메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Protein kinase D interacts with neuronal nitric oxide synthase and phosphorylates the activatory residue serine1412

Author keywords

[No Author keywords available]

Indexed keywords

NEURONAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE; PROTEIN KINASE B; PROTEIN KINASE D; PROTEIN KINASE D1; PROTEIN KINASE D2; UNCLASSIFIED DRUG; VASODILATOR STIMULATED PHOSPHOPROTEIN;

EID: 84930170749     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0095191     Document Type: Article
Times cited : (8)

References (85)
  • 1
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases: Regulation and function
    • 837a-837d
    • Forstermann U, Sessa WC (2012) Nitric oxide synthases: regulation and function. Eur Heart J 33: 829-837, 837a-837d.
    • (2012) Eur Heart J , vol.33 , pp. 829-837
    • Forstermann, U.1    Sessa, W.C.2
  • 2
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt DS, Hwang PM, Glatt CE, Lowenstein C, Reed RR, et al. (1991) Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature 351: 714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5
  • 3
  • 4
    • 67349230279 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase: Structure, subcellular localization, regulation, and clinical implications
    • Zhou L, Zhu DY (2009) Neuronal nitric oxide synthase: structure, subcellular localization, regulation, and clinical implications. Nitric Oxide 20: 223-230.
    • (2009) Nitric Oxide , vol.20 , pp. 223-230
    • Zhou, L.1    Zhu, D.Y.2
  • 5
    • 79952543583 scopus 로고    scopus 로고
    • Research progress on neurobiology of neuronal nitric oxide synthase
    • Luo CX, Zhu DY (2011) Research progress on neurobiology of neuronal nitric oxide synthase. Neurosci Bull 27: 23-35.
    • (2011) Neurosci Bull , vol.27 , pp. 23-35
    • Luo, C.X.1    Zhu, D.Y.2
  • 6
    • 0030895195 scopus 로고    scopus 로고
    • PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences
    • Stricker NL, Christopherson KS, Yi BA, Schatz PJ, Raab RW, et al. (1997) PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences. Nat Biotechnol 15: 336-342.
    • (1997) Nat Biotechnol , vol.15 , pp. 336-342
    • Stricker, N.L.1    Christopherson, K.S.2    Yi, B.A.3    Schatz, P.J.4    Raab, R.W.5
  • 7
    • 0030995719 scopus 로고    scopus 로고
    • The neuronal nitric oxide synthase PDZ motif binds to -G(D, E)XV carboxyterminal sequences
    • Schepens J, Cuppen E, Wieringa B, Hendriks W (1997) The neuronal nitric oxide synthase PDZ motif binds to -G(D, E)XV carboxyterminal sequences. FEBS Lett 409: 53-56.
    • (1997) FEBS Lett , vol.409 , pp. 53-56
    • Schepens, J.1    Cuppen, E.2    Wieringa, B.3    Hendriks, W.4
  • 8
    • 0031932281 scopus 로고    scopus 로고
    • CAPON: A protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95
    • Jaffrey SR, Snowman AM, Eliasson MJ, Cohen NA, Snyder SH (1998) CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95. Neuron 20: 115-124.
    • (1998) Neuron , vol.20 , pp. 115-124
    • Jaffrey, S.R.1    Snowman, A.M.2    Eliasson, M.J.3    Cohen, N.A.4    Snyder, S.H.5
  • 9
    • 0032916127 scopus 로고    scopus 로고
    • Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide
    • Tochio H, Zhang Q, Mandal P, Li M, Zhang M (1999) Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide. Nat Struct Biol 6: 417-421.
    • (1999) Nat Struct Biol , vol.6 , pp. 417-421
    • Tochio, H.1    Zhang, Q.2    Mandal, P.3    Li, M.4    Zhang, M.5
  • 10
    • 0033537962 scopus 로고    scopus 로고
    • Interaction of neuronal nitric-oxide synthase and phosphofructokinase-M
    • Firestein BL, Bredt DS (1999) Interaction of neuronal nitric-oxide synthase and phosphofructokinase-M. The Journal of biological chemistry 274: 10545-10550.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 10545-10550
    • Firestein, B.L.1    Bredt, D.S.2
  • 11
    • 3142727963 scopus 로고    scopus 로고
    • NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity
    • Saitoh F, Tian QB, Okano A, Sakagami H, Kondo H, et al. (2004) NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity. J Biol Chem 279: 29461-29468.
    • (2004) J Biol Chem , vol.279 , pp. 29461-29468
    • Saitoh, F.1    Tian, Q.B.2    Okano, A.3    Sakagami, H.4    Kondo, H.5
  • 12
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOSsyntrophin complex
    • Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA (1999) Unexpected modes of PDZ domain scaffolding revealed by structure of nNOSsyntrophin complex. Science 284: 812-815.
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 13
    • 0034040448 scopus 로고    scopus 로고
    • Formation of a nativelike beta-hairpin finger structure of a peptide from the extended PDZ domain of neuronal nitric oxide synthase in aqueous solution
    • Wang P, Zhang Q, Tochio H, Fan JS, Zhang M (2000) Formation of a nativelike beta-hairpin finger structure of a peptide from the extended PDZ domain of neuronal nitric oxide synthase in aqueous solution. Eur J Biochem 267: 3116-3122.
