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Volumn 3, Issue 1, 2014, Pages 1-11

Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3β

Author keywords

Drosophila; GSK3b; Phosphorylation; Tau

Indexed keywords


EID: 84979083907     PISSN: None     EISSN: 20466390     Source Type: Journal    
DOI: 10.1242/bio.20136692     Document Type: Article
Times cited : (26)

References (76)
  • 1
    • 0042125603 scopus 로고    scopus 로고
    • Reversible paired helical filamentlike phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals
    • Arendt, T., Stieler, J., Strijkstra, A. M., Hut, R. A., Rüdiger, J., Van der Zee, E. A., Harkany, T., Holzer, M. and Härtig, W. (2003). Reversible paired helical filamentlike phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals. J. Neurosci. 23, 6972-6981.
    • (2003) J. Neurosci , vol.23 , pp. 6972-6981
    • Arendt, T.1    Stieler, J.2    Strijkstra, A.M.3    Hut, R.A.4    Rüdiger, J.5    Van Der Zee, E.A.6    Harkany, T.7    Holzer, M.8    Härtig, W.9
  • 2
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V. M. and Trojanowski, J. Q. (2007). Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat. Rev. Neurosci. 8, 663-672.
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, M.2    Trojanowski, J.Q.3
  • 4
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
    • Brunden, K. R., Trojanowski, J. Q. and Lee, V. M. (2009). Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. Nat. Rev. Drug Discov. 8, 783-793.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 783-793
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 7
    • 33744952341 scopus 로고    scopus 로고
    • FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells
    • Bunker, J. M., Kamath, K., Wilson, L., Jordan, M. A. and Feinstein, S. C. (2006). FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells. J. Biol. Chem. 281, 11856-11863.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11856-11863
    • Bunker, J.M.1    Kamath, K.2    Wilson, L.3    Jordan, M.A.4    Feinstein, S.C.5
  • 9
    • 57649203362 scopus 로고    scopus 로고
    • Dissociation of tau toxicity and phosphorylation: Role of GSK-3beta, MARK and Cdk5 in a Drosophila model
    • Chatterjee, S., Sang, T. K., Lawless, G. M. and Jackson, G. R. (2009). Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum. Mol. Genet. 18, 164-177.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 164-177
    • Chatterjee, S.1    Sang, T.K.2    Lawless, G.M.3    Jackson, G.R.4
  • 10
    • 33744994326 scopus 로고    scopus 로고
    • Biochemical investigation of Tau protein phosphorylation status and its solubility properties in Drosophila
    • Chau, K. W., Chan, W. Y., Shaw, P. C. and Chan, H. Y. (2006). Biochemical investigation of Tau protein phosphorylation status and its solubility properties in Drosophila. Biochem. Biophys. Res. Commun. 346, 150-159.
    • (2006) Biochem. Biophys. Res. Commun , vol.346 , pp. 150-159
    • Chau, K.W.1    Chan, W.Y.2    Shaw, P.C.3    Chan, H.Y.4
  • 11
    • 33646198145 scopus 로고    scopus 로고
    • Tau therapeutic strategies for the treatment of Alzheimer's disease
    • Churcher, I. (2006). Tau therapeutic strategies for the treatment of Alzheimer's disease. Curr. Top. Med. Chem. 6, 579-595.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 579-595
    • Churcher, I.1
  • 12
    • 78149411188 scopus 로고    scopus 로고
    • Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo
    • Cowan, C. M., Bossing, T., Page, A., Shepherd, D. and Mudher, A. (2010). Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo. Acta Neuropathol. 120, 593-604.
    • (2010) Acta Neuropathol , vol.120 , pp. 593-604
    • Cowan, C.M.1    Bossing, T.2    Page, A.3    Shepherd, D.4    Mudher, A.5
  • 14
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble, B. W. and Woodgett, J. R. (2003). GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186.
    • (2003) J. Cell Sci. , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 15
    • 14044270858 scopus 로고    scopus 로고
    • Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly
    • Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M. and Cuenda, A. (2005). Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38delta at Thr50 promotes microtubule assembly. J. Cell Sci. 118, 397-408.
    • (2005) J. Cell Sci. , vol.118 , pp. 397-408
    • Feijoo, C.1    Campbell, D.G.2    Jakes, R.3    Goedert, M.4    Cuenda, A.5
  • 16
    • 77950940279 scopus 로고    scopus 로고
    • Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein
    • Feuillette, S., Miguel, L., Frébourg, T., Campion, D. and Lecourtois, M. (2010). Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein. J. Neurochem. 113, 895-903.
