메뉴 건너뛰기




Volumn 17, Issue 1, 2016, Pages 5-21

Tau in physiology and pathology

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; COFILIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; MICRORNA 132; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 1; TAU PROTEIN; TIDEGLUSIB;

EID: 84951567833     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn.2015.1     Document Type: Review
Times cited : (1377)

References (226)
  • 2
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • First observation and naming of 'paired helical filaments' in the brains of patients with AD
    • Kidd, M. Paired helical filaments in electron microscopy of Alzheimer's disease. Nature 197, 192-193 (1963). First observation and naming of 'paired helical filaments' in the brains of patients with AD.
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 3
    • 0000293742 scopus 로고
    • Über eine eigenartige Erkrankung der Hirnrinde
    • (in German
    • Alzheimer, A. Über eine eigenartige Erkrankung der Hirnrinde. Allg. Z. Psychiatrie Psychisch-gerichtl. Med. 64, 146-148 (in German) (1907).
    • (1907) Allg. Z. Psychiatrie Psychisch-gerichtl. Med , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 5
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5?-splice-site mutations in tau with the inherited dementia ftdp-17
    • Hutton, M. et al. Association of missense and 5?-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393, 702-705 (1998).
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1
  • 6
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid ?-induced deficits in an Alzheimer's disease mouse model
    • Roberson, E. D. et al. Reducing endogenous tau ameliorates amyloid ?-induced deficits in an Alzheimer's disease mouse model. Science 316, 750-754 (2007).
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1
  • 7
    • 84904488776 scopus 로고    scopus 로고
    • Prion-like properties of tau protein: The importance of extracellular tau as a therapeutic target
    • Holmes, B. B. & Diamond, M. I. Prion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic target. J. Biol. Chem. 289, 19855-19861 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 19855-19861
    • Holmes, B.B.1    Diamond, M.I.2
  • 9
    • 84926513913 scopus 로고    scopus 로고
    • Spreading of pathology in neurodegenerative diseases: A focus on human studies
    • Brettschneider, J., Del Tredici, K., Lee, V. M. & Trojanowski, J. Q. Spreading of pathology in neurodegenerative diseases: a focus on human studies. Nat. Rev. Neurosci. 16, 109-120 (2015).
    • (2015) Nat. Rev. Neurosci , vol.16 , pp. 109-120
    • Brettschneider, J.1    Del Tredici, K.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 10
    • 39049193314 scopus 로고    scopus 로고
    • Misregulation of tau alternative splicing in neurodegeneration and dementia
    • Andreadis, A. Misregulation of tau alternative splicing in neurodegeneration and dementia. Prog. Mol. Subcell. Biol. 44, 89-107 (2006).
    • (2006) Prog. Mol. Subcell. Biol , vol.44 , pp. 89-107
    • Andreadis, A.1
  • 11
    • 0028853922 scopus 로고
    • Functional implications for the microtubule-Associated protein tau: Localization in oligodendrocytes
    • LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P. & Binder, L. I. Functional implications for the microtubule-Associated protein tau: localization in oligodendrocytes. Proc. Natl Acad. Sci. USA 92, 10369-10373 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10369-10373
    • LoPresti, P.1    Szuchet, S.2    Papasozomenos, S.C.3    Zinkowski, R.P.4    Binder, L.I.5
  • 12
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee, G., Cowan, N. & Kirschner, M. The primary structure and heterogeneity of tau protein from mouse brain. Science 239, 285-288 (1988).
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 13
    • 80855138704 scopus 로고    scopus 로고
    • Neuropathology of frontotemporal lobar degeneration-tau (ftld-tau
    • Dickson, D. W., Kouri, N., Murray, M. E. & Josephs, K. A. Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau). J. Mol. Neurosci. 45, 384-389 (2011).
    • (2011) J. Mol. Neurosci , vol.45 , pp. 384-389
    • Dickson, D.W.1    Kouri, N.2    Murray, M.E.3    Josephs, K.A.4
  • 14
    • 84864868840 scopus 로고    scopus 로고
    • Loss of fused in sarcoma (fus) promotes pathological tau splicing
    • Orozco, D. et al. Loss of fused in sarcoma (FUS) promotes pathological Tau splicing. EMBO Rep. 13, 759-764 (2012).
    • (2012) EMBO Rep , vol.13 , pp. 759-764
    • Orozco, D.1
  • 15
    • 80053167649 scopus 로고    scopus 로고
    • Microrna-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy
    • Smith, P. Y. et al. MicroRNA-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy. Hum. Mol. Genet. 20, 4016-4024 (2011).
    • (2011) Hum. Mol. Genet , vol.20 , pp. 4016-4024
    • Smith, P.Y.1
  • 16
    • 84922195168 scopus 로고    scopus 로고
    • Dysregulation of microrna-219 promotes neurodegeneration through post-transcriptional regulation of tau
    • Santa-Maria, I. et al. Dysregulation of microRNA-219 promotes neurodegeneration through post-transcriptional regulation of tau. J. Clin. Invest. 125, 681-686 (2015).
    • (2015) J. Clin. Invest , vol.125 , pp. 681-686
    • Santa-Maria, I.1
  • 17
    • 84902440206 scopus 로고    scopus 로고
    • RNA protein granules modulate tau isoform expression and induce neuronal sprouting
    • Moschner, K. et al. RNA protein granules modulate tau isoform expression and induce neuronal sprouting. J. Biol. Chem. 289, 16814-16825 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 16814-16825
    • Moschner, K.1
  • 18
    • 84913553259 scopus 로고    scopus 로고
    • Mitochondrial complex 1 inhibition increases 4-repeat isoform tau by srsf2 upregulation
    • Bruch, J., Xu, H., De Andrade, A. & Hoglinger, G. Mitochondrial complex 1 inhibition increases 4-repeat isoform tau by SRSF2 upregulation. PLoS ONE 9, e113070 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e113070
    • Bruch, J.1    Xu, H.2    De Andrade, A.3    Hoglinger, G.4
  • 19
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-Associated protein tau into Alzheimer-like paired helical filaments
    • Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E. M. & Mandelkow, E. RNA stimulates aggregation of microtubule-Associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett. 399, 344-349 (1996).
    • (1996) FEBS Lett , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 20
    • 84896919828 scopus 로고    scopus 로고
    • A major role for tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions
    • Violet, M. et al. A major role for Tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions. Front. Cell Neurosci. 8, 84 (2014).
    • (2014) Front. Cell Neurosci , vol.8 , pp. 84
    • Violet, M.1
  • 21
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert, M. & Jakes, R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 9, 4225-4230 (1990).
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 22
    • 0026729767 scopus 로고
    • Projection domains of map2 and tau determine spacings between microtubules in dendrites and axons
    • Chen, J., Kanai, Y., Cowan, N. J. & Hirokawa, N. Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 360, 674-677 (1992).
    • (1992) Nature , vol.360 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 23
    • 0028143749 scopus 로고
    • Regulation of microtubule-microtubule spacing and bundling
    • Frappier, T. F., Georgieff, I. S., Brown, K. & Shelanski, M. L. ? regulation of microtubule-microtubule spacing and bundling. J. Neurochem. 63, 2288-2294 (1994).
    • (1994) J. Neurochem , vol.63 , pp. 2288-2294
    • Frappier, T.F.1    Georgieff, I.S.2    Brown, K.3    Shelanski, M.L.4
  • 24
    • 84893529375 scopus 로고    scopus 로고
    • Profiling murine tau with 0n, 1n and 2n isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1n isoform being enriched in the nucleus
    • Liu, C. & Gotz, J. Profiling murine tau with 0N, 1N and 2N isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1N isoform being enriched in the nucleus. PLoS ONE 8, e84849 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e84849
    • Liu, C.1    Gotz, J.2
  • 25
    • 84862027756 scopus 로고    scopus 로고
    • Tau isoform composition influences rate and extent of filament formation
    • Zhong, Q., Congdon, E. E., Nagaraja, H. N. & Kuret, J. Tau isoform composition influences rate and extent of filament formation. J. Biol. Chem. 287, 20711-20719 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 20711-20719
    • Zhong, Q.1    Congdon, E.E.2    Nagaraja, H.N.3    Kuret, J.4
  • 26
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik, K. S., Orecchio, L. D., Bakalis, S. & Neve, R. L. Developmentally regulated expression of specific tau sequences. Neuron 2, 1389-1397 (1989).
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3    Neve, R.L.4
  • 27
    • 0038292060 scopus 로고    scopus 로고
    • Isoforms changes of tau protein during development in various species
    • Takuma, H., Arawaka, S. & Mori, H. Isoforms changes of tau protein during development in various species. Brain Res. Dev. Brain Res. 142, 121-127 (2003).
    • (2003) Brain Res. Dev. Brain Res , vol.142 , pp. 121-127
    • Takuma, H.1    Arawaka, S.2    Mori, H.3
  • 28
    • 84860177836 scopus 로고    scopus 로고
    • Tau isoform with three microtubule binding domains is a marker of new axons generated from the subgranular zone in the hippocampal dentate gyrus: Implications for Alzheimer's disease
    • Llorens-Martin, M. et al. Tau isoform with three microtubule binding domains is a marker of new axons generated from the subgranular zone in the hippocampal dentate gyrus: implications for Alzheimer's disease. J. Alzheimers Dis. 29, 921-930 (2012).
