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Volumn 10, Issue 12, 2014, Pages

The Tau Tubulin Kinases TTBK1/2 Promote Accumulation of Pathological TDP-43

Author keywords

[No Author keywords available]

Indexed keywords

TAR DNA BINDING PROTEIN; TUBULIN; TUBULIN KINASE 1; TUBULIN KINASE 2; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; PROTEIN SERINE THREONINE KINASE; TAU-TUBULIN KINASE;

EID: 84919663858     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004803     Document Type: Article
Times cited : (94)

References (65)
  • 1
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351: 602–611.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5
  • 2
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314: 130–133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5
  • 3
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford NJ, Zhang YJ, Baker M, Gass JM, Finch NA, et al. (2008) Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 4: e1000193.
    • (2008) PLoS Genet , vol.4 , pp. 1000193
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3    Gass, J.M.4    Finch, N.A.5
  • 4
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 1668–1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5
  • 5
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40: 572–574.
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Spiegelman, D.4    McConkey, B.J.5
  • 6
    • 41949100148 scopus 로고    scopus 로고
    • TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis
    • Van Deerlin VM, Leverenz JB, Bekris LM, Bird TD, Yuan W, et al. (2008) TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol 7: 409–416.
    • (2008) Lancet Neurol , vol.7 , pp. 409-416
    • Van Deerlin, V.M.1    Leverenz, J.B.2    Bekris, L.M.3    Bird, T.D.4    Yuan, W.5
  • 7
    • 51649124062 scopus 로고    scopus 로고
    • Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations
    • Kuhnlein P, Sperfeld AD, Vanmassenhove B, Van Deerlin V, Lee VM, et al. (2008) Two German kindreds with familial amyotrophic lateral sclerosis due to TARDBP mutations. Arch Neurol 65: 1185–1189.
    • (2008) Arch Neurol , vol.65 , pp. 1185-1189
    • Kuhnlein, P.1    Sperfeld, A.D.2    Vanmassenhove, B.3    Van Deerlin, V.4    Lee, V.M.5
  • 9
    • 58149398638 scopus 로고    scopus 로고
    • Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease
    • Schwab C, Arai T, Hasegawa M, Yu S, McGeer PL, (2008) Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease. J Neuropathol Exp Neurol 67: 1159–1165.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 1159-1165
    • Schwab, C.1    Arai, T.2    Hasegawa, M.3    Yu, S.4    McGeer, P.L.5
  • 11
    • 36348972414 scopus 로고    scopus 로고
    • Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
    • Higashi S, Iseki E, Yamamoto R, Minegishi M, Hino H, et al. (2007) Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies. Brain Res 1184: 284–294.
    • (2007) Brain Res , vol.1184 , pp. 284-294
    • Higashi, S.1    Iseki, E.2    Yamamoto, R.3    Minegishi, M.4    Hino, H.5
  • 12
    • 34249949338 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
    • Amador-Ortiz C, Lin WL, Ahmed Z, Personett D, Davies P, et al. (2007) TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease. Ann Neurol 61: 435–445.
    • (2007) Ann Neurol , vol.61 , pp. 435-445
    • Amador-Ortiz, C.1    Lin, W.L.2    Ahmed, Z.3    Personett, D.4    Davies, P.5
  • 13
  • 14
    • 78649750391 scopus 로고    scopus 로고
    • Phosphorylation Promotes Neurotoxicity in a Caenorhabditis elegans Model of TDP-43 Proteinopathy
    • Liachko NF, Guthrie CR, Kraemer BC, (2010) Phosphorylation Promotes Neurotoxicity in a Caenorhabditis elegans Model of TDP-43 Proteinopathy. J Neurosci 30: 16208–16219.
    • (2010) J Neurosci , vol.30 , pp. 16208-16219
    • Liachko, N.F.1    Guthrie, C.R.2    Kraemer, B.C.3
  • 15
    • 77950360176 scopus 로고    scopus 로고
    • Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
    • Kabashi E, Lin L, Tradewell ML, Dion PA, Bercier V, et al. (2010) Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo. Hum Mol Genet 19: 671–683.
    • (2010) Hum Mol Genet , vol.19 , pp. 671-683
    • Kabashi, E.1    Lin, L.2    Tradewell, M.L.3    Dion, P.A.4    Bercier, V.5
  • 16
    • 70350356317 scopus 로고    scopus 로고
    • Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching
    • Lu Y, Ferris J, Gao FB, (2009) Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching. Mol Brain 2: 30.
