메뉴 건너뛰기




Volumn 10, Issue 3, 2013, Pages 217-228

Immunotherapy for targeting tau pathology in Alzheimer's disease and tauopathies

Author keywords

Efficacy; Immunotherapy; Neurofibrillary tangles; Safety; Tau; Tauopathy

Indexed keywords

ALUMINUM POTASSIUM SULFATE; ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; ANTIBODY; FREUND ADJUVANT; IMMUNOLOGICAL ADJUVANT; KEYHOLE LIMPET HEMOCYANIN; PERTUSSIS TOXIN; PHF1 ANTIBODY; RECOMBINANT TAU PROTEIN; TAU PROTEIN; TAU PROTEIN[195-213]; TAU PROTEIN[207-220]; TAU PROTEIN[224-238]; TAU PROTEIN[379-408]; TAU PROTEIN[395-406]; TAU PROTEIN[420-426]; UNCLASSIFIED DRUG;

EID: 84876873579     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/1567205011310030001     Document Type: Review
Times cited : (49)

References (129)
  • 1
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer betaamyloid peptide
    • Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer betaamyloid peptide. Proc Natl Acad Sci USA 93: 452-455 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 3
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid betapeptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, Burke RL, Games D, Grajeda H, et al. Peripherally administered antibodies against amyloid betapeptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med 6: 916-919 (2000).
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3    Burke, R.L.4    Games, D.5    Grajeda, H.6
  • 4
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition
    • Das P, Murphy MP, Younkin LH, Younkin SG, Golde TE. Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition. Neurobiol Aging 22: 721-727 (2001).
    • (2001) Neurobiol Aging , vol.22 , pp. 721-727
    • Das, P.1    Murphy, M.P.2    Younkin, L.H.3    Younkin, S.G.4    Golde, T.E.5
  • 5
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J, Mathews PM, Jiang Y, Schmidt SD, et al. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 408: 979-982 (2000).
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3    Mathews, P.M.4    Jiang, Y.5    Schmidt, S.D.6
  • 6
    • 0034530636 scopus 로고    scopus 로고
    • Nasal A beta treatment induces anti-A beta antibody production and decreases cerebral amyloid burden in PD-APP mice
    • Lemere CA, Maron R, Spooner ET, Grenfell TJ, Mori C, Desai R, et al. Nasal A beta treatment induces anti-A beta antibody production and decreases cerebral amyloid burden in PD-APP mice. Ann NY Acad Sci 920: 328-331 (2000).
    • (2000) Ann NY Acad Sci , vol.920 , pp. 328-331
    • Lemere, C.A.1    Maron, R.2    Spooner, E.T.3    Grenfell, T.J.4    Mori, C.5    Desai, R.6
  • 7
    • 33646938005 scopus 로고    scopus 로고
    • Short amyloid-beta (Abeta) immunogens reduce cerebral Abeta load and learning deficits in an Alzheimer's disease mouse model in the absence of an Abeta-specific cellular immune response
    • Maier M, Seabrook TJ, Lazo ND, Jiang L, Das P, Janus C, et al. Short amyloid-beta (Abeta) immunogens reduce cerebral Abeta load and learning deficits in an Alzheimer's disease mouse model in the absence of an Abeta-specific cellular immune response. J Neurosci 26: 4717-4728 (2006).
    • (2006) J Neurosci , vol.26 , pp. 4717-4728
    • Maier, M.1    Seabrook, T.J.2    Lazo, N.D.3    Jiang, L.4    Das, P.5    Janus, C.6
  • 8
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan D, Diamond DM, Gottschall PE, Ugen KE, Dickey C, Hardy J, et al. A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 408: 982-985 (2000).
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3    Ugen, K.E.4    Dickey, C.5    Hardy, J.6
  • 9
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimerdisease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, Gordon G, Grajeda H, Guido T, et al. Immunization with amyloid-beta attenuates Alzheimerdisease-like pathology in the PDAPP mouse. Nature 400: 173-177 (1999).
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 10
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice
    • Sigurdsson EM, Scholtzova H, Mehta PD, Frangione B, Wisniewski T. Immunization with a nontoxic/nonfibrillar amyloid-beta homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice. Am J Pathol 159: 439-447 (2001).
    • (2001) Am J Pathol , vol.159 , pp. 439-447
    • Sigurdsson, E.M.1    Scholtzova, H.2    Mehta, P.D.3    Frangione, B.4    Wisniewski, T.5
  • 11
    • 0033801852 scopus 로고    scopus 로고
    • Nasal administration of amyloid-beta peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease
    • Weiner HL, Lemere CA, Maron R, Spooner ET, Grenfell TJ, Mori C, et al. Nasal administration of amyloid-beta peptide decreases cerebral amyloid burden in a mouse model of Alzheimer's disease. Ann Neurol 48: 567-579 (2000).
    • (2000) Ann Neurol , vol.48 , pp. 567-579
    • Weiner, H.L.1    Lemere, C.A.2    Maron, R.3    Spooner, E.T.4    Grenfell, T.J.5    Mori, C.6
  • 12
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: A case report
    • Nicoll JA, Wilkinson D, Holmes C, Steart P, Markham H, Weller RO. Neuropathology of human Alzheimer disease after immunization with amyloid-beta peptide: a case report. Nat Med 9: 448-452 (2003).
    • (2003) Nat Med , vol.9 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 13
    • 77949300796 scopus 로고    scopus 로고
    • 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: A phase 2, double-blind, placebo-controlled, ascending-dose study
    • Rinne JO, Brooks DJ, Rossor MN, Fox NC, Bullock R, Klunk WE, et al. 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: a phase 2, double-blind, placebo-controlled, ascending-dose study. Lancet Neurol 9: 363-372 (2010).