    • (2010) J. Neurochem. , vol.113 , pp. 895-903
    • Feuillette, S.1    Miguel, L.2    Frébourg, T.3    Campion, D.4    Lecourtois, M.5
  • 17
    • 0032870947 scopus 로고    scopus 로고
    • A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Am
    • Ghoshal, N., Smiley, J. F., DeMaggio, A. J., Hoekstra, M. F., Cochran, E. J., Binder, L. I. and Kuret, J. (1999). A new molecular link between the fibrillar and granulovacuolar lesions of Alzheimer's disease. Am. J. Pathol. 155, 1163-1172.
    • (1999) J. Pathol. , vol.155 , pp. 1163-1172
    • Ghoshal, N.1    Smiley, J.F.2    DeMaggio, A.J.3    Hoekstra, M.F.4    Cochran, E.J.5    Binder, L.I.6    Kuret, J.7
  • 19
    • 0345701340 scopus 로고    scopus 로고
    • Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells
    • Gómez-Ramos, A., Díaz-Nido, J., Smith, M. A., Perry, G. and Avila, J. (2003). Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells. J. Neurosci. Res. 71, 863-870.
    • (2003) J. Neurosci. Res. , vol.71 , pp. 863-870
    • Gómez-Ramos, A.1    Díaz-Nido, J.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 20
    • 33947587957 scopus 로고    scopus 로고
    • Differential changes in phosphorylation of tau at PHF-1 and 12E8 epitopes during brain ischemia and reperfusion in gerbils
    • Gordon-Krajcer, W., Kozniewska, E., Lazarewicz, J. W. and Ksiezak-Reding, H. (2007). Differential changes in phosphorylation of tau at PHF-1 and 12E8 epitopes during brain ischemia and reperfusion in gerbils. Neurochem. Res. 32, 729-737.
    • (2007) Neurochem. Res , vol.32 , pp. 729-737
    • Gordon-Krajcer, W.1    Kozniewska, E.2    Lazarewicz, J.W.3    Ksiezak-Reding, H.4
  • 21
    • 2442458847 scopus 로고    scopus 로고
    • Construction of transgenic Drosophila by using the site-specific integrase from phage phiC31
    • Groth, A. C., Fish, M., Nusse, R. and Calos, M. P. (2004). Construction of transgenic Drosophila by using the site-specific integrase from phage phiC31. Genetics 166, 1775-1782.
    • (2004) Genetics , vol.166 , pp. 1775-1782
    • Groth, A.C.1    Fish, M.2    Nusse, R.3    Calos, M.P.4
  • 22
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J. P. and Anderton, B. H. (1992). Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 23
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • Hanger, D. P., Betts, J. C., Loviny, T. L., Blackstock, W. P. and Anderton, B. H. (1998). New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J. Neurochem. 71, 2465-2476.
    • (1998) J. Neurochem. , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3    Blackstock, W.P.4    Anderton, B.H.5
  • 25
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H. and Noble, W. (2009). Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119.
    • (2009) Trends Mol. Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 26
    • 0034640005 scopus 로고    scopus 로고
    • Untangling tau-related dementia
    • Heutink, P. (2000). Untangling tau-related dementia. Hum. Mol. Genet. 9, 979-986.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 979-986
    • Heutink, P.1
  • 27
    • 57549090404 scopus 로고    scopus 로고
    • Levels of soluble and insoluble tau reflect overall status of tau phosphorylation in vivo
    • Hirata-Fukae, C., Li, H. F., Ma, L., Hoe, H. S., Rebeck, G. W., Aisen, P. S. and Matsuoka, Y. (2009). Levels of soluble and insoluble tau reflect overall status of tau phosphorylation in vivo. Neurosci. Lett. 450, 51-55.
    • (2009) Neurosci. Lett. , vol.450 , pp. 51-55
    • Hirata-Fukae, C.1    Li, H.F.2    Ma, L.3    Hoe, H.S.4    Rebeck, G.W.5    Aisen, P.S.6    Matsuoka, Y.7
  • 28
    • 33750894549 scopus 로고    scopus 로고
    • Multiple roles for glycogen synthase kinase-3 as a drug target in Alzheimer's disease
    • Huang, H. C. and Klein, P. S. (2006). Multiple roles for glycogen synthase kinase-3 as a drug target in Alzheimer's disease. Curr. Drug Targets 7, 1389-1397.
