메뉴 건너뛰기




Volumn 40, Issue S1, 2014, Pages

Intracellular and extracellular roles for tau in neurodegenerative disease

Author keywords

Alzheimer's disease; endocytosis; microtubules; neurodegeneration; phosphorylation; tau; tau release; tauopathy

Indexed keywords

TAU PROTEIN;

EID: 84901769091     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-132054     Document Type: Review
Times cited : (51)

References (114)
  • 2
    • 0032886469 scopus 로고    scopus 로고
    • Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease
    • Komori T (1999) Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease. Brain Pathol 9, 663-679. (Pubitemid 29470960)
    • (1999) Brain Pathology , vol.9 , Issue.4 , pp. 663-679
    • Komori, T.1
  • 4
    • 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 EM, Mandelkow E (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro. J Cell Biol 118, 573-584.
    • (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
  • 5
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther RA, Olesen OF, Jakes R, Goedert M (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease. FEBS Lett 309, 199-202.
    • (1992) FEBS Lett , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 6
    • 0028121105 scopus 로고
    • Assembly of Alzheimer-like filaments from full-length tau protein
    • DOI 10.1016/0014-5793(94)80260-2
    • Crowther RA, Olesen OF, Smith MJ, Jakes R, Goedert M (1994) Assembly of Alzheimer-like filaments from fulllength tau protein. FEBS Lett 337, 135-138. (Pubitemid 24024159)
    • (1994) FEBS Letters , vol.337 , Issue.2 , pp. 135-138
    • Crowther, R.A.1
  • 7
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • DOI 10.1038/383550a0
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA (1996) Assembly of microtubuleassociated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553. (Pubitemid 26346185)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 8
    • 84885455505 scopus 로고    scopus 로고
    • Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein
    • MorozovaOA,March ZM, Robinson AS, ColbyDW(2013) Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein. Biochemistry (Mosc) 52, 6960-6967.
    • (2013) Biochemistry (Mosc) , vol.52 , pp. 6960-6967
    • Morozova, O.A.1    March, Z.M.2    Robinson, A.S.3    Colby, D.W.4
  • 9
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W (2009) Tau phosphorylation: The therapeutic challenge for neurodegenerative disease. Trends Mol Med 15, 112-119.
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 12
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • DOI 10.1016/0896-6273(93)90063-W
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y (1993) Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10, 1151-1160. (Pubitemid 23194405)
    • (1993) Neuron , vol.10 , Issue.6 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 14
    • 84857035370 scopus 로고    scopus 로고
    • Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: A mass spectrometry approach
    • Thomas SN, Funk KE, Wan Y, Liao Z, Davies P, Kuret J, Yang AJ (2012) Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: A mass spectrometry approach. Acta Neuropathol 123, 105-117.
    • (2012) Acta Neuropathol , vol.123 , pp. 105-117
    • Thomas, S.N.1    Funk, K.E.2    Wan, Y.3    Liao, Z.4    Davies, P.5    Kuret, J.6    Yang, A.J.7
  • 17
    • 70949100259 scopus 로고    scopus 로고
    • Mediators of tau phosphorylation in the pathogenesis of Alzheimer's disease
    • Hanger DP, Seereeram A, NobleW(2009) Mediators of tau phosphorylation in the pathogenesis of Alzheimer's disease. Expert Rev Neurother 9, 1647-1666.