    • (2012) J. Alzheimers Dis , vol.29 , pp. 921-930
    • Llorens-Martin, M.1
  • 29
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cdna encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-Associated protein tau
    • Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E. & Klug, A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-Associated protein tau. Proc. Natl Acad. Sci. USA 85, 4051-4055 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 30
    • 73549106818 scopus 로고    scopus 로고
    • Overexpression of wild-type murine tau results in progressive tauopathy and neurodegeneration
    • Adams, S. J. et al. Overexpression of wild-type murine tau results in progressive tauopathy and neurodegeneration. Am. J. Pathol. 175, 1598-1609 (2009).
    • (2009) Am. J. Pathol , vol.175 , pp. 1598-1609
    • Adams, S.J.1
  • 31
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee, G., Newman, S. T., Gard, D. L., Band, H. & Panchamoorthy, G. Tau interacts with src-family non-receptor tyrosine kinases. J. Cell Sci. 111, 3167-3177 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 32
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-? Toxicity in Alzheimer's disease mouse models
    • Ittner, L. M. et al. Dendritic function of tau mediates amyloid-? toxicity in Alzheimer's disease mouse models. Cell 142, 387-397 (2010).
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1
  • 33
    • 0022257253 scopus 로고
    • Mise en evidence immunologique de la proteine tau au nivea u des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer
    • (in French
    • Brion, J. P., Passareiro, H., Nunez, J. & Flament-Durand, J. Mise en evidence immunologique de la proteine tau au nivea u des lesions de degenerescence neurofibrillaire de la maladie d'Alzheimer. Arch. Biol. (Bruxelles) 95, 229-235 (in French) (1985).
    • (1985) Arch. Biol. (Bruxelles , vol.95 , pp. 229-235
    • Brion, J.P.1    Passareiro, H.2    Nunez, J.3    Flament-Durand, J.4
  • 34
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-Associated protein ?tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal, I. et al. Abnormal phosphorylation of the microtubule-Associated protein ? (tau) in Alzheimer cytoskeletal pathology. Proc. Natl Acad. Sci. USA 83, 4913-4917 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1
  • 35
    • 61349120815 scopus 로고    scopus 로고
    • Structural polymorphism of 441-residue tau at single residue resolution
    • Mukrasch, M. D. et al. Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol. 7, e34 (2009).
    • (2009) PLoS Biol , vol.7 , pp. e34
    • Mukrasch, M.D.1
  • 36
    • 84935895529 scopus 로고    scopus 로고
    • Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
    • Kadavath, H. et al. Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proc. Natl Acad. Sci. USA 112, 7501-7506 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 7501-7506
    • Kadavath, H.1
  • 37
    • 84905976762 scopus 로고    scopus 로고
    • Alternative conformations of the Tau repeat domain in complex with an engineered binding protein
    • Gruning, C. S. et al. Alternative conformations of the Tau repeat domain in complex with an engineered binding protein. J. Biol. Chem. 289, 23209-23218 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 23209-23218
    • Gruning, C.S.1
  • 39
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • Wischik, C. M. et al. Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc. Natl Acad. Sci. USA 85, 4506-4510 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4506-4510
    • Wischik, C.M.1
  • 40
    • 84875279731 scopus 로고    scopus 로고
    • The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
    • Wegmann, S., Medalsy, I. D., Mandelkow, E. & Muller, D. J. The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush. Proc. Natl Acad. Sci. USA 110, E313-E321 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E313-E321
    • Wegmann, S.1    Medalsy, I.D.2    Mandelkow, E.3    Muller, D.J.4
  • 41
    • 0026711059 scopus 로고
    • Fetal-type phosphorylation of the tau in paired helical filaments
    • Kanemaru, K., Takio, K., Miura, R., Titani, K. & Ihara, Y. Fetal-type phosphorylation of the tau in paired helical filaments. J. Neurochem. 58, 1667-1675 (1992).
    • (1992) J. Neurochem , vol.58 , pp. 1667-1675
    • Kanemaru, K.1    Takio, K.2    Miura, R.3    Titani, K.4    Ihara, Y.5
  • 42
    • 0027361281 scopus 로고
    • Microtubule-Associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • K?pke, E. et al. Microtubule-Associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24374-24384 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 24374-24384
    • Kpke, E.1
  • 43
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo, E. S. et al. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002 (1994).
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1
  • 44
    • 84938421302 scopus 로고    scopus 로고
    • Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice
    • Morris, M. et al. Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice. Nat. Neurosci. 18, 1183-1189 (2015).
    • (2015) Nat. Neurosci , vol.18 , pp. 1183-1189
    • Morris, M.1
  • 45
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H. & Noble, W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119 (2009).
    • (2009) Trends Mol. Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 46
    • 84922823517 scopus 로고    scopus 로고
    • Tau monoclonal antibody generation based on humanized yeast models: Impact on tau oligomerization and diagnostics
    • Rosseels, J. et al. Tau monoclonal antibody generation based on humanized yeast models: impact on Tau oligomerization and diagnostics. J. Biol. Chem. 290, 4059-4074 (2015).
    • (2015) J. Biol. Chem , vol.290 , pp. 4059-4074
    • Rosseels, J.1
  • 47
    • 23744482703 scopus 로고    scopus 로고
    • Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates
    • Vega, I. E. et al. Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res. Mol. Brain Res. 138, 135-144 (2005).
    • (2005) Brain Res. Mol. Brain Res , vol.138 , pp. 135-144
    • Vega, I.E.1
  • 48
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C. X., Singh, T. J., Grundke-Iqbal, I. & Iqbal, K. Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 61, 921-927 (1993).
    • (1993) J. Neurochem , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 49
    • 44849144122 scopus 로고    scopus 로고
    • Ipp2a1 affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2a
    • Chen, S., Li, B., Grundke-Iqbal, I. & Iqbal, K. IPP2A1 affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2A. J. Biol. Chem. 283, 10513-10521 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 10513-10521
    • Chen, S.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 50
    • 5644293035 scopus 로고    scopus 로고
    • Downregulation of protein phosphatase 2a carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis
    • Sontag, E. et al. Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J. Neuropathol. Exp. Neurol. 63, 1080-1091 (2004).
    • (2004) J. Neuropathol. Exp. Neurol , vol.63 , pp. 1080-1091
    • Sontag, E.1
  • 51
    • 12144289492 scopus 로고    scopus 로고
    • Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: Implications for Alzheimer's disease
    • Planel, E. et al. Alterations in glucose metabolism induce hypothermia leading to tau hyperphosphorylation through differential inhibition of kinase and phosphatase activities: implications for Alzheimer's disease. J. Neurosci. 24, 2401-2411 (2004).
    • (2004) J. Neurosci , vol.24 , pp. 2401-2411
    • Planel, E.1
  • 52
    • 0042125603 scopus 로고    scopus 로고
    • Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals
    • Arendt, T. et al. Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals. J. Neurosci. 23, 6972-6981 (2003).
    • (2003) J. Neurosci , vol.23 , pp. 6972-6981
    • Arendt, T.1
  • 53
    • 33947536100 scopus 로고    scopus 로고
    • Anesthesia leads to tau hyperphosphorylation through inhibition of phosphatase activity by hypothermia
    • Planel, E. et al. Anesthesia leads to tau hyperphosphorylation through inhibition of phosphatase activity by hypothermia. J. Neurosci. 27, 3090-3097 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 3090-3097
    • Planel, E.1
  • 54
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase pin1 restores the function of Alzheimer-Associated phosphorylated tau protein
    • Lu, P. J., Wulf, G., Zhou, X. Z., Davies, P. & Lu, K. P. The prolyl isomerase Pin1 restores the function of Alzheimer-Associated phosphorylated tau protein. Nature 399, 784-788 (1999).
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 55
    • 84937849044 scopus 로고    scopus 로고
    • Antibody against early driver of neurodegeneration cis p-tau blocks brain injury and tauopathy
    • Kondo, A. et al. Antibody against early driver of neurodegeneration cis P-tau blocks brain injury and tauopathy. Nature 523, 431-436 (2015).
    • (2015) Nature , vol.523 , pp. 431-436
    • Kondo, A.1
  • 56
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover, B. R. et al. Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 68, 1067-1081 (2010).
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1
  • 57
    • 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. & Mandelkow, E. M. 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).
    • (2007) J. Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 58
    • 77956587739 scopus 로고    scopus 로고
    • A? Oligomers cause localized ca2+ elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines
    • Zempel, H., Thies, E., Mandelkow, E. & Mandelkow, E. M. A? oligomers cause localized Ca2+ elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J. Neurosci. 30, 11938-11950 (2010).
    • (2010) J. Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 59
    • 33646080573 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: In vitro evidence and implications for tangle formation in vivo
    • Guillozet-Bongaarts, A. L. et al. Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J. Neurochem. 97, 1005-1014 (2006).
    • (2006) J. Neurochem , vol.97 , pp. 1005-1014
    • Guillozet-Bongaarts, A.L.1
  • 60
    • 33847369469 scopus 로고    scopus 로고
    • The high-Affinity hsp90-chip complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey, C. A. et al. The high-Affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J. Clin. Invest. 117, 648-658 (2007).