    • (2000) Eur J Biochem , vol.267 , pp. 3116-3122
    • Wang, P.1    Zhang, Q.2    Tochio, H.3    Fan, J.S.4    Zhang, M.5
  • 14
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
    • Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, et al. (1996) Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell 84: 757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5
  • 15
    • 0033600913 scopus 로고    scopus 로고
    • PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain
    • Christopherson KS, Hillier BJ, Lim WA, Bredt DS (1999) PSD-95 assembles a ternary complex with the N-methyl-D-aspartic acid receptor and a bivalent neuronal NO synthase PDZ domain. J Biol Chem 274: 27467-27473.
    • (1999) J Biol Chem , vol.274 , pp. 27467-27473
    • Christopherson, K.S.1    Hillier, B.J.2    Lim, W.A.3    Bredt, D.S.4
  • 16
    • 0033546347 scopus 로고    scopus 로고
    • Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein
    • Sattler R, Xiong Z, Lu WY, Hafner M, MacDonald JF, et al. (1999) Specific coupling of NMDA receptor activation to nitric oxide neurotoxicity by PSD-95 protein. Science 284: 1845-1848.
    • (1999) Science , vol.284 , pp. 1845-1848
    • Sattler, R.1    Xiong, Z.2    Lu, W.Y.3    Hafner, M.4    MacDonald, J.F.5
  • 17
    • 34548636072 scopus 로고    scopus 로고
    • PDZ protein interactions underlying NMDA receptor-mediated excitotoxicity and neuroprotection by PSD-95 inhibitors
    • Cui H, Hayashi A, Sun HS, Belmares MP, Cobey C, et al. (2007) PDZ protein interactions underlying NMDA receptor-mediated excitotoxicity and neuroprotection by PSD-95 inhibitors. J Neurosci 27: 9901-9915.
    • (2007) J Neurosci , vol.27 , pp. 9901-9915
    • Cui, H.1    Hayashi, A.2    Sun, H.S.3    Belmares, M.P.4    Cobey, C.5
  • 18
    • 84856450634 scopus 로고    scopus 로고
    • The PSD-95/nNOS complex: New drugs for depression?
    • Doucet MV, Harkin A, Dev KK (2012) The PSD-95/nNOS complex: new drugs for depression? Pharmacol Ther 133: 218-229.
    • (2012) Pharmacol Ther , vol.133 , pp. 218-229
    • Doucet, M.V.1    Harkin, A.2    Dev, K.K.3
  • 19
    • 70350365279 scopus 로고    scopus 로고
    • Kidins220/ARMS downregulation by excitotoxic activation of NMDARs reveals its involvement in neuronal survival and death pathways
    • Lopez-Menendez C, Gascon S, Sobrado M, Vidaurre OG, Higuero AM, et al. (2009) Kidins220/ARMS downregulation by excitotoxic activation of NMDARs reveals its involvement in neuronal survival and death pathways. J Cell Sci 122: 3554-3565.
    • (2009) J Cell Sci , vol.122 , pp. 3554-3565
    • Lopez-Menendez, C.1    Gascon, S.2    Sobrado, M.3    Vidaurre, O.G.4    Higuero, A.M.5
  • 20
    • 0034704111 scopus 로고    scopus 로고
    • Identification and cloning of Kidins220, a novel neuronal substrate of protein kinase D
    • Iglesias T, Cabrera-Poch N, Mitchell MP, Naven TJ, Rozengurt E, et al. (2000) Identification and cloning of Kidins220, a novel neuronal substrate of protein kinase D. J Biol Chem 275: 40048-40056.
    • (2000) J Biol Chem , vol.275 , pp. 40048-40056
    • Iglesias, T.1    Cabrera-Poch, N.2    Mitchell, M.P.3    Naven, T.J.4    Rozengurt, E.5
  • 21
    • 0035141510 scopus 로고    scopus 로고
    • An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors
    • Kong H, Boulter J, Weber JL, Lai C, Chao MV (2001) An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors. J Neurosci 21: 176-185.
    • (2001) J Neurosci , vol.21 , pp. 176-185
    • Kong, H.1    Boulter, J.2    Weber, J.L.3    Lai, C.4    Chao, M.V.5
  • 22
    • 79955061032 scopus 로고    scopus 로고
    • Protein kinase D signaling: Multiple biological functions in health and disease
    • Rozengurt E (2011) Protein kinase D signaling: multiple biological functions in health and disease. Physiology 26: 23-33.
    • (2011) Physiology , vol.26 , pp. 23-33
    • Rozengurt, E.1
  • 23
    • 52049118759 scopus 로고    scopus 로고
    • Both the establishment and maintenance of neuronal polarity require the activity of protein kinase D in the Golgi apparatus
    • Yin DM, Huang YH, Zhu YB, Wang Y (2008) Both the establishment and maintenance of neuronal polarity require the activity of protein kinase D in the Golgi apparatus. J Neurosci 28: 8832-8843.
    • (2008) J Neurosci , vol.28 , pp. 8832-8843
    • Yin, D.M.1    Huang, Y.H.2    Zhu, Y.B.3    Wang, Y.4
  • 24
    • 55249101834 scopus 로고    scopus 로고
    • Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons
    • Bisbal M, Conde C, Donoso M, Bollati F, Sesma J, et al. (2008) Protein kinase d regulates trafficking of dendritic membrane proteins in developing neurons. J Neurosci 28: 9297-9308.