    • (2009) Expert Rev Neurother , vol.9 , pp. 1647-1666
    • Hanger, D.P.1    Seereeram, A.2    Noble, W.3
  • 20
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • DOI 10.1083/jcb.103.6.2739
    • Drubin DG, Kirschner MW (1986) Tau protein function in living cells. J Cell Biol 103, 2739-2746. (Pubitemid 17008019)
    • (1986) Journal of Cell Biology , vol.103 , Issue.6 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 21
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • DOI 10.1016/0896-6273(93)90279-Z
    • Biernat J, Gustke N, Drewes G, Mandelkow EM, Mandelkow E (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11, 153-163. (Pubitemid 23222542)
    • (1993) Neuron , vol.11 , Issue.1 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 23
    • 0030240325 scopus 로고    scopus 로고
    • Reduction of Acetylated α-Tubulin Immunoreactivity in Neurofibrillary Tangle-bearing Neurons in Alzheimer's Disease
    • Hempen B, Brion JP (1996) Reduction of acetylated tubulin immunoreactivity in neurofibrillary tanglebearing neurons in Alzheimer's disease. J Neuropathol Exp Neurol 55, 964-972. (Pubitemid 126449410)
    • (1996) Journal of Neuropathology and Experimental Neurology , vol.55 , Issue.9 , pp. 964-972
    • Hempen, B.1    Brion, J.-P.2
  • 25
    • 0036047004 scopus 로고    scopus 로고
    • Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease
    • DOI 10.1385/NMM:2:2:151
    • Terwel D, Dewachter I, Van Leuven F (2002) Axonal transport, tau protein, and neurodegeneration in Alzheimer's disease. Neuromolecular Med 2, 151-165. (Pubitemid 37012502)
    • (2002) NeuroMolecular Medicine , vol.2 , Issue.2 , pp. 151-165
    • Terwel, D.1    Dewachter, I.2    Van Leuven, F.3
  • 30
    • 0036899825 scopus 로고    scopus 로고
    • Kinesin motors and disease
    • DOI 10.1016/S0962-8924(02)02400-5, PII S0962892402024005
    • Mandelkow E, Mandelkow EM (2002) Kinesin motors and disease. Trends Cell Biol 12, 585-591. (Pubitemid 35461857)
    • (2002) Trends in Cell Biology , vol.12 , Issue.12 , pp. 585-591
    • Mandelkow, E.1    Mandelkow, E.-M.2
  • 31
    • 84879796952 scopus 로고    scopus 로고
    • Axonal degeneration in Alzheimer's disease: When signaling abnormalities meet the axonal transport system
    • Kanaan NM, Pigino GF, Brady ST, Lazarov O, Binder LI, Morfini GA (2013) Axonal degeneration in Alzheimer's disease: When signaling abnormalities meet the axonal transport system. Exp Neurol 246, 44-53.
    • (2013) Exp Neurol , vol.246 , pp. 44-53
    • Kanaan, N.M.1    Pigino, G.F.2    Brady, S.T.3    Lazarov, O.4    Binder, L.I.5    Morfini, G.A.6
  • 32
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • DOI 10.1126/science.1152993
    • Dixit R, Ross JL, Goldman YE, Holzbaur EL (2008) Differential regulation of dynein and kinesin motor proteins by tau. Science 319, 1086-1089. (Pubitemid 351300789)
    • (2008) Science , vol.319 , Issue.5866 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.F.4
  • 33
    • 84868514765 scopus 로고    scopus 로고
    • Microtubule stabilizing agents as potential treatment for Alzheimer's disease and related neurodegenerative tauopathies
    • Ballatore C, Brunden KR, Huryn DM, Trojanowski JQ, Lee VM, Smith AB, 3rd (2012) Microtubule stabilizing agents as potential treatment for Alzheimer's disease and related neurodegenerative tauopathies. J Med Chem 55, 8979-8996.
    • (2012) J Med Chem , vol.55 , pp. 8979-8996
    • Ballatore, C.1    Brunden, K.R.2    Huryn, D.M.3    Trojanowski, J.Q.4    Lee, V.M.5    Smith III, A.B.6
  • 34
    • 80055108264 scopus 로고    scopus 로고
    • Microtubules (tau) as an emerging therapeutic target: NAP (davunetide)
    • Gozes I (2011) Microtubules (tau) as an emerging therapeutic target: NAP (davunetide). Curr Pharm Des 17, 3413-3417.
    • (2011) Curr Pharm des , vol.17 , pp. 3413-3417
    • Gozes, I.1
  • 35
    • 84877914479 scopus 로고    scopus 로고
    • NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: Protection against impairments in axonal transport
    • Jouroukhin Y, Ostritsky R, Assaf Y, Pelled G, Giladi E, Gozes I (2013) NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: Protection against impairments in axonal transport. Neurobiol Dis 56, 79-94.