    • (2010) Lancet Neurol , vol.9 , pp. 363-372
    • Rinne, J.O.1    Brooks, D.J.2    Rossor, M.N.3    Fox, N.C.4    Bullock, R.5    Klunk, W.E.6
  • 14
    • 20944448555 scopus 로고    scopus 로고
    • Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial
    • Gilman S, Koller M, Black RS, Jenkins L, Griffith SG, Fox NC, et al. Clinical effects of Abeta immunization (AN1792) in patients with AD in an interrupted trial. Neurology 64: 1553-1562 (2005).
    • (2005) Neurology , vol.64 , pp. 1553-1562
    • Gilman, S.1    Koller, M.2    Black, R.S.3    Jenkins, L.4    Griffith, S.G.5    Fox, N.C.6
  • 15
    • 10744230547 scopus 로고    scopus 로고
    • Hock C 2003 Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo JM, Gilman S, Dartigues JF, Laurent B, Puel M, Kirby LC, et al. Dubois B, Eisner L, Flitman S, Michel BF, Boada M, Frank A, Hock C 2003 Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 61: 46-54 (2003).
    • (2003) Neurology , vol.61 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3    Laurent, B.4    Puel, M.5    Kirby, L.C.6
  • 16
  • 19
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-beta immunotherapy?
    • Lemere CA, Masliah E. Can Alzheimer disease be prevented by amyloid-beta immunotherapy? Nat Rev Neurol 6: 108-119
    • Nat Rev Neurol , vol.6 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 21
    • 47149112621 scopus 로고    scopus 로고
    • Long-term effects of Abeta42 immunisation in Alzheimer's disease: Follow-up of a randomised, placebocontrolled phase I trial
    • Holmes C, Boche D, Wilkinson D, Yadegarfar G, Hopkins V, Bayer A, et al. Long-term effects of Abeta42 immunisation in Alzheimer's disease: follow-up of a randomised, placebocontrolled phase I trial. Lancet 372: 216-223 (2008).
    • (2008) Lancet , vol.372 , pp. 216-223
    • Holmes, C.1    Boche, D.2    Wilkinson, D.3    Yadegarfar, G.4    Hopkins, V.5    Bayer, A.6
  • 22
    • 77951086901 scopus 로고    scopus 로고
    • Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid beta monoclonal antibody in subjects with Alzheimer disease
    • Siemers ER, Friedrich S, Dean RA, Gonzales CR, Farlow MR, Paul SM, Demattos RB. Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid beta monoclonal antibody in subjects with Alzheimer disease. Clin Neuropharmacol 33: 67-73 (2010).
    • (2010) Clin Neuropharmacol , vol.33 , pp. 67-73
    • Siemers, E.R.1    Friedrich, S.2    Dean, R.A.3    Gonzales, C.R.4    Farlow, M.R.5    Paul, S.M.6    Demattos, R.B.7
  • 23
    • 65249163018 scopus 로고    scopus 로고
    • Clinical trials of bapineuzumab, a [-amyloid-targeted immunotherapy in patients with mild to moderate Alzheimer's disease
    • [abstract O3-04-05]
    • Grundman M, Black R. Clinical trials of bapineuzumab, a [-amyloid-targeted immunotherapy in patients with mild to moderate Alzheimer's disease. [abstract O3-04-05] Alzheimers Dementia 4:T166 (2008).
    • (2008) Alzheimers Dementia , vol.4
    • Grundman, M.1    Black, R.2
  • 24
    • 79959944588 scopus 로고    scopus 로고
    • gamma-secretase inhibitors and modulators for the treatment of Alzheimer's disease: Disappointments and hopes
    • Imbimbo BP, Giardina GA. gamma-secretase inhibitors and modulators for the treatment of Alzheimer's disease: disappointments and hopes. Curr Top Med Chem 11: 1555-1570 (2011).
    • (2011) Curr Top Med Chem , vol.11 , pp. 1555-1570
    • Imbimbo, B.P.1    Giardina, G.A.2
  • 27
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow EM, Stamer K, Vogel R, Thies E, Mandelkow E Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 24: 1079-1085 (2003).
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 31
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH, Garcia-Munoz A, Shepardson NE, Smith I, et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14: 837-842 (2008).
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5    Smith, I.6
  • 32
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimerrelated changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimerrelated changes. Acta Neuropathol 82: 239-259 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 33
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42: 631-639 (1992).
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 34
    • 0028861585 scopus 로고
    • Neocortical neurofibrillary tangles correlate with dementia severity in Alzheimer's disease
    • Bierer LM, Hof PR, Purohit DP, Carlin L, Schmeidler J, Davis KL, et al. Neocortical neurofibrillary tangles correlate with dementia severity in Alzheimer's disease. Arch Neurol 52: 81-88 (1995).
    • (1995) Arch Neurol , vol.52 , pp. 81-88
    • Bierer, L.M.1    Hof, P.R.2    Purohit, D.P.3    Carlin, L.4    Schmeidler, J.5    Davis, K.L.6
  • 37
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, van Eersel J, et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 142: 387-397 (2010).
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    van Eersel, J.6
  • 38
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T, et al. Reducing endogenous tau ameliorates amyloid beta-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    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 39
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 293:1491-1495 (2001)
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 40
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL, Chisholm L, Corral A, Jones G, et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 293:1487-1491 (2001).