    • (2007) J. Clin. Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1
  • 61
    • 68949105821 scopus 로고    scopus 로고
    • Phosphorylated tau interacts with c-jun n-terminal kinase-interacting protein 1 (jip1) in Alzheimer disease
    • Ittner, L. M., Ke, Y. D. & Gotz, J. Phosphorylated Tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease. J. Biol. Chem. 284, 20909-20916 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 20909-20916
    • Ittner, L.M.1    Ke, Y.D.2    Gotz, J.3
  • 62
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between fyn and tau
    • Bhaskar, K., Yen, S. H. & Lee, G. Disease-related modifications in tau affect the interaction between Fyn and Tau. J. Biol. Chem. 280, 35119-35125 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 63
    • 49649119504 scopus 로고    scopus 로고
    • Phosphorylation regulates tau interactions with src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase c?1, grb2, and src family kinases
    • Reynolds, C. H. et al. Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase C?1, Grb2, and Src family kinases. J. Biol. Chem. 283, 18177-18186 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 18177-18186
    • Reynolds, C.H.1
  • 64
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min, S. W. et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67, 953-966 (2010).
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1
  • 65
    • 84890357149 scopus 로고    scopus 로고
    • Acetylation of the kxgs motifs in tau is a critical determinant in modulation of tau aggregation and clearance
    • Cook, C. et al. Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance. Hum. Mol. Genet. 23, 104-116 (2014).
    • (2014) Hum. Mol. Genet , vol.23 , pp. 104-116
    • Cook, C.1
  • 66
  • 67
    • 84880638106 scopus 로고    scopus 로고
    • Acetylated tau neuropathology in sporadic and hereditary tauopathies
    • Irwin, D. J. et al. Acetylated tau neuropathology in sporadic and hereditary tauopathies. Am. J. Pathol. 183, 344-351 (2013).
    • (2013) Am. J. Pathol , vol.183 , pp. 344-351
    • Irwin, D.J.1
  • 68
    • 84943637753 scopus 로고    scopus 로고
    • Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
    • Min, S. W. et al. Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits. Nat. Med. 21, 1154-1162 (2015).
    • (2015) Nat. Med , vol.21 , pp. 1154-1162
    • Min, S.W.1
  • 69
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimer's disease
    • Martin, L., Latypova, X. & Terro, F. Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem. Int. 58, 458-471 (2011).
    • (2011) Neurochem. Int , vol.58 , pp. 458-471
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 70
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule-Associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
    • Wang, J. Z., Grundke-Iqbal, I. & Iqbal, K. Glycosylation of microtubule-Associated protein tau: an abnormal posttranslational modification in Alzheimer's disease. Nat. Med. 2, 871-875 (1996).
    • (1996) Nat. Med , vol.2 , pp. 871-875
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 71
    • 0037049240 scopus 로고    scopus 로고
    • Aberrant glycosylation modulates phosphorylation of tau by protein kinase a and dephosphorylation of tau by protein phosphatase 2a and
    • Liu, F., Zaidi, T., Iqbal, K., Grundke-Iqbal, I. & Gong, C. X. Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and Neuroscience 115, 829-837 (2002).
    • (2002) Neuroscience , vol.115 , pp. 829-837
    • Liu, F.1    Zaidi, T.2    Iqbal, K.3    Grundke-Iqbal, I.4    Gong, C.X.5
  • 72
    • 3242739968 scopus 로고    scopus 로고
    • O-glcnacylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W. & Gong, C. X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc. Natl Acad. Sci. USA 101, 10804-10809 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 73
    • 84897117088 scopus 로고    scopus 로고
    • O-glcnac modification of tau directly inhibits its aggregation without perturbing the conformational properties of tau monomers
    • Yuzwa, S. A., Cheung, A. H., Okon, M., McIntosh, L. P. & Vocadlo, D. J. O-GlcNAc modification of tau directly inhibits its aggregation without perturbing the conformational properties of tau monomers. J. Mol. Biol. 426, 1736-1752 (2014).
    • (2014) J. Mol. Biol , vol.426 , pp. 1736-1752
    • Yuzwa, S.A.1    Cheung, A.H.2    Okon, M.3    McIntosh, L.P.4    Vocadlo, D.J.5
  • 74
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid ?-peptide
    • Yan, S. D. et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid ?-peptide. Nat. Med. 1, 693-699 (1995).
    • (1995) Nat. Med , vol.1 , pp. 693-699
    • Yan, S.D.1
  • 75
    • 4544300178 scopus 로고    scopus 로고
    • Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo
    • Watanabe, A. et al. Molecular aging of tau: disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. J. Neurochem. 90, 1302-1311 (2004).
    • (2004) J. Neurochem , vol.90 , pp. 1302-1311
    • Watanabe, A.1
  • 76
    • 0029133373 scopus 로고
    • Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain
    • Ledesma, M. D., Bonay, P. & Avila, J. Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain. J. Neurochem. 65, 1658-1664 (1995).
    • (1995) J. Neurochem , vol.65 , pp. 1658-1664
    • Ledesma, M.D.1    Bonay, P.2    Avila, J.3
  • 77
    • 84857034716 scopus 로고    scopus 로고
    • Selective tau tyrosine nitration in non-Ad tauopathies
    • Reyes, J. F., Geula, C., Vana, L. & Binder, L. I. Selective tau tyrosine nitration in non-AD tauopathies. Acta Neuropathol. 123, 119-132 (2012).
    • (2012) Acta Neuropathol , vol.123 , pp. 119-132
    • Reyes, J.F.1    Geula, C.2    Vana, L.3    Binder, L.I.4
  • 78
    • 84904602584 scopus 로고    scopus 로고
    • Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity
    • Funk, K. E. et al. Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity. Biochem. J. 462, 77-88 (2014).
    • (2014) Biochem. J , vol.462 , pp. 77-88
    • Funk, K.E.1
  • 79
    • 1042266624 scopus 로고    scopus 로고
    • Chip-hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura, H., Schwartz, D., Gygi, S. P. & Kosik, K. S. CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 80
    • 11144356089 scopus 로고    scopus 로고
    • Chip and hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli, L. et al. CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13, 703-714 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 703-714
    • Petrucelli, L.1
  • 81
    • 21344463770 scopus 로고    scopus 로고
    • Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
    • Babu, J. R., Geetha, T. & Wooten, M. W. Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J. Neurochem. 94, 192-203 (2005).
    • (2005) J. Neurochem , vol.94 , pp. 192-203
    • Babu, J.R.1    Geetha, T.2    Wooten, M.W.3
  • 82
    • 84875231510 scopus 로고    scopus 로고
    • Why do cellular proteins linked to k63-polyubiquitin chains not associate with proteasomes?
    • Nathan, J. A., Kim, H. T., Ting, L., Gygi, S. P. & Goldberg, A. L. Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes? EMBO J. 32, 552-565 (2013).
    • (2013) EMBO J , vol.32 , pp. 552-565
    • Nathan, J.A.1    Kim, H.T.2    Ting, L.3    Gygi, S.P.4    Goldberg, A.L.5
  • 83
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (sumo) modification of natively unfolded proteins tau and alpha-synuclein
    • Dorval, V. & Fraser, P. E. Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein. J. Biol. Chem. 281, 9919-9924 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 84
    • 0344826098 scopus 로고    scopus 로고
    • Sumo-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease
    • Pountney, D. L. et al. SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease. Exp. Neurol. 184, 436-446 (2003).
    • (2003) Exp. Neurol , vol.184 , pp. 436-446
    • Pountney, D.L.1
  • 85
    • 84915749668 scopus 로고    scopus 로고
    • Sumoylation at k340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
    • Luo, H. B. et al. SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination. Proc. Natl Acad. Sci. USA 111, 16586-16591 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 16586-16591
    • Luo, H.B.1
  • 86
    • 84930729049 scopus 로고    scopus 로고
    • Nh2-truncated human tau induces deregulated mitophagy in neurons by aberrant recruitment of parkin and uchl-1: Implications in Alzheimer's disease
    • Corsetti, V. et al. NH2-truncated human tau induces deregulated mitophagy in neurons by aberrant recruitment of Parkin and UCHL-1: implications in Alzheimer's disease. Hum. Mol. Genet. 24, 3058-3081 (2015).
    • (2015) Hum. Mol. Genet , vol.24 , pp. 3058-3081
    • Corsetti, V.1
  • 87
    • 78449296170 scopus 로고    scopus 로고
    • Cleavage of tau by calpain in Alzheimer's disease: The quest for the toxic 17 kd fragment
    • Garg, S., Timm, T., Mandelkow, E. M., Mandelkow, E. & Wang, Y. Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment. Neurobiol. Aging 32, 1-14 (2011).
    • (2011) Neurobiol. Aging , vol.32 , pp. 1-14
    • Garg, S.1    Timm, T.2    Mandelkow, E.M.3    Mandelkow, E.4    Wang, Y.5
  • 88
    • 84929353239 scopus 로고    scopus 로고
    • Role of the tau n-terminal region in microtubule stabilization revealed by new endogenous truncated forms
    • Derisbourg, M. et al. Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms. Sci. Rep. 5, 9659 (2015).