    • (2013) Neurobiol Dis , vol.56 , pp. 79-94
    • Jouroukhin, Y.1    Ostritsky, R.2    Assaf, Y.3    Pelled, G.4    Giladi, E.5    Gozes, I.6
  • 36
    • 84875241051 scopus 로고    scopus 로고
    • HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila
    • Xiong Y, Zhao K, Wu J, Xu Z, Jin S, Zhang YQ (2013) HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila. Proc Natl Acad Sci U S A 110, 4604-4609.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 4604-4609
    • Xiong, Y.1    Zhao, K.2    Wu, J.3    Xu, Z.4    Jin, S.5    Zhang, Y.Q.6
  • 37
    • 67749133983 scopus 로고    scopus 로고
    • Cytoskeletal pathologies of Alzheimer disease
    • Bamburg JR, Bloom GS (2009) Cytoskeletal pathologies of Alzheimer disease. Cell Motil Cytoskeleton 66, 635-649.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 635-649
    • Bamburg, J.R.1    Bloom, G.S.2
  • 39
    • 84863011855 scopus 로고    scopus 로고
    • Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model
    • Lee S, Kim W, Li Z, Hall GF (2012) Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model. Int J Alzheimers Dis 2012, 172837.
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 172837
    • Lee, S.1    Kim, W.2    Li, Z.3    Hall, G.F.4
  • 40
    • 74949109318 scopus 로고    scopus 로고
    • Differential effects of Tau on the integrity and function of neurons essential for learning in Drosophila
    • Kosmidis S, Grammenoudi S, Papanikolopoulou K, Skoulakis EM (2010) Differential effects of Tau on the integrity and function of neurons essential for learning in Drosophila. J Neurosci 30, 464-477.
    • (2010) J Neurosci , vol.30 , pp. 464-477
    • Kosmidis, S.1    Grammenoudi, S.2    Papanikolopoulou, K.3    Skoulakis, E.M.4
  • 42
    • 57649203362 scopus 로고    scopus 로고
    • Dissociation of tau toxicity and phosphorylation: Role of GSK-3beta, MARK and Cdk5 in a Drosophila model
    • Chatterjee S, Sang TK, Lawless GM, Jackson GR (2009) Dissociation of tau toxicity and phosphorylation: Role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum Mol Genet 18, 164-177.
    • (2009) Hum Mol Genet , vol.18 , pp. 164-177
    • Chatterjee, S.1    Sang, T.K.2    Lawless, G.M.3    Jackson, G.R.4
  • 43
    • 84979083907 scopus 로고    scopus 로고
    • Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3
    • Povellato G, Tuxworth RI, Hanger DP, Tear G (2014) Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3. Biol Open 3, 1-11.
    • (2014) Biol Open , vol.3 , pp. 1-11
    • Povellato, G.1    Tuxworth, R.I.2    Hanger, D.P.3    Tear, G.4
  • 46
    • 0027469909 scopus 로고
    • A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau
    • Wang Y, Loomis PA, Zinkowski RP, Binder LI (1993) A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau. J Cell Biol 121, 257-267. (Pubitemid 23110871)
    • (1993) Journal of Cell Biology , vol.121 , Issue.2 , pp. 257-267
    • Wang, Y.1    Loomis, P.A.2    Zinkowski, R.P.3    Binder, L.I.4
  • 47
    • 0029161154 scopus 로고
    • Localization and in situ phosphorylation state of nuclear tau
    • Greenwood JA, Johnson GVW (1995) Localization and in situ phosphorylation state of nuclear tau. Exp Cell Res 220, 332-337.
    • (1995) Exp Cell Res , vol.220 , pp. 332-337
    • Greenwood, J.A.1    Johnson, G.V.W.2
  • 48
    • 0343603369 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic tau proteins from human nonneuronal cells share common structural and functional features with brain tau
    • Cross DC, Munoz JP, Hernandez P, Maccioni RB (2000) Nuclear and cytoplasmic tau proteins from human nonneuronal cells share common structural and functional features with brain tau. J Cell Biochem 78, 305-317. (Pubitemid 30415906)
    • (2000) Journal of Cellular Biochemistry , vol.78 , Issue.2 , pp. 305-317
    • Cross, D.C.1    Munoz, J.P.2    Hernandez, P.3    Maccioni, R.B.4
  • 49
    • 33745184916 scopus 로고    scopus 로고
    • Tau protein binds to pericentromeric DNA: A putative role for nuclear tau in nucleolar organization
    • DOI 10.1242/jcs.02907
    • Sjoberg MK, Shestakova E, Mansuroglu Z, Maccioni RB, Bonnefoy E (2006) Tau protein binds to pericentromeric DNA: A putative role for nuclear tau in nucleolar organization. J Cell Sci 119, 2025-2034. (Pubitemid 43904957)
    • (2006) Journal of Cell Science , vol.119 , Issue.10 , pp. 2025-2034
    • Sjoberg, M.K.1    Shestakova, E.2    Mansuroglu, Z.3    Maccioni, R.B.4    Bonnefoy, E.5
  • 50
    • 0029040690 scopus 로고
    • Presence of tau in isolated nuclei from human brain
    • Brady RM, Zinkowski RP, Binder LI (1995) Presence of tau in isolated nuclei from human brain. Neurobiol Aging 16, 479-486.