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3    Chisholm, L.4    Corral, A.5    Jones, G.6
  • 41
    • 14544304591 scopus 로고    scopus 로고
    • Chronic nicotine administration exacerbates tau pathology in a transgenic model of Alzheimer's disease
    • Oddo S, Caccamo A, Green KN, Liang K, Tran L, Chen Y, et al. Chronic nicotine administration exacerbates tau pathology in a transgenic model of Alzheimer's disease. Proc Natl Acad Sci USA 102: 3046-3051 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3046-3051
    • Oddo, S.1    Caccamo, A.2    Green, K.N.3    Liang, K.4    Tran, L.5    Chen, Y.6
  • 43
    • 34447116398 scopus 로고    scopus 로고
    • Abeta treatment and P301L tau expression in an Alzheimer's disease tissue culture model act synergistically to promote aberrant cell cycle reentry
    • Hoerndli FJ, Pelech S, Papassotiropoulos A, Gotz J. Abeta treatment and P301L tau expression in an Alzheimer's disease tissue culture model act synergistically to promote aberrant cell cycle reentry. Eur J Neurosci 26: 60-72 (2007).
    • (2007) Eur J Neurosci , vol.26 , pp. 60-72
    • Hoerndli, F.J.1    Pelech, S.2    Papassotiropoulos, A.3    Gotz, J.4
  • 44
    • 73949142307 scopus 로고    scopus 로고
    • Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice
    • Rhein V, Song X, Wiesner A, Ittner LM, Baysang G, Meier F, et al. Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice. Proc Natl Acad Sci USA 106: 20057-20062 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20057-20062
    • Rhein, V.1    Song, X.2    Wiesner, A.3    Ittner, L.M.4    Baysang, G.5    Meier, F.6
  • 45
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM. Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43: 321-332 (2004).
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 47
    • 67649363905 scopus 로고    scopus 로고
    • Amyloid reduction by amyloid-beta vaccination also reduces mouse tau pathology and protects from neuron loss in two mouse models of Alzheimer's disease
    • Wilcock DM, Gharkholonarehe N, Van Nostrand WE, Davis J, Vitek MP, Colton CA. Amyloid reduction by amyloid-beta vaccination also reduces mouse tau pathology and protects from neuron loss in two mouse models of Alzheimer's disease. J Neurosci 29: 7957-7965 (2009).
    • (2009) J Neurosci , vol.29 , pp. 7957-7965
    • Wilcock, D.M.1    Gharkholonarehe, N.2    van Nostrand, W.E.3    Davis, J.4    Vitek, M.P.5    Colton, C.A.6
  • 48
    • 31844439888 scopus 로고    scopus 로고
    • Antibodies against beta-amyloid reduce Abeta oligomers, glycogen synthase kinase-3beta activation and tau phosphorylation in vivo and in vitro
    • Ma QL, Lim GP, Harris-White ME, Yang F, Ambegaokar SS, Ubeda OJ, et al. Antibodies against beta-amyloid reduce Abeta oligomers, glycogen synthase kinase-3beta activation and tau phosphorylation in vivo and in vitro. J Neurosci Res 83: 374-384 (2006).
    • (2006) J Neurosci Res , vol.83 , pp. 374-384
    • Ma, Q.L.1    Lim, G.P.2    Harris-White, M.E.3    Yang, F.4    Ambegaokar, S.S.5    Ubeda, O.J.6
  • 49
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • Oddo S, Vasilevko V, Caccamo A, Kitazawa M, Cribbs DH, La-Ferla FM. Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem 281: 39413-39423 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    La-Ferla, F.M.6
  • 50
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid-beta immunization in Alzheimer's disease
    • Ferrer I, Boada Rovira M, Sanchez Guerra ML, Rey MJ, Costa-Jussa F. Neuropathology and pathogenesis of encephalitis following amyloid-beta immunization in Alzheimer's disease. Brain Pathol 14: 11-20 (2004).
    • (2004) Brain Pathol , vol.14 , pp. 11-20
    • Ferrer, I.1    Boada Rovira, M.2    Sanchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussa, F.5
  • 51
    • 19944429065 scopus 로고    scopus 로고
    • Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
    • Masliah E, Hansen L, Adame A, Crews L, Bard F, Lee C, et al. Abeta vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease. Neurology 64:129-131 (2005).
    • (2005) Neurology , vol.64 , pp. 129-131
    • Masliah, E.1    Hansen, L.2    Adame, A.3    Crews, L.4    Bard, F.5    Lee, C.6
  • 52
    • 77953872812 scopus 로고    scopus 로고
    • Reduction of aggregated Tau in neuronal processes but not in the cell bodies after Abeta42 immunisation in Alzheimer's disease
    • Boche D, Donald J, Love S, Harris S, Neal JW, Holmes C, et al. Reduction of aggregated Tau in neuronal processes but not in the cell bodies after Abeta42 immunisation in Alzheimer's disease. Acta Neuropathol 120: 13-20 (2010).
    • (2010) Acta Neuropathol , vol.120 , pp. 13-20
    • Boche, D.1    Donald, J.2    Love, S.3    Harris, S.4    Neal, J.W.5    Holmes, C.6
  • 53
    • 77951893095 scopus 로고    scopus 로고
    • Beneficial effect of human anti-amyloid-beta active immunization on neurite morphology and tau pathology
    • Serrano-Pozo A, William CM, Ferrer I, Uro-Coste E, Delisle MB, Maurage CA, et al. Beneficial effect of human anti-amyloid-beta active immunization on neurite morphology and tau pathology. Brain 133: 1312-1327 (2010).
    • (2010) Brain , vol.133 , pp. 1312-1327
    • Serrano-Pozo, A.1    William, C.M.2    Ferrer, I.3    Uro-Coste, E.4    Delisle, M.B.5    Maurage, C.A.6
  • 54
    • 33749614555 scopus 로고    scopus 로고
    • Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein
    • Rosenmann H, Grigoriadis N, Karussis D, Boimel M, Touloumi O, Ovadia H, et al. Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein. Arch Neurol 63: 1459-1467 (2006).