    • (2009) Mol Brain , vol.2 , pp. 30
    • Lu, Y.1    Ferris, J.2    Gao, F.B.3
  • 17
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I, Bell S, Cairns NJ, Miller TM, Baloh RH, (2009) TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci U S A 106: 18809–18814.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 19
    • 77950421249 scopus 로고    scopus 로고
    • transgenic rat model of neurodegeneration caused by mutation in the TDP gene
    • Zhou H, Huang C, Chen H, Wang D, Landel CP, et al. (2010) transgenic rat model of neurodegeneration caused by mutation in the TDP gene. PLoS Genet 6: e1000887.
    • (2010) PLoS Genet , vol.6 , pp. 1000887
    • Zhou, H.1    Huang, C.2    Chen, H.3    Wang, D.4    Landel, C.P.5
  • 20
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM, Trojanowski JQ, (2012) Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 13: 38–50.
    • (2012) Nat Rev Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 21
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, et al. (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64: 60–70.
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3    Kametani, F.4    Yoshida, M.5
  • 22
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann M, Kwong LK, Lee EB, Kremmer E, Flatley A, et al. (2009) Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol 117: 137–149.
    • (2009) Acta Neuropathol , vol.117 , pp. 137-149
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3    Kremmer, E.4    Flatley, A.5
  • 23
    • 84883297079 scopus 로고    scopus 로고
    • CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration
    • Liachko NF, McMillan PJ, Guthrie CR, Bird TD, Leverenz JB, et al. (2013) CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration. Ann Neurol 74: 39–52.
    • (2013) Ann Neurol , vol.74 , pp. 39-52
    • Liachko, N.F.1    McMillan, P.J.2    Guthrie, C.R.3    Bird, T.D.4    Leverenz, J.B.5
  • 24
    • 84897437573 scopus 로고    scopus 로고
    • Protein Kinase CK-1 Inhibitors As New Potential Drugs for Amyotrophic Lateral Sclerosis
    • Salado IG, Redondo M, Bello ML, Perez C, Liachko NF, et al. (2014) Protein Kinase CK-1 Inhibitors As New Potential Drugs for Amyotrophic Lateral Sclerosis. J Med Chem 57: 2755–2772.
    • (2014) J Med Chem , vol.57 , pp. 2755-2772
    • Salado, I.G.1    Redondo, M.2    Bello, M.L.3    Perez, C.4    Liachko, N.F.5
  • 25
    • 38549135536 scopus 로고    scopus 로고
    • Genomic overview of protein kinases
    • Manning G, (2005) Genomic overview of protein kinases. WormBook 1–19.
    • (2005) WormBook , pp. 1-19
    • Manning, G.1
  • 27
    • 48249102000 scopus 로고    scopus 로고
    • Phylogeny.fr: robust phylogenetic analysis for the non-specialist
    • Dereeper A, Guignon V, Blanc G, Audic S, Buffet S, et al. (2008) Phylogeny.fr: robust phylogenetic analysis for the non-specialist. Nucleic Acids Res 36: W465–469.
    • (2008) Nucleic Acids Res , vol.36 , pp. W465-469
    • Dereeper, A.1    Guignon, V.2    Blanc, G.3    Audic, S.4    Buffet, S.5
  • 29
    • 64049100454 scopus 로고    scopus 로고
    • Protein kinase D is an essential regulator of C. elegans innate immunity
    • Ren M, Feng H, Fu Y, Land M, Rubin CS, (2009) Protein kinase D is an essential regulator of C. elegans innate immunity. Immunity 30: 521–532.
    • (2009) Immunity , vol.30 , pp. 521-532
    • Ren, M.1    Feng, H.2    Fu, Y.3    Land, M.4    Rubin, C.S.5
  • 30
    • 79961026124 scopus 로고    scopus 로고
    • Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology
    • Fu Y, Rubin CS, (2011) Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology. EMBO Rep 12: 785–796.
    • (2011) EMBO Rep , vol.12 , pp. 785-796
    • Fu, Y.1    Rubin, C.S.2
  • 31
    • 33746879943 scopus 로고    scopus 로고
    • Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation
    • Sato S, Cerny RL, Buescher JL, Ikezu T, (2006) Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. J Neurochem 98: 1573–1584.
