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Volumn 9789400727748, Issue , 2012, Pages 135-188

The role of Aβ and tau oligomers in the pathogenesis of Alzheimer's disease

Author keywords

Alzheimer's disease; A oligomers; Neurofibrillary tangles; Neuropathology; Tau oligomers

Indexed keywords


EID: 84878626491     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-2774-8_5     Document Type: Chapter
Times cited : (8)

References (412)
  • 2
    • 0026454599 scopus 로고
    • Thrombin accumulation in brains of patients with Alzheimer's disease
    • Akiyama H, Ikeda K, Kondo H, McGeer PL (1992) Thrombin accumulation in brains of patients with Alzheimer's disease. Neurosci Lett 146:152-154
    • (1992) Neurosci Lett , vol.146 , pp. 152-154
    • Akiyama, H.1    Ikeda, K.2    Kondo, H.3    McGeer, P.L.4
  • 4
    • 0035851157 scopus 로고    scopus 로고
    • Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein
    • Alonso AD, Zaidi T, Novak M, Barra HS, Grundke-Iqbal I, Iqbal K (2001) Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein. J Biol Chem 276:37967-37973
    • (2001) J Biol Chem , vol.276 , pp. 37967-37973
    • Alonso, A.D.1    Zaidi, T.2    Novak, M.3    Barra, H.S.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 6
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG (2003) Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 161:41-54
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 9
    • 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 (2005) Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 25:5446-5454
    • (2005) J Neurosci , vol.25 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 10
    • 0026488111 scopus 로고
    • Structure and novel exons of the human tau gene
    • Andreadis A, Brown WM, Kosik KS (1992) Structure and novel exons of the human tau gene. Biochemistry 31:10626-10633
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 11
    • 33644905917 scopus 로고    scopus 로고
    • Thrombin and prothrombin are expressed by neurons and glial cells and accumulate in neurofibrillary tangles in Alzheimer disease brain
    • Arai T, Miklossy J, Klegeris A, Guo JP, McGeer PL (2006) Thrombin and prothrombin are expressed by neurons and glial cells and accumulate in neurofibrillary tangles in Alzheimer disease brain. J Neuropathol Exp Neurol 65:19-25
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 19-25
    • Arai, T.1    Miklossy, J.2    Klegeris, A.3    Guo, J.P.4    McGeer, P.L.5
  • 13
    • 34547214510 scopus 로고    scopus 로고
    • A b ion channels. Prospects for treating Alzheimer's disease with A b channel blockers
    • Arispe N, Diaz JC, Simakova O (2007) A b ion channels. Prospects for treating Alzheimer's disease with A b channel blockers. Biochim Biophys Acta 1768:1952-1965
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1952-1965
    • Arispe, N.1    Diaz, J.C.2    Simakova, O.3
  • 14
    • 33845954777 scopus 로고    scopus 로고
    • It may take inflammation, phosphorylation and ubiquitination to 'tangle' in Alzheimer's disease
    • Arnaud L, Robakis NK, Figueiredo-Pereira ME (2006) It may take inflammation, phosphorylation and ubiquitination to 'tangle' in Alzheimer's disease. Neurodegener Dis 3:313-319
    • (2006) Neurodegener Dis , vol.3 , pp. 313-319
    • Arnaud, L.1    Robakis, N.K.2    Figueiredo-Pereira, M.E.3
  • 15
    • 0345561533 scopus 로고    scopus 로고
    • Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations
    • Arrasate M, Perez M, Armas-Portela R, Avila J (1999) Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations. FEBS Lett 446:199-202
    • (1999) FEBS Lett , vol.446 , pp. 199-202
    • Arrasate, M.1    Perez, M.2    Armas-Portela, R.3    Avila, J.4
  • 16
    • 77953675879 scopus 로고    scopus 로고
    • Probing the biology of Alzheimer's disease in mice
    • Ashe KH, Zahs KR (2010) Probing the biology of Alzheimer's disease in mice. Neuron 66:631-645
    • (2010) Neuron , vol.66 , pp. 631-645
    • Ashe, K.H.1    Zahs, K.R.2
  • 21
    • 0029845397 scopus 로고    scopus 로고
    • Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L
    • Bednarski E, Lynch G (1996) Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L. J Neurochem 67:1846-1855
    • (1996) J Neurochem , vol.67 , pp. 1846-1855
    • Bednarski, E.1    Lynch, G.2
  • 24
  • 25
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and Tau
