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Volumn 21, Issue 12, 2016, Pages 1790-1798

Co-expression of truncated and full-length tau induces severe neurotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

DOXYCYCLINE; TAU PROTEIN; TETRACYCLINE; ISOPROTEIN;

EID: 84989928964     PISSN: 13594184     EISSN: 14765578     Source Type: Journal    
DOI: 10.1038/mp.2015.228     Document Type: Article
Times cited : (43)

References (65)
  • 1
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini MG, Goedert M. Tau pathology and neurodegeneration. Lancet Neurol 2013; 12: 609-622
    • (2013) Lancet Neurol , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 2
    • 84901036009 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau at synapses in Alzheimer's disease
    • Spires-Jones TL, Hyman BT. The intersection of amyloid beta and tau at synapses in Alzheimer's disease. Neuron 2014; 82: 756-771
    • (2014) Neuron , vol.82 , pp. 756-771
    • Spires-Jones, T.L.1    Hyman, B.T.2
  • 3
    • 84896719812 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration through global chromatin relaxation
    • Frost B, Hemberg M, Lewis J, Feany MB. Tau promotes neurodegeneration through global chromatin relaxation. Nat Neurosci 2014; 17: 357-366
    • (2014) Nat Neurosci , vol.17 , pp. 357-366
    • Frost, B.1    Hemberg, M.2    Lewis, J.3    Feany, M.B.4
  • 4
    • 84922392905 scopus 로고    scopus 로고
    • Asparagine endopeptidase cleaves tau and promotes neurodegeneration
    • Rosenmann H. Asparagine endopeptidase cleaves tau and promotes neurodegeneration. Nat Med 2014; 20: 1236-1238
    • (2014) Nat Med , vol.20 , pp. 1236-1238
    • Rosenmann, H.1
  • 5
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M. The amyloid state of proteins in human diseases. Cell 2012; 148: 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 6
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of amyloid beta-protein and amyloid deposits in Alzheimer disease
    • Masters CL, Selkoe DJ. Biochemistry of amyloid beta-protein and amyloid deposits in Alzheimer disease. Cold Spring Harb Perspect Med 2012; 2: a006262
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 7
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • Vidal R, Frangione B, Rostagno A, Mead S, Revesz T, Plant G, et al. A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 1999; 399: 776-781
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5    Plant, G.6
  • 8
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba M, Nakajo S, Tu PH, Tomita T, Nakaya K, Lee VM, et al. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am J Pathol 1998; 152: 879-884
    • (1998) Am J Pathol , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6
  • 10
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006; 314: 130-133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 11
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 2006; 351: 602-611
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5    Mori, H.6
  • 12
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka T, Kametani F, Arai T, Akiyama H, Hasegawa M. Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum Mol Genet 2009; 18: 3353-3364
    • (2009) Hum Mol Genet , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 13
    • 84876832401 scopus 로고    scopus 로고
    • Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway
    • Brower CS, Piatkov KI, Varshavsky A. Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway. Mol Cell 2013; 50: 161-171
    • (2013) Mol Cell , vol.50 , pp. 161-171
    • Brower, C.S.1    Piatkov, K.I.2    Varshavsky, A.3
  • 19
    • 84949032533 scopus 로고    scopus 로고
    • The twenty-four KDa C-terminal tau fragment increases with aging in tauopathy mice: Implications of prion-like properties
    • Matsumoto SE, Motoi Y, Ishiguro K, Tabira T, Kametani F, Hasegawa M, et al. The twenty-four KDa C-terminal tau fragment increases with aging in tauopathy mice: implications of prion-like properties. Hum Mol Genet 2015; 24: 6403-6416
    • (2015) Hum Mol Genet , vol.24 , pp. 6403-6416