    • (2006) J Neurochem , vol.98 , pp. 1573-1584
    • Sato, S.1    Cerny, R.L.2    Buescher, J.L.3    Ikezu, T.4
  • 32
    • 0025074778 scopus 로고
    • Phosphate groups as substrate determinants for casein kinase I action
    • Flotow H, Graves PR, Wang AQ, Fiol CJ, Roeske RW, et al. (1990) Phosphate groups as substrate determinants for casein kinase I action. J Biol Chem 265: 14264–14269.
    • (1990) J Biol Chem , vol.265 , pp. 14264-14269
    • Flotow, H.1    Graves, P.R.2    Wang, A.Q.3    Fiol, C.J.4    Roeske, R.W.5
  • 33
    • 78649637949 scopus 로고    scopus 로고
    • Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity
    • Streets AJ, Needham AJ, Gill SK, Ong AC, (2010) Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity. Mol Biol Cell 21: 3853–3865.
    • (2010) Mol Biol Cell , vol.21 , pp. 3853-3865
    • Streets, A.J.1    Needham, A.J.2    Gill, S.K.3    Ong, A.C.4
  • 34
    • 0242712991 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases
    • Sturany S, Van Lint J, Muller F, Wilda M, Hameister H, et al. (2001) Molecular cloning and characterization of the human protein kinase D2. A novel member of the protein kinase D family of serine threonine kinases. J Biol Chem 276: 3310–3318.
    • (2001) J Biol Chem , vol.276 , pp. 3310-3318
    • Sturany, S.1    Van Lint, J.2    Muller, F.3    Wilda, M.4    Hameister, H.5
  • 36
    • 84856574050 scopus 로고    scopus 로고
    • Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies
    • Iguchi Y, Katsuno M, Takagi S, Ishigaki S, Niwa J, et al. (2012) Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies. Neurobiol Dis 45: 862–870.
    • (2012) Neurobiol Dis , vol.45 , pp. 862-870
    • Iguchi, Y.1    Katsuno, M.2    Takagi, S.3    Ishigaki, S.4    Niwa, J.5
  • 37
    • 12244297111 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and death in motor neurons exposed to the glutathione-depleting agent ethacrynic acid
    • Rizzardini M, Lupi M, Bernasconi S, Mangolini A, Cantoni L, (2003) Mitochondrial dysfunction and death in motor neurons exposed to the glutathione-depleting agent ethacrynic acid. J Neurol Sci 207: 51–58.
    • (2003) J Neurol Sci , vol.207 , pp. 51-58
    • Rizzardini, M.1    Lupi, M.2    Bernasconi, S.3    Mangolini, A.4    Cantoni, L.5
  • 39
    • 0035896451 scopus 로고    scopus 로고
    • Tau-tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found in paired helical filament-tau
    • Tomizawa K, Omori A, Ohtake A, Sato K, Takahashi M, (2001) Tau-tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found in paired helical filament-tau. Febs Letters 492: 221–227.
    • (2001) Febs Letters , vol.492 , pp. 221-227
    • Tomizawa, K.1    Omori, A.2    Ohtake, A.3    Sato, K.4    Takahashi, M.5
  • 41
    • 48749088629 scopus 로고    scopus 로고
    • Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
    • Inukai Y, Nonaka T, Arai T, Yoshida M, Hashizume Y, et al. (2008) Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett 582: 2899–2904.
    • (2008) FEBS Lett , vol.582 , pp. 2899-2904
    • Inukai, Y.1    Nonaka, T.2    Arai, T.3    Yoshida, M.4    Hashizume, Y.5
  • 44
    • 84893012138 scopus 로고    scopus 로고
    • TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo
    • Choksi DK, Roy B, Chatterjee S, Yusuff T, Bakhoum MF, et al. (2014) TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo. Hum Mol Genet 23: 1025–1035.
    • (2014) Hum Mol Genet , vol.23 , pp. 1025-1035
    • Choksi, D.K.1    Roy, B.2    Chatterjee, S.3    Yusuff, T.4    Bakhoum, M.F.5
  • 45
    • 84897052708 scopus 로고    scopus 로고
    • Casein Kinase II Induced Polymerization of Soluble TDP-43 into Filaments Is Inhibited by Heat Shock Proteins
    • Carlomagno Y, Zhang Y, Davis M, Lin WL, Cook C, et al. (2014) Casein Kinase II Induced Polymerization of Soluble TDP-43 into Filaments Is Inhibited by Heat Shock Proteins. PLoS One 9: e90452.