    • (2008) J Neurosci , vol.28 , pp. 9297-9308
    • Bisbal, M.1    Conde, C.2    Donoso, M.3    Bollati, F.4    Sesma, J.5
  • 25
    • 65249145271 scopus 로고    scopus 로고
    • Protein kinase D controls the integrity of Golgi apparatus and the maintenance of dendritic arborization in hippocampal neurons
    • Czondor K, Ellwanger K, Fuchs YF, Lutz S, Gulyas M, et al. (2009) Protein kinase D controls the integrity of Golgi apparatus and the maintenance of dendritic arborization in hippocampal neurons. Mol Biol Cell 20: 2108-2120.
    • (2009) Mol Biol Cell , vol.20 , pp. 2108-2120
    • Czondor, K.1    Ellwanger, K.2    Fuchs, Y.F.3    Lutz, S.4    Gulyas, M.5
  • 26
    • 33745815978 scopus 로고    scopus 로고
    • Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif
    • Sanchez-Ruiloba L, Cabrera-Poch N, Rodriguez-Martinez M, Lopez-Menendez C, Jean-Mairet RM, et al. (2006) Protein kinase D intracellular localization and activity control kinase D-interacting substrate of 220-kDa traffic through a postsynaptic density-95/discs large/zonula occludens-1-binding motif. J Biol Chem 281: 18888-18900.
    • (2006) J Biol Chem , vol.281 , pp. 18888-18900
    • Sanchez-Ruiloba, L.1    Cabrera-Poch, N.2    Rodriguez-Martinez, M.3    Lopez-Menendez, C.4    Jean-Mairet, R.M.5
  • 27
    • 0033543570 scopus 로고    scopus 로고
    • Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cmu
    • Matthews SA, Rozengurt E, Cantrell D (1999) Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cmu. J Biol Chem 274: 26543-26549.
    • (1999) J Biol Chem , vol.274 , pp. 26543-26549
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3
  • 28
    • 34347370083 scopus 로고    scopus 로고
    • Binding of CAP70 to inducible nitric oxide synthase and implications for the vectorial release of nitric oxide in polarized cells
    • Navarro-Lerida I, Martinez-Moreno M, Ventoso I, Alvarez-Barrientos A, Rodriguez-Crespo I (2007) Binding of CAP70 to inducible nitric oxide synthase and implications for the vectorial release of nitric oxide in polarized cells. Mol Biol Cell 18: 2768-2777.
    • (2007) Mol Biol Cell , vol.18 , pp. 2768-2777
    • Navarro-Lerida, I.1    Martinez-Moreno, M.2    Ventoso, I.3    Alvarez-Barrientos, A.4    Rodriguez-Crespo, I.5
  • 29
    • 0032855089 scopus 로고    scopus 로고
    • Dynamic re-distribution of protein kinase D (PKD) as revealed by a GFP-PKD fusion protein: Dissociation from PKD activation
    • Matthews S, Iglesias T, Cantrell D, Rozengurt E (1999) Dynamic re-distribution of protein kinase D (PKD) as revealed by a GFP-PKD fusion protein: dissociation from PKD activation. FEBS Lett 457: 515-521.
    • (1999) FEBS Lett , vol.457 , pp. 515-521
    • Matthews, S.1    Iglesias, T.2    Cantrell, D.3    Rozengurt, E.4
  • 30
    • 0034659737 scopus 로고    scopus 로고
    • Spatial and temporal regulation of protein kinase D (PKD)
    • Matthews SA, Iglesias T, Rozengurt E, Cantrell D (2000) Spatial and temporal regulation of protein kinase D (PKD). EMBO J 19: 2935-2945.
    • (2000) EMBO J , vol.19 , pp. 2935-2945
    • Matthews, S.A.1    Iglesias, T.2    Rozengurt, E.3    Cantrell, D.4
  • 31
    • 34047148363 scopus 로고    scopus 로고
    • Biphasic coupling of neuronal nitric oxide synthase phosphorylation to the NMDA receptor regulates AMPA receptor trafficking and neuronal cell death
    • Rameau GA, Tukey DS, Garcin-Hosfield ED, Titcombe RF, Misra C, et al. (2007) Biphasic coupling of neuronal nitric oxide synthase phosphorylation to the NMDA receptor regulates AMPA receptor trafficking and neuronal cell death. J Neurosci 27: 3445-3455.
    • (2007) J Neurosci , vol.27 , pp. 3445-3455
    • Rameau, G.A.1    Tukey, D.S.2    Garcin-Hosfield, E.D.3    Titcombe, R.F.4    Misra, C.5
  • 32
    • 0039702796 scopus 로고    scopus 로고
    • Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis
    • Rodriguez-Crespo I, Nishida CR, Knudsen GM, de Montellano PR (1999) Mutation of the five conserved histidines in the endothelial nitric-oxide synthase hemoprotein domain. No evidence for a non-heme metal requirement for catalysis. J Biol Chem 274: 21617-21624.
    • (1999) J Biol Chem , vol.274 , pp. 21617-21624
    • Rodriguez-Crespo, I.1    Nishida, C.R.2    Knudsen, G.M.3    De Montellano, P.R.4
  • 33
    • 0030446051 scopus 로고    scopus 로고
    • Human endothelial nitric oxide synthase: Expression in Escherichia coli, coexpression with calmodulin, and characterization
    • Rodriguez-Crespo I, Ortiz de Montellano PR (1996) Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. Arch Biochem Biophys 336: 151-156.