    • Matsumoto, S.E.1    Motoi, Y.2    Ishiguro, K.3    Tabira, T.4    Kametani, F.5    Hasegawa, M.6
  • 20
    • 84878078532 scopus 로고    scopus 로고
    • An enzyme-generated fragment of tau measured in serum shows an inverse correlation to cognitive function
    • Henriksen K, Wang Y, Sorensen MG, Barascuk N, Suhy J, Pedersen JT, et al. An enzyme-generated fragment of tau measured in serum shows an inverse correlation to cognitive function. PLoS One 2013; 8: e64990
    • (2013) Plos One , vol.8 , pp. e64990
    • Henriksen, K.1    Wang, Y.2    Sorensen, M.G.3    Barascuk, N.4    Suhy, J.5    Pedersen, J.T.6
  • 21
    • 78149391828 scopus 로고    scopus 로고
    • Alzheimer disease: Caspases first
    • Avila J. Alzheimer disease: caspases first. Nat Rev Neurol 2010; 6: 587-588
    • (2010) Nat Rev Neurol , vol.6 , pp. 587-588
    • Avila, J.1
  • 22
    • 84910669129 scopus 로고    scopus 로고
    • Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease
    • Zhang Z, Song M, Liu X, Kang SS, Kwon IS, Duong DM, et al. Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease. Nat Med 2014; 20: 1254-1262
    • (2014) Nat Med , vol.20 , pp. 1254-1262
    • Zhang, Z.1    Song, M.2    Liu, X.3    Kang, S.S.4    Kwon, I.S.5    Duong, D.M.6
  • 23
    • 38749144389 scopus 로고    scopus 로고
    • Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy
    • Delobel P, Lavenir I, Fraser G, Ingram E, Holzer M, Ghetti B, et al. Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy. Am J Pathol 2008; 172: 123-131
    • (2008) Am J Pathol , vol.172 , pp. 123-131
    • Delobel, P.1    Lavenir, I.2    Fraser, G.3    Ingram, E.4    Holzer, M.5    Ghetti, B.6
  • 24
    • 80052163592 scopus 로고    scopus 로고
    • Immunoelectron microscopic and biochemical studies of caspase-cleaved tau in a mouse model of tauopathy
    • Lin WL, Dickson DW, Sahara N. Immunoelectron microscopic and biochemical studies of caspase-cleaved tau in a mouse model of tauopathy. J Neuropathol Exp Neurol 2011; 70: 779-787
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 779-787
    • Lin, W.L.1    Dickson, D.W.2    Sahara, N.3
  • 25
    • 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 CM, Crowther RA, Walker JE, 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 1988; 85: 4051-4055
    • (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
  • 26
  • 27
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M, Spillantini MG, Cairns NJ, Crowther RA. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 1992; 8: 159-168
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 28
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • Abraha A, Ghoshal N, Gamblin TC, Cryns V, Berry RW, Kuret J, et al. C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J Cell Sci 2000; 113: 3737-3745
    • (2000) J Cell Sci , vol.113 , pp. 3737-3745
    • Abraha, A.1    Ghoshal, N.2    Gamblin, T.C.3    Cryns, V.4    Berry, R.W.5    Kuret, J.6
  • 30
    • 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 YP, Biernat J, Pickhardt M, Mandelkow E, Mandelkow EM. 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 2007; 104: 10252-10257
    • (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
  • 32
    • 0036850725 scopus 로고    scopus 로고
    • Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein
    • Allen B, Ingram E, Takao M, Smith MJ, Jakes R, Virdee K, et al. Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein. J Neurosci 2002; 22: 9340-9351
    • (2002) J Neurosci , vol.22 , pp. 9340-9351
    • Allen, B.1    Ingram, E.2    Takao, M.3    Smith, M.J.4    Jakes, R.5    Virdee, K.6
  • 33
    • 16944366420 scopus 로고    scopus 로고
    • Endogenous serine protease inhibitor modulates epileptic activity and hippocampal long-term potentiation
    • Luthi A, Putten H, Botteri FM, Mansuy IM, Meins M, Frey U, et al. Endogenous serine protease inhibitor modulates epileptic activity and hippocampal long-term potentiation. J Neurosci 1997; 17: 4688-4699
    • (1997) J Neurosci , vol.17 , pp. 4688-4699
    • Luthi, A.1    Putten, H.2    Botteri, F.M.3    Mansuy, I.M.4    Meins, M.5    Frey, U.6