    • (2015) Sci. Rep , vol.5 , pp. 9659
    • Derisbourg, M.1
  • 89
    • 0021334090 scopus 로고
    • Studies on the expression of the microtubule-Associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes
    • Drubin, D. G., Caput, D. & Kirschner, M. W. Studies on the expression of the microtubule-Associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes. J. Cell Biol. 98, 1090-1097 (1984).
    • (1984) J. Cell Biol , vol.98 , pp. 1090-1097
    • Drubin, D.G.1    Caput, D.2    Kirschner, M.W.3
  • 90
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of tau in the central nervous system
    • Papasozomenos, S. C. & Binder, L. I. Phosphorylation determines two distinct species of Tau in the central nervous system. Cell. Motil. Cytoskeleton 8, 210-226 (1987).
    • (1987) Cell. Motil. Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 91
    • 79953003312 scopus 로고    scopus 로고
    • Nuclear tau, a key player in neuronal DNA protection
    • Sultan, A. et al. Nuclear tau, a key player in neuronal DNA protection. J. Biol. Chem. 286, 4566-4575 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 4566-4575
    • Sultan, A.1
  • 92
    • 0027195313 scopus 로고
    • Subcellular localization of tau mRNA in differentiating neuronal cell culture: Implications for neuronal polarity
    • Litman, P., Barg, J., Rindzoonski, L. & Ginzburg, I. Subcellular localization of tau mRNA in differentiating neuronal cell culture: implications for neuronal polarity. Neuron 10, 627-638 (1993).
    • (1993) Neuron , vol.10 , pp. 627-638
    • Litman, P.1    Barg, J.2    Rindzoonski, L.3    Ginzburg, I.4
  • 93
    • 0035448939 scopus 로고    scopus 로고
    • Axonal tau mRNA localization coincides with tau protein in living neuronal cells and depends on axonal targeting signal
    • Aronov, S., Aranda, G., Behar, L. & Ginzburg, I. Axonal tau mRNA localization coincides with tau protein in living neuronal cells and depends on axonal targeting signal. J. Neurosci. 21, 6577-6587 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 6577-6587
    • Aronov, S.1    Aranda, G.2    Behar, L.3    Ginzburg, I.4
  • 94
    • 70350455151 scopus 로고    scopus 로고
    • Specification of neuronal polarity regulated by local translation of crmp2 and tau via the mtor-p70s6k pathway
    • Morita, T. & Sobue, K. Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway. J. Biol. Chem. 284, 27734-27745 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 27734-27745
    • Morita, T.1    Sobue, K.2
  • 95
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubule-Associated protein 2c in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • Hirokawa, N., Funakoshi, T., Sato-Harada, R. & Kanai, Y. Selective stabilization of tau in axons and microtubule-Associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J. Cell Biol. 132, 667-679 (1996).
    • (1996) J. Cell Biol , vol.132 , pp. 667-679
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 96
    • 0024442369 scopus 로고
    • Tau in situ hybridization in normal and Alzheimer brain: Localization in the somatodendritic compartment
    • Kosik, K. S., Crandall, J. E., Mufson, E. J. & Neve, R. L. Tau in situ hybridization in normal and Alzheimer brain: localization in the somatodendritic compartment. Ann. Neurol. 26, 352-361 (1989).
    • (1989) Ann. Neurol , vol.26 , pp. 352-361
    • Kosik, K.S.1    Crandall, J.E.2    Mufson, E.J.3    Neve, R.L.4
  • 97
    • 82455208974 scopus 로고    scopus 로고
    • Novel diffusion barrier for axonal retention of tau in neurons and its failure in neurodegeneration
    • Li, X. et al. Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration. EMBO J. 30, 4825-4837 (2011).
    • (2011) EMBO J , vol.30 , pp. 4825-4837
    • Li, X.1
  • 98
    • 10944256690 scopus 로고    scopus 로고
    • Inability of tau to properly regulate neuronal microtubule dynamics: A loss-of-function mechanism by which tau might mediate neuronal cell death
    • Feinstein, S. C. & Wilson, L. Inability of tau to properly regulate neuronal microtubule dynamics: a loss-of-function mechanism by which tau might mediate neuronal cell death. Biochim. Biophys. Acta 1739, 268-279 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 268-279
    • Feinstein, S.C.1    Wilson, L.2
  • 99
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow, E. M. & Mandelkow, E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2, a006247 (2012).
    • (2012) Cold Spring Harb. Perspect. Med , vol.2 , pp. a006247
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 100
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and app vesicles in neurons and enhances oxidative stress
    • Stamer, K., Vogel, R., Thies, E., Mandelkow, E. & Mandelkow, E. M. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156, 1051-1063 (2002).
    • (2002) J. Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 101
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • Dixit, R., Ross, J. L., Goldman, Y. E. & Holzbaur, E. L. Differential regulation of dynein and kinesin motor proteins by tau. Science 319, 1086-1089 (2008).
    • (2008) Science , vol.319 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 103
    • 34548620157 scopus 로고    scopus 로고
    • Swimming against the tide: Mobility of the microtubule-Associated protein tau in neurons
    • Konzack, S., Thies, E., Marx, A., Mandelkow, E. M. & Mandelkow, E. Swimming against the tide: mobility of the microtubule-Associated protein tau in neurons. J. Neurosci. 27, 9916-9927 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 9916-9927
    • Konzack, S.1    Thies, E.2    Marx, A.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 104
    • 27844470590 scopus 로고    scopus 로고
    • Molecular motors implicated in the axonal transport of tau and ?-synuclein
    • Utton, M. A., Noble, W. J., Hill, J. E., Anderton, B. H. & Hanger, D. P. Molecular motors implicated in the axonal transport of tau and ?-synuclein. J. Cell Sci. 118, 4645-4654 (2005).
    • (2005) J. Cell Sci , vol.118 , pp. 4645-4654
    • Utton, M.A.1    Noble, W.J.2    Hill, J.E.3    Anderton, B.H.4    Hanger, D.P.5
  • 105
    • 79960032374 scopus 로고    scopus 로고
    • Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases
    • Kanaan, N. M. et al. Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J. Neurosci. 31, 9858-9868 (2011).
    • (2011) J. Neurosci , vol.31 , pp. 9858-9868
    • Kanaan, N.M.1
  • 106
    • 35649028013 scopus 로고    scopus 로고
    • Interaction of tau protein with the dynactin complex
    • Magnani, E. et al. Interaction of tau protein with the dynactin complex. EMBO J. 26, 4546-4554 (2007).
    • (2007) EMBO J , vol.26 , pp. 4546-4554
    • Magnani, E.1
  • 107
    • 39549117998 scopus 로고    scopus 로고
    • Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice
    • Yuan, A., Kumar, A., Peterhoff, C., Duff, K. & Nixon, R. A. Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. J. Neurosci. 28, 1682-1687 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 1682-1687
    • Yuan, A.1    Kumar, A.2    Peterhoff, C.3    Duff, K.4    Nixon, R.A.5
  • 108
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • Caceres, A. & Kosik, K. S. Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343, 461-463 (1990).
    • (1990) Nature , vol.343 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 109
    • 0025883663 scopus 로고
    • Overexpression of tau in a nonneuronal cell induces long cellular processes
    • Knops, J. et al. Overexpression of tau in a nonneuronal cell induces long cellular processes. J. Cell Biol. 114, 725-733 (1991).
    • (1991) J. Cell Biol , vol.114 , pp. 725-733
    • Knops, J.1
  • 110
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson, H. N. et al. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114, 1179-1187 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 1179-1187
    • Dawson, H.N.1
  • 111
    • 0028301455 scopus 로고
    • Altered microtubule organization in small-calibre axons of mice lacking tau protein
    • Harada, A. et al. Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369, 488-491 (1994).
    • (1994) Nature , vol.369 , pp. 488-491
    • Harada, A.1
  • 112
    • 84964696705 scopus 로고    scopus 로고
    • Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer inverted question marks disease
    • Tai, H. C. et al. Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer inverted question marks disease. Acta Neuropathol. Commun. 2, 146 (2014).
    • (2014) Acta Neuropathol. Commun , vol.2 , pp. 146
    • Tai, H.C.1
  • 113
    • 84866361333 scopus 로고    scopus 로고
    • Interaction of endogenous tau protein with synaptic proteins is regulated by n-methyl-d-Aspartate receptor-dependent tau phosphorylation
    • Mondragon-Rodriguez, S. et al. Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-d-Aspartate receptor-dependent tau phosphorylation. J. Biol. Chem. 287, 32040-32053 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 32040-32053
    • Mondragon-Rodriguez, S.1
  • 114
    • 84899474632 scopus 로고    scopus 로고
    • Activity-dependent tau protein translocation to excitatory synapse is disrupted by exposure to amyloid-? Oligomers
    • Frandemiche, M. L. et al. Activity-dependent tau protein translocation to excitatory synapse is disrupted by exposure to amyloid-? oligomers. J. Neurosci. 34, 6084-6097 (2014).