    • Bhaskar K, Yen SH, Lee G (2005) Disease-related modifications in tau affect the interaction between Fyn and Tau. J Biol Chem 280:35119-35125
    • (2005) J Biol Chem , vol.280 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 27
    • 77956504025 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy
    • Bhaskar K, Hobbs GA, Yen SH, Lee G (2010a) Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy. Neuropathol Appl Neurobiol 36:462-477
    • (2010) Neuropathol Appl Neurobiol , vol.36 , pp. 462-477
    • Bhaskar, K.1    Hobbs, G.A.2    Yen, S.H.3    Lee, G.4
  • 29
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J, Gustke N, Drewes G, Mandelkow EM, Mandelkow E (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11:153-163
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 30
    • 33846570982 scopus 로고    scopus 로고
    • Learning decreases A b 56 and tau pathology and ameliorates behavioral decline in 3×Tg-AD mice
    • Billings LM, Green KN, Mcgaugh JL, Laferla FM (2007) Learning decreases A b 56 and tau pathology and ameliorates behavioral decline in 3×Tg-AD mice. J Neurosci 27:751-761
    • (2007) J Neurosci , vol.27 , pp. 751-761
    • Billings, L.M.1    Green, K.N.2    McGaugh, J.L.3    Laferla, F.M.4
  • 31
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder LI, Frankfurter A, Rebhun LI (1985) The distribution of tau in the mammalian central nervous system. J Cell Biol 101:1371-1378
    • (1985) J Cell Biol , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 33
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid b-protein oligomerization
    • Bitan G, Vollers SS, Teplow DB (2003b) Elucidation of primary structure elements controlling early amyloid b-protein oligomerization. J Biol Chem 278:34882-34889
    • (2003) J Biol Chem , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 34
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which A b facilitates tau pathology
    • Blurton-Jones M, Laferla FM (2006) Pathways by which A b facilitates tau pathology. Curr Alzheimer Res 3:437-448
    • (2006) Curr Alzheimer Res , vol.3 , pp. 437-448
    • Blurton-Jones, M.1    Laferla, F.M.2
  • 36
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E, Braak H, Mandelkow EM (1994) A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol 87:554-567
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 37
    • 49149098525 scopus 로고    scopus 로고
    • Tau aggregates: Toxic, inert, or protective species?
    • Bretteville A, Planel E (2008) Tau aggregates: toxic, inert, or protective species? J Alzheimers Dis 14:431-436
    • (2008) J Alzheimers Dis , vol.14 , pp. 431-436
    • Bretteville, A.1    Planel, E.2
  • 38
    • 84880188055 scopus 로고    scopus 로고
    • Immunological demonstration of tau protein in neurofibrillary tangles of Alzheimer's disease
    • Brion JP (2006) Immunological demonstration of tau protein in neurofibrillary tangles of Alzheimer's disease. J Alzheimers Dis 9:177-185
    • (2006) J Alzheimers Dis , vol.9 , pp. 177-185
    • Brion, J.P.1
  • 42
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of b amyloid neurotoxicity
    • Busciglio J, Lorenzo A, Yankner BA (1992) Methodological variables in the assessment of b amyloid neurotoxicity. Neurobiol Aging 13:609-612
    • (1992) Neurobiol Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 43
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner KA, Kirschner MW (1991) Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 115:717-730
    • (1991) J Cell Biol , vol.115 , pp. 717-730
    • Butner, K.A.1    Kirschner, M.W.2
  • 44
    • 34249696007 scopus 로고    scopus 로고
    • Rapid, concurrent alterations in pre-and postsynaptic structure induced by naturally secreted amyloid-b protein
    • Calabrese B, Shaked GM, Tabarean IV, Braga J, Koo EH, Halpain S (2007) Rapid, concurrent alterations in pre-and postsynaptic structure induced by naturally secreted amyloid-b protein. Mol Cell Neurosci 35:183-193
    • (2007) Mol Cell Neurosci , vol.35 , pp. 183-193
    • Calabrese, B.1    Shaked, G.M.2    Tabarean, I.V.3    Braga, J.4    Koo, E.H.5    Halpain, S.6
  • 45
    • 75949127362 scopus 로고    scopus 로고
    • Inflammation, microglia, and Alzheimer's disease
    • Cameron B, Landreth GE (2010) Inflammation, microglia, and Alzheimer's disease. Neurobiol Dis 37:503-509