  • 34
    • 84855472423 scopus 로고    scopus 로고
    • Mutant TDP-43 in motor neurons promotes the onset and progression of ALS in rats
    • Huang C, Tong J, Bi F, Zhou H, Xia XG. Mutant TDP-43 in motor neurons promotes the onset and progression of ALS in rats. J Clin Invest 2012; 122: 107-118
    • (2012) J Clin Invest , vol.122 , pp. 107-118
    • Huang, C.1    Tong, J.2    Bi, F.3    Zhou, H.4    Xia, X.G.5
  • 35
    • 78751683605 scopus 로고    scopus 로고
    • Impaired muscle growth and response to insulin-like growth factor 1 in dysferlinmediated muscular dystrophy
    • Demonbreun AR, Fahrenbach JP, Deveaux K, Earley JU, Pytel P, McNally EM. Impaired muscle growth and response to insulin-like growth factor 1 in dysferlinmediated muscular dystrophy. Hum Mol Genet 2011; 20: 779-789
    • (2011) Hum Mol Genet , vol.20 , pp. 779-789
    • Demonbreun, A.R.1    Fahrenbach, J.P.2    Deveaux, K.3    Earley, J.U.4    Pytel, P.5    McNally, E.M.6
  • 39
    • 84861189566 scopus 로고    scopus 로고
    • First transgenic rat model developing progressive cortical neurofibrillary tangles
    • Filipcik P, Zilka N, Bugos O, Kucerak J, Koson P, Novak P, et al. First transgenic rat model developing progressive cortical neurofibrillary tangles. Neurobiol Aging 2012; 33: 1448-1456
    • (2012) Neurobiol Aging , vol.33 , pp. 1448-1456
    • Filipcik, P.1    Zilka, N.2    Bugos, O.3    Kucerak, J.4    Koson, P.5    Novak, P.6
  • 42
    • 84883502695 scopus 로고    scopus 로고
    • Formation and propagation of tau oligomeric seeds
    • Gerson JE, Kayed R. Formation and propagation of tau oligomeric seeds. Front Neurol 2013; 4: 93
    • (2013) Front Neurol , vol.4 , pp. 93
    • Gerson, J.E.1    Kayed, R.2
  • 43
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
    • Maeda S, Sahara N, Saito Y, Murayama S, Ikai A, Takashima A. Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer's disease. Neurosci Res 2006; 54: 197-201
    • (2006) Neurosci Res , vol.54 , pp. 197-201
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, S.4    Ikai, A.5    Takashima, A.6
  • 44
    • 79959571777 scopus 로고    scopus 로고
    • Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease
    • Patterson KR, Remmers C, Fu Y, Brooker S, Kanaan NM, Vana L, et al. Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J Biol Chem 2011; 286: 23063-23076
    • (2011) J Biol Chem , vol.286 , pp. 23063-23076
    • Patterson, K.R.1    Remmers, C.2    Fu, Y.3    Brooker, S.4    Kanaan, N.M.5    Vana, L.6
  • 46
    • 0042697305 scopus 로고    scopus 로고
    • Tripletransgenic model of Alzheimer's disease with plaques and tangles: Intracellular Abeta and synaptic dysfunction
    • Oddo S, Caccamo A, Shepherd JD, Murphy MP, Golde TE, Kayed R, et al. Tripletransgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron 2003; 39: 409-421
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 47
    • 33646519920 scopus 로고    scopus 로고
    • Regionspecific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • Spires TL, Orne JD, SantaCruz K, Pitstick R, Carlson GA, Ashe KH, et al. Regionspecific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy. Am J Pathol 2006; 168: 1598-1607
    • (2006) Am J Pathol , vol.168 , pp. 1598-1607
    • Spires, T.L.1    Orne, J.D.2    SantaCruz, K.3    Pitstick, R.4    Carlson, G.A.5    Ashe, K.H.6
  • 48
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • Berger Z, Roder H, Hanna A, Carlson A, Rangachari V, Yue M, et al. Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J Neurosci 2007; 27: 3650-3662
    • (2007) J Neurosci , vol.27 , pp. 3650-3662
    • Berger, Z.1    Roder, H.2    Hanna, A.3    Carlson, A.4    Rangachari, V.5    Yue, M.6
  • 50
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 2005; 309: 476-481
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 51
    • 84896697812 scopus 로고    scopus 로고
    • Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
    • Clavaguera F, Hench J, Lavenir I, Schweighauser G, Frank S, Goedert M, et al. Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice. Acta Neuropathol 2014; 127: 299-301