    • (2006) Curr. Drug Targets , vol.7 , pp. 1389-1397
    • Huang, H.C.1    Klein, P.S.2
  • 30
    • 34948883291 scopus 로고    scopus 로고
    • Increase in the relative expression of tau with four microtubule binding repeat regions in frontotemporal lobar degeneration and progressive supranuclear palsy brains
    • Ingelsson, M., Ramasamy, K., Russ, C., Freeman, S. H., Orne, J., Raju, S., Matsui, T., Growdon, J. H., Frosch, M. P., Ghetti, B. et al. (2007). Increase in the relative expression of tau with four microtubule binding repeat regions in frontotemporal lobar degeneration and progressive supranuclear palsy brains. Acta Neuropathol. 114, 471-479.
    • (2007) Acta Neuropathol , vol.114 , pp. 471-479
    • Ingelsson, M.1    Ramasamy, K.2    Russ, C.3    Freeman, S.H.4    Orne, J.5    Raju, S.6    Matsui, T.7    Growdon, J.H.8    Frosch, M.P.9    Ghetti, B.10
  • 32
    • 0035134081 scopus 로고    scopus 로고
    • Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice
    • Ishihara, T., Zhang, B., Higuchi, M., Yoshiyama, Y., Trojanowski, J. Q. and Lee, V. M. (2001). Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice. Am. J. Pathol. 158, 555-562.
    • (2001) Am. J. Pathol. , vol.158 , pp. 555-562
    • Ishihara, T.1    Zhang, B.2    Higuchi, M.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, M.6
  • 33
    • 0037118247 scopus 로고    scopus 로고
    • Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila
    • Jackson, G. R., Wiedau-Pazos, M., Sang, T. K., Wagle, N., Brown, C. A., Massachi, S. and Geschwind, D. H. (2002). Human wild-type tau interacts with wingless pathway components and produces neurofibrillary pathology in Drosophila. Neuron 34, 509-519.
    • (2002) Neuron , vol.34 , pp. 509-519
    • Jackson, G.R.1    Wiedau-Pazos, M.2    Sang, T.K.3    Wagle, N.4    Brown, C.A.5    Massachi, S.6    Geschwind, D.H.7
  • 34
    • 33748174617 scopus 로고    scopus 로고
    • A genomic screen for modifiers of tauopathy identifies puromycin-sensitive aminopeptidase as an inhibitor of tau-induced neurodegeneration
    • Karsten, S. L., Sang, T. K., Gehman, L. T., Chatterjee, S., Liu, J., Lawless, G. M., Sengupta, S., Berry, R. W., Pomakian, J., Oh, H. S. et al. (2006). A genomic screen for modifiers of tauopathy identifies puromycin-sensitive aminopeptidase as an inhibitor of tau-induced neurodegeneration. Neuron 51, 549-560.
    • (2006) Neuron , vol.51 , pp. 549-560
    • Karsten, S.L.1    Sang, T.K.2    Gehman, L.T.3    Chatterjee, S.4    Liu, J.5    Lawless, G.M.6    Sengupta, S.7    Berry, R.W.8    Pomakian, J.9    Oh, H.S.10
  • 35
    • 58149381905 scopus 로고    scopus 로고
    • Modeling tauopathy in the fruit fly Drosophila melanogaster
    • Khurana, V. (2008). Modeling tauopathy in the fruit fly Drosophila melanogaster. J. Alzheimers Dis. 15, 541-553.
    • (2008) J. Alzheimers Dis. , vol.15 , pp. 541-553
    • Khurana, V.1
  • 36
    • 31944434543 scopus 로고    scopus 로고
    • TOR-mediated cell-cycle activation causes neurodegeneration in a Drosophila tauopathy model
    • Khurana, V., Lu, Y., Steinhilb, M. L., Oldham, S., Shulman, J. M. and Feany, M. B. (2006). TOR-mediated cell-cycle activation causes neurodegeneration in a Drosophila tauopathy model. Curr. Biol. 16, 230-241.
    • (2006) Curr. Biol , vol.16 , pp. 230-241
    • Khurana, V.1    Lu, Y.2    Steinhilb, M.L.3    Oldham, S.4    Shulman, J.M.5    Feany, M.B.6
  • 37
    • 33846533244 scopus 로고    scopus 로고
    • The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease
    • Kimura, R., Kamino, K., Yamamoto, M., Nuripa, A., Kida, T., Kazui, H., Hashimoto, R., Tanaka, T., Kudo, T., Yamagata, H. et al. (2007). The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease. Hum. Mol. Genet. 16, 15-23.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 15-23
    • Kimura, R.1    Kamino, K.2    Yamamoto, M.3    Nuripa, A.4    Kida, T.5    Kazui, H.6    Hashimoto, R.7    Tanaka, T.8    Kudo, T.9    Yamagata, H.10
  • 38
    • 0030723127 scopus 로고    scopus 로고
    • Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain
    • Kuret, J., Johnson, G. S., Cha, D., Christenson, E. R., DeMaggio, A. J. and Hoekstra, M. F. (1997). Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain. J. Neurochem. 69, 2506-2515.