    • (2006) Arch Neurol , vol.63 , pp. 1459-1467
    • Rosenmann, H.1    Grigoriadis, N.2    Karussis, D.3    Boimel, M.4    Touloumi, O.5    Ovadia, H.6
  • 55
    • 0037317234 scopus 로고    scopus 로고
    • Vaccination with amyloid-beta peptide induces autoimmune encephalomyelitis in C57/BL6 mice
    • Furlan R, Brambilla E, Sanvito F, Roccatagliata L, Olivieri S, Bergami A, et al. Vaccination with amyloid-beta peptide induces autoimmune encephalomyelitis in C57/BL6 mice. Brain 126: 285-291 (2003).
    • (2003) Brain , vol.126 , pp. 285-291
    • Furlan, R.1    Brambilla, E.2    Sanvito, F.3    Roccatagliata, L.4    Olivieri, S.5    Bergami, A.6
  • 56
    • 33645517069 scopus 로고    scopus 로고
    • Abeta-induced meningoencephalitis is IFNgamma-dependent and is associated with T cell-dependent clearance of Abeta in a mouse model of Alzheimer's disease
    • Monsonego A, Imitola J, Petrovic S, Zota V, Nemirovsky A, Baron R, et al. Abeta-induced meningoencephalitis is IFNgamma-dependent and is associated with T cell-dependent clearance of Abeta in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 103: 5048-5053 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5048-5053
    • Monsonego, A.1    Imitola, J.2    Petrovic, S.3    Zota, V.4    Nemirovsky, A.5    Baron, R.6
  • 57
    • 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 et al. 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
  • 58
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J, McGowan E, Rockwood J, Melrose H, Nacharaju P, Van Slegtenhorst M, et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat Genet 25: 402-405 (2000).
    • (2000) Nat Genet , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3    Melrose, H.4    Nacharaju, P.5    van Slegtenhorst, M.6
  • 59
    • 0026758096 scopus 로고
    • Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes
    • Mercken M, Vandermeeren M, Lubke U, Six J, Boons J, Van de Voorde A, et al. Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes. Acta Neuropathol 84: 265-272 (1992).
    • (1992) Acta Neuropathol , vol.84 , pp. 265-272
    • Mercken, M.1    Vandermeeren, M.2    Lubke, U.3    Six, J.4    Boons, J.5    van de Voorde, A.6
  • 60
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognizes tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M, Jakes R, Vanmechelen E. Monoclonal antibody AT8 recognizes tau protein phosphorylated at both serine 202 and threonine 205. Neurosci Lett 189: 167-169 (1995).
    • (1995) Neurosci Lett , vol.189 , pp. 167-169
    • Goedert, M.1    Jakes, R.2    Vanmechelen, E.3
  • 61
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhofer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E et al. Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem 252: 542-552 (1998).
    • (1998) Eur J Biochem , vol.252 , pp. 542-552
    • Zheng-Fischhofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6
  • 62
    • 44949185340 scopus 로고    scopus 로고
    • A novel transgenic mouse expressing double mutant tau driven by its natural promoter exhibits tauopathy characteristics
    • Rosenmann H, Grigoriadis N, Eldar-Levy H, Avital A, Rozenstein L, Touloumi O, et al. A novel transgenic mouse expressing double mutant tau driven by its natural promoter exhibits tauopathy characteristics. Exp Neurol 212: 71-84 (2008).
    • (2008) Exp Neurol , vol.212 , pp. 71-84
    • Rosenmann, H.1    Grigoriadis, N.2    Eldar-Levy, H.3    Avital, A.4    Rozenstein, L.5    Touloumi, O.6
  • 63
    • 77954656338 scopus 로고    scopus 로고
    • Inflammation in the CNS increases Alzheimer's disease related neurofibrillary tangle burden: A study of experimental autoimmune encephalomyelitis in a transgenic animal model for neurofibrillary tangles
    • Boimel M, Grigoriadis N, Lourbopoulos A, Rozenstein L, Touloumi O, Mizrachi R, et al. Inflammation in the CNS increases Alzheimer's disease related neurofibrillary tangle burden: A study of experimental autoimmune encephalomyelitis in a transgenic animal model for neurofibrillary tangles. Neurology 66: 279 (2006).
    • (2006) Neurology , vol.66 , pp. 279
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Rozenstein, L.4    Touloumi, O.5    Mizrachi, R.6
  • 64
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A, Haber E, Abramsky O, Rosenmann H. Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp Neurol 224: 472-485 (2010).
    • (2010) Exp Neurol , vol.224 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5    Rosenmann, H.6
  • 65
    • 78650065372 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model
    • Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model. J Neurosci 30:16559-16566 (2010).
    • (2010) J Neurosci , vol.30 , pp. 16559-16566
    • Boutajangout, A.1    Quartermain, D.2    Sigurdsson, E.M.3
  • 66
    • 82955194797 scopus 로고    scopus 로고
    • Tau-Targeted Immunization Impedes Progression of Neurofibrillary Histopathology in Aged P301L Tau Transgenic Mice
    • Bi M, Ittner A, Ke YD, Gotz J, Ittner LM. Tau-Targeted Immunization Impedes Progression of Neurofibrillary Histopathology in Aged P301L Tau Transgenic Mice. PLoS One 6: e26860 (2011).