    • (2014) J. Neurosci , vol.34 , pp. 6084-6097
    • Frandemiche, M.L.1
  • 116
    • 33745184916 scopus 로고    scopus 로고
    • Tau protein binds to pericentromeric DNA: A putative role for nuclear tau in nucleolar organization
    • Sjoberg, M. K., Shestakova, E., Mansuroglu, Z., Maccioni, R. B. & Bonnefoy, E. Tau protein binds to pericentromeric DNA: a putative role for nuclear tau in nucleolar organization. J. Cell Sci. 119, 2025-2034 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 2025-2034
    • Sjoberg, M.K.1    Shestakova, E.2    Mansuroglu, Z.3    Maccioni, R.B.4    Bonnefoy, E.5
  • 117
    • 84905856215 scopus 로고    scopus 로고
    • Huntington's disease is a four-repeat tauopathy with tau nuclear rods
    • Fernandez-Nogales, M. et al. Huntington's disease is a four-repeat tauopathy with tau nuclear rods. Nat. Med. 20, 881-885 (2014).
    • (2014) Nat. Med , vol.20 , pp. 881-885
    • Fernandez-Nogales, M.1
  • 118
    • 84907876409 scopus 로고    scopus 로고
    • Tau reduction prevents disease in a mouse model of dravet syndrome
    • Gheyara, A. L. et al. Tau reduction prevents disease in a mouse model of Dravet syndrome. Ann. Neurol. 76, 443-456 (2014).
    • (2014) Ann. Neurol , vol.76 , pp. 443-456
    • Gheyara, A.L.1
  • 119
    • 84872729419 scopus 로고    scopus 로고
    • Tau loss attenuates neuronal network hyperexcitability in mouse and drosophila genetic models of epilepsy
    • Holth, J. K. et al. Tau loss attenuates neuronal network hyperexcitability in mouse and Drosophila genetic models of epilepsy. J. Neurosci. 33, 1651-1659 (2013).
    • (2013) J. Neurosci , vol.33 , pp. 1651-1659
    • Holth, J.K.1
  • 120
    • 84869159135 scopus 로고    scopus 로고
    • Lack of tau proteins rescues neuronal cell death and decreases amyloidogenic processing of app in app/ps1 mice
    • Leroy, K. et al. Lack of tau proteins rescues neuronal cell death and decreases amyloidogenic processing of APP in APP/PS1 mice. Am. J. Pathol. 181, 1928-1940 (2012).
    • (2012) Am. J. Pathol , vol.181 , pp. 1928-1940
    • Leroy, K.1
  • 121
    • 84880838441 scopus 로고    scopus 로고
    • Antisense reduction of tau in adult mice protects against seizures
    • DeVos, S. L. et al. Antisense reduction of tau in adult mice protects against seizures. J. Neurosci. 33, 12887-12897 (2013).
    • (2013) J. Neurosci , vol.33 , pp. 12887-12897
    • DeVos, S.L.1
  • 122
    • 84906922815 scopus 로고    scopus 로고
    • Motor and cognitive deficits in aged tau knockout mice in two background strains
    • Lei, P. et al. Motor and cognitive deficits in aged tau knockout mice in two background strains. Mol. Neurodegener. 9, 29 (2014).
    • (2014) Mol. Neurodegener , vol.9 , pp. 29
    • Lei, P.1
  • 123
    • 77951812710 scopus 로고    scopus 로고
    • Essential role of tau phosphorylation in adult hippocampal neurogenesis
    • Hong, X. P. et al. Essential role of tau phosphorylation in adult hippocampal neurogenesis. Hippocampus 20, 1339-1349 (2010).
    • (2010) Hippocampus , vol.20 , pp. 1339-1349
    • Hong, X.P.1
  • 124
    • 70249097351 scopus 로고    scopus 로고
    • Function of tau protein in adult newborn neurons
    • Fuster-Matanzo, A. et al. Function of tau protein in adult newborn neurons. FEBS Lett. 583, 3063-3068 (2009).
    • (2009) FEBS Lett , vol.583 , pp. 3063-3068
    • Fuster-Matanzo, A.1
  • 125
    • 84856708923 scopus 로고    scopus 로고
    • Tau deficiency induces parkinsonism with dementia by impairing app-mediated iron export
    • Lei, P. et al. Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export. Nat. Med. 18, 291-295 (2012).
    • (2012) Nat. Med , vol.18 , pp. 291-295
    • Lei, P.1
  • 126
    • 84888793501 scopus 로고    scopus 로고
    • Microtubule-Associated protein tau is essential for long-term depression in the hippocampus
    • Kimura, T. et al. Microtubule-Associated protein tau is essential for long-term depression in the hippocampus. Phil. Trans. R. Soc. B 369, 20130144 (2014).
    • (2014) Phil. Trans. R. Soc. B , vol.369 , pp. 20130144
    • Kimura, T.1
  • 127
    • 84922913225 scopus 로고    scopus 로고
    • Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion
    • Ahmed, T. et al. Cognition and hippocampal synaptic plasticity in mice with a homozygous tau deletion. Neurobiol. Aging 35, 2474-2478 (2014).
    • (2014) Neurobiol. Aging , vol.35 , pp. 2474-2478
    • Ahmed, T.1
  • 128
    • 0036854327 scopus 로고    scopus 로고
    • Protein kinase mark/par-1 is required for neurite outgrowth and establishment of neuronal polarity
    • Biernat, J. et al. Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity. Mol. Biol. Cell 13, 4013-4028 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4013-4028
    • Biernat, J.1
  • 129
    • 70350435136 scopus 로고    scopus 로고
    • Activated actin-depolymerizing factor/cofilin sequesters phosphorylated microtubule-Associated protein during the assembly of Alzheimer-like neuritic cytoskeletal striations
    • Whiteman, I. T. et al. Activated actin-depolymerizing factor/cofilin sequesters phosphorylated microtubule-Associated protein during the assembly of Alzheimer-like neuritic cytoskeletal striations. J. Neurosci. 29, 12994-13005 (2009).
    • (2009) J. Neurosci , vol.29 , pp. 12994-13005
    • Whiteman, I.T.1
  • 130
    • 84896813856 scopus 로고    scopus 로고
    • Novel mutation in mapt exon 13 (p. N410h) causes corticobasal degeneration
    • Kouri, N. et al. Novel mutation in MAPT exon 13 (p. N410H) causes corticobasal degeneration. Acta Neuropathol. 127, 271-282 (2014).
    • (2014) Acta Neuropathol , vol.127 , pp. 271-282
    • Kouri, N.1
  • 131
    • 84864505483 scopus 로고    scopus 로고
    • Evidence for a role of the rare p. A152t variant in mapt in increasing the risk for ftd-spectrum and Alzheimer's diseases
    • Coppola, G. et al. Evidence for a role of the rare p. A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases. Hum. Mol. Genet. 21, 3500-3512 (2012).
    • (2012) Hum. Mol. Genet , vol.21 , pp. 3500-3512
    • Coppola, G.1
  • 132
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S. et al. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721 (2000).
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1
  • 133
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary ftdp-17
    • Hong, M. et al. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 282, 1914-1917 (1998).
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1
  • 134
    • 84922089484 scopus 로고    scopus 로고
    • Primary age-related tauopathy (part): A common pathology associated with human aging
    • Crary, J. F. et al. Primary age-related tauopathy (PART): a common pathology associated with human aging. Acta Neuropathol. 128, 755-766 (2014).
    • (2014) Acta Neuropathol , vol.128 , pp. 755-766
    • Crary, J.F.1
  • 135
    • 84939962087 scopus 로고    scopus 로고
    • Part, a distinct tauopathy, different from classical sporadic Alzheimer disease
    • Jellinger, K. A. et al. PART, a distinct tauopathy, different from classical sporadic Alzheimer disease. Acta Neuropathol. 129, 757-762 (2015).
    • (2015) Acta Neuropathol , vol.129 , pp. 757-762
    • Jellinger, K.A.1
  • 136
    • 84918519465 scopus 로고    scopus 로고
    • Are cases with tau pathology occurring in the absence of a? Deposits part of the ad-related pathological process?
    • Braak, H. & Del Tredici, K. Are cases with tau pathology occurring in the absence of A? deposits part of the AD-related pathological process? Acta Neuropathol. 128, 767-772 (2014).
    • (2014) Acta Neuropathol , vol.128 , pp. 767-772
    • Braak, H.1    Del Tredici, K.2
  • 137
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of ? Protein into Alzheimer paired helical filaments depends on a local sequence motif (306vqivyk311) forming ? Structure
    • von Bergen, M. et al. Assembly of ? protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming ? structure. Proc. Natl Acad. Sci. USA 97, 5129-5134 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5129-5134
    • Von Bergen, M.1
  • 138
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-? Spines reveal varied steric zippers
    • Sawaya, M. R. et al. Atomic structures of amyloid cross-? spines reveal varied steric zippers. Nature 447, 453-457 (2007).
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1
  • 139
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova, I. et al. Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem. 281, 1205-1214 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1
  • 140
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-Associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M. et al. Assembly of microtubule-Associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553 (1996).
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1
  • 141
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-Associated protein tau in vitro
    • Wille, H., Drewes, G., Biernat, J., Mandelkow, E. M. & Mandelkow, E. Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-Associated protein tau in vitro. J. Cell Biol. 118, 573-584 (1992).