    • (1996) Arch Biochem Biophys , vol.336 , pp. 151-156
    • Rodriguez-Crespo, I.1    Ortiz De Montellano, P.R.2
  • 34
    • 0030894379 scopus 로고    scopus 로고
    • Active site topologies and cofactor-mediated conformational changes of nitricoxide synthases
    • Gerber NC, Rodriguez-Crespo I, Nishida CR, Ortiz de Montellano PR (1997) Active site topologies and cofactor-mediated conformational changes of nitricoxide synthases. J Biol Chem 272: 6285-6290.
    • (1997) J Biol Chem , vol.272 , pp. 6285-6290
    • Gerber, N.C.1    Rodriguez-Crespo, I.2    Nishida, C.R.3    Ortiz De Montellano, P.R.4
  • 35
    • 0033515681 scopus 로고    scopus 로고
    • The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C
    • Waldron RT, Iglesias T, Rozengurt E (1999) The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. J Biol Chem 274: 9224-9230.
    • (1999) J Biol Chem , vol.274 , pp. 9224-9230
    • Waldron, R.T.1    Iglesias, T.2    Rozengurt, E.3
  • 36
    • 0031982706 scopus 로고    scopus 로고
    • Protein kinase D activation by mutations within its pleckstrin homology domain
    • Iglesias T, Rozengurt E (1998) Protein kinase D activation by mutations within its pleckstrin homology domain. J Biol Chem 273: 410-416.
    • (1998) J Biol Chem , vol.273 , pp. 410-416
    • Iglesias, T.1    Rozengurt, E.2
  • 37
    • 3142582003 scopus 로고    scopus 로고
    • Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells
    • Cabrera-Poch N, Sanchez-Ruiloba L, Rodriguez-Martinez M, Iglesias T (2004) Lipid raft disruption triggers protein kinase C and Src-dependent protein kinase D activation and Kidins220 phosphorylation in neuronal cells. J Biol Chem 279: 28592-28602.
    • (2004) J Biol Chem , vol.279 , pp. 28592-28602
    • Cabrera-Poch, N.1    Sanchez-Ruiloba, L.2    Rodriguez-Martinez, M.3    Iglesias, T.4
  • 38
    • 0031012892 scopus 로고    scopus 로고
    • Determination of the specific substrate sequence motifs of protein kinase C isozymes
    • Nishikawa K, Toker A, Johannes FJ, Songyang Z, Cantley LC (1997) Determination of the specific substrate sequence motifs of protein kinase C isozymes. J Biol Chem 272: 952-960.
    • (1997) J Biol Chem , vol.272 , pp. 952-960
    • Nishikawa, K.1    Toker, A.2    Johannes, F.J.3    Songyang, Z.4    Cantley, L.C.5
  • 39
    • 4444354274 scopus 로고    scopus 로고
    • Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase
    • Garcin ED, Bruns CM, Lloyd SJ, Hosfield DJ, Tiso M, et al. (2004) Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase. J Biol Chem 279: 37918-37927.
    • (2004) J Biol Chem , vol.279 , pp. 37918-37927
    • Garcin, E.D.1    Bruns, C.M.2    Lloyd, S.J.3    Hosfield, D.J.4    Tiso, M.5
  • 40
    • 67349096401 scopus 로고    scopus 로고
    • Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot
    • Eiseler T, Doppler H, Yan IK, Kitatani K, Mizuno K, et al. (2009) Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot. Nat Cell Biol 11: 545-556.
    • (2009) Nat Cell Biol , vol.11 , pp. 545-556
    • Eiseler, T.1    Doppler, H.2    Yan, I.K.3    Kitatani, K.4    Mizuno, K.5
  • 41
    • 77953315696 scopus 로고    scopus 로고
    • Protein kinase D controls actin polymerization and cell motility through phosphorylation of cortactin
    • Eiseler T, Hausser A, De Kimpe L, Van Lint J, Pfizenmaier K (2010) Protein kinase D controls actin polymerization and cell motility through phosphorylation of cortactin. J Biol Chem 285: 18672-18683.
    • (2010) J Biol Chem , vol.285 , pp. 18672-18683
    • Eiseler, T.1    Hausser, A.2    De Kimpe, L.3    Van Lint, J.4    Pfizenmaier, K.5
  • 42
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase C isoenzymes
    • Gschwendt M, Dieterich S, Rennecke J, Kittstein W, Mueller HJ, Johannes FJ (1996) Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase C isoenzymes. FEBS Lett 392: 77-80.
    • (1996) FEBS Lett , vol.392 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.J.5    Johannes, F.J.6
  • 43
    • 73449116098 scopus 로고    scopus 로고
    • Protein kinase D mediates synergistic expression of COX-2 induced by TNF-{alpha} and bradykinin in human colonic myofibroblasts
    • Yoo J, Chung C, Slice L, Sinnett-Smith J, Rozengurt E (2009) Protein kinase D mediates synergistic expression of COX-2 induced by TNF-{alpha} and bradykinin in human colonic myofibroblasts. Am J Physiol Cell Physiol 297: C1576-1587.
