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Volumn 4, Issue 2, 2012, Pages 213-238

Immunotherapy for Alzheimer's disease: From anti-β-amyloid to tau-based immunization strategies

Author keywords

.amyloid; active immunotherapy; Alzheimer's disease; bapineuzumab; monoclonal antibody; passive immunotherapy; polyclonal antibody; solanezumab; tau protein

Indexed keywords

4 BENZYL 2 METHYL 1,2,4 THIAZOLIDINE 3,5 DIONE; ALZHEIMER DISEASE VACCINE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; BAPINEUZUMAB; BENZOTHIAZOLE; CRENEZUMAB; DAVUNETIDE; DNA VACCINE; EHT 0202; EHT0202; EPOTHILONE A; GANTENERUMAB; IMMUNOGLOBULIN G; LITHIUM; METHYLENE BLUE; NEWGAM; PACLITAXEL; PBT 2; PHOSPHOPROTEIN PHOSPHATASE 2A; PLACEBO; PONEZUMAB; QS 21; RECOMBINANT HUMAN TAU PROTEIN; RECOMBINANT PROTEIN; RHODANINE; SEMAGACESTAT; SOLANEZUMAB; TAU PROTEIN; TIDEGLUSIB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID;

EID: 84857558439     PISSN: 1750743X     EISSN: 17507448     Source Type: Journal    
DOI: 10.2217/imt.11.170     Document Type: Review
Times cited : (114)

References (223)
  • 1
    • 67650844275 scopus 로고    scopus 로고
    • Epidemiology of Alzheimers disease: Occurrence determinants and strategies toward intervention
    • Qiu C, Kivipelto M, von Strauss E. Epidemiology of Alzheimers disease: occurrence, determinants, and strategies toward intervention. Dialogues Clin. Neurosci. 11(2), 111-128 (2009).
    • (2009) Dialogues Clin. Neurosci. , vol.11 , Issue.2 , pp. 111-128
    • Qiu, C.1    Kivipelto, M.2    Von Strauss, E.3
  • 2
    • 79952730699 scopus 로고    scopus 로고
    • Alzheimers disease facts and figures
    • Alzheimers Association. 2011
    • Thies W, Bleiler L; Alzheimers Association. 2011 Alzheimers disease facts and figures. Alzheimers Dement. 7(2), 208-244 (2011).
    • (2011) Alzheimers Dement. , vol.7 , Issue.2 , pp. 208-244
    • Thies, W.1    Bleiler, L.2
  • 3
    • 77949768182 scopus 로고    scopus 로고
    • Towards disease-modifying treatment of Alzheimers disease: Drugs targeting beta?amyloid
    • Frisardi V, Solfrizzi V, Imbimbo PB et al. Towards disease-modifying treatment of Alzheimers disease: drugs targeting beta?amyloid. Curr. Alzheimer Res. 7(1), 40-55 (2010).
    • (2010) Curr. Alzheimer Res. , vol.7 , Issue.1 , pp. 40-55
    • Frisardi, V.1    Solfrizzi, V.2    Imbimbo, P.B.3
  • 4
    • 70349093083 scopus 로고    scopus 로고
    • Disease-modifying approach to the treatment of Alzheimers disease: From alpha secretase activators to gamma secretase inhibitors and modulators
    • Panza F, Solfrizzi V, Frisardi V et al. Disease-modifying approach to the treatment of Alzheimers disease: from alpha?secretase activators to gamma?secretase inhibitors and modulators. Drugs Aging 26(7), 537-555 (2009).
    • (2009) Drugs Aging , vol.26 , Issue.7 , pp. 537-555
    • Panza, F.1    Solfrizzi, V.2    Frisardi, V.3
  • 5
    • 77649256879 scopus 로고    scopus 로고
    • Beyond the neurotransmitter-focused approach in treating Alzheimers disease: Drugs targeting beta amyloid and tau protein
    • Panza F, Solfrizzi V, Frisardi V et al. Beyond the neurotransmitter- focused approach in treating Alzheimers disease: drugs targeting beta?amyloid and tau protein. Aging Clin. Exp. Res. 21(6), 386-406 (2009).
    • (2009) Aging Clin. Exp. Res. , vol.21 , Issue.6 , pp. 386-406
    • Panza, F.1    Solfrizzi, V.2    Frisardi, V.3
  • 7
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimers disease
    • Khachaturian ZS. Diagnosis of Alzheimers disease. Arch. Neurol. 42(11), 1097-1105 (1985).
    • (1985) Arch. Neurol. , vol.42 , Issue.11 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 8
    • 0025908356 scopus 로고
    • The consortium to establish a registry for Alzheimers disease CERAD Part II. standardization of the neuropathologic assessment of Alzheimers disease
    • Mirra SS, Heyman A, McKeel D et al. The consortium to establish a registry for Alzheimers disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimers disease. Neurology 41(4), 479-486 (1991).
    • (1991) Neurology , vol.41 , Issue.4 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3
  • 9
    • 0032749171 scopus 로고    scopus 로고
    • Application of the national institute on aging NIA-reagan institute criteria for the neuropathological diagnosis of alzheimer disease
    • Newell KL, Hyman BT, Growdon JH, Hedley-Whyte ET. Application of the National Institute on Aging (NIA)-Reagan Institute criteria for the neuropathological diagnosis of Alzheimer disease. J. Neuropathol. Exp. Neurol. 58(11), 1147-1155 (1999).
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , Issue.11 , pp. 1147-1155
    • Newell, K.L.1    Hyman, B.T.2    Growdon, J.H.3    Hedley-Whyte, E.T.4
  • 10
    • 0027939401 scopus 로고
    • Early phosphorylation of tau in Alzheimers disease occurs at Ser-202 and is preferentially located within neurites
    • Su JH, Cummings BJ, Cotman CW. Early phosphorylation of tau in Alzheimers disease occurs at Ser-202 and is preferentially located within neurites. NeuroReport 5(17), 2358-2362 (1994).
    • (1994) NeuroReport , vol.5 , Issue.17 , pp. 2358-2362
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 11
    • 0030580439 scopus 로고    scopus 로고
    • Plaque biogenesis in brain aging and Alzheimers disease: I progressive changes in phosphorylation states of paired helical filaments and neurofilaments
    • Su JH, Cummings BJ, Cotman CW. Plaque biogenesis in brain aging and Alzheimers disease: I. Progressive changes in phosphorylation states of paired helical filaments and neurofilaments. Brain Res. 739(1-2), 79-87 (1996).
    • (1996) Brain Res. , vol.739 , Issue.1-2 , pp. 79-87
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 12
    • 0031128758 scopus 로고    scopus 로고
    • Rediscovery of the case described by alois Alzheimer in 1911: Historical histological and molecular genetic analysis
    • Graeber MB, Kosel S, Egensperger R et al. Rediscovery of the case described by Alois Alzheimer in 1911: historical, histological and molecular genetic analysis. Neurogenetics 1(1), 73-80 (1997).
    • (1997) Neurogenetics , vol.1 , Issue.1 , pp. 73-80
    • Graeber, M.B.1    Kosel, S.2    Egensperger, R.3
  • 13
    • 56349119351 scopus 로고    scopus 로고
    • Linking Ab and tau in late-onset Alzheimers disease: A dual pathway hypothesis
    • Small SA, Duff K. Linking Ab and tau in late-onset Alzheimers disease: A dual pathway hypothesis. Neuron 60(4), 534-542 (2008).
    • (2008) Neuron , vol.60 , Issue.4 , pp. 534-542
    • Small, S.A.1    Duff, K.2
  • 14
    • 0035477333 scopus 로고    scopus 로고
    • The cell biology of Alzheimers disease: Uncovering the secrets of secretases
    • Walter J, Kaether C, Steiner H, Haass C. The cell biology of Alzheimers disease: uncovering the secrets of secretases. Curr. Opin. Neurobiol. 11(5), 585-590 (2001).
    • (2001) Curr. Opin. Neurobiol. , vol.11 , Issue.5 , pp. 585-590
    • Walter, J.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 15
    • 0026646605 scopus 로고    scopus 로고
    • Isolation and quantification of soluble Alzheimers b-peptide from biological fluids
    • Seubert P, Vigo-Pelfry C, Esch F et al. Isolation and quantification of soluble Alzheimers b-peptide from biological fluids. Nature 359(6393), 325-327 (1996).
    • (1996) Nature , vol.359 , Issue.6393 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfry, C.2    Esch, F.3
  • 16
    • 0028169925 scopus 로고
    • Visualization of Ab42 43 and Ab40 in senile plaques with specific Ab monoclonals: Evidence that the initially deposited species is Ab42 43
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Ab42(43) and Ab40 in senile plaques with specific Ab monoclonals: Evidence that the initially deposited species is Ab42(43). Neuron 13(1), 45-53 (1993).
    • (1993) Neuron , vol.13 , Issue.1 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 17
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimers disease
    • Hardy J, Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimers disease. Trends Pharmacol. Sci. 12(5), 383-388 (1991).
    • (1991) Trends Pharmacol. Sci. , vol.12 , Issue.5 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 18
    • 79953276681 scopus 로고    scopus 로고
    • The pathogenesis of Alzheimers disease: A reevaluation of the Amyloid Cascade Hypothesis
    • Armstrong RA. The pathogenesis of Alzheimers disease: A reevaluation of the "Amyloid Cascade Hypothesis". Int. J. Alzheimers Dis. 2011, 630865 (2011)
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 630865
    • Armstrong, R.A.1
  • 20
    • 0028942632 scopus 로고
    • Tau protein directly interacts with the amyloid b protein precursor: Implications for Alzheimers disease
    • Smith MA, Siedlak SL, Richey PL et al. Tau protein directly interacts with the amyloid b?protein precursor: Implications for Alzheimers disease. Nat. Med. 1(4), 365-369 (1995).
    • (1995) Nat. Med. , vol.1 , Issue.4 , pp. 365-369
    • Smith, M.A.1    Siedlak, S.L.2    Richey, P.L.3
  • 21
    • 0027322817 scopus 로고
    • B amyloid protein precursor and t mRNA levels versus b amyloid plaque and neurofibrillary tangles in the aged human brain
    • Oyama F, Shimada H, Oyama R, Titani K, Ihara Y. b?amyloid protein precursor and t mRNA levels versus b?amyloid plaque and neurofibrillary tangles in the aged human brain. J. Neurochem. 60(5), 1658-1664 (1993).
    • (1993) J. Neurochem. , vol.60 , Issue.5 , pp. 1658-1664
    • Oyama, F.1    Shimada, H.2    Oyama, R.3    Titani, K.4    Ihara, Y.5
  • 22
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-b protein dimers isolated directly from Alzheimers brains impair synaptic plasticity and memory
    • Shankar GM, Li S, Mehta TH et al. Amyloid-b protein dimers isolated directly from Alzheimers brains impair synaptic plasticity and memory. Nat. Med. 14(8), 837-842 (2008).
    • (2008) Nat. Med. , vol.14 , Issue.8 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3
  • 23
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid b-protein impair synaptic plasticity and behavior
    • Selkoe DJ. Soluble oligomers of the amyloid b-protein impair synaptic plasticity and behavior. Behav. Brain Res. 192(1), 106-113 (2008).
    • (2008) Behav. Brain Res. , vol.192 , Issue.1 , pp. 106-113
    • Selkoe, D.J.1
  • 24
    • 62649174753 scopus 로고    scopus 로고
    • Oligomeric amyloid b associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
    • USA
    • Koffie RM, Meyer-Luehmann M, Hashimoto T et al. Oligomeric amyloid b associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. Proc. Natl Acad. Sci. USA 106(10), 4012-4017 (2009).
    • (2009) Proc. Natl Acad. Sci. , vol.106 , Issue.10 , pp. 4012-4017
    • Koffie, R.M.1    Meyer-Luehmann, M.2    Hashimoto, T.3
  • 25
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid b protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar GM, Bloodgood BL, Townsend M, Walsh DM, Selkoe DJ, Sabatini BL. Natural oligomers of the Alzheimer amyloidβ protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27(11), 2866-2875 (2007).
    • (2007) J. Neurosci. , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 26
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid b protein assembly in the brain impairs memory
    • Lesnè S, Koh MT, Kotilinek L et al. A specific amyloidβ protein assembly in the brain impairs memory. Nature 440(7082), 352-357 (2006).
    • (2006) Nature , vol.440 , Issue.7082 , pp. 352-357
    • Lesnè, S.1    Koh, M.T.2    Kotilinek, L.3
  • 27
    • 79951617234 scopus 로고    scopus 로고
    • Therapeutic intervention for Alzheimers disease with g secretase inhibitors: Still a viable option
    • Imbimbo BP, Panza F, Frisardi V et al. Therapeutic intervention for Alzheimers disease with g?secretase inhibitors: Still a viable option? Expert Opin. Investig. Drugs 20(3), 325-341 (2011).
