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Volumn 137, Issue 10, 2014, Pages 2834-2846

Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer's disease

Author keywords

Lipid rafts; Tau immunotherapy; Tau pS422 antibody

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ANTIBODY; DRUG DERIVATIVE; MONOCLONAL ANTIBODY; SARCOSINE; SARKOSYL; TAU PROTEIN;

EID: 84908377705     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/awu213     Document Type: Article
Times cited : (162)

References (55)
  • 1
    • 84899944338 scopus 로고    scopus 로고
    • A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity
    • Ahmed Z, Cooper J, Murray TK, Garn K, McNaughton E, Clarke H, et al. A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity. Acta Neuropathol 2014; 127: 667-83.
    • (2014) Acta Neuropathol , vol.127 , pp. 667-683
    • Ahmed, Z.1    Cooper, J.2    Murray, T.K.3    Garn, K.4    McNaughton, E.5    Clarke, H.6
  • 2
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci 2007; 27: 9115-29.
    • (2007) J Neurosci , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 3
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack JC, Schneider A, Mandelkow EM, Hyman BT. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol 2002; 103: 26-35.
    • (2002) Acta Neuropathol , vol.103 , pp. 26-35
    • Augustinack, J.C.1    Schneider, A.2    Mandelkow, E.M.3    Hyman, B.T.4
  • 4
    • 79960563632 scopus 로고    scopus 로고
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain
    • Boutajangout A, Ingadottir J, Davies P, Sigurdsson EM. Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. J Neurochem 2011; 118: 658-67.
    • (2011) J Neurochem , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 5
    • 0344859874 scopus 로고    scopus 로고
    • Phosphorylated serine422 on tau proteins is a pathological epitope found in several diseases with neurofibrillary degeneration
    • Bussiere T, Hof PR, Mailliot C, Brown CD, Caillet-Boudin ML, Perl DP, et al. Phosphorylated serine422 on tau proteins is a pathological epitope found in several diseases with neurofibrillary degeneration. Acta Neuropathol 1999; 97: 221-30.
    • (1999) Acta Neuropathol , vol.97 , pp. 221-230
    • Bussiere, T.1    Hof, P.R.2    Mailliot, C.3    Brown, C.D.4    Caillet-Boudin, M.L.5    Perl, D.P.6
  • 6
    • 84896269359 scopus 로고    scopus 로고
    • Passive immunization with Tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles
    • Castillo-Carranza DL, Sengupta U, Guerrero-Munoz MJ, Lasagna-Reeves CA, Gerson JE, Singh G, et al. Passive immunization with Tau oligomer monoclonal antibody reverses tauopathy phenotypes without affecting hyperphosphorylated neurofibrillary tangles. J Neuroscience 2014; 34: 4260-72.
    • (2014) J Neuroscience , vol.34 , pp. 4260-4272
    • Castillo-Carranza, D.L.1    Sengupta, U.2    Guerrero-Munoz, M.J.3    Lasagna-Reeves, C.A.4    Gerson, J.E.5    Singh, G.6
  • 7
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti-Tau antibodies in two transgenic models: Reduction of Tau pathology and delay of disease progression
    • Chai X, Wu S, Murray TK, Kinley R, Cella CV, Sims H, et al. Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. J Biol Chem 2011; 286: 34457-67.
    • (2011) J Biol Chem , vol.286 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3    Kinley, R.4    Cella, C.V.5    Sims, H.6
  • 9
    • 0347088995 scopus 로고    scopus 로고
    • Motor training compensates for cerebellar dysfunctions caused by oligodendrocyte ablation
    • Collin L, Usiello A, Erbs E, Mathis C, Borrelli E. Motor training compensates for cerebellar dysfunctions caused by oligodendrocyte ablation. Proc Natl Acad Sci USA 2004; 101: 325-30.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 325-330
    • Collin, L.1    Usiello, A.2    Erbs, E.3    Mathis, C.4    Borrelli, E.5
  • 10
    • 49149109927 scopus 로고    scopus 로고
    • Is Tau aggregation toxic or protective?