    • (2010) Neurobiol Dis , vol.37 , pp. 503-509
    • Cameron, B.1    Landreth, G.E.2
  • 48
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267-298
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 49
    • 0032859650 scopus 로고    scopus 로고
    • Overexpression of four-repeat tau mRNA isoforms in progressive supranuclear palsy but not in Alzheimer's disease
    • Chambers CB, Lee JM, Troncoso JC, Reich S, Muma NA (1999) Overexpression of four-repeat tau mRNA isoforms in progressive supranuclear palsy but not in Alzheimer's disease. Ann Neurol 46:325-332
    • (1999) Ann Neurol , vol.46 , pp. 325-332
    • Chambers, C.B.1    Lee, J.M.2    Troncoso, J.C.3    Reich, S.4    Muma, N.A.5
  • 50
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous amyloid-b oligomers and its application to Alzheimer's disease drug candidate screening
    • Chang L, Bakhos L, Wang Z, Venton DL, Klein WL (2003) Femtomole immunodetection of synthetic and endogenous amyloid-b oligomers and its application to Alzheimer's disease drug candidate screening. J Mol Neurosci 20:305-313
    • (2003) J Mol Neurosci , vol.20 , pp. 305-313
    • Chang, L.1    Bakhos, L.2    Wang, Z.3    Venton, D.L.4    Klein, W.L.5
  • 52
    • 17144395539 scopus 로고    scopus 로고
    • Triggers of full-length tau aggregation: A role for partially folded intermediates
    • Chirita CN, Congdon EE, Yin H, Kuret J (2005) Triggers of full-length tau aggregation: A role for partially folded intermediates. Biochemistry 44:5862-5872
    • (2005) Biochemistry , vol.44 , pp. 5862-5872
    • Chirita, C.N.1    Congdon, E.E.2    Yin, H.3    Kuret, J.4
  • 53
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3 b (GSK3 b ) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • Cho JH, Johnson GV (2004) Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3 b (GSK3 b ) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J Neurochem 88:349-358
    • (2004) J Neurochem , vol.88 , pp. 349-358
    • Cho, J.H.1    Johnson, G.V.2
  • 57
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland DW, Hwo SY, Kirschner MW (1977) Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J Mol Biol 116:207-225
    • (1977) J Mol Biol , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 58
    • 49149109927 scopus 로고    scopus 로고
    • Is tau aggregation toxic or protective?
    • Congdon EE, Duff KE (2008) Is tau aggregation toxic or protective? J Alzheimers Dis 14:453-457
    • (2008) J Alzheimers Dis , vol.14 , pp. 453-457
    • Congdon, E.E.1    Duff, K.E.2
  • 59
    • 0016211732 scopus 로고
    • Pick's disease. Histological and clinical correlations
    • Constantinidis J, Richard J, Tissot R (1974) Pick's disease. Histological and clinical correlations. Eur Neurol 11:208-217
    • (1974) Eur Neurol , vol.11 , pp. 208-217
    • Constantinidis, J.1    Richard, J.2    Tissot, R.3
  • 63
    • 78149411188 scopus 로고    scopus 로고
    • Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo
    • Cowan CM, Bossing T, Page A, Shepherd D, Mudher A (2010) Soluble hyper-phosphorylated tau causes microtubule breakdown and functionally compromises normal tau in vivo. Acta Neuropathol 120:593-604
    • (2010) Acta Neuropathol , vol.120 , pp. 593-604
    • Cowan, C.M.1    Bossing, T.2    Page, A.3    Shepherd, D.4    Mudher, A.5
  • 64
    • 0020686674 scopus 로고
    • Alzheimer's disease: A disorder of cortical cholinergic innervation
    • Coyle JT, Price DL, Delong MR (1983) Alzheimer's disease: A disorder of cortical cholinergic innervation. Science 219:1184-1190
    • (1983) Science , vol.219 , pp. 1184-1190
    • Coyle, J.T.1    Price, D.L.2    Delong, M.R.3
  • 65
    • 0030464914 scopus 로고    scopus 로고
    • B-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease
    • Cummings BJ, Pike CJ, Shankle R, Cotman CW (1996) b-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol Aging 17:921-933
    • (1996) Neurobiol Aging , vol.17 , pp. 921-933
    • Cummings, B.J.1    Pike, C.J.2    Shankle, R.3    Cotman, C.W.4
  • 66
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-b binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain CC, Ali F, Volitakis I, Cherny RA, Norton RS, Beyreuther K, Barrow CJ, Masters CL, Bush AI, Barnham KJ (2001) Alzheimer's disease amyloid-b binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J Biol Chem 276:20466-20473