    • (1992) J. Cell Biol , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 142
    • 1242337344 scopus 로고    scopus 로고
    • Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers
    • Hernandez, F., Cuadros, R. & Avila, J. Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers. Neurosci. Lett. 357, 143-146 (2004).
    • (2004) Neurosci. Lett , vol.357 , pp. 143-146
    • Hernandez, F.1    Cuadros, R.2    Avila, J.3
  • 143
    • 84897005564 scopus 로고    scopus 로고
    • Immunophilin fkbp52 induces tau-p301l filamentous assembly in vitro and modulates its activity in a model of tauopathy
    • Giustiniani, J. et al. Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy. Proc. Natl Acad. Sci. USA 111, 4584-4589 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 4584-4589
    • Giustiniani, J.1
  • 144
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak, E., Braak, H. & Mandelkow, E. M. A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. 87, 554-567 (1994).
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 145
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-Assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso, A., Zaidi, T., Novak, M., Grundke-Iqbal, I. & Iqbal, K. Hyperphosphorylation induces self-Assembly of tau into tangles of paired helical filaments/straight filaments. Proc. Natl Acad. Sci. USA 98, 6923-6928 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 146
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (ser262, ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E. & Mandelkow, E. M. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 3549-3558 (1999).
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 147
    • 84917706097 scopus 로고    scopus 로고
    • Oligomer formation of tau protein hyperphosphorylated in cells
    • Tepper, K. et al. Oligomer formation of tau protein hyperphosphorylated in cells. J. Biol. Chem. 289, 34389-34407 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 34389-34407
    • Tepper, K.1
  • 148
    • 84864389698 scopus 로고    scopus 로고
    • Degradation of tau protein by autophagy and proteasomal pathways
    • Wang, Y. & Mandelkow, E. Degradation of tau protein by autophagy and proteasomal pathways. Biochem. Soc. Trans. 40, 644-652 (2012).
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 644-652
    • Wang, Y.1    Mandelkow, E.2
  • 149
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • Zilka, N. et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 580, 3582-3588 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 3582-3588
    • Zilka, N.1
  • 150
    • 77951540816 scopus 로고    scopus 로고
    • Caspase activation precedes and leads to tangles
    • de Calignon, A. et al. Caspase activation precedes and leads to tangles. Nature 464, 1201-1204 (2010).
    • (2010) Nature , vol.464 , pp. 1201-1204
    • De Calignon, A.1
  • 151
    • 84910669129 scopus 로고    scopus 로고
    • Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease
    • Zhang, Z. et al. Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease. Nat. Med. 20, 1254-1262 (2014).
    • (2014) Nat. Med , vol.20 , pp. 1254-1262
    • Zhang, Z.1
  • 152
    • 34547203592 scopus 로고    scopus 로고
    • Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model
    • Wang, Y. P., Biernat, J., Pickhardt, M., Mandelkow, E. & Mandelkow, E. M. Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model. Proc. Natl Acad. Sci. USA 104, 10252-10257 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10252-10257
    • Wang, Y.P.1    Biernat, J.2    Pickhardt, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 153
    • 84865074623 scopus 로고    scopus 로고
    • Inhibition of tau aggregation in a novel caenorhabditis elegans model of tauopathy mitigates proteotoxicity
    • Fatouros, C. et al. Inhibition of tau aggregation in a novel Caenorhabditis elegans model of tauopathy mitigates proteotoxicity. Hum. Mol. Genet. 21, 3587-3603 (2012).
    • (2012) Hum. Mol. Genet , vol.21 , pp. 3587-3603
    • Fatouros, C.1
  • 154
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera, F. et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol. 11, 909-913 (2009).
    • (2009) Nat. Cell Biol , vol.11 , pp. 909-913
    • Clavaguera, F.1
  • 155
    • 84908430607 scopus 로고    scopus 로고
    • Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice
    • Peeraer, E. et al. Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice. Neurobiol. Dis. 73, 83-95 (2015).
    • (2015) Neurobiol. Dis , vol.73 , pp. 83-95
    • Peeraer, E.1
  • 156
    • 84896697812 scopus 로고    scopus 로고
    • Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
    • Clavaguera, F. et al. Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice. Acta Neuropathol. 127, 299-301 (2014).
    • (2014) Acta Neuropathol , vol.127 , pp. 299-301
    • Clavaguera, F.1
  • 157
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • Sanders, D. W. et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 82, 1271-1288 (2014).
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, D.W.1
  • 158
    • 0035138764 scopus 로고    scopus 로고
    • Loss of brain tau defines novel sporadic and familial tauopathies with frontotemporal dementia
    • Zhukareva, V. et al. Loss of brain tau defines novel sporadic and familial tauopathies with frontotemporal dementia. Ann. Neurol. 49, 165-175 (2001).
    • (2001) Ann. Neurol , vol.49 , pp. 165-175
    • Zhukareva, V.1
  • 159
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • Gomez-Isla, T. et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann. Neurol. 41, 17-24 (1997).
    • (1997) Ann. Neurol , vol.41 , pp. 17-24
    • Gomez-Isla, T.1
  • 160
    • 0033028074 scopus 로고    scopus 로고
    • Neurons may live for decades with neurofibrillary tangles
    • Morsch, R., Simon, W. & Coleman, P. D. Neurons may live for decades with neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 58, 188-197 (1999).
    • (1999) J. Neuropathol. Exp. Neurol , vol.58 , pp. 188-197
    • Morsch, R.1    Simon, W.2    Coleman, P.D.3
  • 161
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer, C. et al. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J. Neurosci. 25, 5446-5454 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 5446-5454
    • Andorfer, C.1
  • 162
    • 38549120646 scopus 로고    scopus 로고
    • In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons
    • Spires-Jones, T. L. et al. In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons. J. Neurosci. 28, 862-867 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 862-867
    • Spires-Jones, T.L.1
  • 163
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1
  • 164
    • 84864382491 scopus 로고    scopus 로고
    • Cognitive defects are reversible in inducible mice expressing pro-Aggregant full-length human tau
    • Van der Jeugd, A. et al. Cognitive defects are reversible in inducible mice expressing pro-Aggregant full-length human Tau. Acta Neuropathol. 123, 787-805 (2012).
    • (2012) Acta Neuropathol , vol.123 , pp. 787-805
    • Van Der Jeugd, A.1
  • 165
    • 79951818085 scopus 로고    scopus 로고
    • Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic tau mutant
    • Sydow, A. et al. Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant. J. Neurosci. 31, 2511-2525 (2011).
    • (2011) J. Neurosci , vol.31 , pp. 2511-2525
    • Sydow, A.1
  • 166
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • Alonso Adel, C., Li, B., Grundke-Iqbal, I. & Iqbal, K. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc. Natl Acad. Sci. USA 103, 8864-8869 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8864-8869
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 167
    • 34248190279 scopus 로고    scopus 로고
    • A? Oligomers - A decade of discovery
    • Walsh, D. M. & Selkoe, D. J. A? oligomers - a decade of discovery. J. Neurochem. 101, 1172-1184 (2007).
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 168
    • 84858965241 scopus 로고    scopus 로고
    • Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
    • Lasagna-Reeves, C. A. et al. Identification of oligomers at early stages of tau aggregation in Alzheimer's disease. FASEB J. 26, 1946-1959 (2012).
    • (2012) FASEB J , vol.26 , pp. 1946-1959
    • Lasagna-Reeves, C.A.1
  • 169
    • 33947691643 scopus 로고    scopus 로고
    • Granular tau oligomers as intermediates of tau filaments
    • Maeda, S. et al. Granular tau oligomers as intermediates of tau filaments. Biochemistry 46, 3856-3861 (2007).
    • (2007) Biochemistry , vol.46 , pp. 3856-3861
    • Maeda, S.1
  • 170
    • 84885463056 scopus 로고    scopus 로고
    • Trimeric tau is toxic to human neuronal cells at low nanomolar concentrations
    • Tian, H. et al. Trimeric tau is toxic to human neuronal cells at low nanomolar concentrations. Int. J. Cell Biol. 2013, 260787 (2013).
    • (2013) Int. J. Cell Biol , vol.2013 , pp. 260787
    • Tian, H.1
  • 171
    • 84871568308 scopus 로고    scopus 로고
    • Tau oligomers impair artificial membrane integrity and cellular viability
    • Flach, K. et al. Tau oligomers impair artificial membrane integrity and cellular viability. J. Biol. Chem. 287, 43223-43233 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 43223-43233
    • Flach, K.1
  • 172
    • 0033070197 scopus 로고    scopus 로고
    • High prevalence of mutations in the microtubule-Associated protein tau in a population study of frontotemporal dementia in the netherlands
    • Rizzu, P. et al. High prevalence of mutations in the microtubule-Associated protein tau in a population study of frontotemporal dementia in the Netherlands. Am. J. Hum. Genet. 64, 414-421 (1999).