    • Congdon EE, Duff KE. Is Tau aggregation toxic or protective? J Alzheimers Dis 2008; 14: 453-7.
    • (2008) J Alzheimers Dis , vol.14 , pp. 453-457
    • Congdon, E.E.1    Duff, K.E.2
  • 11
    • 84890282160 scopus 로고    scopus 로고
    • Antibody uptake into neurons occurs primarily via clathrin-dependent Fcg receptor endocytosis and is a prerequisite for acute Tau protein clearance
    • Congdon EE, Gu J, Sait HB, Sigurdsson EM. Antibody uptake into neurons occurs primarily via clathrin-dependent Fcg receptor endocytosis and is a prerequisite for acute Tau protein clearance. J Biol Chem 2013; 288: 35452-65.
    • (2013) J Biol Chem , vol.288 , pp. 35452-35465
    • Congdon, E.E.1    Gu, J.2    Sait, H.B.3    Sigurdsson, E.M.4
  • 12
    • 84876908676 scopus 로고    scopus 로고
    • Tau passive immunotherapy in mutant P301L mice: Antibody affinity versus specificity
    • d'Abramo C, Acker CM, Jimenez HT, Davies P. Tau passive immunotherapy in mutant P301L mice: antibody affinity versus specificity. PLoS One 2013; 8: e62402.
    • (2013) PLoS One , vol.8 , pp. e62402
    • D'Abramo, C.1    Acker, C.M.2    Jimenez, H.T.3    Davies, P.4
  • 14
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein
    • Eidenmuller J, Fath T, Maas T, Pool M, Sontag E, Brandt R. Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. Biochem J 2001; 357 (Pt 3): 759-67.
    • (2001) Biochem J , vol.357 , pp. 759-767
    • Eidenmuller, J.1    Fath, T.2    Maas, T.3    Pool, M.4    Sontag, E.5    Brandt, R.6
  • 15
    • 0034624227 scopus 로고    scopus 로고
    • Immature human NT2 cells grafted into mouse brain differentiate into neuronal and glial cell types
    • Ferrari A, Ehler E, Nitsch RM, Gotz J. Immature human NT2 cells grafted into mouse brain differentiate into neuronal and glial cell types. FEBS Lett 2000; 486: 121-5.
    • (2000) FEBS Lett , vol.486 , pp. 121-125
    • Ferrari, A.1    Ehler, E.2    Nitsch, R.M.3    Gotz, J.4
  • 16
    • 0141960033 scopus 로고    scopus 로고
    • Beta-Amyloid induces paired helical filament-like tau filaments in tissue culture
    • Ferrari A, Hoerndli F, Baechi T, Nitsch RM, Götz J. beta-Amyloid induces paired helical filament-like tau filaments in tissue culture. J Biol Chem 2003; 278: 40162-8.
    • (2003) J Biol Chem , vol.278 , pp. 40162-40168
    • Ferrari, A.1    Hoerndli, F.2    Baechi, T.3    Nitsch, R.M.4    Götz, J.5
  • 17
    • 84876722731 scopus 로고    scopus 로고
    • Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis
    • Freeman D, Cedillos R, Choyke S, Lukic Z, McGuire K, Marvin S, et al. Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis. PLoS One 2013; 8: e62143.
    • (2013) PLoS One , vol.8 , pp. e62143
    • Freeman, D.1    Cedillos, R.2    Choyke, S.3    Lukic, Z.4    McGuire, K.5    Marvin, S.6
  • 18
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost B, Diamond MI. Prion-like mechanisms in neurodegenerative diseases. Nat Rev Neurosci 2010; 11: 155-9.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 19
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • Goedert M, Clavaguera F, Tolnay M. The propagation of prion-like protein inclusions in neurodegenerative diseases. Trends Neurosci 2010; 33: 317-25.