    • (1997) J. Neurochem. , vol.69 , pp. 2506-2515
    • Kuret, J.1    Johnson, G.S.2    Cha, D.3    Christenson, E.R.4    DeMaggio, A.J.5    Hoekstra, M.F.6
  • 42
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall, G. and Cole, R. D. (1984). Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259, 5301-5305.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 44
    • 0028675873 scopus 로고
    • Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells
    • Lovestone, S., Reynolds, C. H., Latimer, D., Davis, D. R., Anderton, B. H., Gallo, J. M., Hanger, D., Mulot, S., Marquardt, B., Stabel, S. et al. (1994). Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr. Biol. 4, 1077-1086.
    • (1994) Curr. Biol , vol.4 , pp. 1077-1086
    • Lovestone, S.1    Reynolds, C.H.2    Latimer, D.3    Davis, D.R.4    Anderton, B.H.5    Gallo, J.M.6    Hanger, D.7    Mulot, S.8    Marquardt, B.9    Stabel, S.10
  • 45
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas, J. J., Hernández, F., Gómez-Ramos, P., Morán, M. A., Hen, R. and Avila, J. (2001). Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 20, 27-39.
    • (2001) EMBO J. , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernández, F.2    Gómez-Ramos, P.3    Morán, M.A.4    Hen, R.5    Avila, J.6
  • 46
    • 0035232501 scopus 로고    scopus 로고
    • Tau proteins with frontotemporal dementia-17 mutations have both altered expression levels and phosphorylation profiles in differentiated neuroblastoma cells
    • Mack, T. G., Dayanandan, R., Van Slegtenhorst, M., Whone, A., Hutton, M., Lovestone, S. and Anderton, B. H. (2001). Tau proteins with frontotemporal dementia-17 mutations have both altered expression levels and phosphorylation profiles in differentiated neuroblastoma cells. Neuroscience 108, 701-712.
    • (2001) Neuroscience , vol.108 , pp. 701-712
    • Mack, T.G.1    Dayanandan, R.2    Van Slegtenhorst, M.3    Whone, A.4    Hutton, M.5    Lovestone, S.6    Anderton, B.H.7
  • 48
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimer's disease
    • Martin, L., Latypova, X. and Terro, F. (2011). Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem. Int. 58, 458-471.
    • (2011) Neurochem. Int , vol.58 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 49
    • 34447503455 scopus 로고    scopus 로고
    • Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
    • Mazanetz, M. P. and Fischer, P. M. (2007). Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat. Rev. Drug Discov. 6, 464-479.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 464-479
    • Mazanetz, M.P.1    Fischer, P.M.2
  • 53
    • 0036514504 scopus 로고    scopus 로고
    • Modelling neurodegenerative diseases in Drosophila: A fruitful approach? Nat
    • Muqit, M. M. and Feany, M. B. (2002). Modelling neurodegenerative diseases in Drosophila: a fruitful approach? Nat. Rev. Neurosci. 3, 237-243.
    • (2002) Rev. Neurosci , vol.3 , pp. 237-243
    • Muqit, M.M.1    Feany, M.B.2
  • 54
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura, I., Yang, Y. and Lu, B. (2004). PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116, 671-682.
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.2    Lu, B.3
  • 56
    • 77956299400 scopus 로고    scopus 로고
    • Splinkerette PCR for mapping transposable elements in Drosophila
    • Potter, C. J. and Luo, L. (2010). Splinkerette PCR for mapping transposable elements in Drosophila. PLoS ONE 5, e10168.
    • (2010) PLoS ONE , vol.5 , pp. e10168
    • Potter, C.J.1    Luo, L.2
  • 59
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman, J. M. and Feany, M. B. (2003). Genetic modifiers of tauopathy in Drosophila. Genetics 165, 1233-1242.
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 60
    • 0019967916 scopus 로고
    • Transposition of cloned P elements into Drosophila germ line chromosomes
    • Spradling, A. C. and Rubin, G. M. (1982). Transposition of cloned P elements into Drosophila germ line chromosomes. Science 218, 341-347.
    • (1982) Science , vol.218 , pp. 341-347
    • Spradling, A.C.1    Rubin, G.M.2
  • 64
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies, E. and Mandelkow, E. M. (2007). Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J. Neurosci. 27, 2896-2907.