    • (2009) Am J Physiol Cell Physiol , vol.297 , pp. C1576-1587
    • Yoo, J.1    Chung, C.2    Slice, L.3    Sinnett-Smith, J.4    Rozengurt, E.5
  • 44
    • 77956318603 scopus 로고    scopus 로고
    • Nitric oxide signaling in brain function, dysfunction, and dementia
    • Steinert JR, Chernova T, Forsythe ID (2010) Nitric oxide signaling in brain function, dysfunction, and dementia. Neuroscientist 16: 435-452.
    • (2010) Neuroscientist , vol.16 , pp. 435-452
    • Steinert, J.R.1    Chernova, T.2    Forsythe, I.D.3
  • 45
    • 45149088480 scopus 로고    scopus 로고
    • Concepts of neural nitric oxide-mediated transmission
    • Garthwaite J (2008) Concepts of neural nitric oxide-mediated transmission. Eur J Neurosci 27: 2783-2802.
    • (2008) Eur J Neurosci , vol.27 , pp. 2783-2802
    • Garthwaite, J.1
  • 46
    • 79955988456 scopus 로고    scopus 로고
    • Protein kinase Adependent neuronal nitric oxide synthase activation mediates the enhancement of baroreflex response by adrenomedullin in the nucleus tractus solitarii of rats
    • Yen DH, Chen LC, Shen YC, Chiu YC, Ho IC, et al. (2011) Protein kinase Adependent neuronal nitric oxide synthase activation mediates the enhancement of baroreflex response by adrenomedullin in the nucleus tractus solitarii of rats. J Biomed Sci 18: 32.
    • (2011) J Biomed Sci , vol.18 , pp. 32
    • Yen, D.H.1    Chen, L.C.2    Shen, Y.C.3    Chiu, Y.C.4    Ho, I.C.5
  • 47
    • 0033667964 scopus 로고    scopus 로고
    • AMPK signaling in contracting human skeletal muscle: Acetyl-CoA carboxylase and NO synthase phosphorylation
    • Chen ZP, McConell GK, Michell BJ, Snow RJ, Canny BJ, et al. (2000) AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation. Am J Physiol Endocrinol Metab 279: E1202-1206.
    • (2000) Am J Physiol Endocrinol Metab , vol.279 , pp. E1202-E1206
    • Chen, Z.P.1    McConell, G.K.2    Michell, B.J.3    Snow, R.J.4    Canny, B.J.5
  • 48
    • 84869061341 scopus 로고    scopus 로고
    • Calcium-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors trigger neuronal nitric-oxide synthase activation to promote nerve cell death in an Src kinase-dependent fashion
    • Socodato R, Santiago FN, Portugal CC, Domingues AF, Santiago AR, et al. (2012) Calcium-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors trigger neuronal nitric-oxide synthase activation to promote nerve cell death in an Src kinase-dependent fashion. J Biol Chem 287: 38680-38694.
    • (2012) J Biol Chem , vol.287 , pp. 38680-38694
    • Socodato, R.1    Santiago, F.N.2    Portugal, C.C.3    Domingues, A.F.4    Santiago, A.R.5
  • 49
    • 70350439864 scopus 로고    scopus 로고
    • Regulation of VASP phosphorylation in cardiac myocytes: Differential regulation by cyclic nucleotides and modulation of protein expression in diabetic and hypertrophic heart
    • Sartoretto JL, Jin BY, Bauer M, Gertler FB, Liao R, et al. (2009) Regulation of VASP phosphorylation in cardiac myocytes: differential regulation by cyclic nucleotides and modulation of protein expression in diabetic and hypertrophic heart. Am J Physiol Heart Circ Physiol 297: H1697-1710.
    • (2009) Am J Physiol Heart Circ Physiol , vol.297 , pp. H1697-1710
    • Sartoretto, J.L.1    Jin, B.Y.2    Bauer, M.3    Gertler, F.B.4    Liao, R.5
  • 50
    • 0032493663 scopus 로고    scopus 로고
    • Analysis and regulation of vasodilator-stimulated phosphoprotein serine 239 phosphorylation in vitro and in intact cells using a phosphospecific monoclonal antibody
    • Smolenski A, Bachmann C, Reinhard K, Honig-Liedl P, Jarchau T, et al. (1998) Analysis and regulation of vasodilator-stimulated phosphoprotein serine 239 phosphorylation in vitro and in intact cells using a phosphospecific monoclonal antibody. J Biol Chem 273: 20029-20035.
    • (1998) J Biol Chem , vol.273 , pp. 20029-20035
    • Smolenski, A.1    Bachmann, C.2    Reinhard, K.3    Honig-Liedl, P.4    Jarchau, T.5
  • 51
    • 0034711470 scopus 로고    scopus 로고
    • Vasodilator-stimulated phosphoprotein serine 239 phosphorylation as a sensitive monitor of defective nitric oxide/cGMP signaling and endothelial dysfunction
    • Oelze M, Mollnau H, Hoffmann N, Warnholtz A, Bodenschatz M, et al. (2000) Vasodilator-stimulated phosphoprotein serine 239 phosphorylation as a sensitive monitor of defective nitric oxide/cGMP signaling and endothelial dysfunction. Circ Res 87: 999-1005.