    • (2011) PLoS One , vol.6
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 67
    • 0035808361 scopus 로고    scopus 로고
    • Tau filament formation in transgenic mice expressing P301L tau
    • Gotz J, Chen F, Barmettler R, Nitsch RM. Tau filament formation in transgenic mice expressing P301L tau. J Biol Chem 276: 529-534 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 529-534
    • Gotz, J.1    Chen, F.2    Barmettler, R.3    Nitsch, R.M.4
  • 68
    • 84860531636 scopus 로고    scopus 로고
    • Targeting phospho-Ser422 by active tau immunotherapy in the THY-22Tau mouse model: A suitable therapeitic approach
    • Troquier L, Caillierez R, Burnouf S, Fernandez-Gomez F, Grosjean M, Zommer N et al. Targeting phospho-Ser422 by active tau immunotherapy in the THY-22Tau mouse model: a suitable therapeitic approach. Curr Alzheimer Res 9: 397-405 (2012).
    • (2012) Curr Alzheimer Res , vol.9 , pp. 397-405
    • Troquier, L.1    Caillierez, R.2    Burnouf, S.3    Fernandez-Gomez, F.4    Grosjean, M.5    Zommer, N.6
  • 69
    • 33746652117 scopus 로고    scopus 로고
    • Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits
    • Schindowski K, Bretteville A, Leroy K, Begard S, Brion JP, Hamdane M, et al. Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits. Am J Pathol 169: 599-616 (2006).
    • (2006) Am J Pathol , vol.169 , pp. 599-616
    • Schindowski, K.1    Bretteville, A.2    Leroy, K.3    Begard, S.4    Brion, J.P.5    Hamdane, M.6
  • 70
    • 78650945635 scopus 로고    scopus 로고
    • Tau vaccine: Active immunization with a misfolded tau protein attenuates tau pathology in a transgenic rat model of tauopathy
    • Novac M. Tau vaccine: active immunization with a misfolded tau protein attenuates tau pathology in a transgenic rat model of tauopathy. Alzheimers dement 5: P93 (2009).
    • (2009) Alzheimers dement , vol.5
    • Novac, M.1
  • 71
    • 80855125085 scopus 로고    scopus 로고
    • Protein Tau: Target for immunotherapy: Pre-clinical evaluationin transgenic mice
    • Theunis C, Crespo Biel N, Borghgraef P, Devijver H, Gafner V et al. Protein Tau: target for immunotherapy: pre-clinical evaluationin transgenic mice. Neurodegener Dis 8: Suppl 1 (2011).
    • (2011) Neurodegener Dis , vol.8 , Issue.SUPPL. 1
    • Theunis, C.1    Crespo Biel, N.2    Borghgraef, P.3    Devijver, H.4    Gafner, V.5
  • 72
    • 84888201595 scopus 로고    scopus 로고
    • Molecular mediators of amiloidosis-inflammation coupling in Alzheimer' disease: In vivo evidence in humans and animal models
    • Higuchi N. Molecular mediators of amiloidosis-inflammation coupling in Alzheimer' disease: in vivo evidence in humans and animal models. Neurodegener Dis 8: Suppl 1 (2011).
    • (2011) Neurodegener Dis , vol.8 , Issue.SUPPL. 1
    • Higuchi, N.1
  • 74
    • 20044388897 scopus 로고    scopus 로고
    • Effects of different anti-tau antibodies on tau fibrillogenesis: RTA-1 and RTA-2 counteract tau aggregation
    • Taniguchi T, Sumida M, Hiraoka S, Tomoo K, Kakehi T, Minoura K et al. Effects of different anti-tau antibodies on tau fibrillogenesis: RTA-1 and RTA-2 counteract tau aggregation. FEBS Lett 579: 1399-1404 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 1399-1404
    • Taniguchi, T.1    Sumida, M.2    Hiraoka, S.3    Tomoo, K.4    Kakehi, T.5    Minoura, K.6
  • 75
    • 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 118: 658-667 (2011).
    • (2011) J Neurochem , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 76
    • 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 286: 34457-34467 (2011).
    • (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
  • 77
    • 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 22: 9340-9351 (2002).
    • (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
  • 79
    • 84888199348 scopus 로고    scopus 로고
    • AD Vaccine Targeting Tau Promising in Early Animal Studies
    • Friedman R. AD Vaccine Targeting Tau Promising in Early Animal Studies. Neurology Today 11: 20 (2011).
    • (2011) Neurology Today , vol.11 , pp. 20
    • Friedman, R.1
  • 80
  • 81
    • 80855148339 scopus 로고    scopus 로고
    • Opposing roles of microglial activation in amyloid depositing and tau depositing transgenic mice
    • Morgan D, Lee D, Brownlow M, Selenica M, Reid P, Alvarez J et al. Opposing roles of microglial activation in amyloid depositing and tau depositing transgenic mice. Neurodegener Dis 1: Suppl 1 (2011).
    • (2011) Neurodegener Dis , vol.1 , Issue.SUPPL. 1
    • Morgan, D.1    Lee, D.2    Brownlow, M.3    Selenica, M.4    Reid, P.5    Alvarez, J.6
  • 82
    • 33750681275 scopus 로고    scopus 로고
    • Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimer's disease and healthy subjects
    • Rosenmann H, Meiner Z, Geylis V, Abramsky O, Steinitz M. Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimer's disease and healthy subjects. Neurosci Lett 410: 90-93 (2006).
    • (2006) Neurosci Lett , vol.410 , pp. 90-93
    • Rosenmann, H.1    Meiner, Z.2    Geylis, V.3    Abramsky, O.4    Steinitz, M.5
  • 83
    • 2442643119 scopus 로고    scopus 로고
    • Are the extracellular [correction of extracelluar] pathways a conduit for the delivery of therapeutics to the brain?