    • (2001) J Biol Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3    Cherny, R.A.4    Norton, R.S.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Bush, A.I.9    Barnham, K.J.10
  • 68
    • 0023106967 scopus 로고
    • A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease
    • Davies CA, Mann DM, Sumpter PQ, Yates PO (1987) A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease. J Neurol Sci 78:151-164
    • (1987) J Neurol Sci , vol.78 , pp. 151-164
    • Davies, C.A.1    Mann, D.M.2    Sumpter, P.Q.3    Yates, P.O.4
  • 70
    • 77952945262 scopus 로고    scopus 로고
    • Tau deficiency leads to the upregulation of BAF-57, a protein involved in neuron-specific gene repression
    • De Barreda EG, Dawson HN, Vitek MP, Avila J (2010) Tau deficiency leads to the upregulation of BAF-57, a protein involved in neuron-specific gene repression. FEBS Lett 584:2265-2270
    • (2010) FEBS Lett , vol.584 , pp. 2265-2270
    • De Barreda, E.G.1    Dawson, H.N.2    Vitek, M.P.3    Avila, J.4
  • 74
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • Dekosky ST, Scheff SW (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann Neurol 27:457-464
    • (1990) Ann Neurol , vol.27 , pp. 457-464
    • Dekosky, S.T.1    Scheff, S.W.2
  • 78
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 80
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid b induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A, Mina E, Glabe C, Busciglio J (2006) Different conformations of amyloid b induce neurotoxicity by distinct mechanisms in human cortical neurons. J Neurosci 26:6011-6018
    • (2006) J Neurosci , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 81
    • 65249093004 scopus 로고    scopus 로고
    • A role for synaptic zinc in activity-dependent A b oligomer formation and accumulation at excitatory synapses
    • Deshpande A, Kawai H, Metherate R, Glabe CG, Busciglio J (2009) A role for synaptic zinc in activity-dependent A b oligomer formation and accumulation at excitatory synapses. J Neurosci 29:4004-4015
    • (2009) J Neurosci , vol.29 , pp. 4004-4015
    • Deshpande, A.1    Kawai, H.2    Metherate, R.3    Glabe, C.G.4    Busciglio, J.5
  • 84
    • 0031901513 scopus 로고    scopus 로고
    • Pick's disease: A modern approach
    • Dickson DW (1998) Pick's disease: A modern approach. Brain Pathol 8:339-354
    • (1998) Brain Pathol , vol.8 , pp. 339-354
    • Dickson, D.W.1
  • 85
    • 0023260938 scopus 로고
    • A monoclonal antibody that recognizes a phosphorylated epitope in Alzheimer neurofibrillary tangles, neurofilaments and tau proteins immunostains granulovacuolar degeneration
    • Dickson DW, Ksiezak-Reding H, Davies P, Yen SH (1987) A monoclonal antibody that recognizes a phosphorylated epitope in Alzheimer neurofibrillary tangles, neurofilaments and tau proteins immunostains granulovacuolar degeneration. Acta Neuropathol 73:254-258
    • (1987) Acta Neuropathol , vol.73 , pp. 254-258
    • Dickson, D.W.1    Ksiezak-Reding, H.2    Davies, P.3    Yen, S.H.4
  • 86
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • discussion 98-304
    • Dickson DW, Crystal HA, Bevona C, Honer W, Vincent I, Davies P (1995) Correlations of synaptic and pathological markers with cognition of the elderly. Neurobiol Aging 16:285-298, discussion 98-304
    • (1995) Neurobiol Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1    Crystal, H.A.2    Bevona, C.3    Honer, W.4    Vincent, I.5    Davies, P.6
  • 87
    • 0037151046 scopus 로고    scopus 로고
    • Accelerated plaque accumulation, associative learning deficits, and up-regulation of a 7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins
    • Dineley KT, Xia X, Bui D, Sweatt JD, Zheng H (2002) Accelerated plaque accumulation, associative learning deficits, and up-regulation of a 7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins. J Biol Chem 277:22768-22780
    • (2002) J Biol Chem , vol.277 , pp. 22768-22780
    • Dineley, K.T.1    Xia, X.2    Bui, D.3    Sweatt, J.D.4    Zheng, H.5
  • 89
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-b within isolated senile plaque cores: Raman microscopic evidence
    • Dong J, Atwood CS, Anderson VE, Siedlak SL, Smith MA, Perry G, Carey PR (2003) Metal binding and oxidation of amyloid-b within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42:2768-2773
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 90