    • (2000) Circ Res , vol.87 , pp. 999-1005
    • Oelze, M.1    Mollnau, H.2    Hoffmann, N.3    Warnholtz, A.4    Bodenschatz, M.5
  • 52
    • 0035494421 scopus 로고    scopus 로고
    • In vivo requirement of the alphasyntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4
    • Adams ME, Mueller HA, Froehner SC (2001) In vivo requirement of the alphasyntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. J Cell Biol 155: 113-122.
    • (2001) J Cell Biol , vol.155 , pp. 113-122
    • Adams, M.E.1    Mueller, H.A.2    Froehner, S.C.3
  • 53
    • 77955899173 scopus 로고    scopus 로고
    • The alpha-syntrophin PH and PDZ domains scaffold acetylcholine receptors, utrophin, and neuronal nitric oxide synthase at the neuromuscular junction
    • Adams ME, Anderson KN, Froehner SC (2010) The alpha-syntrophin PH and PDZ domains scaffold acetylcholine receptors, utrophin, and neuronal nitric oxide synthase at the neuromuscular junction. J Neurosci 30: 11004-11010.
    • (2010) J Neurosci , vol.30 , pp. 11004-11010
    • Adams, M.E.1    Anderson, K.N.2    Froehner, S.C.3
  • 54
    • 0032538539 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites required for protein kinase D activation
    • Iglesias T, Waldron RT, Rozengurt E (1998) Identification of in vivo phosphorylation sites required for protein kinase D activation. J Biol Chem 273: 27662-27667.
    • (1998) J Biol Chem , vol.273 , pp. 27662-27667
    • Iglesias, T.1    Waldron, R.T.2    Rozengurt, E.3
  • 55
    • 0037414763 scopus 로고    scopus 로고
    • Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain
    • Waldron RT, Rozengurt E (2003) Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain. J Biol Chem 278: 154-163.
    • (2003) J Biol Chem , vol.278 , pp. 154-163
    • Waldron, R.T.1    Rozengurt, E.2
  • 56
    • 0038043212 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation
    • Storz P, Doppler H, Johannes FJ, Toker A (2003) Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation. J Biol Chem 278: 17969-17976.
    • (2003) J Biol Chem , vol.278 , pp. 17969-17976
    • Storz, P.1    Doppler, H.2    Johannes, F.J.3    Toker, A.4
  • 57
    • 36148962891 scopus 로고    scopus 로고
    • A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation
    • Doppler H, Storz P (2007) A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation. J Biol Chem 282: 31873-31881.
    • (2007) J Biol Chem , vol.282 , pp. 31873-31881
    • Doppler, H.1    Storz, P.2
  • 58
    • 21444460483 scopus 로고    scopus 로고
    • Protein kinase D specifically mediates apoptosis signal-regulating kinase 1-JNK signaling induced by H2O2 but not tumor necrosis factor
    • Zhang W, Zheng S, Storz P, Min W (2005) Protein kinase D specifically mediates apoptosis signal-regulating kinase 1-JNK signaling induced by H2O2 but not tumor necrosis factor. J Biol Chem 280: 19036-19044.
    • (2005) J Biol Chem , vol.280 , pp. 19036-19044
    • Zhang, W.1    Zheng, S.2    Storz, P.3    Min, W.4
  • 59
    • 17644370387 scopus 로고    scopus 로고
    • A phosphorylation statespecific antibody recognizes Hsp27, a novel substrate of protein kinase D
    • Doppler H, Storz P, Li J, Comb MJ, Toker A (2005) A phosphorylation statespecific antibody recognizes Hsp27, a novel substrate of protein kinase D. J Biol Chem 280: 15013-15019.
    • (2005) J Biol Chem , vol.280 , pp. 15013-15019
    • Doppler, H.1    Storz, P.2    Li, J.3    Comb, M.J.4    Toker, A.5
  • 60
    • 9344230851 scopus 로고    scopus 로고
    • Protein kinase D is a novel mediator of cardiac troponin i phosphorylation and regulates myofilament function
    • Haworth RS, Cuello F, Herron TJ, Franzen G, Kentish JC, et al. (2004) Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function. Circ Res 95: 1091-1099.
    • (2004) Circ Res , vol.95 , pp. 1091-1099
    • Haworth, R.S.1    Cuello, F.2    Herron, T.J.3    Franzen, G.4    Kentish, J.C.5
  • 61
    • 78049284317 scopus 로고    scopus 로고
    • Protein kinase D1 suppresses epithelial-to-mesenchymal transition through phosphorylation of snail
    • Du C, Zhang C, Hassan S, Biswas MH, Balaji KC (2010) Protein kinase D1 suppresses epithelial-to-mesenchymal transition through phosphorylation of snail. Cancer Res 70: 7810-7819.
    • (2010) Cancer Res , vol.70 , pp. 7810-7819
    • Du, C.1    Zhang, C.2    Hassan, S.3    Biswas, M.H.4    Balaji, K.C.5
  • 62
    • 67651005347 scopus 로고    scopus 로고
    • Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like
    • Peterburs P, Heering J, Link G, Pfizenmaier K, Olayioye MA, et al. (2009) Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like. Cancer Res 69: 5634-5638.
    • (2009) Cancer Res , vol.69 , pp. 5634-5638
    • Peterburs, P.1    Heering, J.2    Link, G.3    Pfizenmaier, K.4    Olayioye, M.A.5
  • 63
    • 0036142091 scopus 로고    scopus 로고
    • The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins
    • Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, et al. (2002) The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol 22: 916-926.