    • Banks WA. Are the extracellular [correction of extracelluar] pathways a conduit for the delivery of therapeutics to the brain? Curr Pharm Des 10: 1365-1370 (2004).
    • (2004) Curr Pharm Des , vol.10 , pp. 1365-1370
    • Banks, W.A.1
  • 84
    • 0023640751 scopus 로고
    • Intraneuronal IgG in the central nervous system: Uptake by retrograde axonal transport
    • Fabian RH, Petroff G. Intraneuronal IgG in the central nervous system: uptake by retrograde axonal transport. Neurology 37: 1780-1784 (1987).
    • (1987) Neurology , vol.37 , pp. 1780-1784
    • Fabian, R.H.1    Petroff, G.2
  • 85
    • 0026754727 scopus 로고
    • Localization patterns for immunoglobulins and albumins in the brain suggest diverse mechanisms for their transport across the blood-brain barrier (BBB)
    • Kozlowski GP, Sterzl I, Nilaver G. Localization patterns for immunoglobulins and albumins in the brain suggest diverse mechanisms for their transport across the blood-brain barrier (BBB). Prog Brain Res 91: 149-154 (1992).
    • (1992) Prog Brain Res , vol.91 , pp. 149-154
    • Kozlowski, G.P.1    Sterzl, I.2    Nilaver, G.3
  • 86
    • 0016840819 scopus 로고
    • Radioimmunoassays for Ig classes G, A, M, D, and E in spinal fluids: Normal values of different age groups
    • Nerenberg ST, Prasad R. Radioimmunoassays for Ig classes G, A, M, D, and E in spinal fluids: normal values of different age groups. J Lab Clin Med 86: 887-898 (1975).
    • (1975) J Lab Clin Med , vol.86 , pp. 887-898
    • Nerenberg, S.T.1    Prasad, R.2
  • 87
    • 0025213058 scopus 로고
    • A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig
    • Zlokovic BV, Skundric DS, Segal MB, Lipovac MN, Mackic JB, Davson H. A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig. Exp Neurol 107: 263-270 (1990).
    • (1990) Exp Neurol , vol.107 , pp. 263-270
    • Zlokovic, B.V.1    Skundric, D.S.2    Segal, M.B.3    Lipovac, M.N.4    McKic, J.B.5    Davson, H.6
  • 88
    • 77249169130 scopus 로고    scopus 로고
    • Mild experimental autoimmune encephalitis as a tool to induce bloodbrain barrier dysfunction
    • Boettger MK, Weishaupt A, Geis C, Toyka KV, Sommer C. Mild experimental autoimmune encephalitis as a tool to induce bloodbrain barrier dysfunction. J Neural Transm 117: 165-169 (2010).
    • (2010) J Neural Transm , vol.117 , pp. 165-169
    • Boettger, M.K.1    Weishaupt, A.2    Geis, C.3    Toyka, K.V.4    Sommer, C.5
  • 89
    • 0023237250 scopus 로고
    • Bloodbrain barrier in Alzheimer dementia and in non-demented elderly. An immunocytochemical study
    • Alafuzoff I, Adolfsson R, Grundke-Iqbal I, Winblad B. Bloodbrain barrier in Alzheimer dementia and in non-demented elderly. An immunocytochemical study. Acta Neuropathol 73: 160-166 (1987).
    • (1987) Acta Neuropathol , vol.73 , pp. 160-166
    • Alafuzoff, I.1    Adolfsson, R.2    Grundke-Iqbal, I.3    Winblad, B.4
  • 90
    • 80855148196 scopus 로고    scopus 로고
    • Immunotherapy for tauopathies
    • Gu J, Sigurdsson EM. Immunotherapy for tauopathies. J Mol Neurosci 45: 690-695 (2011).
    • (2011) J Mol Neurosci , vol.45 , pp. 690-695
    • Gu, J.1    Sigurdsson, E.M.2
  • 92
    • 0036953160 scopus 로고    scopus 로고
    • Passage of amyloid beta protein antibody across the bloodbrain barrier in a mouse model of Alzheimer's disease
    • Banks WA, Terrell B, Farr SA, Robinson SM, Nonaka N, Morley JE. Passage of amyloid beta protein antibody across the bloodbrain barrier in a mouse model of Alzheimer's disease. Peptides 23: 2223-2226 (2002).
    • (2002) Peptides , vol.23 , pp. 2223-2226
    • Banks, W.A.1    Terrell, B.2    Farr, S.A.3    Robinson, S.M.4    Nonaka, N.5    Morley, J.E.6
  • 93
    • 70249127559 scopus 로고    scopus 로고
    • Tau-focused immunotherapy for Alzheimer's disease and related tauopathies
    • Sigurdsson EM. Tau-focused immunotherapy for Alzheimer's disease and related tauopathies. Curr Alzheimer Res 6: 446-450 (2009).
    • (2009) Curr Alzheimer Res , vol.6 , pp. 446-450
    • Sigurdsson, E.M.1
  • 94
    • 0025237590 scopus 로고
    • Uptake of antineuronal IgM by CNS neurons: Comparison with antineuronal IgG
    • Fabian RH. Uptake of antineuronal IgM by CNS neurons: comparison with antineuronal IgG. Neurology 40: 419-422 (1990).
    • (1990) Neurology , vol.40 , pp. 419-422
    • Fabian, R.H.1
  • 95
    • 0028963740 scopus 로고
    • Uptake of systemically administered human anticerebellar antibody by rat Purkinje cells following blood-brain barrier disruption
    • Greenlee JE, Burns JB, Rose JW, Jaeckle KA, Clawson S. Uptake of systemically administered human anticerebellar antibody by rat Purkinje cells following blood-brain barrier disruption. Acta Neuropathol 89: 341-345 (1995).