    • (2011) Expert Opin. Investig. Drugs , vol.20 , Issue.3 , pp. 325-341
    • Imbimbo, B.P.1    Panza, F.2    Frisardi, V.3
  • 28
    • 79954458099 scopus 로고    scopus 로고
    • EHT0202 in Alzheimers disease: A 3 month randomized placebo-controlled double-blind study
    • Vellas B, Sol O, Snyder P et al. EHT0202 in Alzheimers disease: A 3?month, randomized, placebo-controlled, double-blind study. Curr. Alzheimer Res. 8(2), 203-212 (2011).
    • (2011) Curr. Alzheimer Res. , vol.8 , Issue.2 , pp. 203-212
    • Vellas, B.1    Sol, O.2    Snyder, P.3
  • 29
    • 48949098573 scopus 로고    scopus 로고
    • PBT2-201-EURO study group safety efficacy and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimers disease: A Phase IIa double-blind randomised placebo-controlled trial
    • Lannfelt, L, Blennow K, Zetterberg H et al.; PBT2-201-EURO study group. Safety, efficacy, and biomarker findings of PBT2 in targeting Abeta as a modifying therapy for Alzheimers disease: A Phase IIa, double-blind, randomised, placebo-controlled trial. Lancet Neurol. 7(9), 779-786 (2008).
    • (2008) Lancet Neurol. , vol.7 , Issue.9 , pp. 779-786
    • Lannfelt, L.1    Blennow, K.2    Zetterberg, H.3
  • 30
    • 77954344206 scopus 로고    scopus 로고
    • PBT2 rapidly improves cognition in Alzheimers disease: Additional phase II analyses
    • Faux NG, Ritchie CW, Gunn A et al. PBT2 rapidly improves cognition in Alzheimers disease: Additional Phase II analyses. J. Alzheimers Dis. 20(2), 509-516 (2010).
    • (2010) J. Alzheimers Dis. , vol.20 , Issue.2 , pp. 509-516
    • Faux, N.G.1    Ritchie, C.W.2    Gunn, A.3
  • 31
    • 48949085739 scopus 로고    scopus 로고
    • Amyloid-beta immunisation for Alzheimers disease
    • Wisniewski T, Konietzko U. Amyloid-beta immunisation for Alzheimers disease. Lancet Neurol. 7(9), 805-811 (2008).
    • (2008) Lancet Neurol. , vol.7 , Issue.9 , pp. 805-811
    • Wisniewski, T.1    Konietzko, U.2
  • 32
    • 77949886394 scopus 로고    scopus 로고
    • Abeta DNA vaccination for Alzheimers disease: Focus on disease prevention
    • Cribbs DH. Abeta DNA vaccination for Alzheimers disease: focus on disease prevention. CNS Neurol. Disord. Drug Targets 9(2), 207-216 (2010).
    • (2010) CNS Neurol. Disord. Drug Targets , vol.9 , Issue.2 , pp. 207-216
    • Cribbs, D.H.1
  • 33
    • 78650861616 scopus 로고    scopus 로고
    • TAU aggregation is a therapeutic target for Alzheimers disease
    • Takashima A. TAU aggregation is a therapeutic target for Alzheimers disease. Curr. Alzheimer Res. 7(8), 665-669 (2010).
    • (2010) Curr. Alzheimer Res. , vol.7 , Issue.8 , pp. 665-669
    • Takashima, A.1
  • 34
    • 33947101532 scopus 로고    scopus 로고
    • A brief history of tau: The evolving view of the microtubule-associated protein tau in neurodegenerative diseases
    • Lace GL, Wharton SB, Ince PG. A brief history of tau: The evolving view of the microtubule-associated protein tau in neurodegenerative diseases. Clin. Neuropathol. 26(2), 43-58 (2007).
    • (2007) Clin. Neuropathol. , vol.26 , Issue.2 , pp. 43-58
    • Lace, G.L.1    Wharton, S.B.2    Ince, P.G.3
  • 35
    • 0346124139 scopus 로고    scopus 로고
    • Cerebrospinal fluid tau and b amyloid: How well do these biomarkers reflect autopsy-confirmed dementia diagnoses
    • Clark CM, Xie S, Chittams J et al. Cerebrospinal fluid tau and b?amyloid: how well do these biomarkers reflect autopsy-confirmed dementia diagnoses? Arch. Neurol. 60(12), 1696-1702 (2003).
    • (2003) Arch. Neurol. , vol.60 , Issue.12 , pp. 1696-1702
    • Clark, C.M.1    Xie, S.2    Chittams, J.3
  • 36
    • 34249990083 scopus 로고    scopus 로고
    • Assembly of two distinct dimers and higher-order oligomers from full-length tau
    • Sahara N, Maeda S, Murayama M et al. Assembly of two distinct dimers and higher-order oligomers from full-length tau. Eur. J. Neurosci. 25(10), 3020-3029 (2007).
    • (2007) Eur. J. Neurosci. , vol.25 , Issue.10 , pp. 3020-3029
    • Sahara, N.1    Maeda, S.2    Murayama, M.3
  • 37
    • 78649660787 scopus 로고    scopus 로고
    • Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss
    • Kimura T, Fukuda T, Sahara N et al. Aggregation of detergent-insoluble tau is involved in neuronal loss but not in synaptic loss. J. Biol. Chem. 285(49), 38692-38699 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.49 , pp. 38692-38699
    • Kimura, T.1    Fukuda, T.2    Sahara, N.3
  • 38
    • 33947691643 scopus 로고    scopus 로고
    • Granular tau oligomers as intermediates of tau filaments
    • Maeda S, Sahara N, Saito Y et al. Granular tau oligomers as intermediates of tau filaments. Biochemistry 46(12), 3856-3861 (2007).
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3856-3861
    • Maeda, S.1    Sahara, N.2    Saito, Y.3
  • 39
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimers disease
    • Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimers disease. Neurology 42(3 Pt 1), 631-639 (1992).
    • (1992) Neurology , vol.42 , Issue.3 PART 1 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 40
    • 67649199941 scopus 로고    scopus 로고
    • Can lithium or valproate untie tangles in Alzheimers disease
    • Tariot PN, Aisen PS. Can lithium or valproate untie tangles in Alzheimers disease? J. Clin. Psychiatry 70(6), 919-921 (2009).
    • (2009) J.Clin. Psychiatry , vol.70 , Issue.6 , pp. 919-921
    • Tariot, P.N.1    Aisen, P.S.2
  • 41
    • 78650931711 scopus 로고    scopus 로고
    • Recent developments in tau-based therapeutics for neurodegenerative diseases
    • Medina M. Recent developments in tau-based therapeutics for neurodegenerative diseases. Recent Pat. CNS Drug Discov. 6(1), 20-30 (2011).
    • (2011) Recent Pat. CNS Drug Discov. , vol.6 , Issue.1 , pp. 20-30
    • Medina, M.1
  • 42
    • 33847662852 scopus 로고    scopus 로고
    • Protein oligomers in neurodegeneration: Lessons from the Alzheimers amyloid beta-peptide
    • Haass C, Selkoe DJ. Protein oligomers in neurodegeneration: lessons from the Alzheimers amyloid beta-peptide. Nat. Rev. Mol. Cell. Biol. 8(2), 101-112 (2007).
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 44
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimers disease and related tauopathies
    • Brunden KR, Trojanowski JQ, Lee VM. Advances in tau-focused drug discovery for Alzheimers disease and related tauopathies. Nat. Rev. Drug Discov. 8(10), 783-793 (2009).
    • (2009) Nat. Rev. Drug Discov. , vol.8 , Issue.10 , pp. 783-793
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 45
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer C, Acker CM, Kress Y, Hof PR, Duff K, Davies P. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J. Neurosci. 25(22), 5446-5454 (2005).
    • (2005) J. Neurosci. , vol.25 , Issue.22 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 47
    • 77951782384 scopus 로고    scopus 로고
    • Current therapeutic targets for the treatment of Alzheimers disease
    • Grill JD, Cummings JL. Current therapeutic targets for the treatment of Alzheimers disease. Expert Rev. Neurother. 10(5), 711-728 (2010).
    • (2010) Expert Rev. Neurother. , vol.10 , Issue.5 , pp. 711-728
    • Grill, J.D.1    Cummings, J.L.2
  • 49
    • 23044439880 scopus 로고    scopus 로고
    • Cyanine dye N744 inhibits tau fibrillization by blocking filament extension: Implications for the treatment of tauopathic neurodegenerative diseases
    • Necula M, Chirita CN, Kuret J. Cyanine dye N744 inhibits tau fibrillization by blocking filament extension: Implications for the treatment of tauopathic neurodegenerative diseases. Biochemistry 44(30), 10227-10237 (2005).
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10227-10237
    • Necula, M.1    Chirita, C.N.2    Kuret, J.3
  • 50
    • 34548691220 scopus 로고    scopus 로고
    • N-phenylamine derivatives as aggregation inhibitors in cell models of tauopathy
    • Pickhardt M, Biernat J, Khlistunova I et al. N-phenylamine derivatives as aggregation inhibitors in cell models of tauopathy. Curr. Alzheimer Res. 4(4), 397-402 (2007).
    • (2007) Curr. Alzheimer Res. , vol.4 , Issue.4 , pp. 397-402
    • Pickhardt, M.1    Biernat, J.2    Khlistunova, I.3
  • 51
    • 37349128195 scopus 로고    scopus 로고
    • Rhodanine-based tau aggregation inhibitors in cell models of tauopathy. Angew
    • Bulic B, Pickhardt M, Khlistunova I et al. Rhodanine-based tau aggregation inhibitors in cell models of tauopathy. Angew. Chem. Int. Ed. Engl. 46(48), 9215-9219 (2007).
    • (2007) Chem. Int. Ed. Engl. , vol.46 , Issue.48 , pp. 9215-9219
    • Bulic, B.1    Pickhardt, M.2    Khlistunova, I.3
  • 52
    • 34548502687 scopus 로고    scopus 로고
    • Phenylthiazolyl-hydrazide and its derivatives are potent inhibitors of tau aggregation and toxicity in vitro and in cells
    • Pickhardt M, Larbig G, Khlistunova I et al. Phenylthiazolyl-hydrazide and its derivatives are potent inhibitors of tau aggregation and toxicity in vitro and in cells. Biochemistry 46, 10016-10023 (2007).
    • (2007) Biochemistry , vol.46 , pp. 10016-10023
    • Pickhardt, M.1    Larbig, G.2    Khlistunova, I.3
  • 53
    • 13544251748 scopus 로고    scopus 로고
    • Anthraquinones inhibit tau aggregation and dissolve Alzheimers paired helical filaments in vitro and in cells
    • Pickhardt M, Gazova Z, von Bergen M et al. Anthraquinones inhibit tau aggregation and dissolve Alzheimers paired helical filaments in vitro and in cells. J. Biol. Chem. 280(5), 3628-3635 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.5 , pp. 3628-3635
    • Pickhardt, M.1    Gazova, Z.2    Von Bergen, M.3
  • 54
    • 68849086671 scopus 로고    scopus 로고
    • Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening
    • Crowe A, Huang W, Ballatore C et al. Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening. Biochemistry 48(32), 7732-7745 (2009).
    • (2009) Biochemistry , vol.48 , Issue.32 , pp. 7732-7745
    • Crowe, A.1    Huang, W.2    Ballatore, C.3
  • 55
    • 37849030399 scopus 로고    scopus 로고
    • Interactions of methylene blue with human disulfide reductases and their orthologues from Plasmodium falciparum
    • Buchholz K, Schirmer RH, Eubel JK et al. Interactions of methylene blue with human disulfide reductases and their orthologues from Plasmodium falciparum. Antimicrob. Agents Chemother. 52(1), 183-191 (2008).
    • (2008) Antimicrob. Agents Chemother. , vol.52 , Issue.1 , pp. 183-191
    • Buchholz, K.1    Schirmer, R.H.2    Eubel, J.K.3
  • 56
    • 67349200953 scopus 로고    scopus 로고
    • Tau aggregation inhibitor TAI therapy with rember™ arrests disease progression in mild and moderate Alzheimers disease over 50 weeks
    • Wischik CM, Bentham P, Wischik DJ, Seng KM. Tau aggregation inhibitor (TAI) therapy with Rember™ arrests disease progression in mild and moderate Alzheimers disease over 50 weeks. Alzheimers Dement. 4(Suppl. 1), T167 (2008).