    • (2002) Mol Cell Biol , vol.22 , pp. 916-926
    • Wang, Y.1    Waldron, R.T.2    Dhaka, A.3    Patel, A.4    Riley, M.M.5
  • 64
    • 79952321053 scopus 로고    scopus 로고
    • A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration
    • Ziegler S, Eiseler T, Scholz RP, Beck A, Link G, et al. (2011) A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration. Mol Biol Cell 22: 570-580.
    • (2011) Mol Biol Cell , vol.22 , pp. 570-580
    • Ziegler, S.1    Eiseler, T.2    Scholz, R.P.3    Beck, A.4    Link, G.5
  • 65
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • Fugmann T, Hausser A, Schoffler P, Schmid S, Pfizenmaier K, et al. (2007) Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J Cell Biol 178: 15-22.
    • (2007) J Cell Biol , vol.178 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schoffler, P.3    Schmid, S.4    Pfizenmaier, K.5
  • 66
    • 77954204064 scopus 로고    scopus 로고
    • Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation
    • Nhek S, Ngo M, Yang X, Ng MM, Field SJ, et al. (2010) Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation. Mol Biol Cell 21: 2327-2337.
    • (2010) Mol Biol Cell , vol.21 , pp. 2327-2337
    • Nhek, S.1    Ngo, M.2    Yang, X.3    Ng, M.M.4    Field, S.J.5
  • 67
    • 34848867249 scopus 로고    scopus 로고
    • Protein kinase D-mediated phosphorylation and nuclear export of sphingosine kinase 2
    • Ding G, Sonoda H, Yu H, Kajimoto T, Goparaju SK, et al. (2007) Protein kinase D-mediated phosphorylation and nuclear export of sphingosine kinase 2. J Biol Chem 282: 27493-27502.
    • (2007) J Biol Chem , vol.282 , pp. 27493-27502
    • Ding, G.1    Sonoda, H.2    Yu, H.3    Kajimoto, T.4    Goparaju, S.K.5
  • 68
    • 84858605175 scopus 로고    scopus 로고
    • Protein kinase D regulates RhoA activity via rhotekin phosphorylation
    • Pusapati GV, Eiseler T, Rykx A, Vandoninck S, Derua R, et al. (2012) Protein kinase D regulates RhoA activity via rhotekin phosphorylation. J Biol Chem 287: 9473-9483.
    • (2012) J Biol Chem , vol.287 , pp. 9473-9483
    • Pusapati, G.V.1    Eiseler, T.2    Rykx, A.3    Vandoninck, S.4    Derua, R.5
  • 69
    • 26944446652 scopus 로고    scopus 로고
    • Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol- 4 kinase IIIbeta at the Golgi complex
    • Hausser A, Storz P, Martens S, Link G, Toker A, et al. (2005) Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol- 4 kinase IIIbeta at the Golgi complex. Nat Cell Biol 7: 880-886.
    • (2005) Nat Cell Biol , vol.7 , pp. 880-886
    • Hausser, A.1    Storz, P.2    Martens, S.3    Link, G.4    Toker, A.5
  • 70
    • 4544315655 scopus 로고    scopus 로고
    • Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5
    • Vega RB, Harrison BC, Meadows E, Roberts CR, Papst PJ, et al. (2004) Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5. Mol Cell Biol 24: 8374-8385.
    • (2004) Mol Cell Biol , vol.24 , pp. 8374-8385
    • Vega, R.B.1    Harrison, B.C.2    Meadows, E.3    Roberts, C.R.4    Papst, P.J.5
  • 71
    • 12544257169 scopus 로고    scopus 로고
    • E-cadherin phosphorylation by protein kinase D1/protein kinase Cmu is associated with altered cellular aggregation and motility in prostate cancer
    • Jaggi M, Rao PS, Smith DJ, Wheelock MJ, Johnson KR, et al. (2005) E-cadherin phosphorylation by protein kinase D1/protein kinase Cmu is associated with altered cellular aggregation and motility in prostate cancer. Cancer Res 65: 483-492.
    • (2005) Cancer Res , vol.65 , pp. 483-492
    • Jaggi, M.1    Rao, P.S.2    Smith, D.J.3    Wheelock, M.J.4    Johnson, K.R.5
  • 72
    • 59149100469 scopus 로고    scopus 로고
    • Protein kinase D1-mediated phosphorylation and subcellular localization of beta-catenin
    • Du C, Jaggi M, Zhang C, Balaji KC (2009) Protein kinase D1-mediated phosphorylation and subcellular localization of beta-catenin. Cancer Res 69: 1117-1124.
    • (2009) Cancer Res , vol.69 , pp. 1117-1124
    • Du, C.1    Jaggi, M.2    Zhang, C.3    Balaji, K.C.4
  • 73
    • 34447529462 scopus 로고    scopus 로고
    • Protein kinase D induces transcription through direct phosphorylation of the cAMP-response element-binding protein
    • Johannessen M, Delghandi MP, Rykx A, Dragset M, Vandenheede JR, et al. (2007) Protein kinase D induces transcription through direct phosphorylation of the cAMP-response element-binding protein. J Biol Chem 282: 14777-14787.