    • 23844434232 scopus 로고    scopus 로고
    • Untangling memory deficits
    • Duff K, Planel E (2005) Untangling memory deficits. Nat Med 11:826-827
    • (2005) Nat Med , vol.11 , pp. 826-827
    • Duff, K.1    Planel, E.2
  • 91
    • 67650484613 scopus 로고    scopus 로고
    • Deletion of the a 7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer's disease
    • Dziewczapolski G, Glogowski CM, Masliah E, Heinemann SF (2009) Deletion of the a 7 nicotinic acetylcholine receptor gene improves cognitive deficits and synaptic pathology in a mouse model of Alzheimer's disease. J Neurosci 29:8805-8815
    • (2009) J Neurosci , vol.29 , pp. 8805-8815
    • Dziewczapolski, G.1    Glogowski, C.M.2    Masliah, E.3    Heinemann, S.F.4
  • 96
    • 77951671969 scopus 로고    scopus 로고
    • Cerebrospinal fluid biomarkers of Alzheimer's disease
    • Fagan AM, Holtzman DM (2010) Cerebrospinal fluid biomarkers of Alzheimer's disease. Biomark Med 4:51-63
    • (2010) Biomark Med , vol.4 , pp. 51-63
    • Fagan, A.M.1    Holtzman, D.M.2
  • 97
    • 77953916565 scopus 로고    scopus 로고
    • Dual functions of b-amyloid oligomer and fibril in Cu(II)-induced H 2 O 2 production
    • Fang CL, Wu WH, Liu Q, Sun X, Ma Y, Zhao YF, Li YM (2010) Dual functions of b-amyloid oligomer and fibril in Cu(II)-induced H 2 O 2 production. Regul Pept 163:1-6
    • (2010) Regul Pept , vol.163 , pp. 1-6
    • Fang, C.L.1    Wu, W.H.2    Liu, Q.3    Sun, X.4    Ma, Y.5    Zhao, Y.F.6    Li, Y.M.7
  • 98
    • 15244347753 scopus 로고    scopus 로고
    • Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K
    • Fasulo L, Ugolini G, Cattaneo A (2005) Apoptotic effect of caspase-3 cleaved tau in hippocampal neurons and its potentiation by tau FTDP-mutation N279K. J Alzheimers Dis 7:3-13
    • (2005) J Alzheimers Dis , vol.7 , pp. 3-13
    • Fasulo, L.1    Ugolini, G.2    Cattaneo, A.3
  • 99
    • 0029062956 scopus 로고
    • Widespread cytoskeletal pathology characterizes corticobasal degeneration
    • Feany MB, Dickson DW (1995) Widespread cytoskeletal pathology characterizes corticobasal degeneration. Am J Pathol 146:1388-1396
    • (1995) Am J Pathol , vol.146 , pp. 1388-1396
    • Feany, M.B.1    Dickson, D.W.2
  • 100
    • 0030049067 scopus 로고    scopus 로고
    • Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration
    • Feany MB, Mattiace LA, Dickson DW (1996) Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration. J Neuropathol Exp Neurol 55:53-67
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 53-67
    • Feany, M.B.1    Mattiace, L.A.2    Dickson, D.W.3
  • 101
    • 0025857173 scopus 로고
    • Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type
    • Flament S, Delacourte A, Verny M, Hauw JJ, Javoy-Agid F (1991) Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol 81:591-596
    • (1991) Acta Neuropathol , vol.81 , pp. 591-596
    • Flament, S.1    Delacourte, A.2    Verny, M.3    Hauw, J.J.4    Javoy-Agid, F.5
  • 102
    • 0030977392 scopus 로고    scopus 로고
    • Frontotemporal dementia and parkinsonism linked to chromosome 17: A consensus conference. Conference Participants
    • Foster NL, Wilhelmsen K, Sima AA, Jones MZ, D'amato CJ, Gilman S (1997) Frontotemporal dementia and parkinsonism linked to chromosome 17: A consensus conference. Conference Participants. Ann Neurol 41:706-715
    • (1997) Ann Neurol , vol.41 , pp. 706-715
    • Foster, N.L.1    Wilhelmsen, K.2    Sima, A.A.3    Jones, M.Z.4    D'Amato, C.J.5    Gilman, S.6
  • 108
    • 49149098756 scopus 로고    scopus 로고
    • Truncation of tau protein and its pathological significance in Alzheimer's disease
    • Garcia-Sierra F, Mondragon-Rodriguez S, Basurto-Islas G (2008) Truncation of tau protein and its pathological significance in Alzheimer's disease. J Alzheimers Dis 14:401-409
    • (2008) J Alzheimers Dis , vol.14 , pp. 401-409
    • Garcia-Sierra, F.1    Mondragon-Rodriguez, S.2    Basurto-Islas, G.3
  • 109
    • 0035399785 scopus 로고    scopus 로고
    • Microglia in neurodegeneration: Molecular aspects
    • Gebicke-Haerter PJ (2001) Microglia in neurodegeneration: molecular aspects. Microsc Res Tech 54:47-58
    • (2001) Microsc Res Tech , vol.54 , pp. 47-58
    • Gebicke-Haerter, P.J.1
  • 110
    • 0032747284 scopus 로고    scopus 로고
    • Age-related decline in memory function: Is it associated with a loss of synapses?