    • (1995) Acta Neuropathol , vol.89 , pp. 341-345
    • Greenlee, J.E.1    Burns, J.B.2    Rose, J.W.3    Jaeckle, K.A.4    Clawson, S.5
  • 96
    • 0023203429 scopus 로고
    • Accumulation of circulating endogenous and exogenous immunoglobulins by hypothalamic magnocellular neurons
    • Meeker ML, Meeker RB, Hayward JN. Accumulation of circulating endogenous and exogenous immunoglobulins by hypothalamic magnocellular neurons. Brain Res 423: 45-55 (1987).
    • (1987) Brain Res , vol.423 , pp. 45-55
    • Meeker, M.L.1    Meeker, R.B.2    Hayward, J.N.3
  • 97
    • 0036645381 scopus 로고    scopus 로고
    • Immunoglobulin Fc gamma receptor promotes immunoglobulin uptake, immunoglobulin-mediated calcium increase, and neurotransmitter release in motor neurons
    • Mohamed HA, Mosier DR, Zou LL, Siklos L, Alexianu ME, Engelhardt JI, et al. Immunoglobulin Fc gamma receptor promotes immunoglobulin uptake, immunoglobulin-mediated calcium increase, and neurotransmitter release in motor neurons. J Neurosci Res 69: 110-116 (2002).
    • (2002) J Neurosci Res , vol.69 , pp. 110-116
    • Mohamed, H.A.1    Mosier, D.R.2    Zou, L.L.3    Siklos, L.4    Alexianu, M.E.5    Engelhardt, J.I.6
  • 98
    • 0030921110 scopus 로고    scopus 로고
    • Immunoglobulin molecules are present in early-generated neuronal populations in the rat cerebral cortex and retina
    • Upender MB, Dunn JA, Wilson SM, Naegele JR. Immunoglobulin molecules are present in early-generated neuronal populations in the rat cerebral cortex and retina. J Comp Neurol 384: 271-282 (1997).
    • (1997) J Comp Neurol , vol.384 , pp. 271-282
    • Upender, M.B.1    Dunn, J.A.2    Wilson, S.M.3    Naegele, J.R.4
  • 99
    • 0025986452 scopus 로고
    • Detection of the anti-Hu antibody in specific regions of the nervous system and tumor from patients with paraneoplastic encephalomyelitis/ sensory neuronopathy
    • Dalmau J, Furneaux HM, Rosenblum MK, Graus F, Posner JB. Detection of the anti-Hu antibody in specific regions of the nervous system and tumor from patients with paraneoplastic encephalomyelitis/ sensory neuronopathy. Neurology 41: 1757-1764 (1991).
    • (1991) Neurology , vol.41 , pp. 1757-1764
    • Dalmau, J.1    Furneaux, H.M.2    Rosenblum, M.K.3    Graus, F.4    Posner, J.B.5
  • 100
    • 77956393132 scopus 로고    scopus 로고
    • Involvement of Fc receptors in disorders of the central nervous system
    • Okun E, Mattson MP, Arumugam TV. Involvement of Fc receptors in disorders of the central nervous system. Neuromolecular Med 12: 164-178 (2010).
    • (2010) Neuromolecular Med , vol.12 , pp. 164-178
    • Okun, E.1    Mattson, M.P.2    Arumugam, T.V.3
  • 101
    • 0025652124 scopus 로고
    • Low density lipoprotein receptor-related protein mediates endocytosis of monoclonal antibodies in cultured cells and rabbit liver
    • Herz J, Kowal RC, Ho YK, Brown MS, Goldstein JL. Low density lipoprotein receptor-related protein mediates endocytosis of monoclonal antibodies in cultured cells and rabbit liver. J Biol Chem 265: 21355-21362 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 21355-21362
    • Herz, J.1    Kowal, R.C.2    Ho, Y.K.3    Brown, M.S.4    Goldstein, J.L.5
  • 102
    • 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 15: 157-168 (2008).
    • (2008) J Alzheimers Dis , vol.15 , pp. 157-168
    • Sigurdsson, E.M.1
  • 103
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt R, Leger J, Lee G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol 131: 1327-1340 (1995).
    • (1995) J Cell Biol , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 104
    • 0033922393 scopus 로고    scopus 로고
    • Phosphorylation of tau alters its association with the plasma membrane
    • Ekinci FJ, Shea TB. Phosphorylation of tau alters its association with the plasma membrane. Cell Mol Neurobiol 20:497-508 (2000).
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 497-508
    • Ekinci, F.J.1    Shea, T.B.2
  • 105
    • 79951873381 scopus 로고    scopus 로고
    • The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner
    • Gauthier-Kemper A, Weissmann C, Golovyashkina N, Sebo-Lemke Z, Drewes G, Gerke V, et al. The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner. J Cell Biol 192: 647-661 (2011).
    • (2011) J Cell Biol , vol.192 , pp. 647-661
    • Gauthier-Kemper, A.1    Weissmann, C.2    Golovyashkina, N.3    Sebo-Lemke, Z.4    Drewes, G.5    Gerke, V.6
  • 106
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H, Kondo J, Ihara Y. Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235:1641-1644 (1987).
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 107
    • 84857641625 scopus 로고    scopus 로고
    • Ubiquitin is Associated with Early Truncation of Tau Protein at Aspartic Acid(421) during the Maturation of Neurofibrillary Tangles in Alzheimer's Disease
    • Garcia-Sierra F, Jarero-Basulto JJ, Kristofikova Z, Majer E, Binder LI, Ripova D. Ubiquitin is Associated with Early Truncation of Tau Protein at Aspartic Acid(421) during the Maturation of Neurofibrillary Tangles in Alzheimer's Disease. Brain Pathol 22: 240-50 (2012).