    • (2014) PLoS One , vol.9 , pp. 90452
    • Carlomagno, Y.1    Zhang, Y.2    Davis, M.3    Lin, W.L.4    Cook, C.5
  • 46
    • 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 DP, Betts JC, Loviny TLF, Blackstock WP, Anderton BH, (1998) New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. Journal of Neurochemistry 71: 2465–2476.
    • (1998) Journal of Neurochemistry , vol.71 , pp. 2465-2476
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.F.3    Blackstock, W.P.4    Anderton, B.H.5
  • 47
    • 44649137415 scopus 로고    scopus 로고
    • Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies
    • Uryu K, Nakashima-Yasuda H, Forman MS, Kwong LK, Clark CM, et al. (2008) Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies. J Neuropathol Exp Neurol 67: 555–564.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 555-564
    • Uryu, K.1    Nakashima-Yasuda, H.2    Forman, M.S.3    Kwong, L.K.4    Clark, C.M.5
  • 48
    • 77953870659 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 pathology and hippocampal sclerosis in progressive supranuclear palsy
    • Yokota O, Davidson Y, Bigio EH, Ishizu H, Terada S, et al. (2010) Phosphorylated TDP-43 pathology and hippocampal sclerosis in progressive supranuclear palsy. Acta Neuropathol 120: 55–66.
    • (2010) Acta Neuropathol , vol.120 , pp. 55-66
    • Yokota, O.1    Davidson, Y.2    Bigio, E.H.3    Ishizu, H.4    Terada, S.5
  • 49
    • 79960835044 scopus 로고    scopus 로고
    • Neuropathological background of phenotypical variability in frontotemporal dementia
    • Josephs KA, Hodges JR, Snowden JS, Mackenzie IR, Neumann M, et al. (2011) Neuropathological background of phenotypical variability in frontotemporal dementia. Acta Neuropathol 122: 137–153.
    • (2011) Acta Neuropathol , vol.122 , pp. 137-153
    • Josephs, K.A.1    Hodges, J.R.2    Snowden, J.S.3    Mackenzie, I.R.4    Neumann, M.5
  • 51
    • 79951514142 scopus 로고    scopus 로고
    • Tau-tubulin kinase-1 gene variants are associated with Alzheimer's disease in Han Chinese
    • Yu NN, Yu JT, Xiao JT, Zhang HW, Lu RC, et al. (2011) Tau-tubulin kinase-1 gene variants are associated with Alzheimer's disease in Han Chinese. Neurosci Lett 491: 83–86.
    • (2011) Neurosci Lett , vol.491 , pp. 83-86
    • Yu, N.N.1    Yu, J.T.2    Xiao, J.T.3    Zhang, H.W.4    Lu, R.C.5
  • 52
    • 84879198442 scopus 로고    scopus 로고
    • Tau-tubulin kinase 1 expression, phosphorylation and co-localization with phospho-Ser422 tau in the Alzheimer's disease brain
    • Lund H, Cowburn RF, Gustafsson E, Stromberg K, Svensson A, et al. (2013) Tau-tubulin kinase 1 expression, phosphorylation and co-localization with phospho-Ser422 tau in the Alzheimer's disease brain. Brain Pathol 23: 378–389.
    • (2013) Brain Pathol , vol.23 , pp. 378-389
    • Lund, H.1    Cowburn, R.F.2    Gustafsson, E.3    Stromberg, K.4    Svensson, A.5
  • 53
    • 58149379158 scopus 로고    scopus 로고
    • Spatial learning impairment, enhanced CDK5/p35 activity, and downregulation of NMDA receptor expression in transgenic mice expressing tau-tubulin kinase 1
    • Sato S, Xu J, Okuyama S, Martinez LB, Walsh SM, et al. (2008) Spatial learning impairment, enhanced CDK5/p35 activity, and downregulation of NMDA receptor expression in transgenic mice expressing tau-tubulin kinase 1. J Neurosci 28: 14511–14521.
    • (2008) J Neurosci , vol.28 , pp. 14511-14521
    • Sato, S.1    Xu, J.2    Okuyama, S.3    Martinez, L.B.4    Walsh, S.M.5
  • 54
    • 77955780870 scopus 로고    scopus 로고
    • Tau-tubulin kinase 1 enhances prefibrillar tau aggregation and motor neuron degeneration in P301L FTDP-17 tau-mutant mice
    • Xu J, Sato S, Okuyama S, Swan RJ, Jacobsen MT, et al. (2010) Tau-tubulin kinase 1 enhances prefibrillar tau aggregation and motor neuron degeneration in P301L FTDP-17 tau-mutant mice. FASEB J 24: 2904–2915.