    • (2007) J Biol Chem , vol.282 , pp. 14777-14787
    • Johannessen, M.1    Delghandi, M.P.2    Rykx, A.3    Dragset, M.4    Vandenheede, J.R.5
  • 74
    • 28244474850 scopus 로고    scopus 로고
    • C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase
    • Tiso M, Konas DW, Panda K, Garcin ED, Sharma M, et al. (2005) C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase. J Biol Chem 280: 39208-39219.
    • (2005) J Biol Chem , vol.280 , pp. 39208-39219
    • Tiso, M.1    Konas, D.W.2    Panda, K.3    Garcin, E.D.4    Sharma, M.5
  • 75
    • 0035846945 scopus 로고    scopus 로고
    • Neuronal nitric-oxide synthase mutant (Ser-1412-Asp) demonstrates surprising connections between heme reduction, NO complex formation, and catalysis
    • Adak S, Santolini J, Tikunova S, Wang Q, Johnson JD, et al. (2001) Neuronal nitric-oxide synthase mutant (Ser-1412-Asp) demonstrates surprising connections between heme reduction, NO complex formation, and catalysis. J Biol Chem 276: 1244-1252.
    • (2001) J Biol Chem , vol.276 , pp. 1244-1252
    • Adak, S.1    Santolini, J.2    Tikunova, S.3    Wang, Q.4    Johnson, J.D.5
  • 76
    • 77955356174 scopus 로고    scopus 로고
    • Mu-opioid receptors transiently activate the Akt-nNOS pathway to produce sustained potentiation of PKC-mediated NMDAR-CaMKII signaling
    • Sanchez-Blazquez P, Rodriguez-Munoz M, Garzon J (2010) Mu-opioid receptors transiently activate the Akt-nNOS pathway to produce sustained potentiation of PKC-mediated NMDAR-CaMKII signaling. PLoS One 5: e11278.
    • (2010) PLoS One , vol.5 , pp. e11278
    • Sanchez-Blazquez, P.1    Rodriguez-Munoz, M.2    Garzon, J.3
  • 77
    • 0033542414 scopus 로고    scopus 로고
    • Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
    • Fulton D, Gratton JP, McCabe TJ, Fontana J, Fujio Y, et al. (1999) Regulation of endothelium-derived nitric oxide production by the protein kinase Akt. Nature 399: 597-601.
    • (1999) Nature , vol.399 , pp. 597-601
    • Fulton, D.1    Gratton, J.P.2    McCabe, T.J.3    Fontana, J.4    Fujio, Y.5
  • 79
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler S, Fleming I, Fisslthaler B, Hermann C, Busse R, et al. (1999) Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399: 601-605.
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5
  • 81
    • 34250731849 scopus 로고    scopus 로고
    • Life history of eNOS: Partners and pathways
    • Dudzinski DM, Michel T (2007) Life history of eNOS: partners and pathways. Cardiovasc Res 75: 247-260.
    • (2007) Cardiovasc Res , vol.75 , pp. 247-260
    • Dudzinski, D.M.1    Michel, T.2
  • 82
    • 0034054493 scopus 로고    scopus 로고
    • Enhanced electron flux and reduced calmodulin dissociation may explain ''calcium-independent'' eNOS activation by phosphorylation
    • McCabe TJ, Fulton D, Roman LJ, Sessa WC (2000) Enhanced electron flux and reduced calmodulin dissociation may explain ''calcium-independent'' eNOS activation by phosphorylation. J Biol Chem 275: 6123-6128.
    • (2000) J Biol Chem , vol.275 , pp. 6123-6128
    • McCabe, T.J.1    Fulton, D.2    Roman, L.J.3    Sessa, W.C.4
  • 83
    • 0043234527 scopus 로고    scopus 로고
    • Synergistic activation of endothelial nitricoxide synthase (eNOS) by HSP90 and Akt: Calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex
    • Takahashi S, Mendelsohn ME (2003) Synergistic activation of endothelial nitricoxide synthase (eNOS) by HSP90 and Akt: calcium-independent eNOS activation involves formation of an HSP90-Akt-CaM-bound eNOS complex. J Biol Chem 278: 30821-30827.
    • (2003) J Biol Chem , vol.278 , pp. 30821-30827
    • Takahashi, S.1    Mendelsohn, M.E.2
  • 84
    • 0041355355 scopus 로고    scopus 로고
    • Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells
    • Morrow VA, Foufelle F, Connell JM, Petrie JR, Gould GW, et al. (2003) Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells. J Biol Chem 278: 31629-31639.
    • (2003) J Biol Chem , vol.278 , pp. 31629-31639
    • Morrow, V.A.1    Foufelle, F.2    Connell, J.M.3    Petrie, J.R.4    Gould, G.W.5
  • 85
    • 81855197043 scopus 로고    scopus 로고
    • Chk1 and Hsp90 cooperatively regulate phosphorylation of endothelial nitric oxide synthase at serine 1179
    • Park JH, Kim WS, Kim JY, Park MH, Nam JH, et al. (2011) Chk1 and Hsp90 cooperatively regulate phosphorylation of endothelial nitric oxide synthase at serine 1179. Free Radic Biol Med 51: 2217-2226.
    • (2011) Free Radic Biol Med , vol.51 , pp. 2217-2226
    • Park, J.H.1    Kim, W.S.2    Kim, J.Y.3    Park, M.H.4    Nam, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.