    • (2012) Brain Pathol , vol.22 , pp. 240-250
    • Garcia-Sierra, F.1    Jarero-Basulto, J.J.2    Kristofikova, Z.3    Majer, E.4    Binder, L.I.5    Ripova, D.6
  • 108
    • 0035680685 scopus 로고    scopus 로고
    • FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain
    • Lim F, Hernandez F, Lucas JJ, Gomez-Ramos P, Moran MA, Avila J. FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain. Mol Cell Neurosci 18:702-714 (2001).
    • (2001) Mol Cell Neurosci , vol.18 , pp. 702-714
    • Lim, F.1    Hernandez, F.2    Lucas, J.J.3    Gomez-Ramos, P.4    Moran, M.A.5    Avila, J.6
  • 109
    • 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 32: 1091-1105 (2003).
    • (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
  • 110
    • 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 2: 59 (2011).
    • (2011) Front Psychiatry , vol.2 , pp. 59
    • Krishnamurthy, P.K.1    Deng, Y.2    Sigurdsson, E.M.3
  • 111
    • 34547110577 scopus 로고    scopus 로고
    • Internalized antibodies to the Abeta domain of APP reduce neuronal Abeta and protect against synaptic alterations
    • Tampellini D, Magrane J, Takahashi RH, Li F, Lin MT, Almeida CG et al. Internalized antibodies to the Abeta domain of APP reduce neuronal Abeta and protect against synaptic alterations. J Biol Chem 282: 18895-18906 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 18895-18906
    • Tampellini, D.1    Magrane, J.2    Takahashi, R.H.3    Li, F.4    Lin, M.T.5    Almeida, C.G.6
  • 112
    • 20444413356 scopus 로고    scopus 로고
    • Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease
    • Masliah E, Rockenstein E, Adame A, Alford M, Crews L, Hashimoto M, et al. Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease. Neuron 46: 857-868 (2005).
    • (2005) Neuron , vol.46 , pp. 857-868
    • Masliah, E.1    Rockenstein, E.2    Adame, A.3    Alford, M.4    Crews, L.5    Hashimoto, M.6
  • 113
    • 79955757052 scopus 로고    scopus 로고
    • Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease
    • Masliah E, Rockenstein E, Mante M, Crews L, Spencer B, Adame A et al. Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease. PLoS One 6: e19338 (2011).
    • (2011) PLoS One , vol.6
    • Masliah, E.1    Rockenstein, E.2    Mante, M.3    Crews, L.4    Spencer, B.5    Adame, A.6
  • 114
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357: 500-503 (1992).
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 115
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • Yamazaki T, Koo EH, Selkoe DJ. Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. J Cell Sci 109 (Pt 5): 999-1008 (1996).
    • (1996) J Cell Sci , vol.109 , Issue.PART 5 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 119
    • 58849106655 scopus 로고    scopus 로고
    • Inhibition of autophagy causes tau proteolysis by activating calpain in rat brain
    • Zhang JY, Peng C, Shi H, Wang S, Wang Q, Wang JZ. Inhibition of autophagy causes tau proteolysis by activating calpain in rat brain. J Alzheimers Dis 16: 39-47 (2009).
    • (2009) J Alzheimers Dis , vol.16 , pp. 39-47
    • Zhang, J.Y.1    Peng, C.2    Shi, H.3    Wang, S.4    Wang, Q.5    Wang, J.Z.6
  • 120
    • 0030774852 scopus 로고    scopus 로고
    • Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration
    • Kenessey A, Nacharaju P, Ko LW, Yen SH. Degradation of tau by lysosomal enzyme cathepsin D: implication for Alzheimer neurofibrillary degeneration. J Neurochem 69: 2026-2038 (1997).
    • (1997) J Neurochem , vol.69 , pp. 2026-2038
    • Kenessey, A.1    Nacharaju, P.2    Ko, L.W.3    Yen, S.H.4
  • 121
    • 0141539641 scopus 로고    scopus 로고
    • Neuronal and microglial cathepsins in aging and agerelated diseases
    • Nakanishi H. Neuronal and microglial cathepsins in aging and agerelated diseases. Ageing Res Rev 2: 367-381 (2003).
    • (2003) Ageing Res Rev , vol.2 , pp. 367-381
    • Nakanishi, H.1
  • 123
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284: 12845-12852 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 124
    • 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. Interneuronal transfer of human tau between Lamprey central neurons in situ. J Alzheimers Dis 19: 647-664 (2010).
    • (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
  • 126
    • 84857077700 scopus 로고    scopus 로고
    • Tau-targeted treatment strategies in Alzheimer's disease
    • Gotz J, Ittner A, Ittner LM. Tau-targeted treatment strategies in Alzheimer's disease. Br J Pharmacol 165: 1246-59 (2011).
    • (2011) Br J Pharmacol , vol.165 , pp. 1246-1259
    • Gotz, J.1    Ittner, A.2    Ittner, L.M.3
  • 127
    • 0034996076 scopus 로고    scopus 로고
    • Microglial activation parallels system degeneration in progressive supranuclear palsy and corticobasal degeneration
    • Ishizawa K, Dickson DW. Microglial activation parallels system degeneration in progressive supranuclear palsy and corticobasal degeneration. J Neuropathol Exp Neurol 60: 647-657 (2001).
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 647-657
    • Ishizawa, K.1    Dickson, D.W.2
  • 129
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama Y, Higuchi M, Zhang B, Huang SM, Iwata N, Saido TC, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 53: 337-351 (2007).
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3    Huang, S.M.4    Iwata, N.5    Saido, T.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.