    • (2007) J. Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 65
    • 58949100352 scopus 로고    scopus 로고
    • Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathways
    • Tuxworth, R. I., Vivancos, V., O'Hare, M. B. and Tear, G. (2009). Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathways. Hum. Mol. Genet. 18, 667-678.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 667-678
    • Tuxworth, R.I.1    Vivancos, V.2    O'Hare, M.B.3    Tear, G.4
  • 66
    • 0031737206 scopus 로고    scopus 로고
    • Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activity
    • Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T. and Hisanaga, S. (1998). Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activity. J. Biochem. 124, 738-746.
    • (1998) J. Biochem. , vol.124 , pp. 738-746
    • Wada, Y.1    Ishiguro, K.2    Itoh, T.J.3    Uchida, T.4    Hotani, H.5    Saito, T.6    Kishimoto, T.7    Hisanaga, S.8
  • 67
    • 4444333265 scopus 로고    scopus 로고
    • Transient cerebral ischemia induces site-specific hyperphosphorylation of tau protein
    • Wen, Y., Yang, S., Liu, R. and Simpkins, J. W. (2004). Transient cerebral ischemia induces site-specific hyperphosphorylation of tau protein. Brain Res. 1022, 30-38.
    • (2004) Brain Res , vol.1022 , pp. 30-38
    • Wen, Y.1    Yang, S.2    Liu, R.3    Simpkins, J.W.4
  • 68
    • 0025222679 scopus 로고
    • Position effects on eukaryotic gene expression
    • Wilson, C., Bellen, H. J. and Gehring, W. J. (1990). Position effects on eukaryotic gene expression. Annu. Rev. Cell Biol. 6, 679-714.
    • (1990) Annu. Rev. Cell Biol , vol.6 , pp. 679-714
    • Wilson, C.1    Bellen, H.J.2    Gehring, W.J.3
  • 70
    • 0035340356 scopus 로고    scopus 로고
    • The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site
    • Woods, Y. L., Rena, G., Morrice, N., Barthel, A., Becker, W., Guo, S., Unterman, T. G. and Cohen, P. (2001). The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site. Biochem. J. 355, 597-607.
    • (2001) Biochem J. , vol.355 , pp. 597-607
    • Woods, Y.L.1    Rena, G.2    Morrice, N.3    Barthel, A.4    Becker, W.5    Guo, S.6    Unterman, T.G.7    Cohen, P.8
  • 72
    • 61349097283 scopus 로고    scopus 로고
    • Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases
    • Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y., Iqbal, K., Grundke-Iqbal, I. and Gong, C. X. (2009). Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases. J. Neurochem. 108, 1480-1494.
    • (2009) J. Neurochem , vol.108 , pp. 1480-1494
    • Yu, Y.1    Run, X.2    Liang, Z.3    Li, Y.4    Liu, F.5    Liu, Y.6    Iqbal, K.7    Grundke-Iqbal, I.8    Gong, C.X.9
  • 73
    • 2342466091 scopus 로고    scopus 로고
    • Oxidative stress promotes tau dephosphorylation in neuronal cells: The roles of cdk5 and PP1. Free Radic
    • Zambrano, C. A., Egaña, J. T., Núñez, M. T., Maccioni, R. B. and González-Billault, C. (2004). Oxidative stress promotes tau dephosphorylation in neuronal cells: the roles of cdk5 and PP1. Free Radic. Biol. Med. 36, 1393-1402.
    • (2004) Biol. Med. , vol.36 , pp. 1393-1402
    • Zambrano, C.A.1    Egaña, J.T.2    Núñez, M.T.3    Maccioni, R.B.4    González-Billault, C.5
  • 76
    • 0036790527 scopus 로고    scopus 로고
    • Biochemical analysis of tau proteins in argyrophilic grain disease, Alzheimer's disease, and Pick's disease: A comparative study
    • Zhukareva, V., Shah, K., Uryu, K., Braak, H., Del Tredici, K., Sundarraj, S., Clark, C., Trojanowski, J. Q. and Lee, V. M. (2002). Biochemical analysis of tau proteins in argyrophilic grain disease, Alzheimer's disease, and Pick's disease: a comparative study. Am. J. Pathol. 161, 1135-1141.
    • (2002) Am. J. Pathol. , vol.161 , pp. 1135-1141
    • Zhukareva, V.1    Shah, K.2    Uryu, K.3    Braak, H.4    Del Tredici, K.5    Sundarraj, S.6    Clark, C.7    Trojanowski, J.Q.8    Lee, M.9


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