    • (1999) Am. J. Hum. Genet , vol.64 , pp. 414-421
    • Rizzu, P.1
  • 173
    • 38549129613 scopus 로고    scopus 로고
    • The potential for ?-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous tau in inducible mouse models of tauopathy
    • Mocanu, M. M. et al. The potential for ?-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J. Neurosci. 28, 737-748 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 737-748
    • Mocanu, M.M.1
  • 174
    • 35748954923 scopus 로고    scopus 로고
    • The ?-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy
    • Eckermann, K. et al. The ?-propensity of Tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. J. Biol. Chem. 282, 31755-31765 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 31755-31765
    • Eckermann, K.1
  • 175
    • 57049139853 scopus 로고    scopus 로고
    • Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone
    • Sarkar, M., Kuret, J. & Lee, G. Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone. J. Neurosci. Res. 86, 2763-2773 (2008).
    • (2008) J. Neurosci. Res , vol.86 , pp. 2763-2773
    • Sarkar, M.1    Kuret, J.2    Lee, G.3
  • 176
    • 70349987102 scopus 로고    scopus 로고
    • Tau fragmentation, aggregation and clearance: The dual role of lysosomal processing
    • Wang, Y. et al. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum. Mol. Genet. 18, 4153-4170 (2009).
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4153-4170
    • Wang, Y.1
  • 177
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of f-Actin mediates tau-induced neuronal degeneration in vivo
    • Fulga, T. A. et al. Abnormal bundling and accumulation of F-Actin mediates tau-induced neuronal degeneration in vivo. Nat. Cell Biol. 9, 139-148 (2007).
    • (2007) Nat. Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1
  • 178
    • 65449156394 scopus 로고    scopus 로고
    • Sut-2 potentiates tau-induced neurotoxicity in caenorhabditis elegans
    • Guthrie, C. R., Schellenberg, G. D. & Kraemer, B. C. SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans. Hum. Mol. Genet. 18, 1825-1838 (2009).
    • (2009) Hum. Mol. Genet , vol.18 , pp. 1825-1838
    • Guthrie, C.R.1    Schellenberg, G.D.2    Kraemer, B.C.3
  • 179
    • 34548389257 scopus 로고    scopus 로고
    • Sut-1 enables tau-induced neurotoxicity in c. Elegans
    • Kraemer, B. C. & Schellenberg, G. D. SUT-1 enables tau-induced neurotoxicity in C. elegans. Hum. Mol. Genet. 16, 1959-1971 (2007).
    • (2007) Hum. Mol. Genet , vol.16 , pp. 1959-1971
    • Kraemer, B.C.1    Schellenberg, G.D.2
  • 180
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-? Oligomers induce synaptic damage via tau-dependent microtubule severing by ttll6 and spastin
    • Zempel, H. et al. Amyloid-? oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin. EMBO J. 32, 2920-2937 (2013).
    • (2013) EMBO J , vol.32 , pp. 2920-2937
    • Zempel, H.1
  • 181
    • 84877879701 scopus 로고    scopus 로고
    • Amyloid-? Signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease
    • Seward, M. E. et al. Amyloid-? signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease. J. Cell Sci. 126, 1278-1286 (2013).
    • (2013) J. Cell Sci , vol.126 , pp. 1278-1286
    • Seward, M.E.1
  • 182
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular a? and synaptic dysfunction
    • Oddo, S. et al. Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular A? and synaptic dysfunction. Neuron 39, 409-421 (2003).
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1
  • 183
    • 85018198790 scopus 로고    scopus 로고
    • Pro-Aggregant tau impairs mossy fiber plasticity due to structural changes and ca++ dysregulation
    • Decker, J. M. et al. Pro-Aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation. Acta Neuropathol. Commun. 3, 23 (2015).
    • (2015) Acta Neuropathol. Commun , vol.3 , pp. 23
    • Decker, J.M.1
  • 184
    • 84938709394 scopus 로고    scopus 로고
    • Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain
    • Maphis, N. et al. Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain. Brain 138, 1738-1755 (2015).
    • (2015) Brain , vol.138 , pp. 1738-1755
    • Maphis, N.1
  • 185
    • 84901047429 scopus 로고    scopus 로고
    • Proteostasis and the aging proteome in health and disease
    • Morimoto, R. I. & Cuervo, A. M. Proteostasis and the aging proteome in health and disease. J. Gerontol. A Biol. Sci. Med. Sci. 69 (Suppl. 1), 33-38 (2014).
    • (2014) J. Gerontol. A Biol. Sci. Med. Sci , vol.69 , pp. 33-38
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 186
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • Pooler, A. M., Phillips, E. C., Lau, D. H., Noble, W. & Hanger, D. P. Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep. 14, 389-394 (2013).
    • (2013) EMBO Rep , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 187
    • 84896830709 scopus 로고    scopus 로고
    • Neuronal activity regulates extracellular tau in vivo
    • Yamada, K. et al. Neuronal activity regulates extracellular tau in vivo. J. Exp. Med. 211, 387-393 (2014).
    • (2014) J. Exp. Med , vol.211 , pp. 387-393
    • Yamada, K.1
  • 188
    • 0031025396 scopus 로고    scopus 로고
    • The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments
    • Johnson, G. V. et al. The tau protein in human cerebrospinal fluid in Alzheimer's disease consists of proteolytically derived fragments. J. Neurochem. 68, 430-433 (1997).
    • (1997) J. Neurochem , vol.68 , pp. 430-433
    • Johnson, G.V.1
  • 189
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in p301s human tau transgenic mice
    • Yamada, K. et al. In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. J. Neurosci. 31, 13110-13117 (2011).
    • (2011) J. Neurosci , vol.31 , pp. 13110-13117
    • Yamada, K.1
  • 190
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • Takamori, S. et al. Molecular anatomy of a trafficking organelle. Cell 127, 831-846 (2006).
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1
  • 191
    • 84871141635 scopus 로고    scopus 로고
    • Extracellular tau levels are influenced by variability in tau that is associated with tauopathies
    • Karch, C. M., Jeng, A. T. & Goate, A. M. Extracellular Tau levels are influenced by variability in Tau that is associated with tauopathies. J. Biol. Chem. 287, 42751-42762 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 42751-42762
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 192
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. & Rabouille, C. Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 10, 148-155 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 193
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through m1 and m3 muscarinic receptors in neuronal cells
    • Gomez-Ramos, A., Diaz-Hernandez, M., Rubio, A., Miras-Portugal, M. T. & Avila, J. Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Mol. Cell. Neurosci. 37, 673-681 (2008).
    • (2008) Mol. Cell. Neurosci , vol.37 , pp. 673-681
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 194
    • 69049090784 scopus 로고    scopus 로고
    • Characteristics and consequences of muscarinic receptor activation by tau protein
    • Gomez-Ramos, A. et al. Characteristics and consequences of muscarinic receptor activation by tau protein. Eur. Neuropsychopharmacol. 19, 708-717 (2009).
    • (2009) Eur. Neuropsychopharmacol , vol.19 , pp. 708-717
    • Gomez-Ramos, A.1
  • 195
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo, J. L. & Lee, V. M. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J. Biol. Chem. 286, 15317-15331 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 196
    • 84891905725 scopus 로고    scopus 로고
    • Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology
    • Michel, C. H. et al. Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology. J. Biol. Chem. 289, 956-967 (2014).
    • (2014) J. Biol. Chem , vol.289 , pp. 956-967
    • Michel, C.H.1
  • 197
    • 84882306577 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
    • Holmes, B. B. et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc. Natl Acad. Sci. USA 110, E3138-E3147 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E3138-E3147
    • Holmes, B.B.1
  • 198
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H. & Braak, E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 82, 239-259 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 199
    • 0029967367 scopus 로고    scopus 로고
    • Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis
    • Braak, H. & Braak, E. Development of Alzheimer-related neurofibrillary changes in the neocortex inversely recapitulates cortical myelogenesis. Acta Neuropathol. 92, 197-201 (1996).
    • (1996) Acta Neuropathol , vol.92 , pp. 197-201
    • Braak, H.1    Braak, E.2
  • 200
    • 84884879594 scopus 로고    scopus 로고
    • Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease
    • Yan, M. H., Wang, X. & Zhu, X. Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic. Biol. Med. 62, 90-101 (2013).
    • (2013) Free Radic. Biol. Med , vol.62 , pp. 90-101
    • Yan, M.H.1    Wang, X.2    Zhu, X.3
  • 201
    • 84925267195 scopus 로고    scopus 로고
    • Myelination of the nervous system: Mechanisms and functions
    • Nave, K. A. & Werner, H. B. Myelination of the nervous system: mechanisms and functions. Annu. Rev. Cell Dev. Biol. 30, 503-533 (2014).
    • (2014) Annu. Rev. Cell Dev. Biol , vol.30 , pp. 503-533
    • Nave, K.A.1    Werner, H.B.2
  • 202
    • 0021145680 scopus 로고
    • Alzheimer's disease: Cell-specific pathology isolates the hippocampal formation
    • Hyman, B. T., Van Hoesen, G. W., Damasio, A. R. & Barnes, C. L. Alzheimer's disease: cell-specific pathology isolates the hippocampal formation. Science 225, 1168-1170 (1984).