    • (1995) Neurobiol Aging , vol.16 , pp. 479-486
    • Brady, R.M.1    Zinkowski, R.P.2    Binder, L.I.3
  • 51
    • 49749097123 scopus 로고    scopus 로고
    • Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation
    • Wei Y, Qu MH, Wang XS, Chen L, Wang DL, Liu Y, Hua Q, He RQ (2008) Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation. PLoS ONE 3, e2600.
    • (2008) PLoS ONE , vol.3
    • Wei, Y.1    Qu, M.H.2    Wang, X.S.3    Chen, L.4    Wang, D.L.5    Liu, Y.6    Hua, Q.7    He, R.Q.8
  • 53
    • 77953544705 scopus 로고    scopus 로고
    • New evidences on Tau-DNA interactions and relevance to neurodegeneration
    • Padmaraju V, Indi SS, Rao KS (2010) New evidences on Tau-DNA interactions and relevance to neurodegeneration. Neurochem Int 57, 51-57.
    • (2010) Neurochem Int , vol.57 , pp. 51-57
    • Padmaraju, V.1    Indi, S.S.2    Rao, K.S.3
  • 55
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 Connects glycogen synthase kinase-3β to tau within a brain microtubule-associated tau phosphorylation complex
    • DOI 10.1074/jbc.M211491200
    • Agarwal-Mawal A, Qureshi HY, Cafferty PW, Yuan Z, Han D, Lin R, Paudel HK (2003) 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubuleassociated tau phosphorylation complex. J Biol Chem 278, 12722-12728. (Pubitemid 36800034)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3    Yuan, Z.4    Han, D.5    Lin, R.6    Paudel, H.K.7
  • 57
    • 79961025441 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau
    • Usardi A, Pooler AM, Seereeram A, Reynolds CH, Derkinderen P, Anderton B, Hanger DP, Noble W, Williamson R (2011) Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau. FEBS J 278, 2927-2937.
    • (2011) FEBS J , vol.278 , pp. 2927-2937
    • Usardi, A.1    Pooler, A.M.2    Seereeram, A.3    Reynolds, C.H.4    Derkinderen, P.5    Anderton, B.6    Hanger, D.P.7    Noble, W.8    Williamson, R.9
  • 59
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A
    • DOI 10.1016/S0896-6273(00)80250-0
    • Sontag E, Nunbhakdi-Craig V, Lee G, Bloom GS, Mumby MC (1996) Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron 17, 1201-1207. (Pubitemid 27021104)
    • (1996) Neuron , vol.17 , Issue.6 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 60
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule- associated protein tau
    • DOI 10.1074/jbc.273.34.21901
    • Liao H, Li Y, Brautigan DL, Gundersen GG (1998) Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau. J Biol Chem 273, 21901-21908. (Pubitemid 28405368)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.34 , pp. 21901-21908
    • Liao, H.1    Li, Y.2    Brautigan, D.L.3    Gundersen, G.G.4
  • 62
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt R, Lger J, Lee G (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol 131, 1327-1340.