    • (2008) Alzheimers Dement. , vol.4 , Issue.1
    • Wischik, C.M.1    Bentham, P.2    Wischik, D.J.3    Seng, K.M.4
  • 57
    • 77958566761 scopus 로고    scopus 로고
    • Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
    • O'Leary JC 3rd, Li Q, Marinec P et al. Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden. Mol. Neurodegener. 5, 45 (2010).
    • (2010) Mol. Neurodegener. , vol.5 , Issue.45
    • O'Leary III, J.C.1    Li, Q.2    Marinec, P.3
  • 58
    • 65249128503 scopus 로고    scopus 로고
    • Challenges in the conduct of disease-modifying trials in AD: Practical experience from a phase 2 trial of tau-aggregation inhibitor therapy
    • Wischik C, Staff R. Challenges in the conduct of disease-modifying trials in AD: Practical experience from a Phase 2 trial of tau-aggregation inhibitor therapy. J. Nutr. Health Aging 13(4), 367-369 (2009).
    • (2009) J. Nutr. Health Aging , vol.13 , Issue.4 , pp. 367-369
    • Wischik, C.1    Staff, R.2
  • 59
    • 77649263106 scopus 로고    scopus 로고
    • Tau aggregation inhibitor TAI therapy with rember™ arrests the trajectory of rCBF decline in brain regions affected by tau pathology in mild and moderate Alzheimers disease AD
    • Staff RT, Ahearn TS, Murray AD et al. Tau aggregation inhibitor (TAI) therapy with Rember™ arrests the trajectory of rCBF decline in brain regions affected by tau pathology in mild and moderate Alzheimers disease (AD). Alzheimers Dement. 4(Suppl. 2), T775 (2008).
    • (2008) Alzheimers Dement. , vol.4 , Issue.2
    • Staff, R.T.1    Ahearn, T.S.2    Murray, A.D.3
  • 60
    • 68949213262 scopus 로고    scopus 로고
    • Tau aggregation inhibitor TAI therapy with rember™ changes glucose metabolism in the medial temporal lobes in mild and moderate Alzheimers disease AD
    • Murray AD, Staff RT, Ahearn TS et al. Tau aggregation inhibitor (TAI) therapy with Rember™ changes glucose metabolism in the medial temporal lobes in mild and moderate Alzheimers disease (AD). Alzheimers Dement. 4(Suppl. 2), T786 (2008).
    • (2008) Alzheimers Dement. , vol.4 , Issue.2
    • Murray, A.D.1    Staff, R.T.2    Ahearn, T.S.3
  • 61
    • 33646570598 scopus 로고    scopus 로고
    • Small molecule inhibitors of alpha-synuclein filament assembly
    • Masuda M, Suzuki N, Taniguchi S et al. Small molecule inhibitors of alpha-synuclein filament assembly. Biochemistry 45(19), 6085-6094 (2009).
    • (2009) Biochemistry , vol.45 , Issue.19 , pp. 6085-6094
    • Masuda, M.1    Suzuki, N.2    Taniguchi, S.3
  • 62
    • 46749113005 scopus 로고    scopus 로고
    • Tau-based treatment strategies in neurodegenerative diseases
    • Schneider A, Mandelkow E. Tau-based treatment strategies in neurodegenerative diseases. Neurotherapeutics 5(3), 443-457 (2008).
    • (2008) Neurotherapeutics , vol.5 , Issue.3 , pp. 443-457
    • Schneider, A.1    Mandelkow, E.2
  • 63
    • 17044461433 scopus 로고    scopus 로고
    • The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimers disease
    • Illenberger S, Zheng-Fischhofer Q, Preuss U et al. The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: Implications for Alzheimers disease. Mol. Biol. Cell 9(6), 1495-1512 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , Issue.6 , pp. 1495-1512
    • Illenberger, S.1    Zheng-Fischhofer, Q.2    Preuss, U.3
  • 64
    • 40449087334 scopus 로고    scopus 로고
    • Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3b mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing
    • Wen Y, Planel E, Herman M et al. Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3b mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing. J. Neurosci. 28(10), 2624-2632 (2008).
    • (2008) J. Neurosci. , vol.28 , Issue.10 , pp. 2624-2632
    • Wen, Y.1    Planel, E.2    Herman, M.3
  • 65
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F, Angelo M, Giese KP. The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 281(35), 25457-25465 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.35 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 66
    • 0030779517 scopus 로고    scopus 로고
    • An open trial of valproate for agitation in geriatric neuropsychiatric disorders
    • Porsteinsson AP, Tariot PN, Erb R, Gaile S. An open trial of valproate for agitation in geriatric neuropsychiatric disorders. Am. J. Geriatr. Psychiatry 5(4), 344-351 (1997).
    • (1997) Am. J. Geriatr. Psychiatry , vol.5 , Issue.4 , pp. 344-351
    • Porsteinsson, A.P.1    Tariot, P.N.2    Erb, R.3    Gaile, S.4
  • 67
    • 0038679746 scopus 로고    scopus 로고
    • Valproate therapy for agitation in dementia: Open-label extension of a double-blind trial
    • Porsteinsson AP, Tariot PN, Jakimovich LJ et al. Valproate therapy for agitation in dementia: open-label extension of a double-blind trial. Am. J. Geriatr. Psychiatry 11(4), 434-440 (2003).
    • (2003) Am. J. Geriatr. Psychiatry , vol.11 , Issue.4 , pp. 434-440
    • Porsteinsson, A.P.1    Tariot, P.N.2    Jakimovich, L.J.3
  • 68
    • 65549090537 scopus 로고    scopus 로고
    • Increase of BDNF serum concentration in lithium treated patients with early Alzheimers disease
    • Leyhe T, Eschweiler GW, Stransky E et al. Increase of BDNF serum concentration in lithium treated patients with early Alzheimers disease. J. Alzheimers Dis. 16(3), 649-656 (2009).
    • (2009) J. Alzheimers Dis. , vol.16 , Issue.3 , pp. 649-656
    • Leyhe, T.1    Eschweiler, G.W.2    Stransky, E.3
  • 69
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in Alzheimers disease: A randomized single-blind placebo-controlled multicenter 10 week study
    • Hampel H, Ewers M, Burger K et al. Lithium trial in Alzheimers disease: A randomized, single-blind, placebo-controlled, multicenter 10?week study. J. Clin. Psychiatry 70(6), 922-931 (2009).
    • (2009) J. Clin. Psychiatry , vol.70 , Issue.6 , pp. 922-931
    • Hampel, H.1    Ewers, M.2    Burger, K.3
  • 70
    • 77951777616 scopus 로고    scopus 로고
    • The ADCS valproate neuroprotection trial: Primary efficacy and safety results
    • Tariot PN, Aisen P, Cummings J et al. The ADCS valproate neuroprotection trial: Primary efficacy and safety results. Alzheimers Dement. 5(4), P84-P85 (2009).
    • (2009) Alzheimers Dement. , vol.5 , Issue.4
    • Tariot, P.N.1    Aisen, P.2    Cummings, J.3
  • 71
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease
    • Gong CX, Iqbal K. Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease. Curr. Med. Chem. 15(23), 2321-2328 (2008).
    • (2008) Curr. Med. Chem. , vol.15 , Issue.23 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 72
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatise 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins S, Crameri A, Evans DR, Hemmings BA, Nitsch RM, Gotz J. Reduced protein phosphatise 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276(41), 38193-38200 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.41 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Gotz, J.6
  • 73
    • 0028786849 scopus 로고
    • Paired helical filament-like phosphorylation of tau deposition of b/A4 amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A
    • Arendt T, Holzer M, Fruth R, Bruckner MK, Gartner U. Paired helical filament-like phosphorylation of tau, deposition of b/A4?amyloid and memory impairment in rat induced by chronic inhibition of phosphatase 1 and 2A. Neuroscience 69(3), 691-698 (1995).
    • (1995) Neuroscience , vol.69 , Issue.3 , pp. 691-698
    • Arendt, T.1    Holzer, M.2    Fruth, R.3    Bruckner, M.K.4    Gartner, U.5
  • 74
    • 18544370897 scopus 로고    scopus 로고
    • Significance and mechanism of Alzheimer neurofibrillary degeneration and therapeutic targets to inhibit this lesion
    • Iqbal K, Alonso Adel C, El-Akkad E et al. Significance and mechanism of Alzheimer neurofibrillary degeneration and therapeutic targets to inhibit this lesion. J. Mol. Neurosci. 19(1-2), 95-99 (2002).
    • (2002) J. Mol. Neurosci. , vol.19 , Issue.1-2 , pp. 95-99
    • Iqbal, K.1    Alonso Adel, C.2    El-Akkad, E.3
  • 76
    • 77952549757 scopus 로고    scopus 로고
    • Targeting Abeta and tau in Alzheimers disease an early interim report
    • Golde TE, Petrucelli L, Lewis J. Targeting Abeta and tau in Alzheimers disease, an early interim report. Exp. Neurol. 223(2), 252-266 (2010).
    • (2010) Exp. Neurol. , vol.223 , Issue.2 , pp. 252-266
    • Golde, T.E.1    Petrucelli, L.2    Lewis, J.3
  • 77
    • 0033049956 scopus 로고    scopus 로고
    • Complete sequence of a novel protein containing a femtomolar-activity- dependent neuroprotective peptide
    • Bassan M, Zamostiano R et al. Complete sequence of a novel protein containing a femtomolar-activity-dependent neuroprotective peptide. J. Neurochem. 72(3), 1283-1293 (1999).
    • (1999) J. Neurochem. , vol.72 , Issue.3 , pp. 1283-1293
    • Bassan, M.1    Zamostiano, R.2
  • 78
    • 34548260005 scopus 로고    scopus 로고
    • Looking for novel ways to treat the hallmarks of Alzheimers disease
    • Stewart AJ, Fox A, Morimoto BH, Gozes I. Looking for novel ways to treat the hallmarks of Alzheimers disease. Expert Opin. Investig. Drugs 16(8), 1183-1196 (2007).
    • (2007) Expert Opin. Investig. Drugs , vol.16 , Issue.8 , pp. 1183-1196
    • Stewart, A.J.1    Fox, A.2    Morimoto, B.H.3    Gozes, I.4
  • 79
    • 0034083868 scopus 로고    scopus 로고
    • Activity-dependent neurotrophic factor: Intranasal administration of femtomolar-acting peptides improve performance in a water maze
    • Gozes I, Giladi E, Pinhasov A, Bardea A, Brenneman DE. Activity-dependent neurotrophic factor: Intranasal administration of femtomolar-acting peptides improve performance in a water maze. J. Pharmacol. Exp. Ther. 293(3), 1091-1098 (2000).
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , Issue.3 , pp. 1091-1098
    • Gozes, I.1    Giladi, E.2    Pinhasov, A.3    Bardea, A.4    Brenneman, D.E.5
  • 81
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloidβ attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W et al. Immunization with amyloidβ attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400(6740), 173-177 (1999).
    • (1999) Nature , vol.400 , Issue.6740 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 82
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimers disease
    • Morgan D, Diamond D, Gottschall P et al. A beta peptide vaccination prevents memory loss in an animal model of Alzheimers disease. Nature 408(6815), 982-985 (2000).
    • (2000) Nature , vol.408 , Issue.6815 , pp. 982-985
    • Morgan, D.1    Diamond, D.2    Gottschall, P.3
  • 83
    • 77954956280 scopus 로고    scopus 로고
    • Immunization with the SDPM1 peptide lowers amyloid plaque burden and improves cognitive function in the APPswePSEN1 A246E transgenic mouse model of Alzheimers disease
    • Wang CM, Devries S, Camboni M, Glass M, Martin PT. Immunization with the SDPM1 peptide lowers amyloid plaque burden and improves cognitive function in the APPswePSEN1(A246E) transgenic mouse model of Alzheimers disease. Neurobiol. Dis. 39(3), 409-422 (2010).
    • (2010) Neurobiol. Dis. , vol.39 , Issue.3 , pp. 409-422
    • Wang, C.M.1    Devries, S.2    Camboni, M.3    Glass, M.4    Martin, P.T.5
  • 84
    • 79959670013 scopus 로고    scopus 로고
    • The second-generation active Ab immunotherapy CAD106 reduces amyloid accumulation in APP transgenic mice while minimizing potential side effects
    • Wiessner C, Wiederhold KH, Tissot AC et al. The second-generation active Ab immunotherapy CAD106 reduces amyloid accumulation in APP transgenic mice while minimizing potential side effects. J. Neurosci. 31(25), 9323-9331 (2011).