    • (1984) Science , vol.225 , pp. 1168-1170
    • Hyman, B.T.1    Van Hoesen, G.W.2    Damasio, A.R.3    Barnes, C.L.4
  • 203
    • 85018215020 scopus 로고    scopus 로고
    • Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-Aggregant human tau
    • Hochgrafe, K. et al. Preventive methylene blue treatment preserves cognition in mice expressing full-length pro-Aggregant human Tau. Acta Neuropathol. Commun. 3, 25 (2015).
    • (2015) Acta Neuropathol. Commun , vol.3 , pp. 25
    • Hochgrafe, K.1
  • 204
    • 84921531217 scopus 로고    scopus 로고
    • Tau aggregation inhibitor therapy: An exploratory phase 2 study in mild or moderate Alzheimer's disease
    • Wischik, C. M. et al. Tau aggregation inhibitor therapy: an exploratory phase 2 study in mild or moderate Alzheimer's disease. J. Alzheimers Dis. 44, 705-720 (2015).
    • (2015) J. Alzheimers Dis , vol.44 , pp. 705-720
    • Wischik, C.M.1
  • 205
    • 79960065022 scopus 로고    scopus 로고
    • Structure-based design of non-natural amino-Acid inhibitors of amyloid fibril formation
    • Sievers, S. A. et al. Structure-based design of non-natural amino-Acid inhibitors of amyloid fibril formation. Nature 475, 96-100 (2011).
    • (2011) Nature , vol.475 , pp. 96-100
    • Sievers, S.A.1
  • 206
    • 84924106368 scopus 로고    scopus 로고
    • A phase II trial of tideglusib in Alzheimer's disease
    • Lovestone, S. et al. A phase II trial of tideglusib in Alzheimer's disease. J. Alzheimers Dis. 45, 75-88 (2015).
    • (2015) J. Alzheimers Dis , vol.45 , pp. 75-88
    • Lovestone, S.1
  • 207
    • 84898056494 scopus 로고    scopus 로고
    • Tideglusib reduces progression of brain atrophy in progressive supranuclear palsy in a randomized trial
    • Hoglinger, G. U. et al. Tideglusib reduces progression of brain atrophy in progressive supranuclear palsy in a randomized trial. Mov. Disord. 29, 479-487 (2014).
    • (2014) Mov. Disord , vol.29 , pp. 479-487
    • Hoglinger, G.U.1
  • 208
    • 84902545124 scopus 로고    scopus 로고
    • Davunetide in patients with progressive supranuclear palsy: A randomised, double-blind, placebo-controlled phase 2/3 trial
    • Boxer, A. L. et al. Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial. Lancet Neurol. 13, 676-685 (2014).
    • (2014) Lancet Neurol , vol.13 , pp. 676-685
    • Boxer, A.L.1
  • 209
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone d improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden, K. R. et al. Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J. Neurosci. 30, 13861-13866 (2010).
    • (2010) J. Neurosci , vol.30 , pp. 13861-13866
    • Brunden, K.R.1
  • 210
    • 37249013214 scopus 로고    scopus 로고
    • US National Library of Medicine [online]
    • US National Library of Medicine. ClinicalTrials.gov [online], https://clinicaltrials.gov/ct2/show/NCT01492374 (2015).
    • (2015) ClinicalTrials.Gov
  • 211
    • 84907051284 scopus 로고    scopus 로고
    • Targeting hsp90 and its co-chaperones to treat Alzheimer's disease
    • Blair, L. J., Sabbagh, J. J. & Dickey, C. A. Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease. Expert Opin. Ther. Targets 18, 1219-1232 (2014).
    • (2014) Expert Opin. Ther. Targets , vol.18 , pp. 1219-1232
    • Blair, L.J.1    Sabbagh, J.J.2    Dickey, C.A.3
  • 212
    • 84896837095 scopus 로고    scopus 로고
    • Hsp90-tau complex reveals molecular basis for specificity in chaperone action
    • This is a structural study that demonstrates the interaction between HSP90 and tau
    • Karagoz, G. E. et al. Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell 156, 963-974 (2014). This is a structural study that demonstrates the interaction between HSP90 and tau.
    • (2014) Cell , vol.156 , pp. 963-974
    • Karagoz, G.E.1
  • 213
    • 84877109118 scopus 로고    scopus 로고
    • Rapamycin attenuates the progression of tau pathology in p301s tau transgenic mice
    • Ozcelik, S. et al. Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice. PLoS ONE 8, e62459 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e62459
    • Ozcelik, S.1
  • 214
    • 84862285881 scopus 로고    scopus 로고
    • Autophagic degradation of tau in primary neurons and its enhancement by trehalose
    • Kruger, U., Wang, Y., Kumar, S. & Mandelkow, E. M. Autophagic degradation of tau in primary neurons and its enhancement by trehalose. Neurobiol. Aging 33, 2291-2305 (2012).
    • (2012) Neurobiol. Aging , vol.33 , pp. 2291-2305
    • Kruger, U.1    Wang, Y.2    Kumar, S.3    Mandelkow, E.M.4
  • 215
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • Berger, Z. et al. Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum. Mol. Genet. 15, 433-442 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 433-442
    • Berger, Z.1
  • 216
    • 84896837399 scopus 로고    scopus 로고
    • Tau immunotherapy and imaging
    • Sigurdsson, E. M. Tau immunotherapy and imaging. Neurodegener. Dis. 13, 103-106 (2014).
    • (2014) Neurodegener. Dis , vol.13 , pp. 103-106
    • Sigurdsson, E.M.1
  • 217
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni, A. A., Boutajangout, A., Quartermain, D. & Sigurdsson, E. M. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J. Neurosci. 27, 9115-9129 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 218
    • 84891864287 scopus 로고    scopus 로고
    • Open questions for Alzheimer's disease immunotherapy
    • Golde, T. E. Open questions for Alzheimer's disease immunotherapy. Alzheimers Res. Ther. 6, 3 (2014).
    • (2014) Alzheimers Res. Ther , vol.6 , pp. 3
    • Golde, T.E.1
  • 219
    • 84890282160 scopus 로고    scopus 로고
    • Antibody uptake into neurons occurs primarily via clathrin-dependent fc? Receptor endocytosis and is a prerequisite for acute tau protein clearance
    • Congdon, E. E., Gu, J., Sait, H. B. & Sigurdsson, E. M. Antibody uptake into neurons occurs primarily via clathrin-dependent Fc? receptor endocytosis and is a prerequisite for acute tau protein clearance. J. Biol. Chem. 288, 35452-35465 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 35452-35465
    • Congdon, E.E.1    Gu, J.2    Sait, H.B.3    Sigurdsson, E.M.4
  • 220
    • 84908377705 scopus 로고    scopus 로고
    • Neuronal uptake of tau/ps422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer's disease
    • Collin, L. et al. Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer's disease. Brain 137, 2834-2846 (2014).
    • (2014) Brain , vol.137 , pp. 2834-2846
    • Collin, L.1
  • 221
    • 84876908676 scopus 로고    scopus 로고
    • Tau passive immunotherapy in mutant p301l mice: Antibody affinity versus specificity
    • d'Abramo, C., Acker, C. M., Jimenez, H. T. & Davies, P. Tau passive immunotherapy in mutant P301L mice: antibody affinity versus specificity. PLoS ONE 8, e62402 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e62402
    • D'Abramo, C.1    Acker, C.M.2    Jimenez, H.T.3    Davies, P.4
  • 222
    • 84896269359 scopus 로고    scopus 로고
    • Passive immunization with tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles
    • Castillo-Carranza, D. L. et al. Passive immunization with Tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles. J. Neurosci. 34, 4260-4272 (2014).
    • (2014) J. Neurosci , vol.34 , pp. 4260-4272
    • Castillo-Carranza, D.L.1
  • 223
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • Yanamandra, K. et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 80, 402-414 (2013).
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1
  • 224
    • 0022827447 scopus 로고
    • Identification of cdna clones for the human microtubule-Associated protein tau and chromosomal localization of the genes for tau and microtubule-Associated protein 2
    • Neve, R. L., Harris, P., Kosik, K. S., Kurnit, D. M. & Donlon, T. A. Identification of cDNA clones for the human microtubule-Associated protein tau and chromosomal localization of the genes for tau and microtubule-Associated protein 2. Brain Res. 387, 271-280 (1986).
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 225
    • 84865791125 scopus 로고    scopus 로고
    • Mapt expression and splicing is differentially regulated by brain region: Relation to genotype and implication for tauopathies
    • Trabzuni, D. et al. MAPT expression and splicing is differentially regulated by brain region: relation to genotype and implication for tauopathies. Hum. Mol. Genet. 21, 4094-4103 (2012).
    • (2012) Hum. Mol. Genet , vol.21 , pp. 4094-4103
    • Trabzuni, D.1
  • 226
    • 4944230199 scopus 로고    scopus 로고
    • Expression of tau mRNA and soluble tau isoforms in affected and non-Affected brain areas in Alzheimer's disease
    • Boutajangout, A., Boom, A., Leroy, K. & Brion, J. P. Expression of tau mRNA and soluble tau isoforms in affected and non-Affected brain areas in Alzheimer's disease. FEBS Lett. 576, 183-189 (2004).
    • (2004) FEBS Lett , vol.576 , pp. 183-189
    • Boutajangout, A.1    Boom, A.2    Leroy, K.3    Brion, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.