    • (1995) J Cell Biol , vol.131 , pp. 1327-1340
    • Brandt, R.1    Lger, J.2    Lee, G.3
  • 63
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • DOI 10.1074/jbc.M000389200
    • Maas T, Eidenmuller J, Brandt R (2000) Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem 275, 15733-15740. (Pubitemid 30366871)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15733-15740
    • Maas, T.1    Eidenmuller, J.2    Brandt, R.3
  • 64
    • 17544393297 scopus 로고    scopus 로고
    • Tau dephosphorylation at Tau-1 site correlates with its association to cell membrane
    • DOI 10.1023/A:1007583214722
    • Arrasate M, Perez M, Avila J (2000) Tau dephosphorylation at tau-1 site correlates with its association to cell membrane. Neurochem Res 25, 43-50. (Pubitemid 30074274)
    • (2000) Neurochemical Research , vol.25 , Issue.1 , pp. 43-50
    • Arrasate, M.1    Perez, M.2    Avila, J.3
  • 66
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates β-amyloid-induced neurodegeneration
    • DOI 10.1523/JNEUROSCI.1125-05.2005
    • Park SY, Ferreira A (2005) The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci 25, 5365-5375. (Pubitemid 40770916)
    • (2005) Journal of Neuroscience , vol.25 , Issue.22 , pp. 5365-5375
    • Park, S.-Y.1    Ferreira, A.2
  • 68
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E (1991) Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82, 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 69
    • 80054904670 scopus 로고    scopus 로고
    • Stages of the pathologic process in Alzheimer disease: Age categories from 1 to 100 years
    • Braak H, Thal DR, Ghebremedhin E, Del Tredici K (2011) Stages of the pathologic process in Alzheimer disease: Age categories from 1 to 100 years. J Neuropathol Exp Neurol 70, 960-969.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 960-969
    • Braak, H.1    Thal, D.R.2    Ghebremedhin, E.3    Del Tredici, K.4
  • 78
    • 84980053087 scopus 로고    scopus 로고
    • Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model
    • Le MN, Kim W, Lee S, McKee AC, Hall GF (2012) Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model. Am J Neurodegener Dis 1, 316-333.
    • (2012) Am J Neurodegener Dis , vol.1 , pp. 316-333
    • Le, M.N.1    Kim, W.2    Lee, S.3    McKee, A.C.4    Hall, G.F.5
  • 79
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B, Diamond MI (2010) Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 11, 155-159.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 80
    • 84862003756 scopus 로고    scopus 로고
    • Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes
    • Santa-Maria I, Varghese M, Ksiezak-Reding H, Dzhun A, Wang J, Pasinetti GM (2012) Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes. J Biol Chem 287, 20522-20533.
    • (2012) J Biol Chem , vol.287 , pp. 20522-20533
    • Santa-Maria, I.1    Varghese, M.2    Ksiezak-Reding, H.3    Dzhun, A.4    Wang, J.5    Pasinetti, G.M.6
  • 84
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • DOI 10.1016/S0968-0004(03)00031-8
    • BeltingM(2003) Heparan sulfate proteoglycan as a plasma membrane carrier. Trends Biochem Sci 28, 145-151. (Pubitemid 36293852)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.3 , pp. 145-151
    • Belting, M.1
  • 86
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type Tau fibrils specified by templated conformation change
    • Frost B, Ollesch J, Wille H, Diamond MI (2009) Conformational diversity of wild-type Tau fibrils specified by templated conformation change. J Biol Chem 284, 3546-3551.
    • (2009) J Biol Chem , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 87
    • 79959945013 scopus 로고    scopus 로고
    • Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture
    • Garwood CJ, Pooler AM, Atherton J, Hanger DP, Noble W (2011) Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture. Cell Death Dis 2, e167.
    • (2011) Cell Death Dis , vol.2
    • Garwood, C.J.1    Pooler, A.M.2    Atherton, J.3    Hanger, D.P.4    Noble, W.5
  • 88
    • 68849123079 scopus 로고    scopus 로고
    • Accumulation of tau induced in neurites by microglial proinflammatory mediators
    • Gorlovoy P, Larionov S, Pham TT, Neumann H (2009) Accumulation of tau induced in neurites by microglial proinflammatory mediators. FASEB J 23, 2502-2513.