    • (2011) J. Neurosci. , vol.31 , Issue.25 , pp. 9323-9331
    • Wiessner, C.1    Wiederhold, K.H.2    Tissot, A.C.3
  • 85
    • 0034884382 scopus 로고    scopus 로고
    • Immunization with a non-toxic/non-fibrillar amyloidβ homologous peptide reduces Alzheimers disease associated pathology in transgenic mice
    • Sigurdsson EM, Scholtzova H, Mehta P, Frangione B, Wisniewski T. Immunization with a non-toxic/non-fibrillar amyloidβ homologous peptide reduces Alzheimers disease associated pathology in transgenic mice. Am. J. Pathol. 159(2), 439-447 (2001).
    • (2001) Am. J. Pathol. , vol.159 , Issue.2 , pp. 439-447
    • Sigurdsson, E.M.1    Scholtzova, H.2    Mehta, P.3    Frangione, B.4    Wisniewski, T.5
  • 86
    • 33646938005 scopus 로고    scopus 로고
    • Short amyloid beta Abeta immunogens reduce cerebral a beta load and learning deficits in an Alzheimers disease mouse model in the absence of an Abeta-specific cellular immune response
    • Maier M, Seabrook TJ, Lazo ND et al. Short amyloid beta (Abeta) immunogens reduce cerebral Abeta load and learning deficits in an Alzheimers disease mouse model in the absence of an Abeta-specific cellular immune response. J. Neurosci. 26(18), 4717-4728 (2006).
    • (2006) J. Neurosci. , vol.26 , Issue.18 , pp. 4717-4728
    • Maier, M.1    Seabrook, T.J.2    Lazo, N.D.3
  • 87
    • 0034633632 scopus 로고    scopus 로고
    • Immunization against Alzheimers beta amyloid plaques via EFRH phage administration
    • USA
    • Frenkel D, Katz O, Solomon B. Immunization against Alzheimers beta ?amyloid plaques via EFRH phage administration. Proc. Natl Acad. Sci. USA 97(21), 11455-11459 (2000).
    • (2000) Proc. Natl Acad. Sci. , vol.97 , Issue.21 , pp. 11455-11459
    • Frenkel, D.1    Katz, O.2    Solomon, B.3
  • 88
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R et al. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat. Med. 6(8), 916-919 (2000).
    • (2000) Nat. Med. , vol.6 , Issue.8 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3
  • 89
    • 79953699669 scopus 로고    scopus 로고
    • Chronic intranasal treatment with an anti-Ab 30-42 scFv antibody ameliorates amyloid pathology in a transgenic mouse model of Alzheimers disease
    • Cattepoel S, Hanenberg M, Kulic L, Nitsch RM. Chronic intranasal treatment with an anti-Ab(30-42) scFv antibody ameliorates amyloid pathology in a transgenic mouse model of Alzheimers disease. PLoS ONE 6(4), E18296 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.4
    • Cattepoel, S.1    Hanenberg, M.2    Kulic, L.3    Nitsch, R.M.4
  • 90
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid b deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • Bacskai BJ, Kajdasz ST, Christie RH et al. Imaging of amyloidβ deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy. Nat. Med. 7(3), 369-372 (2001).
    • (2001) Nat. Med. , vol.7 , Issue.3 , pp. 369-372
    • Bacskai, B.J.1    Kajdasz, S.T.2    Christie, R.H.3
  • 91
    • 0030058382 scopus 로고    scopus 로고
    • Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer b amyloid peptide
    • USA
    • Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer b?amyloid peptide. Proc. Natl Acad. Sci. USA 93(1), 452-455 (1996).
    • (1996) Proc. Natl Acad. Sci. , vol.93 , Issue.1 , pp. 452-455
    • Solomon, B.1    Koppel, R.2    Hanan, E.3    Katzav, T.4
  • 92
    • 0141457897 scopus 로고    scopus 로고
    • Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice
    • Das P, Howard V, Loosbrock N, Dickson D, Murphy MP, Golde TE. Amyloid-beta immunization effectively reduces amyloid deposition in FcRgamma-/- knock-out mice. J. Neurosci. 23(24), 8532-8538 (2003).
    • (2003) J. Neurosci. , vol.23 , Issue.24 , pp. 8532-8538
    • Das, P.1    Howard, V.2    Loosbrock, N.3    Dickson, D.4    Murphy, M.P.5    Golde, T.E.6
  • 93
    • 3242694207 scopus 로고    scopus 로고
    • An attenuated immune response is sufficient to enhance cognition in an Alzheimers disease mouse model immunized with amyloid b derivatives
    • Sigurdsson EM, Knudsen E, Asuni A et al. An attenuated immune response is sufficient to enhance cognition in an Alzheimers disease mouse model immunized with amyloidβ derivatives. J. Neurosci. 24(28), 6277-6282 (2004).
    • (2004) J. Neurosci. , vol.24 , Issue.28 , pp. 6277-6282
    • Sigurdsson, E.M.1    Knudsen, E.2    Asuni, A.3
  • 94
    • 47949132196 scopus 로고    scopus 로고
    • Active and passive immunotherapy for neurodegenerative disorders
    • Brody DL, Holtzman DM. Active and passive immunotherapy for neurodegenerative disorders. Annu. Rev. Neurosci. 31, 175-193 (2008).
    • (2008) Annu. Rev. Neurosci. , vol.31 , pp. 175-193
    • Brody, D.L.1    Holtzman, D.M.2
  • 95
    • 33749614555 scopus 로고    scopus 로고
    • Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein
    • Rosenmann H, Grigoriadis N, Karussis D et al. Tauopathy-like abnormalities and neurologic deficits in mice immunized with neuronal tau protein. Arch. Neurol. 63(10), 1459-1467 (2006).
    • (2006) Arch. Neurol. , vol.63 , Issue.10 , pp. 1459-1467
    • Rosenmann, H.1    Grigoriadis, N.2    Karussis, D.3
  • 96
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy safety of immunization with phosphorylated tau against neurofibrillary and tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A et al. Efficacy safety of immunization with phosphorylated tau against neurofibrillary and tangles in mice. Exp. Neurol. 224(2), 472-485 (2010).
    • (2010) Exp. Neurol. , vol.224 , Issue.2 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3
  • 97
    • 78650945635 scopus 로고    scopus 로고
    • Tau vaccine: Active immunization with misfloded tau protein attenuates tau pathology in the transgenic rat model of tauopathy
    • (Abstract)
    • Novak M. Tau vaccine: Active immunization with misfloded tau protein attenuates tau pathology in the transgenic rat model of tauopathy. Alzheimers Dement. 5(Suppl. 1), P93 (2009) (Abstract).
    • (2009) Alzheimers Dement. , vol.5 , Issue.1
    • Novak, M.1
  • 98
    • 54249107245 scopus 로고    scopus 로고
    • Chaperone-like antibodies targeting misfolded tau protein: New vistas in the immunotherapy of neurodegenerative foldopathies
    • Zilka N, Kontsekova E, Novak M. Chaperone-like antibodies targeting misfolded tau protein: new vistas in the immunotherapy of neurodegenerative foldopathies. J. Alzheimers Dis. 15(2), 169-179 (2008).
    • (2008) J. Alzheimers Dis. , vol.15 , Issue.2 , pp. 169-179
    • Zilka, N.1    Kontsekova, E.2    Novak, M.3
  • 99
    • 68149124522 scopus 로고    scopus 로고
    • Chaperone-like antibodies in neurodegenerative tauopathies: Implication for immunotherapy
    • Kontsekova E, Ivanovova N, Handzusova M, Novak M. Chaperone-like antibodies in neurodegenerative tauopathies: Implication for immunotherapy. Cell. Mol. Neurobiol. 29(6-7), 793-798 (2009).
    • (2009) Cell. Mol. Neurobiol. , vol.29 , Issue.6-7 , pp. 793-798
    • Kontsekova, E.1    Ivanovova, N.2    Handzusova, M.3    Novak, M.4
  • 100
    • 49149098525 scopus 로고    scopus 로고
    • Tau aggregates: Toxic inert or protective species
    • Bretteville A, Planel E. Tau aggregates: Toxic, inert, or protective species? J. Alzheimers Dis. 14(4), 431-436 (2008).
    • (2008) J. Alzheimers Dis. , vol.14 , Issue.4 , pp. 431-436
    • Bretteville, A.1    Planel, E.2
  • 101
    • 49149109927 scopus 로고    scopus 로고
    • Is tau aggregation toxic or protective
    • Congdon EE, Duff KE. Is tau aggregation toxic or protective? J. Alzheimers Dis. 14(4), 453-457 (2008).
    • (2008) J. Alzheimers Dis. , vol.14 , Issue.4 , pp. 453-457
    • Congdon, E.E.1    Duff, K.E.2
  • 102
    • 67049136162 scopus 로고    scopus 로고
    • Prefilament tau species as potential targets for immunotherapy for Alzheimer disease and related disorders
    • Kayed R, Jackson GR. Prefilament tau species as potential targets for immunotherapy for Alzheimer disease and related disorders. Curr. Opin. Immunol. 21(3), 359-363 (2009)
    • (2009) Curr. Opin. Immunol. , vol.21 , Issue.3 , pp. 359-363
    • Kayed, R.1    Jackson, G.R.2
  • 103
    • 34248190279 scopus 로고    scopus 로고
    • Abeta oligomers - A decade of discovery
    • Walsh DM, Selkoe DJ. Abeta oligomers - a decade of discovery. J. Neurochem. 101(5), 1172-1184 (2007).
    • (2007) J. Neurochem. , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 104
    • 11444267243 scopus 로고    scopus 로고
    • Evaluation of the safety and immunogenicity of synthetic Ab42 AN1792 in patients with AD
    • Bayer AJ, Bullock R, Jones RW et al. Evaluation of the safety and immunogenicity of synthetic Ab42 (AN1792) in patients with AD. Neurology 64(1), 94-101 (2005).
    • (2005) Neurology , vol.64 , Issue.1 , pp. 94-101
    • Bayer, A.J.1    Bullock, R.2    Jones, R.W.3
  • 105
    • 40449086748 scopus 로고    scopus 로고
    • Progress in the active immunotherapeutic approach to Alzheimers disease: Clinical investigations into AN1792- associated meningoencephalitis
    • Pride M, Seubert P, Grundman M, Hagen M, Eldridge J, Black RS. Progress in the active immunotherapeutic approach to Alzheimers disease: Clinical investigations into AN1792- associated meningoencephalitis. Neurodegener. Dis. 5(3-4), 194-196 (2008).
    • (2008) Neurodegener. Dis. , vol.5 , Issue.3-4 , pp. 194-196
    • Pride, M.1    Seubert, P.2    Grundman, M.3    Hagen, M.4    Eldridge, J.5    Black, R.S.6
  • 106
    • 10744230547 scopus 로고    scopus 로고
    • Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization
    • Orgogozo JM, Gilman S, Dartigues JF et al. Subacute meningoencephalitis in a subset of patients with AD after Abeta42 immunization. Neurology 61(1), 46-54 (2003).
    • (2003) Neurology , vol.61 , Issue.1 , pp. 46-54
    • Orgogozo, J.M.1    Gilman, S.2    Dartigues, J.F.3
  • 107
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid beta immunization in Alzheimers disease
    • Ferrer I, Boada Rovira M, Sánchez Guerra ML, Rey MJ, Costa-Jussá F. Neuropathology and pathogenesis of encephalitis following amyloid?beta immunization in Alzheimers disease. Brain Pathol. 14(1), 11-20 (2004).
    • (2004) Brain Pathol. , vol.14 , Issue.1 , pp. 11-20
    • Ferrer, I.1    Boada Rovira, M.2    Sánchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussá, F.5
  • 108
    • 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(4), 448?452 (2003).
    • (2003) Nat. Med. , vol.9 , Issue.4 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 109
    • 77956507245 scopus 로고    scopus 로고
    • T cells specifically targeted to amyloid plaques enhance plaque clearance in a mouse model of Alzheimers disease
    • Fisher Y, Nemirovsky A, Baron R, Monsonego A. T cells specifically targeted to amyloid plaques enhance plaque clearance in a mouse model of Alzheimers disease. PLoS ONE 26, 5(5), E10830 (2010).
    • (2010) PLoS ONE 26 , vol.5 , Issue.5
    • Fisher, Y.1    Nemirovsky, A.2    Baron, R.3    Monsonego, A.4
  • 110
    • 34247113214 scopus 로고    scopus 로고
    • Absence of beta amyloid deposits after immunization in Alzheimer disease with lewy body dementia
    • Bombois S, Maurage CA, Gompel M et al. Absence of beta?amyloid deposits after immunization in Alzheimer disease with Lewy body dementia. Arch. Neurol. 64(4), 583-587 (2007).