    • Geinisman Y (1999) Age-related decline in memory function: is it associated with a loss of synapses? Neurobiol Aging 20:353-356
    • (1999) Neurobiol Aging , vol.20 , pp. 353-356
    • Geinisman, Y.1
  • 111
    • 0026941759 scopus 로고
    • Structural synaptic plasticity associated with the induction of long-term potentiation is preserved in the dentate gyrus of aged rats
    • Geinisman Y, Detoledo-Morrell L, Morrell F, Persina IS, Rossi M (1992) Structural synaptic plasticity associated with the induction of long-term potentiation is preserved in the dentate gyrus of aged rats. Hippocampus 2:445-456
    • (1992) Hippocampus , vol.2 , pp. 445-456
    • Geinisman, Y.1    Detoledo-Morrell, L.2    Morrell, F.3    Persina, I.S.4    Rossi, M.5
  • 113
  • 114
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid b-protein neurotoxicity
    • Geula C, Wu CK, Saroff D, Lorenzo A, Yuan M, Yankner BA (1998) Aging renders the brain vulnerable to amyloid b-protein neurotoxicity. Nat Med 4:827-831
    • (1998) Nat Med , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 115
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 117
    • 0031796883 scopus 로고    scopus 로고
    • Neurofibrillary pathology of Alzheimer's disease and other tauopathies
    • Goedert M (1998) Neurofibrillary pathology of Alzheimer's disease and other tauopathies. Prog Brain Res 117:287-306
    • (1998) Prog Brain Res , vol.117 , pp. 287-306
    • Goedert, M.1
  • 118
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M, Jakes R (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 9:4225-4230
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 119
    • 0002792366 scopus 로고
    • Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau
    • Goedert M, Wischik CM, Crowther RA, Walker JE, Klug A (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. Proc Natl Acad Sci USA 85:4051-4055
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4051-4055
    • Goedert, M.1    Wischik, C.M.2    Crowther, R.A.3    Walker, J.E.4    Klug, A.5
  • 120
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3:519-526
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 121
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms
    • Goedert M, Spillantini MG, Cairns NJ, Crowther RA (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 8:159-168
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 123
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383:550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 124
    • 0032919462 scopus 로고    scopus 로고
    • Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
    • Goedert M, Jakes R, Crowther RA (1999) Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments. FEBS Lett 450:306-311
    • (1999) FEBS Lett , vol.450 , pp. 306-311
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 125
    • 3042857991 scopus 로고    scopus 로고
    • Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture
    • Goldbaum O, Richter-Landsberg C (2004) Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture. J Neurosci 24:5748-5757
    • (2004) J Neurosci , vol.24 , pp. 5748-5757
    • Goldbaum, O.1    Richter-Landsberg, C.2
  • 128
    • 0345701340 scopus 로고    scopus 로고
    • Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells
    • Gomez-Ramos A, Diaz-Nido J, Smith MA, Perry G, Avila J (2003) Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells. J Neurosci Res 71:863-870
    • (2003) J Neurosci Res , vol.71 , pp. 863-870
    • Gomez-Ramos, A.1    Diaz-Nido, J.2    Smith, M.A.3    Perry, G.4    Avila, J.5
  • 129
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode BL, Feinstein SC (1994) Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau. J Cell Biol 124:769-782
    • (1994) J Cell Biol , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 130
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by A b 42 fibrils
    • Gotz J, Chen F, Van Dorpe J, Nitsch RM (2001) Formation of neurofibrillary tangles in P301l tau transgenic mice induced by A b 42 fibrils. Science 293:1491-1495
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 131
  • 132
    • 0024363934 scopus 로고
    • Excitatory amino acids and Alzheimer's disease