    • (2009) FASEB J , vol.23 , pp. 2502-2513
    • Gorlovoy, P.1    Larionov, S.2    Pham, T.T.3    Neumann, H.4
  • 89
    • 33747862732 scopus 로고    scopus 로고
    • Extracellular tau is toxic to neuronal cells
    • DOI 10.1016/j.febslet.2006.07.078, PII S001457930600946X
    • Gómez-Ramos A, Díaz-Hernández M, Cuadros R, Hernández F, Avila J (2006) Extracellular tau is toxic to neuronal cells. FEBS Lett 580, 4842-4850. (Pubitemid 44286844)
    • (2006) FEBS Letters , vol.580 , Issue.20 , pp. 4842-4850
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Cuadros, R.3    Hernandez, F.4    Avila, J.5
  • 90
    • 84871141635 scopus 로고    scopus 로고
    • Extracellular tau levels are influenced by variability in tau that is associated with tauopathies
    • Karch CM, Jeng AT, Goate AM (2012) Extracellular tau levels are influenced by variability in tau that is associated with tauopathies. J Biol Chem 287, 42751-42762.
    • (2012) J Biol Chem , vol.287 , pp. 42751-42762
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 92
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • Chai X, Dage JL, CitronM(2012) Constitutive secretion of tau protein by an unconventional mechanism. Neurobiol Dis 48, 356-366.
    • (2012) Neurobiol Dis , vol.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 93
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • Pooler AM, Phillips EC, Lau DH, Noble W, Hanger DP (2013) Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep 14, 389-394.
    • (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
  • 94
    • 84893488880 scopus 로고    scopus 로고
    • Tangles, toxicity, and tau secretion inAD-newapproaches to a vexing problem
    • Gendreau KL, Hall GF (2013) Tangles, toxicity, and tau secretion inAD-newapproaches to a vexing problem. Front Neurol 4, 160.
    • (2013) Front Neurol , vol.4 , pp. 160
    • Gendreau, K.L.1    Hall, G.F.2
  • 96
    • 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 MT, Avila J (2008) Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Mol Cell Neurosci 37, 673-681.
    • (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
  • 98
    • 84883517531 scopus 로고    scopus 로고
    • The involvement of cholinergic neurons in the spreading of tau pathology
    • Simon D, Hernandez F, Avila J (2013) The involvement of cholinergic neurons in the spreading of tau pathology. Front Neurol 4, 74.
    • (2013) Front Neurol , vol.4 , pp. 74
    • Simon, D.1    Hernandez, F.2    Avila, J.3
  • 99
    • 77049123465 scopus 로고    scopus 로고
    • Interneuronal transfer of human tau between Lamprey central neurons in situ
    • Kim W, Lee S, Jung C, Ahmed A, Lee G, Hall GF (2010) Interneuronal transfer of human tau between Lamprey central neurons in situ. J Alzheimers Dis 19, 647-664.
    • (2010) J Alzheimers Dis , vol.19 , pp. 647-664
    • Kim, W.1    Lee, S.2    Jung, C.3    Ahmed, A.4    Lee, G.5    Hall, G.F.6
  • 103
    • 67650810148 scopus 로고    scopus 로고
    • Monitoring of brain interstitial total tau and beta amyloid proteins by microdialysis in patients with traumatic brain injury
    • Marklund N, Blennow K, Zetterberg H, Ronne-Engstrom E, Enblad P, Hillered L (2009) Monitoring of brain interstitial total tau and beta amyloid proteins by microdialysis in patients with traumatic brain injury. J Neurosurg 110, 1227-1237.
    • (2009) J Neurosurg , vol.110 , pp. 1227-1237
    • Marklund, N.1    Blennow, K.2    Zetterberg, H.3    Ronne-Engstrom, E.4    Enblad, P.5    Hillered, L.6
  • 104
    • 84860142897 scopus 로고    scopus 로고
    • Tau elevations in the brain extracellular space correlate with reduced amyloid-beta levels and predict adverse clinical outcomes after severe traumatic brain injury
    • Magnoni S, Esparza TJ, ConteV, Carbonara M, Carrabba G, Holtzman DM, Zipfel GJ, Stocchetti N, Brody DL (2012) Tau elevations in the brain extracellular space correlate with reduced amyloid-beta levels and predict adverse clinical outcomes after severe traumatic brain injury. Brain 135, 1268-1280.