    • (2007) Arch. Neurol. , vol.64 , Issue.4 , pp. 583-587
    • Bombois, S.1    Maurage, C.A.2    Gompel, M.3
  • 111
    • 19944429065 scopus 로고    scopus 로고
    • Ab vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
    • Masliah E, Hansen L, Adame A et al. Ab vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease. Neurology 64(1), 129-131 (2005).
    • (2005) Neurology , vol.64 , Issue.1 , pp. 129-131
    • Masliah, E.1    Hansen, L.2    Adame, A.3
  • 112
    • 0038100154 scopus 로고    scopus 로고
    • Antibodies against b-amyloid slow cognitive decline in Alzheimers disease
    • Hock C, Konietzko U, Streffer JR et al. Antibodies against b-amyloid slow cognitive decline in Alzheimers disease. Neuron 38(4), 547-554 (2003).
    • (2003) Neuron , vol.38 , Issue.4 , pp. 547-554
    • Hock, C.1    Konietzko, U.2    Streffer, J.R.3
  • 113
    • 47149112621 scopus 로고    scopus 로고
    • Long-term effects of Ab42 immunisation in Alzheimers disease: Follow-up of a randomised placebo-controlled Phase I trial
    • Holmes C, Boche D, Wilkinson D et al. Long-term effects of Ab42 immunisation in Alzheimers disease: follow-up of a randomised, placebo-controlled Phase I trial. Lancet 372(9634), 216-223 (2008).
    • (2008) Lancet , vol.372 , Issue.9634 , pp. 216-223
    • Holmes, C.1    Boche, D.2    Wilkinson, D.3
  • 114
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Ab42 fibrils
    • Götz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Ab42 fibrils. Science 293(5534), 1491-1495 (2001).
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 116
    • 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(3), 321-332 (2004).
    • (2004) Neuron , vol.43 , Issue.3 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 117
    • 77949431000 scopus 로고    scopus 로고
    • Immunization therapy for Alzheimer disease: A comprehensive review of active immunization strategies
    • Tabira T. Immunization therapy for Alzheimer disease: A comprehensive review of active immunization strategies. Tohoku J. Exp. Med. 220(2), 95-106 (2010).
    • (2010) Tohoku J. Exp. Med. , vol.220 , Issue.2 , pp. 95-106
    • Tabira, T.1
  • 118
    • 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(2), 108-119 (2010).
    • (2010) Nat. Rev. Neurol. , vol.6 , Issue.2 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 119
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Ab1-42 immunization in APP transgenic mice with significant amyloid deposition
    • Das P, Murphy M, Younkin L, Younkin S, Golde T. Reduced effectiveness of Ab1-42 immunization in APP transgenic mice with significant amyloid deposition. Neurobiol. Aging 22(5), 721-727 (2010).
    • (2010) Neurobiol. Aging , vol.22 , Issue.5 , pp. 721-727
    • Das, P.1    Murphy, M.2    Younkin, L.3    Younkin, S.4    Golde, T.5
  • 120
    • 0037424110 scopus 로고    scopus 로고
    • Reduction of b amyloid plaques in brain of transgenic mouse model of Alzheimers disease by EFRH-phage immunization
    • Frenkel D, Dewachter I, van Leuven F, Solomon B. Reduction of b?amyloid plaques in brain of transgenic mouse model of Alzheimers disease by EFRH-phage immunization. Vaccine 21(11-12), 1060-1065 (2003).
    • (2003) Vaccine , vol.21 , Issue.11-12 , pp. 1060-1065
    • Frenkel, D.1    Dewachter, I.2    Van Leuven, F.3    Solomon, B.4
  • 121
    • 12444268257 scopus 로고    scopus 로고
    • Prototype Alzheimers disease vaccine using the immunodominant B cell epitope from b amyloid and promiscuous T cell epitope pan HLA DR-binding peptide
    • Agadjanyan MG, Ghochikyan A, Petrushina I et al. Prototype Alzheimers disease vaccine using the immunodominant B cell epitope from b?amyloid and promiscuous T cell epitope pan HLA DR-binding peptide. J. Immunol. 174(3), 1580-1586 (2005).
    • (2005) J. Immunol. , vol.174 , Issue.3 , pp. 1580-1586
    • Agadjanyan, M.G.1    Ghochikyan, A.2    Petrushina, I.3
  • 122
    • 36248941497 scopus 로고    scopus 로고
    • Alzheimers disease peptide epitope vaccine reduces insoluble but not soluble/oligomeric Ab species in amyloid precursor protein transgenic mice
    • Petrushina I, Ghochikyan A, Mktrichyan M et al. Alzheimers disease peptide epitope vaccine reduces insoluble but not soluble/oligomeric Ab species in amyloid precursor protein transgenic mice. J. Neurosci. 27(46), 12721-12731 (2007).
    • (2007) J. Neurosci. , vol.27 , Issue.46 , pp. 12721-12731
    • Petrushina, I.1    Ghochikyan, A.2    Mktrichyan, M.3
  • 124
    • 33745476486 scopus 로고    scopus 로고
    • Nonviral a beta DNA vaccine therapy against Alzheimers disease: Long-term effects and safety
    • USA
    • Okura Y, Miyakoshi A, Kohyama K, Park IK, Staufenbiel M, Matsumoto Y. Nonviral Abeta DNA vaccine therapy against Alzheimers disease: long-term effects and safety. Proc. Natl Acad. Sci. USA 103(25), 9619-9624 (2006).
    • (2006) Proc. Natl Acad. Sci. , vol.103 , Issue.25 , pp. 9619-9624
    • Okura, Y.1    Miyakoshi, A.2    Kohyama, K.3    Park, I.K.4    Staufenbiel, M.5    Matsumoto, Y.6
  • 125
    • 47749107621 scopus 로고    scopus 로고
    • Reducing AD-like pathology in 3xTg-AD mouse model by DNA epitope vaccine - A novel immunotherapeutic strategy
    • Movsesyan N, Ghochikyan A, Mkrtichyan M et al. Reducing AD-like pathology in 3xTg-AD mouse model by DNA epitope vaccine-a novel immunotherapeutic strategy. PLoS ONE 3, E2124 (2008).
    • (2008) PLoS ONE , vol.3
    • Movsesyan, N.1    Ghochikyan, A.2    Mkrtichyan, M.3
  • 126
    • 67649207270 scopus 로고    scopus 로고
    • Vaccination with Ab-displaying virus-like particles reduces soluble and insoluble cerebral Ab and lowers plaque burden in APP transgenic mice
    • Bach P, Tschäpe JA, Kopietz F et al. Vaccination with Ab-displaying virus-like particles reduces soluble and insoluble cerebral Ab and lowers plaque burden in APP transgenic mice. J. Immunol. 182(12), 7613-7624 (2008).
    • (2008) J. Immunol. , vol.182 , Issue.12 , pp. 7613-7624
    • Bach, P.1    Tschäpe, J.A.2    Kopietz, F.3
  • 127
    • 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 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
  • 128
    • 10744225891 scopus 로고    scopus 로고
    • A novel recombinant adeno-associated virus vaccine reduces behavioral impairment and beta?amyloid plaques in a mouse model of Alzheimers disease
    • Zhang J, Wu X, Qin C et al. A novel recombinant adeno-associated virus vaccine reduces behavioral impairment and beta?amyloid plaques in a mouse model of Alzheimers disease. Neurobiol. Dis. 14(3), 365-379 (2003).
    • (2003) Neurobiol. Dis. , vol.14 , Issue.3 , pp. 365-379
    • Zhang, J.1    Wu, X.2    Qin, C.3
  • 129
    • 43949141594 scopus 로고    scopus 로고
    • A nasal proteosome adjuvant activates microglia and prevents amyloid deposition
    • Frenkel D, Puckett L, Petrovic S et al. A nasal proteosome adjuvant activates microglia and prevents amyloid deposition. Ann. Neurol. 63(5), 591?601(2008).
    • (2008) Ann. Neurol. , vol.63 , Issue.5 , pp. 591-601
    • Frenkel, D.1    Puckett, L.2    Petrovic, S.3
  • 130
    • 0033801852 scopus 로고    scopus 로고
    • Nasal administration of amyloid b peptide decreases cerebral amyloid burden in a mouse model of Alzheimers disease
    • Weiner HL, Lemere CA, Maron R et al. Nasal administration of amyloidβ peptide decreases cerebral amyloid burden in a mouse model of Alzheimers disease. Ann. Neurol. 48(4), 567-579 (2000).
    • (2000) Ann. Neurol. , vol.48 , Issue.4 , pp. 567-579
    • Weiner, H.L.1    Lemere, C.A.2    Maron, R.3
  • 131
    • 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. 27(34), 9115-9129 (2007).
    • (2007) J. Neurosci. , vol.27 , Issue.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 132
    • 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 et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 5(4), 402-405 (2000).
    • (2000) Nat. Genet. , vol.5 , Issue.4 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 133
    • 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 et al. A novel transgenic mouse expressing double mutant tau driven by its natural promoter exhibits tauopathy characteristics. Exp. Neurol. 212(1), 71?78 (2008).
    • (2008) Exp. Neurol. , vol.212 , Issue.1 , pp. 71-78
    • Rosenmann, H.1    Grigoriadis, N.2    Eldar-Levy, H.3
  • 134
    • 54249154953 scopus 로고    scopus 로고
    • Tau immunotherapy prevents cognitive decline and clears pathological tau in a tangle mouse model
    • Sigurdsson EM, Quatermain D, Boutajangout A. Tau immunotherapy prevents cognitive decline and clears pathological tau in a tangle mouse model. Alzheimeirs Dement. 4(Suppl. 1), T191 (2008).
    • (2008) Alzheimeirs Dement. , vol.4 , Issue.1
    • Sigurdsson, E.M.1    Quatermain, D.2    Boutajangout, A.3
  • 135
    • 78650940116 scopus 로고    scopus 로고
    • Immunotherapy targeting Alzheimers phosphor-tau epitope within the microtubule binding region of tau clears pathological tau and prevents functional decline in a mouse model of tauopathy
    • Khrisnamurthy PK, Sait HBR, Boutajangout A, Sigurdsson EM. Immunotherapy targeting Alzheimers phosphor-tau epitope within the microtubule binding region of tau clears pathological tau and prevents functional decline in a mouse model of tauopathy. Alzheimeirs Dement. 5(Suppl. 1), P112 (2009).
    • (2009) Alzheimeirs Dement. , vol.5 , Issue.1
    • Khrisnamurthy, P.K.1    Sait, H.B.R.2    Boutajangout, A.3    Sigurdsson, E.M.4
  • 136
    • 0041803006 scopus 로고    scopus 로고
    • Hyperphosphsorylation and aggregation of tau in mice expressing normal human tau isoforms
    • Andorfer C, Kress Y, Espinoza M et al. Hyperphosphsorylation and aggregation of tau in mice expressing normal human tau isoforms. J. Neurochem. 86(3), 582-590 (2003).
    • (2003) J. Neurochem. , vol.86 , Issue.3 , pp. 582-590
    • Andorfer, C.1    Kress, Y.2    Espinoza, M.3
  • 137
    • 54249108302 scopus 로고    scopus 로고
    • Presenilin 1 mutation promotes tau phosphorylation and aggregation in a novel Alzheimers disease mouse model
    • Boutajangout A, Frangione B, Brion JP, Wisniewsky T, Sigurdsson EM. Presenilin 1 mutation promotes tau phosphorylation and aggregation in a novel Alzheimers disease mouse model. Alzheimeirs Dement. 4(Suppl. 1), T185 (2008).
    • (2008) Alzheimeirs Dement. , vol.4 , Issue.1
    • Boutajangout, A.1    Frangione, B.2    Brion, J.P.3    Wisniewsky, T.4    Sigurdsson, E.M.5
  • 138
    • 77956057086 scopus 로고    scopus 로고
    • Murine models of Alzheimers disease and their use in developing immunotherapies
    • Wisniewski T, Sigurdsson EM. Murine models of Alzheimers disease and their use in developing immunotherapies. Biochim. Biophys. Acta 1802(10), 847-859 (2010).
    • (2010) Biochim. Biophys. Acta. , vol.1802 , Issue.10 , pp. 847-859
    • Wisniewski, T.1    Sigurdsson, E.M.2
  • 139
    • 78649360496 scopus 로고    scopus 로고
    • Anti-tau oligomers passive vaccination for the treatment of Alzheimer disease
    • Kayed R. Anti-tau oligomers passive vaccination for the treatment of Alzheimer disease. Hum. Vaccin. 6(11), 931-935 (2010).
    • (2010) Hum. Vaccin. , vol.6 , Issue.11 , pp. 931-935
    • Kayed, R.1
  • 140
    • 67649295517 scopus 로고    scopus 로고
    • Is passive immunization for Alzheimers disease 'alive and well' or 'dead and buried'
    • Jicha GA. Is passive immunization for Alzheimers disease 'alive and well' or 'dead and buried'? Expert Opin. Biol. Ther. 9, 481-491 (2009).