    • (2014) Acta Neuropathol , vol.127 , pp. 299-301
    • Clavaguera, F.1    Hench, J.2    Lavenir, I.3    Schweighauser, G.4    Frank, S.5    Goedert, M.6
  • 54
    • 0025345913 scopus 로고
    • Relative abundance of tau and neurofilament epitopes in hippocampal neurofibrillary tangles
    • Schmidt ML, Lee VM, Trojanowski JQ. Relative abundance of tau and neurofilament epitopes in hippocampal neurofibrillary tangles. Am J Pathol 1990; 136: 1069-1075
    • (1990) Am J Pathol , vol.136 , pp. 1069-1075
    • Schmidt, M.L.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 55
    • 0242600546 scopus 로고    scopus 로고
    • Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation
    • Cash AD, Aliev G, Siedlak SL, Nunomura A, Fujioka H, Zhu X, et al. Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation. Am J Pathol 2003; 162: 1623-1627
    • (2003) Am J Pathol , vol.162 , pp. 1623-1627
    • Cash, A.D.1    Aliev, G.2    Siedlak, S.L.3    Nunomura, A.4    Fujioka, H.5    Zhu, X.6
  • 56
    • 0344874553 scopus 로고    scopus 로고
    • Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes
    • Yoshiyama Y, Zhang B, Bruce J, Trojanowski JQ, Lee VM. Reduction of detyrosinated microtubules and Golgi fragmentation are linked to tau-induced degeneration in astrocytes. J Neurosci 2003; 23: 10662-10671
    • (2003) J Neurosci , vol.23 , pp. 10662-10671
    • Yoshiyama, Y.1    Zhang, B.2    Bruce, J.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 57
    • 84863230105 scopus 로고    scopus 로고
    • The microtubulestabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • Zhang B, Carroll J, Trojanowski JQ, Yao Y, Iba M, Potuzak JS, et al. The microtubulestabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci 2012; 32: 3601-3611
    • (2012) J Neurosci , vol.32 , pp. 3601-3611
    • Zhang, B.1    Carroll, J.2    Trojanowski, J.Q.3    Yao, Y.4    Iba, M.5    Potuzak, J.S.6
  • 60
    • 80053289984 scopus 로고    scopus 로고
    • Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain
    • Kopeikina KJ, Carlson GA, Pitstick R, Ludvigson AE, Peters A, Luebke JI, et al. Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain. Am J Pathol 2011; 179: 2071-2082
    • (2011) Am J Pathol , vol.179 , pp. 2071-2082
    • Kopeikina, K.J.1    Carlson, G.A.2    Pitstick, R.3    Ludvigson, A.E.4    Peters, A.5    Luebke, J.I.6
  • 61
    • 17844387375 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons
    • Liazoghli D, Perreault S, Micheva KD, Desjardins M, Leclerc N. Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons. Am J Pathol 2005; 166: 1499-1514
    • (2005) Am J Pathol , vol.166 , pp. 1499-1514
    • Liazoghli, D.1    Perreault, S.2    Micheva, K.D.3    Desjardins, M.4    Leclerc, N.5
  • 62
    • 0030043292 scopus 로고    scopus 로고
    • In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic
    • Stieber A, Mourelatos Z, Gonatas NK. In Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic. Am J Pathol 1996; 148: 415-426
    • (1996) Am J Pathol , vol.148 , pp. 415-426
    • Stieber, A.1    Mourelatos, Z.2    Gonatas, N.K.3
  • 63
    • 84893763207 scopus 로고    scopus 로고
    • Molecular drivers and cortical spread of lateral entorhinal cortex dysfunction in preclinical Alzheimer's disease
    • Khan UA, Liu L, Provenzano FA, Berman DE, Profaci CP, Sloan R, et al. Molecular drivers and cortical spread of lateral entorhinal cortex dysfunction in preclinical Alzheimer's disease. Nat Neurosci 2013; 17: 304-311
    • (2013) Nat Neurosci , vol.17 , pp. 304-311
    • Khan, U.A.1    Liu, L.2    Provenzano, F.A.3    Berman, D.E.4    Profaci, C.P.5    Sloan, R.6
  • 64
    • 84929353239 scopus 로고    scopus 로고
    • Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms
    • Derisbourg M, Leghay C, Chiappetta G, Fernandez-Gomez FJ, Laurent C, Demeyer D, et al. Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms. Sci Rep 2015; 5: 9659
    • (2015) Sci Rep , vol.5 , pp. 9659
    • Derisbourg, M.1    Leghay, C.2    Chiappetta, G.3    Fernandez-Gomez, F.J.4    Laurent, C.5    Demeyer, D.6
  • 65


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