    • (2010) Trends Neurosci , vol.33 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 20
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L Tau
    • Götz J, Chen F, Barmettler R, Nitsch RM. Tau filament formation in transgenic mice expressing P301L Tau. J Biol Chem 2001; 276: 529-34.
    • (2001) J Biol Chem , vol.276 , pp. 529-534
    • Götz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 21
    • 0343570140 scopus 로고    scopus 로고
    • Distinct role of protein phosphatase 2A subunit Calpha in the regulation of E-cadherin and beta-catenin during development
    • Götz J, Probst A, Mistl C, Nitsch RM, Ehler E. Distinct role of protein phosphatase 2A subunit Calpha in the regulation of E-cadherin and beta-catenin during development. Mech Dev 2000; 93: 83-93.
    • (2000) Mech Dev , vol.93 , pp. 83-93
    • Götz, J.1    Probst, A.2    Mistl, C.3    Nitsch, R.M.4    Ehler, E.5
  • 22
    • 84857404010 scopus 로고    scopus 로고
    • Novel screening cascade identifies MKK4 as key kinase regulating Tau phosphorylation at Ser422
    • Grueninger F, Bohrmann B, Christensen K, Graf M, Roth D, Czech C. Novel screening cascade identifies MKK4 as key kinase regulating Tau phosphorylation at Ser422. Mol Cell Biochem 2011; 357: 199-207.
    • (2011) Mol Cell Biochem , vol.357 , pp. 199-207
    • Grueninger, F.1    Bohrmann, B.2    Christensen, K.3    Graf, M.4    Roth, D.5    Czech, C.6
  • 24
    • 84887837879 scopus 로고    scopus 로고
    • Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathology
    • Gu J, Congdon EE, Sigurdsson EM. Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathology. J Biol Chem 2013; 288: 33081-95.
    • (2013) J Biol Chem , vol.288 , pp. 33081-33095
    • Gu, J.1    Congdon, E.E.2    Sigurdsson, E.M.3
  • 25
    • 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 AL, Cahill ME, Cryns VL, Reynolds MR, Berry RW, Binder LI. Pseudophosphorylation of Tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J Neurochem 2006; 97: 1005-14.
    • (2006) J Neurochem , vol.97 , pp. 1005-1014
    • Guillozet-Bongaarts, A.L.1    Cahill, M.E.2    Cryns, V.L.3    Reynolds, M.R.4    Berry, R.W.5    Binder, L.I.6
  • 26
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo JL, Lee VM. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 2011; 286: 15317-31.
    • (2011) J Biol Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 27
    • 0026546599 scopus 로고
    • An 'anatomical cascade hypothesis' for Alzheimer's disease
    • Hardy J. An 'anatomical cascade hypothesis' for Alzheimer's disease. Trends Neurosci 1992; 15: 200-1.
    • (1992) Trends Neurosci , vol.15 , pp. 200-201
    • Hardy, J.1
  • 29
    • 84859194796 scopus 로고    scopus 로고
    • Interaction of tau protein with model lipid membranes induces tau structural compaction and membrane disruption
    • Jones EM, Dubey M, Camp PJ, Vernon BC, Biernat J, Mandelkow E, et al. Interaction of tau protein with model lipid membranes induces tau structural compaction and membrane disruption. Biochemistry 2012; 51: 2539-50.
    • (2012) Biochemistry , vol.51 , pp. 2539-2550
    • Jones, E.M.1    Dubey, M.2    Camp, P.J.3    Vernon, B.C.4    Biernat, J.5    Mandelkow, E.6
  • 30
    • 33748374920 scopus 로고    scopus 로고
    • Lysosome membrane lipid microdomains: Novel regulators of chaperone-mediated autophagy
    • Kaushik S, Massey AC, Cuervo AM. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J 2006; 25: 3921-33.