    • (2010) FASEB J , vol.24 , pp. 2904-2915
    • Xu, J.1    Sato, S.2    Okuyama, S.3    Swan, R.J.4    Jacobsen, M.T.5
  • 55
    • 36549023424 scopus 로고    scopus 로고
    • Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11
    • Houlden H, Johnson J, Gardner-Thorpe C, Lashley T, Hernandez D, et al. (2007) Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11. Nat Genet 39: 1434–1436.
    • (2007) Nat Genet , vol.39 , pp. 1434-1436
    • Houlden, H.1    Johnson, J.2    Gardner-Thorpe, C.3    Lashley, T.4    Hernandez, D.5
  • 56
    • 79958826704 scopus 로고    scopus 로고
    • TTBK2 kinase substrate specificity and the impact of spinocerebellar-ataxia-causing mutations on expression, activity, localization and development
    • Bouskila M, Esoof N, Gay L, Fang EH, Deak M, et al. (2011) TTBK2 kinase substrate specificity and the impact of spinocerebellar-ataxia-causing mutations on expression, activity, localization and development. Biochem J 437: 157–167.
    • (2011) Biochem J , vol.437 , pp. 157-167
    • Bouskila, M.1    Esoof, N.2    Gay, L.3    Fang, E.H.4    Deak, M.5
  • 57
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S, (1974) The genetics of Caenorhabditis elegans. Genetics 77: 71–94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 58
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms
    • Plowman GD, Sudarsanam S, Bingham J, Whyte D, Hunter T, (1999) The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms. Proc Natl Acad Sci U S A 96: 13603–13610.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13603-13610
    • Plowman, G.D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 59
    • 23144462374 scopus 로고    scopus 로고
    • Somatic misexpression of germline P granules and enhanced RNA interference in retinoblastoma pathway mutants
    • Wang D, Kennedy S, Conte D, Kim JK, Gabel HW, et al. (2005) Somatic misexpression of germline P granules and enhanced RNA interference in retinoblastoma pathway mutants. Nature 436: 593–597.
    • (2005) Nature , vol.436 , pp. 593-597
    • Wang, D.1    Kennedy, S.2    Conte, D.3    Kim, J.K.4    Gabel, H.W.5
  • 60
    • 34548389257 scopus 로고    scopus 로고
    • SUT-1 enables tau-induced neurotoxicity in C. elegans
    • Kraemer BC, Schellenberg GD, (2007) SUT-1 enables tau-induced neurotoxicity in C. elegans. Hum Mol Genet 16: 1959–1971.
    • (2007) Hum Mol Genet , vol.16 , pp. 1959-1971
    • Kraemer, B.C.1    Schellenberg, G.D.2
  • 61
    • 65449156394 scopus 로고    scopus 로고
    • SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans
    • Guthrie CR, Schellenberg GD, Kraemer BC, (2009) SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans. Hum Mol Genet 18: 1825–1838.
    • (2009) Hum Mol Genet , vol.18 , pp. 1825-1838
    • Guthrie, C.R.1    Schellenberg, G.D.2    Kraemer, B.C.3
  • 62
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, et al. (2005) TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 280: 37572–37584.
    • (2005) J Biol Chem , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5
  • 63
    • 84869069719 scopus 로고    scopus 로고
    • The spinocerebellar ataxia-associated gene Tau tubulin kinase 2 controls the initiation of ciliogenesis
    • Goetz SC, Liem KF, Anderson KV, (2012) The spinocerebellar ataxia-associated gene Tau tubulin kinase 2 controls the initiation of ciliogenesis. Cell 151: 847–858.
    • (2012) Cell , vol.151 , pp. 847-858
    • Goetz, S.C.1    Liem, K.F.2    Anderson, K.V.3
  • 64
    • 77956918736 scopus 로고    scopus 로고
    • Sudan Black B treatment reduces autofluorescence and improves resolution of in situ hybridization specific fluorescent signals of brain sections
    • Oliveira VC, Carrara RC, Simoes DL, Saggioro FP, Carlotti CG, et al. (2010) Sudan Black B treatment reduces autofluorescence and improves resolution of in situ hybridization specific fluorescent signals of brain sections. Histol Histopathol 25: 1017–1024.
    • (2010) Histol Histopathol , vol.25 , pp. 1017-1024
    • Oliveira, V.C.1    Carrara, R.C.2    Simoes, D.L.3    Saggioro, F.P.4    Carlotti, C.G.5


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