    • Greenamyre JT, Young AB (1989) Excitatory amino acids and Alzheimer's disease. Neurobiol Aging 10:593-602
    • (1989) Neurobiol Aging , vol.10 , pp. 593-602
    • Greenamyre, J.T.1    Young, A.B.2
  • 133
    • 0025292866 scopus 로고
    • A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis
    • Greenberg SG, Davies P (1990) A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 87: 5827-5831
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5827-5831
    • Greenberg, S.G.1    Davies, P.2
  • 134
    • 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 (1992) Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J Biol Chem 267:564-569
    • (1992) J Biol Chem , vol.267 , pp. 564-569
    • Greenberg, S.G.1    Davies, P.2    Schein, J.D.3    Binder, L.I.4
  • 135
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • Gronroos E, Hellman U, Heldin CH, Ericsson J (2002) Control of Smad7 stability by competition between acetylation and ubiquitination. Mol Cell 10:483-493
    • (2002) Mol Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 138
    • 0026735070 scopus 로고
    • Targeting of cell-surface b-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ (1992) Targeting of cell-surface b-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357:500-503
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 140
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 15:112-119
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 141
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256:184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 142
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297:353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 143
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-b protein
    • Harper JD, Lieber CM, Lansbury PT Jr (1997) Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-b protein. Chem Biol 4:951-959
    • (1997) Chem Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 144
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid b-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ (1999) Protofibrillar intermediates of amyloid b-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 19:8876-8884
    • (1999) J Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 145
    • 47749153411 scopus 로고    scopus 로고
    • Transglutaminase induces protofibril-like amyloid b-protein assemblies that are protease-resistant and inhibit long-term potentiation
    • Hartley DM, Zhao C, Speier AC, Woodard GA, Li S, Li Z, Walz T (2008) Transglutaminase induces protofibril-like amyloid b-protein assemblies that are protease-resistant and inhibit long-term potentiation. J Biol Chem 283:16790-16800
    • (2008) J Biol Chem , vol.283 , pp. 16790-16800
    • Hartley, D.M.1    Zhao, C.2    Speier, A.C.3    Woodard, G.A.4    Li, S.5    Li, Z.6    Walz, T.7
  • 147
    • 1642451941 scopus 로고    scopus 로고
    • In vivo study of acetylcholine esterase in basal forebrain, amygdala, and cortex in mild to moderate Alzheimer disease
    • Herholz K, Weisenbach S, Zundorf G, Lenz O, Schroder H, Bauer B, Kalbe E, Heiss WD (2004) In vivo study of acetylcholine esterase in basal forebrain, amygdala, and cortex in mild to moderate Alzheimer disease. Neuroimage 21:136-143
    • (2004) Neuroimage , vol.21 , pp. 136-143
    • Herholz, K.1    Weisenbach, S.2    Zundorf, G.3    Lenz, O.4    Schroder, H.5    Bauer, B.6    Kalbe, E.7    Heiss, W.D.8
  • 149
    • 77249153190 scopus 로고    scopus 로고
    • Loss of a 7 nicotinic receptors enhances b-amyloid oligomer accumulation, exacerbating early-stage cognitive decline and septohippocampal pathology in a mouse model of Alzheimer's disease
    • Hernandez CM, Kayed R, Zheng H, Sweatt JD, Dineley KT (2010) Loss of a 7 nicotinic receptors enhances b-amyloid oligomer accumulation, exacerbating early-stage cognitive decline and septohippocampal pathology in a mouse model of Alzheimer's disease. J Neurosci 30: 2442-2453
    • (2010) J Neurosci , vol.30 , pp. 2442-2453
    • Hernandez, C.M.1    Kayed, R.2    Zheng, H.3    Sweatt, J.D.4    Dineley, K.T.5
  • 150
    • 34247508686 scopus 로고    scopus 로고
    • Cell cycle regulation in the postmitotic neuron: Oxymoron or new biology?