    • (2006) EMBO J , vol.25 , pp. 3921-3933
    • Kaushik, S.1    Massey, A.C.2    Cuervo, A.M.3
  • 31
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein e and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease
    • Kawarabayashi T, Shoji M, Younkin LH, Wen-Lang L, Dickson DW, Murakami T, et al. Dimeric amyloid beta protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease. J Neurosci 2004; 24: 3801-9.
    • (2004) J Neurosci , vol.24 , pp. 3801-3809
    • Kawarabayashi, T.1    Shoji, M.2    Younkin, L.H.3    Wen-Lang, L.4    Dickson, D.W.5    Murakami, T.6
  • 32
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • Kins S, Kurosinski P, Nitsch RM, Götz J. Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am J Pathol 2003; 163: 833-43.
    • (2003) Am J Pathol , vol.163 , pp. 833-843
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Götz, J.4
  • 33
  • 34
    • 84865607168 scopus 로고    scopus 로고
    • Mechanistic studies of antibody-mediated clearance of Tau aggregates using an ex vivo brain slice model
    • Krishnamurthy PK, Deng Y, Sigurdsson EM. Mechanistic studies of antibody-mediated clearance of Tau aggregates using an ex vivo brain slice model. Front Psychiatry 2011; 2: 59.
    • (2011) Front Psychiatry , vol.2 , pp. 59
    • Krishnamurthy, P.K.1    Deng, Y.2    Sigurdsson, E.M.3
  • 35
    • 80052798018 scopus 로고    scopus 로고
    • Identification of GPCR localization in detergent resistant membranes
    • Kumari R, Francesconi A. Identification of GPCR localization in detergent resistant membranes. Methods Mol Biol 2011; 746: 411-23.
    • (2011) Methods Mol Biol , vol.746 , pp. 411-423
    • Kumari, R.1    Francesconi, A.2
  • 36
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neuro-fibrillary tangles in Alzheimer's disease: Possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I. Early accumulation of p62 in neuro-fibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol Appl Neurobiol 2002; 28: 228-37.
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 37
    • 3442884830 scopus 로고    scopus 로고
    • Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau
    • Lin WL, Lewis J, Yen SH, Hutton M, Dickson DW. Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau. J Neurocytol 2003; 32: 1091-105.
    • (2003) J Neurocytol , vol.32 , pp. 1091-1105
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3    Hutton, M.4    Dickson, D.W.5
  • 39
    • 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
    • Maas T, Eidenmuller J, Brandt R. Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem 2000; 275: 15733-40.
    • (2000) J Biol Chem , vol.275 , pp. 15733-15740
    • Maas, T.1    Eidenmuller, J.2    Brandt, R.3
  • 40
    • 84860215480 scopus 로고    scopus 로고
    • Correlation of Alzheimer disease neuropathologic changes with cognitive status: A review of the literature
    • Nelson PT, Alafuzoff I, Bigio EH, Bouras C, Braak H, Cairns NJ, et al. Correlation of Alzheimer disease neuropathologic changes with cognitive status: a review of the literature. J Neuropathol Exp Neurol 2012; 71: 362-81.
    • (2012) J Neuropathol Exp Neurol , vol.71 , pp. 362-381
    • Nelson, P.T.1    Alafuzoff, I.2    Bigio, E.H.3    Bouras, C.4    Braak, H.5    Cairns, N.J.6
  • 41
    • 57449095649 scopus 로고    scopus 로고
    • Expression of transgenic APP mRNA is the key determinant for beta-amyloid deposition in PS2APP transgenic mice
    • Ozmen L, Albientz A, Czech C, Jacobsen H. Expression of transgenic APP mRNA is the key determinant for beta-amyloid deposition in PS2APP transgenic mice. Neurodegener Dis 2009; 6: 29-36.
