.368 , Issue.6473 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 46
    • 77957254613 scopus 로고    scopus 로고
    • Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis
    • Li H., Wang Z., Wang B., Guo Q., Dolios G., and Tabuchi K. Genetic dissection of the amyloid precursor protein in developmental function and amyloid pathogenesis J. Biol. Chem. 285 2010 30598 30605
    • (2010) J. Biol. Chem. , vol.285 , pp. 30598-30605
    • Li, H.1    Wang, Z.2    Wang, B.3    Guo, Q.4    Dolios, G.5    Tabuchi, K.6
  • 47
    • 52049112089 scopus 로고    scopus 로고
    • Evidence that the amyloid beta precursor protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role
    • Giliberto L., Zhou D., Weldon R., Tamagno E., De Luca P., Tabaton M., and D'Adamio L. Evidence that the amyloid beta precursor protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role Mol. Neurodegener. 3 2008 12
    • (2008) Mol. Neurodegener. , vol.3 , pp. 12
    • Giliberto, L.1    Zhou, D.2    Weldon, R.3    Tamagno, E.4    De Luca, P.5    Tabaton, M.6    D'Adamio, L.7
  • 49
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 50
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 51
    • 1942423758 scopus 로고    scopus 로고
    • Membrane interaction of erythroid spectrin: Surface-density-dependent high-affinity binding to phosphatidylethanolamine
    • DOI 10.1080/09687680310001625800
    • Ray S., and Chakrabarti A. Membrane interaction of erythroid spectrin: surface-density-dependent high-affinity binding to phosphatidylethanolamine Mol. Membr. Biol. 21 2004 93 100 (Pubitemid 38524367)
    • (2004) Molecular Membrane Biology , vol.21 , Issue.2 , pp. 93-100
    • Ray, S.1    Chakrabarti, A.2
  • 52
    • 0035949536 scopus 로고    scopus 로고
    • 3 with the nucleosome: Role of core histone tail domains in the binding process
    • DOI 10.1021/bi010731r
    • Mir M.A., and Dasgupta D. Association of the anticancer antibiotic chromomycin A(3) with the nucleosome: role of core histone tail domains in the binding process Biochemistry 40 2001 11578 11585 (Pubitemid 32911302)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11578-11585
    • Mir, M.A.1    Dasgupta, D.2


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