    • (2009) Expert Opin. Biol. Ther. , vol.9 , pp. 481-491
    • Jicha, G.A.1
  • 141
    • 79955865565 scopus 로고    scopus 로고
    • Monoclonal antibodies against b amyloid ab for the treatment of Alzheimers disease: The ab target at a crossroads
    • Panza F, Frisardi V, Imbimbo BP, Seripa D, Solfrizzi V, Pilotto A. Monoclonal antibodies against βamyloid (Ab) for the treatment of Alzheimers disease: The Ab target at a crossroads. Expert Opin. Biol. Ther. 11(6), 679-686 (2011).
    • (2011) Expert Opin. Biol. Ther. , vol.116 , pp. 679-686
    • Panza, F.1    Frisardi, V.2    Imbimbo, B.P.3    Seripa, D.4    Solfrizzi, V.5    Pilotto, A.6
  • 142
    • 33744499734 scopus 로고    scopus 로고
    • Mechanisms of a beta plaque clearance following passive a beta immunization
    • Morgan D. Mechanisms of A beta plaque clearance following passive A beta immunization. Neurodegener. Dis. 2(5), 261-266 (2005).
    • (2005) Neurodegener. Dis. , vol.2 , Issue.5 , pp. 261-266
    • Morgan, D.1
  • 143
    • 38449088277 scopus 로고    scopus 로고
    • Antibody-based approaches in Alzheimers research: Safety pharmacokinetics metabolism and analytical tools
    • Lichtlen P, Mohajeri MH. Antibody-based approaches in Alzheimers research: Safety, pharmacokinetics, metabolism, and analytical tools. J. Neurochem. 104(4), 859-874 (2008).
    • (2008) J. Neurochem. , vol.104 , Issue.4 , pp. 859-874
    • Lichtlen, P.1    Mohajeri, M.H.2
  • 144
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • Walsh DM, Selkoe DJ. Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11(4), 213-228 (2004).
    • (2004) Protein Pept. Lett. , vol.11 , Issue.4 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 146
    • 78649526412 scopus 로고    scopus 로고
    • Bapineuzumab: Anti-b amyloid monoclonal antibodies for the treatment of Alzheimers disease
    • Panza F, Frisardi V, Imbimbo BP et al. Bapineuzumab: Anti-βamyloid monoclonal antibodies for the treatment of Alzheimers disease. Immunotherapy 2(6), 767-782 (2010).
    • (2010) Immunotherapy , vol.2 , Issue.6 , pp. 767-782
    • Panza, F.1    Frisardi, V.2    Imbimbo, B.P.3
  • 147
    • 80053385682 scopus 로고    scopus 로고
    • Anti-b-Amyloid immunotherapy for Alzheimers disease: Focus on bapineuzumab
    • Panza F, Frisardi V, Imbimbo BP et al. Anti-b-Amyloid immunotherapy for Alzheimers disease: focus on bapineuzumab. Curr. Alzheimer Res. 8(8), 808-817 (2011).
    • (2011) Curr. Alzheimer Res. , vol.8 , Issue.8 , pp. 808-817
    • Panza, F.1    Frisardi, V.2    Imbimbo, B.P.3
  • 148
    • 79955803502 scopus 로고    scopus 로고
    • Solanezumab for Alzheimers disease
    • Samadi H, Sultzer D. Solanezumab for Alzheimers disease. Expert Opin. Biol. Ther. 11(6), 787-798 (2011).
    • (2011) Expert Opin. Biol. Ther. , vol.116 , pp. 787-798
    • Samadi, H.1    Sultzer, D.2
  • 149
    • 79851496064 scopus 로고    scopus 로고
    • Antibody-based therapy in Alzheimers disease
    • Pul R, Dodel R, Stangel M. Antibody-based therapy in Alzheimers disease. Expert Opin. Biol. Ther. 11(3), 343-357 (2011).
    • (2011) Expert Opin. Biol. Ther. , vol.113 , pp. 343-357
    • Pul, R.1    Dodel, R.2    Stangel, M.3
  • 150
    • 34547955761 scopus 로고    scopus 로고
    • Anti-A beta1-11 antibody binds to different beta amyloid species inhibits fibril formation and disaggregates preformed fibrils but not the most toxic oligomers
    • Mamikonyan G, Necula M, Mkrtichyan M et al. Anti-A beta1-11 antibody binds to different beta?amyloid species, inhibits fibril formation, and disaggregates preformed fibrils but not the most toxic oligomers. J. Biol. Chem. 282(31), 22376-22386 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.31 , pp. 22376-22386
    • Mamikonyan, G.1    Necula, M.2    Mkrtichyan, M.3
  • 151
    • 0037107177 scopus 로고    scopus 로고
    • Non-Fc-mediated mechanisms are involved in clearance of amyloid beta in vivo by immunotherapy
    • Bacskai BJ, Kajdasz ST, McLellan ME et al. Non-Fc-mediated mechanisms are involved in clearance of amyloid?beta in vivo by immunotherapy. J. Neurosci. 22(18), 7873-7878 (2002).
    • (2002) J. Neurosci. , vol.22 , Issue.18 , pp. 7873-7878
    • Bacskai, B.J.1    Kajdasz, S.T.2    McLellan, M.E.3
  • 152
    • 26944481138 scopus 로고    scopus 로고
    • The Fab2 fragment of an Abeta-specific monoclonal antibody reduces abeta deposits in the brain
    • Tamura Y, Hamajima K, Matsui K et al. The F(ab)'2 fragment of an Abeta-specific monoclonal antibody reduces Abeta deposits in the brain. Neurobiol. Dis. 20(2), 541-549 (2005)
    • (2005) Neurobiol. Dis. , vol.20 , Issue.2 , pp. 541-549
    • Tamura, Y.1    Hamajima, K.2    Matsui, K.3
  • 153
    • 0031020909 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Abeta42 deposition in a transgenic mouse model of Alzheimers disease
    • USA
    • Johnson-Wood K, Lee M, Motter R et al. Amyloid precursor protein processing and Abeta42 deposition in a transgenic mouse model of Alzheimers disease. Proc. Natl Acad. Sci. USA 94(4), 1550-1555 (1997).
    • (1997) Proc. Natl Acad. Sci. , vol.94 , Issue.4 , pp. 1550-1555
    • Johnson-Wood, K.1    Lee, M.2    Motter, R.3
  • 154
    • 77953282150 scopus 로고    scopus 로고
    • A single ascending dose study of bapineuzumab in patients with Alzheimer disease
    • Black RS, Sperling RA, Safirstein B et al. A single ascending dose study of bapineuzumab in patients with Alzheimer disease. Alzheimer Dis. Assoc. Disord. 24(2), 198-203 (2010).
    • (2010) Alzheimer Dis. Assoc. Disord. , vol.24 , Issue.2 , pp. 198-203
    • Black, R.S.1    Sperling, R.A.2    Safirstein, B.3
  • 155
    • 73349091534 scopus 로고    scopus 로고
    • A Phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease
    • Salloway S, Sperling R, Gilman S et al. A Phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease. Neurology 73(24), 2061-2070 (2009).
    • (2009) Neurology , vol.73 , Issue.24 , pp. 2061-2070
    • Salloway, S.1    Sperling, R.2    Gilman, S.3
  • 156
    • 77949300796 scopus 로고    scopus 로고
    • 11C?PiB PET assessment of change in fibrillar amyloid?beta load in patients with Alzheimers disease treated with bapineuzumab: A Phase 2 double-blind placebo-controlled ascending-dose study
    • Rinne JO, Brooks DJ, Rossor MN et al. 11C?PiB PET assessment of change in fibrillar amyloid?beta load in patients with Alzheimers disease treated with bapineuzumab: A Phase 2, double-blind, placebo-controlled, ascending-dose study. Lancet Neurol. 9(4), 363-372 (2010).
    • (2010) Lancet Neurol. , vol.9 , Issue.4 , pp. 363-372
    • Rinne, J.O.1    Brooks, D.J.2    Rossor, M.N.3
  • 157
    • 70350266228 scopus 로고    scopus 로고
    • Amyloid imaging in aging and dementia: Testing the amyloid hypothesis in vivo
    • Rabinovici GD, Jagust WJ. Amyloid imaging in aging and dementia: Testing the amyloid hypothesis in vivo. Behav. Neurol. 21(1), 117-128 (2009).
    • (2009) Behav. Neurol. , vol.21 , Issue.1 , pp. 117-128
    • Rabinovici, G.D.1    Jagust, W.J.2
  • 158
    • 78649500577 scopus 로고    scopus 로고
    • Immunotherapy with bapineuzumab lowers CSF tau protein levels in patients with Alzheimers disease
    • Blennow K, Zetterberg H, Wei J, Liu E, Black R, Grundman M. Immunotherapy with bapineuzumab lowers CSF tau protein levels in patients with Alzheimers disease. Alzheimers Dement. 6(Suppl.), S134-S135 (2010).
    • (2010) Alzheimers Dement. , vol.6
    • Blennow, K.1    Zetterberg, H.2    Wei, J.3    Liu, E.4    Black, R.5    Grundman, M.6
  • 159
    • 34548706007 scopus 로고    scopus 로고
    • Apolipoprotein E and neurological disease: Therapeutic potential and pharmacogenomic interactions
    • Laskowitz DT, Vitek MP. Apolipoprotein E and neurological disease: Therapeutic potential and pharmacogenomic interactions. Pharmacogenomics 8(8), 959-969 (2008).
    • (2008) Pharmacogenomics , vol.8 , Issue.8 , pp. 959-969
    • Laskowitz, D.T.1    Vitek, M.P.2
  • 160
    • 68249134074 scopus 로고    scopus 로고
    • The role of apolipoprotein E in Alzheimers disease
    • Kim J, Basak JM, Holtzman DM. The role of apolipoprotein E in Alzheimers disease. Neuron 63(3), 287-303 (2009).
    • (2009) Neuron , vol.63 , Issue.3 , pp. 287-303
    • Kim, J.1    Basak, J.M.2    Holtzman, D.M.3
  • 161
    • 0035152093 scopus 로고    scopus 로고
    • Downregulation of microglial activation by apolipoprotein E and apoE-mimetic peptides
    • Laskowitz DT, Thekdi AD, Thekdi SD et al. Downregulation of microglial activation by apolipoprotein E and apoE-mimetic peptides. Exp. Neurol. 167(1), 74-85 (2001).
    • (2001) Exp. Neurol. , vol.167 , Issue.1 , pp. 74-85
    • Laskowitz, D.T.1    Thekdi, A.D.2    Thekdi, S.D.3
  • 162
    • 84899519009 scopus 로고    scopus 로고
    • Are NSAIDs useful to treat Alzheimers disease or mild cognitive impairment
    • Imbimbo BP, Solfrizzi V, Panza F. Are NSAIDs useful to treat Alzheimers disease or mild cognitive impairment? Front. Aging Neurosci. 2, PII19 (2010)
    • (2010) Front. Aging Neurosci. , vol.2
    • Imbimbo, B.P.1    Solfrizzi, V.2    Panza, F.3
  • 163
    • 0037010308 scopus 로고    scopus 로고
    • Amyloid-beta: A vascular sealant that protects against hemorrhage
    • Atwood CS, Bishop GM, Perry G, Smith MA. Amyloid-beta: A vascular sealant that protects against hemorrhage? J. Neurosci. Res. 70(3), 356 (2002)
    • (2002) J. Neurosci. Res. , vol.70 , Issue.3 , pp. 356
    • Atwood, C.S.1    Bishop, G.M.2    Perry, G.3    Smith, M.A.4
  • 165
    • 0037112201 scopus 로고    scopus 로고
    • Cerebral hemorrhage after passive anti-Ab immunotherapy
    • Pfeifer M, Boncristiano S, Bondolfi L et al. Cerebral hemorrhage after passive anti-Ab immunotherapy. Science 298(5597), 1379 (2002).
    • (2002) Science , vol.298 , Issue.5597 , pp. 1379
    • Pfeifer, M.1    Boncristiano, S.2    Bondolfi, L.3
  • 166
    • 19944431509 scopus 로고    scopus 로고
    • Exacerbation of cerebral amyloid angiopathy-associated microhemorrhages in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyoid beta
    • Racke MM, Boone LI, Hepburn DL et al. Exacerbation of cerebral amyloid angiopathy-associated microhemorrhages in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyoid beta. J. Neurosci. 25(3), 629-636 (2005).