    • (2009) Neurodegener Dis , vol.6 , pp. 29-36
    • Ozmen, L.1    Albientz, A.2    Czech, C.3    Jacobsen, H.4
  • 42
    • 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: 23063-76.
    • (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
  • 43
    • 27144469504 scopus 로고    scopus 로고
    • Different tau epitopes define Abeta42-mediated tau insolubility
    • Pennanen L, Götz J. Different Tau epitopes define Abeta42-mediated tau insolubility. Biochem Biophys Res Commun 2005; 337: 1097-101.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 1097-1101
    • Pennanen, L.1    Götz, J.2
  • 44
    • 77955941947 scopus 로고    scopus 로고
    • Functional implications of the association of tau with the plasma membrane
    • Pooler AM, Hanger DP. Functional implications of the association of tau with the plasma membrane. Biochem Soc Trans 2010; 38: 1012-5.
    • (2010) Biochem Soc Trans , vol.38 , pp. 1012-1015
    • Pooler, A.M.1    Hanger, D.P.2
  • 45
    • 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. Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep 2013; 14: 389-94.
    • (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
  • 46
    • 54249156984 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies
    • Sigurdsson EM. Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies. J Alzheimers Dis 2008; 15: 157-68.
    • (2008) J Alzheimers Dis , vol.15 , pp. 157-168
    • Sigurdsson, E.M.1
  • 48
    • 79955073961 scopus 로고    scopus 로고
    • Lipid rafts: Signaling and sorting platforms of cells and their roles in cancer
    • Staubach S, Hanisch FG. Lipid rafts: signaling and sorting platforms of cells and their roles in cancer. Expert Rev Proteomics 2011; 8: 263-77.
    • (2011) Expert Rev Proteomics , vol.8 , pp. 263-277
    • Staubach, S.1    Hanisch, F.G.2
  • 49
  • 50
    • 80055022386 scopus 로고    scopus 로고
    • Progression of tau pathology in cholinergic Basal forebrain neurons in mild cognitive impairment and Alzheimer's disease
    • Vana L, Kanaan NM, Ugwu IC, Wuu J, Mufson EJ, Binder LI. Progression of tau pathology in cholinergic Basal forebrain neurons in mild cognitive impairment and Alzheimer's disease. Am J Pathol 2011; 179: 2533-50.
    • (2011) Am J Pathol , vol.179 , pp. 2533-2550
    • Vana, L.1    Kanaan, N.M.2    Ugwu, I.C.3    Wuu, J.4    Mufson, E.J.5    Binder, L.I.6
  • 51
    • 77953280950 scopus 로고    scopus 로고
    • Membrane rafts in Alzheimer's disease betaamyloid production
    • Vetrivel KS, Thinakaran G. Membrane rafts in Alzheimer's disease betaamyloid production. Biochim Biophys Acta 2010; 1801: 860-7.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 860-867
    • Vetrivel, K.S.1    Thinakaran, G.2
  • 52
  • 53
    • 84875279731 scopus 로고    scopus 로고
    • The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
    • Wegmann S, Medalsy ID, Mandelkow E, Muller DJ. The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush. Proc Natl Acad Sci USA 2013; 110: E313-21.
    • (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
  • 54
    • 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, Kfoury N, Jiang H, Mahan TE, Ma S, Maloney SE, et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 2013; 80: 402-14.
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1    Kfoury, N.2    Jiang, H.3    Mahan, T.E.4    Ma, S.5    Maloney, S.E.6
  • 55
    • 59649088562 scopus 로고    scopus 로고
    • Monitoring autophagy in Alzheimer's disease and related neurodegenerative diseases
    • Yang DS, Lee JH, Nixon RA. Monitoring autophagy in Alzheimer's disease and related neurodegenerative diseases. Methods Enzymol 2009; 453: 111-44.
    • (2009) Methods Enzymol , vol.453 , pp. 111-144
    • Yang, D.S.1    Lee, J.H.2    Nixon, R.A.3


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