    • (2012) Brain , vol.135 , pp. 1268-1280
    • Magnoni, S.1    Esparza, T.J.2    Conte, V.3    Carbonara, M.4    Carrabba, G.5    Holtzman, D.M.6    Zipfel, G.J.7    Stocchetti, N.8    Brody, D.L.9
  • 105
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman S, Kim W, Raya M, Visnick Y, Miro S, Jackson B, McKee AC, Alvarez VE, Lee NC, Hall GF (2012) Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem 287, 3842-3849.
    • (2012) J Biol Chem , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Jackson, B.6    McKee, A.C.7    Alvarez, V.E.8    Lee, N.C.9    Hall, G.F.10
  • 106
    • 44649100169 scopus 로고    scopus 로고
    • Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats
    • DOI 10.1111/j.1471-4159.2008.05321.x
    • Wray S, Saxton M, Anderton BH, Hanger DP (2008) Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats. J Neurochem 105, 2343-2352. (Pubitemid 351782262)
    • (2008) Journal of Neurochemistry , vol.105 , Issue.6 , pp. 2343-2352
    • Wray, S.1    Saxton, M.2    Anderton, B.H.3    Hanger, D.P.4
  • 107
    • 77955943958 scopus 로고    scopus 로고
    • Tau cleavage and tau aggregation in neurodegenerative disease
    • Hanger DP,Wray S (2010) Tau cleavage and tau aggregation in neurodegenerative disease. Biochem Soc Trans 38, 1016-1020.
    • (2010) Biochem Soc Trans , vol.38 , pp. 1016-1020
    • Hanger, D.P.1    Wray, S.2
  • 109
    • 76549087651 scopus 로고    scopus 로고
    • Transition of tau protein from disordered to misordered in Alzheimer's disease
    • Kovacech B, Skrabana R, Novak M (2010) Transition of tau protein from disordered to misordered in Alzheimer's disease. Neurodegener Dis 7, 24-27.
    • (2010) Neurodegener Dis , vol.7 , pp. 24-27
    • Kovacech, B.1    Skrabana, R.2    Novak, M.3
  • 110
    • 24344508845 scopus 로고    scopus 로고
    • Caspase-cleaved tau accumulation in neurodegenerative diseases associated with tau and α-synuclein pathology
    • DOI 10.1007/s00401-005-1027-3
    • Newman J, Rissman RA, Sarsoza F, Kim RC, Dick M, Bennett DA, Cotman CW, Rohn TT, Head E(2005) Caspasecleaved tau accumulation in neurodegenerative diseases associated with tau and alpha-synuclein pathology. Acta Neuropathol 110, 135-144. (Pubitemid 41245202)
    • (2005) Acta Neuropathologica , vol.110 , Issue.2 , pp. 135-144
    • Newman, J.1    Rissman, R.A.2    Sarsoza, F.3    Kim, R.C.4    Dick, M.5    Bennett, D.A.6    Cotman, C.W.7    Rohn, T.T.8    Head, E.9
  • 111
    • 0032589031 scopus 로고    scopus 로고
    • Identitication of synaptic vesicle, pre- and postsynaptic proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing
    • Davidsson P, Puchades M, Blennow K (1999) Identification of synaptic vesicle, pre-and postsynaptic proteins in human cerebrospinal fluid using liquid-phase isoelectric focusing. Electrophoresis 20, 431-437. (Pubitemid 29183400)
    • (1999) Electrophoresis , vol.20 , Issue.3 , pp. 431-437
    • Davidsson, P.1    Puchades, M.2    Blennow, K.3
  • 113
    • 77949423619 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma biomarkers in Alzheimer disease
    • Blennow K, Hampel H, Weiner M, Zetterberg H (2010) Cerebrospinal fluid and plasma biomarkers in Alzheimer disease. Nat Rev Neurol 6, 131-144.
    • (2010) Nat Rev Neurol , vol.6 , pp. 131-144
    • Blennow, K.1    Hampel, H.2    Weiner, M.3    Zetterberg, H.4
  • 114
    • 84886509822 scopus 로고    scopus 로고
    • A role for tau at the synapse in Alzheimer's disease pathogenesis
    • Pooler AM, Noble W, Hanger DP (2014) A role for tau at the synapse in Alzheimer's disease pathogenesis. Neuropharmacology 76, 1-8.
    • (2014) Neuropharmacology , vol.76 , pp. 1-8
    • Pooler, A.M.1    Noble, W.2    Hanger, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.