    • (2005) J. Neurosci. , vol.25 , Issue.3 , pp. 629-636
    • Racke, M.M.1    Boone, L.I.2    Hepburn, D.L.3
  • 167
    • 33845904135 scopus 로고    scopus 로고
    • Amyloid-beta vaccination but not nitro-nonsteroidal anti-inflammatory drug treatment increases vascular amyloid and microhemorrhage while both reduce parenchymal amyloid
    • Wilcock DM, Jantzen PT, Li Q, Morgan D, Gordon MN. Amyloid-beta vaccination, but not nitro-nonsteroidal anti-inflammatory drug treatment, increases vascular amyloid and microhemorrhage while both reduce parenchymal amyloid. Neuroscience 144(3), 950-960 (2007).
    • (2007) Neuroscience , vol.144 , Issue.3 , pp. 950-960
    • Wilcock, D.M.1    Jantzen, P.T.2    Li, Q.3    Morgan, D.4    Gordon, M.N.5
  • 168
    • 58149129243 scopus 로고    scopus 로고
    • Consequence of Abeta immunization on the vasculature of human Alzheimers disease brain
    • Boche D, Zotova E, Weller RO et al. Consequence of Abeta immunization on the vasculature of human Alzheimers disease brain. Brain 131(Pt 12), 3299?3310 (2008).
    • (2008) Brain , vol.131 , Issue.12 , pp. 3299-3310
    • Boche, D.1    Zotova, E.2    Weller, R.O.3
  • 169
    • 33748767945 scopus 로고    scopus 로고
    • Amyloid-beta peptide remnants in AN-1792-immunized Alzheimers disease patients: A biochemical analysis
    • Patton RL, Kalback WM, Esh CL et al. Amyloid-beta peptide remnants in AN-1792-immunized Alzheimers disease patients: A biochemical analysis. Am. J. Pathol. 169(3), 1048-1063 (2006).
    • (2006) Am. J. Pathol. , vol.169 , Issue.3 , pp. 1048-1063
    • Patton, R.L.1    Kalback, W.M.2    Esh, C.L.3
  • 170
    • 64549152492 scopus 로고    scopus 로고
    • AN1792 QS-21-251 study team long-term follow-up of patients immunized with AN1792: Reduced functional decline in antibody responders
    • Vellas B, Black R, Thal LJ et al.; AN1792 (QS?21)-251 Study Team. Long-term follow-up of patients immunized with AN1792: Reduced functional decline in antibody responders. Curr. Alzheimer Res. 6(2), 144-151 (2009).
    • (2009) Curr. Alzheimer Res. , vol.6 , Issue.2 , pp. 144-151
    • Vellas, B.1    Black, R.2    Thal, L.J.3
  • 171
    • 0026646605 scopus 로고    scopus 로고
    • Isolation and quantification of soluble Alzheimers beta-peptide from biological fluids
    • Seubert P, Vigo-Pelfrey C, Esch F et al. Isolation and quantification of
    • (1992) Nature , vol.359 , Issue.6393 , pp. 325-327
    • Seubert, P.1    Vigo-Pelfrey, C.2    Esch, F.3
  • 172
    • 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 et al. 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(2), 67-73 (2010).
    • (2010) Clin. Neuropharmacol. , vol.33 , Issue.2 , pp. 67-73
    • Siemers, E.R.1    Friedrich, S.2    Dean, R.A.3
  • 173
    • 76849103927 scopus 로고    scopus 로고
    • Identification characterization and comparison of amino-terminally truncated Abeta42 peptides in Alzheimers disease brain tissue and in plasma from Alzheimers patients receiving solanezumab immunotherapy treatment
    • DeMattos RB, Racke MM, Gelfanova V et al. Identification, characterization, and comparison of amino-terminally truncated Abeta42 peptides in Alzheimers disease brain tissue and in plasma from Alzheimers patients receiving solanezumab immunotherapy treatment. Alzheimers Dement. 5, P156-P157 (2009).
    • (2009) Alzheimers Dement. , vol.5
    • DeMattos, R.B.1    Racke, M.M.2    Gelfanova, V.3
  • 174
    • 37849012608 scopus 로고    scopus 로고
    • Antibody capture of soluble Abeta does not reduce cortical Abeta amyloidosis in the PDAPP mouse
    • Seubert P, Barbour R, Khan K et al. Antibody capture of soluble Abeta does not reduce cortical Abeta amyloidosis in the PDAPP mouse. Neurodegener. Dis. 5(2), 65-71 (2008).
    • (2008) Neurodegener. Dis. , vol.5 , Issue.2 , pp. 65-71
    • Seubert, P.1    Barbour, R.2    Khan, K.3
  • 175
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-Abeta antibody alters CNS and plasma Abeta clearance and decreases brain Abeta burden in a mouse model of Alzheimers disease
    • USA
    • DeMattos RB, Bales KR, Cummins DJ et al. Peripheral anti-Abeta antibody alters CNS and plasma Abeta clearance and decreases brain Abeta burden in a mouse model of Alzheimers disease. Proc. Natl Acad. Sci. USA 98(15), 8850-8855 (2001).
    • (2001) Proc. Natl Acad. Sci. , vol.98 , Issue.15 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3
  • 176
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimers disease model
    • Dodart JC, Bales KR, Gannon KS et al. Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimers disease model. Nat. Neurosci. 5(5), 452-457 (2002).
    • (2002) Nat. Neurosci. , vol.5 , Issue.5 , pp. 452-457
    • Dodart, J.C.1    Bales, K.R.2    Gannon, K.S.3
  • 177
    • 0037155581 scopus 로고    scopus 로고
    • Brain to plasma amyloid?beta efflux: A measure of brain amyloid burden in a mouse model of Alzheimers disease
    • DeMattos RB, Bales KR, Cummins DJ et al. Brain to plasma amyloid?beta efflux: A measure of brain amyloid burden in a mouse model of Alzheimers disease. Science 295(5563), 2264-2267 (2002).
    • (2002) Science , vol.295 , Issue.5563 , pp. 2264-2267
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3
  • 178
    • 33845639102 scopus 로고    scopus 로고
    • Insights into the mechanisms of action of anti-Abeta antibodies in Alzheimers disease mouse models
    • Levites Y, Smithson LA, Price RW et al. Insights into the mechanisms of action of anti-Abeta antibodies in Alzheimers disease mouse models. FASEB J. 20(14), 2576-2578 (2006).
    • (2006) FASEB J. , vol.20 , Issue.14 , pp. 2576-2578
    • Levites, Y.1    Smithson, L.A.2    Price, R.W.3
  • 179
    • 70349160023 scopus 로고    scopus 로고
    • Abeta immunotherapy: Intracerebral sequestration of Abeta by an anti-Abeta monoclonal antibody 266 with high affinity to soluble Abeta
    • Yamada K, Yabuki C, Seubert P et al. Abeta immunotherapy: Intracerebral sequestration of Abeta by an anti-Abeta monoclonal antibody 266 with high affinity to soluble Abeta. J. Neurosci. 29(36), 11393-11398 (2009).
    • (2009) J. Neurosci. , vol.29 , Issue.36 , pp. 11393-11398
    • Yamada, K.1    Yabuki, C.2    Seubert, P.3
  • 180
    • 65249091605 scopus 로고    scopus 로고
    • P4-346: Safety tolerability and biomarker effects of an Abeta monoclonal antibody administered to patients with Alzheimers disease
    • Siemers ER, Friedrich S, Dean RA et al. P4-346: Safety, tolerability and biomarker effects of an Abeta monoclonal antibody administered to patients with Alzheimers disease. Alzheimers Dement. 4, T774 (2008).
    • (2008) Alzheimers Dement. , vol.4
    • Siemers, E.R.1    Friedrich, S.2    Dean, R.A.3
  • 181
    • 19944431509 scopus 로고    scopus 로고
    • Exacerbation of cerebral amyloid angiopathy-associated microhemorrhage in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyloid beta
    • Racke MM, Boone LI, Hepburn DL et al. Exacerbation of cerebral amyloid angiopathy-associated microhemorrhage in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyloid beta. J. Neurosci. 25(3), 629-636 (2005).
    • (2005) J. Neurosci. , vol.25 , Issue.3 , pp. 629-636
    • Racke, M.M.1    Boone, L.I.2    Hepburn, D.L.3
  • 182
    • 49049089830 scopus 로고    scopus 로고
    • Immunotherapy reduces vascular amyloid-beta in PDAPP mice
    • Schroeter S, Khan K, Barbour R et al. Immunotherapy reduces vascular amyloid-beta in PDAPP mice. J. Neurosci. 28(27), 6787-6793 (2008).
    • (2008) J. Neurosci. , vol.28 , Issue.27 , pp. 6787-6793
    • Schroeter, S.1    Khan, K.2    Barbour, R.3
  • 183
    • 77953352375 scopus 로고    scopus 로고
    • Preliminary population pharmacokinetic modeling of PF-04360365 a humanized anti-amyloid monoclonal antibody in patients with mild-to-moderate Alzheimers disease
    • Nicholas T, Knebel W, Gastonguay MR et al. Preliminary population pharmacokinetic modeling of PF?04360365, a humanized anti?amyloid monoclonal antibody, in patients with mild-to-moderate Alzheimers disease. Alzheimers Dement. 5, P253 (2009).
    • (2009) Alzheimers Dement. , vol.5
    • Nicholas, T.1    Knebel, W.2    Gastonguay, M.R.3
  • 184
    • 77953351430 scopus 로고    scopus 로고
    • Selection of an anti-Abeta antibody that binds various forms of Abeta and blocks toxicity both in vitro and in vivo
    • Watts RJ, Chen M, Atwal J et al. Selection of an anti-Abeta antibody that binds various forms of Abeta and blocks toxicity both in vitro and in vivo. Alzheimers Dement. 5, P426 (2009).
    • (2009) Alzheimers Dement. , vol.5
    • Watts, R.J.1    Chen, M.2    Atwal, J.3
  • 185
    • 76849117025 scopus 로고    scopus 로고
    • Natural human antibodies targeting amyloid aggregates in intravenous immunoglobulin
    • Relkin NR. Natural human antibodies targeting amyloid aggregates in intravenous immunoglobulin. Alzheimers Dement. 4, T101 (2008).
    • (2008) Alzheimers Dement. , vol.4
    • Relkin, N.R.1
  • 186
    • 0036327185 scopus 로고    scopus 로고
    • Human antibodies against amyloid beta peptide: A potential treatment for Alzheimers disease
    • Dodel R, Hampel H, Depboylu C et al. Human antibodies against amyloid beta peptide: A potential treatment for Alzheimers disease. Ann. Neurol. 52(2), 253-256 (2002).
    • (2002) Ann. Neurol. , vol.52 , Issue.2 , pp. 253-256
    • Dodel, R.1    Hampel, H.2    Depboylu, C.3
  • 187
    • 0035845614 scopus 로고    scopus 로고
    • Reduced levels of amyloid beta-peptide antibody in Alzheimer disease
    • Du Y, Dodel R, Hampel H et al. Reduced levels of amyloid beta-peptide antibody in Alzheimer disease. Neurology 57(5), 801-805 (2001).
    • (2001) Neurology , vol.57 , Issue.5 , pp. 801-805
    • Du, Y.1    Dodel, R.2    Hampel, H.3
  • 188
    • 67749122581 scopus 로고    scopus 로고
    • Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimers disease
    • USA
    • Britschgi M, Olin CE, Johns HT et al. Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimers disease. Proc. Natl Acad. Sci. USA 106(29), 12145-12150 (2009).
    • (2009) Proc. Natl Acad. Sci. , vol.106 , Issue.29 , pp. 12145-12150
    • Britschgi, M.1    Olin, C.E.2    Johns, H.T.3
  • 189
    • 33746419618 scopus 로고    scopus 로고
    • Intravenous immunoglobulin enhances the clearance of fibrillar amyloidβ peptide
    • Istrin G, Bosis E, Solomon B. Intravenous immunoglobulin enhances the clearance of fibrillar amyloidβ peptide. J. Neurosci. Res. 84(2), 434-443 (2006).
    • (2006) J. Neurosci. Res. , vol.84 , Issue.2 , pp. 434-443
    • Istrin, G.1    Bosis, E.2    Solomon, B.3
  • 190
    • 0041320819 scopus 로고    scopus 로고
    • Human anti-βamyloid antibodies block b?amyloid fibril formation and prevent b?amyloid?induced neurotoxicity
    • Pt 9
    • Du Y, Wei X, Dodel R et al. Human anti-βamyloid antibodies block b?amyloid fibril formation and prevent b?amyloid?induced neurotoxicity. Brain 126(Pt 9), 1935-1939 (2003).
    • (2003) Brain 126 , pp. 1935-1939
    • Du, Y.1    Wei, X.2    Dodel, R.3
  • 191
    • 31844439888 scopus 로고    scopus 로고
    • Antibodies against βamyloid reduce Ab oligomers glycogen synthase kinase-3b activation and t phosphorylation in vivo and in vitro
    • Ma QL, Lim GP, Harris-White ME et al. Antibodies against βamyloid reduce Ab oligomers, glycogen synthase kinase-3b activation and t phosphorylation in vivo and in vitro. J. Neurosci. Res. 83(3), 374-384 (2006).
    • (2006) J. Neurosci. Res. , vol.83 , Issue.3 , pp. 374-384
    • Ma, Q.L.1    Lim, G.P.2    Harris-White, M.E.3
  • 192
    • 41949107347 scopus 로고    scopus 로고
    • Autoantibody-catalyzed hydrolysis of amyloid beta peptide
    • Taguchi H, Planque S, Nishiyama Y et al. Autoantibody-catalyzed hydrolysis of amyloid beta peptide. J. Biol. Chem. 283(52), 4714-4722 (2008).
    • (2008) J. Biol. Chem. , vol.283 , Issue.52 , pp. 4714-4722
    • Taguchi, H.1    Planque, S.2    Nishiyama, Y.3
  • 193
    • 68949169046 scopus 로고    scopus 로고
    • Iv immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders
    • Fillit H, Hess G, Hill J et al. Iv immunoglobulin is associated with a reduced risk of Alzheimer disease and related disorders. Neurology 73(3), 180-185 (2009).
    • (2009) Neurology , vol.73 , Issue.3 , pp. 180-185
    • Fillit, H.1    Hess, G.2    Hill, J.3
  • 194
    • 77949973336 scopus 로고    scopus 로고
    • Therapeutic effects of piracetam combined with intravenous immunoglobulin premature of Alzheimer type
    • Kountouris D. Therapeutic effects of piracetam combined with intravenous immunoglobulin premature of Alzheimer type. J. Neural Transm. 5, 18 (2000).
    • (2000) J. Neural Transm. , vol.5 , pp. 18
    • Kountouris, D.1
  • 195
    • 4644275963 scopus 로고    scopus 로고
    • Intravenous immunoglobulins containing antibodies against βamyloid for the treatment of Alzheimers disease
    • Dodel RC, Du Y, Depboylu C et al. Intravenous immunoglobulins containing antibodies against βamyloid for the treatment of Alzheimers disease. J. Neurol. Neurosurg. Psychiatry 75(10), 1472-1474 (2004).
    • (2004) J. Neurol. Neurosurg. Psychiatry , vol.75 , Issue.10 , pp. 1472-1474
    • Dodel, R.C.1    Du, Y.2    Depboylu, C.3
  • 196
    • 70049083865 scopus 로고    scopus 로고
    • 18?month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
    • Relkin NR, Szabo P, Adamiak B et al. 18?month study of intravenous immunoglobulin for treatment of mild Alzheimer disease. Neurobiol. Aging 30(11), 1728-1736 (2009).
    • (2009) Neurobiol. Aging , vol.30 , Issue.11 , pp. 1728-1736
    • Relkin, N.R.1    Szabo, P.2    Adamiak, B.3
  • 197
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300(5618), 486-489 (2003).
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 198
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimers disease and frontotemporal dementia
    • Gotz J, Ittner LM. Animal models of Alzheimers disease and frontotemporal dementia. Nat. Rev. Neurosci. 9(7), 532-544 (2008).
    • (2008) Nat. Rev. Neurosci. , vol.9 , Issue.7 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 200
    • 33750681275 scopus 로고    scopus 로고
    • Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimers disease and healthy subjects
    • Rosenmann H, Meiner Z, Geylis V et al. Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimers disease and healthy subjects. Neurosci. Lett. 410(2), 90-93 (2006).
    • (2006) Neurosci. Lett. , vol.410 , Issue.2 , pp. 90-93
    • Rosenmann, H.1    Meiner, Z.2    Geylis, V.3
  • 201
    • 0642370868 scopus 로고    scopus 로고
    • Immunological approach for the treatment of Alzheimers disease
    • Solomon B. Immunological approach for the treatment of Alzheimers disease. J. Mol. Neurosci. 20(3), 283-286 (2003).
    • (2003) J. Mol. Neurosci. , vol.20 , Issue.3 , pp. 283-286
    • Solomon, B.1
  • 202
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin induced tau filament formation by phenothiazines polyphenols and porphyrins
    • Taniguchi S, Suzuki N, Masuda M et al. Inhibition of heparin induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 280(9), 7614-7623 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.9 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3
  • 203
    • 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 et al. Effects of different anti-tau antibodies on tau fibrillogenesis: RTA?1 and RTA?2 counteract tau aggregation. FEBS Lett. 579(6), 1399-1404 (2005).
    • (2005) FEBS Lett. , vol.579 , Issue.6 , pp. 1399-1404
    • Taniguchi, T.1    Sumida, M.2    Hiraoka, S.3
  • 204
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif 306 VQIVYK 311 forming beta structure
    • USA
    • von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc. Natl Acad. Sci. USA 97(10), 5129-5134 (2000).
    • (2000) Proc. Natl Acad. Sci. , vol.97 , Issue.10 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 205
    • 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(4), 658-667 (2011).
    • (2011) J. Neurochem. , vol.118 , Issue.4 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 206
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg SG, Davies P, Schein JD, Binder LI. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267(1), 564-569 (1992).
    • (1992) J. Biol. Chem. , vol.267 , Issue.1 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 207
  • 208
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Abeta causes the onset of early Alzheimers disease related cognitive deficits in transgenic mice
    • Billings LM, Oddo S, Green KN, McGaugh JL, LaFerla FM. Intraneuronal Abeta causes the onset of early Alzheimers disease related cognitive deficits in transgenic mice. Neuron 45(5), 675-688 (2005).
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 209
    • 20444413356 scopus 로고    scopus 로고
    • Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease
    • Masliah E, Rockenstein E, Adame A et al. Effects of alpha-synuclein immunization in a mouse model of Parkinson's disease. Neuron 46(6), 857-868 (2005).
    • (2005) Neuron , vol.46 , Issue.6 , pp. 857-868
    • Masliah, E.1    Rockenstein, E.2    Adame, A.3
  • 210
    • 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 et al. Internalized antibodies to the Abeta domain of APP reduce neuronal Abeta and protect against synaptic alterations. J. Biol. Chem. 282(26), 18895-18906 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.26 , pp. 18895-18906
    • Tampellini, D.1    Magrane, J.2    Takahashi, R.H.3
  • 211
    • 70350543879 scopus 로고    scopus 로고
    • Intrabody gene therapy ameliorates motor cognitive and neuropathological symptoms in multiple mouse models of Huntington's disease
    • Southwell AL, Ko J, Patterson PH. Intrabody gene therapy ameliorates motor, cognitive, and neuropathological symptoms in multiple mouse models of Huntington's disease. J. Neurosci. 29(43), 13589-13602 (2009).
    • (2009) J. Neurosci. , vol.29 , Issue.43 , pp. 13589-13602
    • Southwell, A.L.1    Ko, J.2    Patterson, P.H.3
  • 212
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimers disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ et al. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimers disease mouse model. Science 316(5825), 750-754 (2007).
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3
  • 213
    • 66749084437 scopus 로고    scopus 로고
    • A γsecretase inhibitor decreases amyloidβ production in the central nervous system
    • Bateman RJ, Siemers ER, Mawuenyega KG et al. A γsecretase inhibitor decreases amyloidβ production in the central nervous system. Ann. Neurol. 66(1), 48-54 (2009).
    • (2009) Ann. Neurol. , vol.66 , Issue.1 , pp. 48-54
    • Bateman, R.J.1    Siemers, E.R.2    Mawuenyega, K.G.3
  • 214
    • 70350495442 scopus 로고    scopus 로고
    • Reexamining Alzheimers disease: Evidence for a protective role for amyloid-beta protein precursor and amyloid-beta
    • Castellani RJ, Lee HG, Siedlak SL et al. Reexamining Alzheimers disease: Evidence for a protective role for amyloid-beta protein precursor and amyloid-beta. J. Alzheimers Dis. 18(2), 447-452 (2009).
    • (2009) J. Alzheimers Dis. , vol.18 , Issue.2 , pp. 447-452
    • Castellani, R.J.1    Lee, H.G.2    Siedlak, S.L.3
  • 216
    • 33645220400 scopus 로고    scopus 로고
    • Targeting amyloidβ peptide Ab oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Ab precursor protein APP transgenic mice
    • Lee EB, Leng LZ, Zhang B et al. Targeting amyloidβ peptide (Ab) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Ab precursor protein (APP) transgenic mice. J. Biol. Chem. 281(7), 4292-4299 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.7 , pp. 4292-4299
    • Lee, E.B.1    Leng, L.Z.2    Zhang, B.3
  • 217
    • 33846135452 scopus 로고    scopus 로고
    • Monoclonal antibodies that target pathological assemblies of Ab
    • Lambert MP, Velasco PT, Chang L et al. Monoclonal antibodies that target pathological assemblies of Ab. J. Neurochem. 100(1), 23-35 (2007).
    • (2007) J. Neurochem. , vol.100 , Issue.1 , pp. 23-35
    • Lambert, M.P.1    Velasco, P.T.2    Chang, L.3
  • 218
    • 34447322271 scopus 로고    scopus 로고
    • Research criteria for the diagnosis of Alzheimers disease: Revising the NINCDS-ADRDA criteria
    • Dubois B, Feldman HH, Jacova C et al. Research criteria for the diagnosis of Alzheimers disease: Revising the NINCDS-ADRDA criteria. Lancet Neurol. 6(8), 734-746 (2007).
    • (2007) Lancet Neurol. , vol.6 , Issue.8 , pp. 734-746
    • Dubois, B.1    Feldman, H.H.2    Jacova, C.3
  • 219
    • 77957951112 scopus 로고    scopus 로고
    • Revising the definition of Alzheimers disease: A new lexicon
    • Dubois B, Feldman HH, Jacova C et al. Revising the definition of Alzheimers disease: A new lexicon. Lancet Neurol. 9(11), 1118-1127 (2010).
    • (2010) Lancet Neurol. , vol.9 , Issue.11 , pp. 1118-1127
    • Dubois, B.1    Feldman, H.H.2    Jacova, C.3
  • 220
    • 79956142378 scopus 로고    scopus 로고
    • The diagnosis of dementia due to Alzheimers disease recommendations from the National Institute on Aging-Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease
    • McKhann GM, Knopman DS, Chertkow H et al. The diagnosis of dementia due to Alzheimers disease. Recommendations from the National Institute on Aging-Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease. Alzheimers Dement. 7(3), 263-269 (2011).
    • (2011) Alzheimers Dement. , vol.7 , Issue.3 , pp. 263-269
    • McKhann, G.M.1    Knopman, D.S.2    Chertkow, H.3
  • 221
    • 79956084514 scopus 로고    scopus 로고
    • The diagnosis of mild cognitive impairment due to Alzheimers disease
    • Recommendations from the National Institute on Aging- Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease
    • Albert MS, Dekosky ST, Dickson D et al. The diagnosis of mild cognitive impairment due to Alzheimers disease. Recommendations from the National Institute on Aging- Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease. Alzheimers Dement. 7(3), 270-279 (2011).
    • (2011) Alzheimers Dement. , vol.7 , Issue.3 , pp. 270-279
    • Albert, M.S.1    Dekosky, S.T.2    Dickson, D.3
  • 222
    • 79956098248 scopus 로고    scopus 로고
    • Toward defining the preclinical stages of Alzheimers disease
    • Recommendations from the National Institute on Aging-Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease
    • Sperling RA, Aisen PS, Beckett LA et al. Toward defining the preclinical stages of Alzheimers disease. Recommendations from the National Institute on Aging-Alzheimers Association workgroups on diagnostic guidelines for Alzheimers disease. Alzheimers Dement. 7(3), 280-292 (2011).
    • (2011) Alzheimers Dement. , vol.7 , Issue.3 , pp. 280-292
    • Sperling, R.A.1    Aisen, P.S.2    Beckett, L.A.3
  • 223
    • 77955474351 scopus 로고    scopus 로고
    • Alzheimers disease neuroimaging initiative the Alzheimers disease neuroimaging initiative. progress report and future plans
    • Weiner MW, Aisen PS, Jack CR Jr et al; Alzheimers Disease Neuroimaging Initiative. The Alzheimers disease neuroimaging initiative. progress report and future plans. Alzheimers Dement. 6(3), 202-211 (2010).
    • (2010) Alzheimers Dement. , vol.6 , Issue.3 , pp. 202-211
    • Weiner, M.W.1    Aisen, P.S.2    Jack Jr., C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.