    • Herrup K, Yang Y (2007) Cell cycle regulation in the postmitotic neuron: oxymoron or new biology? Nat Rev Neurosci 8:368-378
    • (2007) Nat Rev Neurosci , vol.8 , pp. 368-378
    • Herrup, K.1    Yang, Y.2
  • 151
    • 61949165896 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide production by copper-bound amyloid b peptide: A theoretical study
    • Hewitt N, Rauk A (2009) Mechanism of hydrogen peroxide production by copper-bound amyloid b peptide: A theoretical study. J Phys Chem B 113:1202-1209
    • (2009) J Phys Chem B , vol.113 , pp. 1202-1209
    • Hewitt, N.1    Rauk, A.2
  • 153
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler A, Drechsel D, Kirschner MW, Martin DW Jr (1989) Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol Cell Biol 9:1381-1388
    • (1989) Mol Cell Biol , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin, D.W.4
  • 155
    • 77649092874 scopus 로고    scopus 로고
    • Amyloid-b 42 oligomer structures from fibrils: A systematic molecular dynamics study
    • Horn AH, Sticht H (2010) Amyloid-b 42 oligomer structures from fibrils: A systematic molecular dynamics study. J Phys Chem B 114:2219-2226
    • (2010) J Phys Chem B , vol.114 , pp. 2219-2226
    • Horn, A.H.1    Sticht, H.2
  • 156
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of b-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3 b
    • Hoshi M, Sato M, Matsumoto S, Noguchi A, Yasutake K, Yoshida N, Sato K (2003) Spherical aggregates of b-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3 b. Proc Natl Acad Sci USA 100:6370-6375
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 158
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-b peptide
    • Hu X, Crick SL, Bu G, Frieden C, Pappu RV, Lee JM (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-b peptide. Proc Natl Acad Sci USA 106:20324-20329
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.M.6
  • 159
    • 0012505469 scopus 로고    scopus 로고
    • Tau could protect DNA double helix structure
    • Hua Q, He RQ (2003) Tau could protect DNA double helix structure. Biochim Biophys Acta 1645:205-211
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 205-211
    • Hua, Q.1    He, R.Q.2
  • 161
    • 0022535539 scopus 로고
    • Perforant pathway changes and the memory impairment of Alzheimer's disease
    • Hyman BT, Van Hoesen GW, Kromer LJ, Damasio AR (1986) Perforant pathway changes and the memory impairment of Alzheimer's disease. Ann Neurol 20:472-481
    • (1986) Ann Neurol , vol.20 , pp. 472-481
    • Hyman, B.T.1    Van Hoesen, G.W.2    Kromer, L.J.3    Damasio, A.R.4
  • 162
    • 0030607177 scopus 로고    scopus 로고
    • Rapid cellular uptake of Alzheimer amyloid b A4 peptide by cultured human neuroblastoma cells
    • Ida N, Masters CL, Beyreuther K (1996) Rapid cellular uptake of Alzheimer amyloid b A4 peptide by cultured human neuroblastoma cells. FEBS Lett 394:174-178
    • (1996) FEBS Lett , vol.394 , pp. 174-178
    • Ida, N.1    Masters, C.L.2    Beyreuther, K.3
  • 164
    • 0034996076 scopus 로고    scopus 로고
    • Microglial activation parallels system degeneration in progressive supranuclear palsy and corticobasal degeneration
    • Ishizawa K, Dickson DW (2001) Microglial activation parallels system degeneration in progressive supranuclear palsy and corticobasal degeneration. J Neuropathol Exp Neurol 60:647-657
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 647-657
    • Ishizawa, K.1    Dickson, D.W.2
  • 167
    • 0027978991 scopus 로고
    • Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics
    • Iwatsubo T, Hasegawa M, Ihara Y (1994) Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. Acta Neuropathol 88:129-136
    • (1994) Acta Neuropathol , vol.88 , pp. 129-136
    • Iwatsubo, T.1    Hasegawa, M.2    Ihara, Y.3
  • 170
    • 34547914869 scopus 로고    scopus 로고
    • Redox reactions of copper complexes formed with different b-amyloid peptides and their neuropathological [ correction of neuropathalogical] relevance
    • Jiang D, Men L, Wang J, Zhang Y, Chickenyen S, Wang Y, Zhou F (2007) Redox reactions of copper complexes formed with different b-amyloid peptides and their neuropathological [ correction of neuropathalogical] relevance. Biochemistry 46:9270-9282
    • (2007) Biochemistry , vol.46 , pp. 9270-9282
    • Jiang, D.1    Men, L.2    Wang, J.3    Zhang, Y.4    Chickenyen, S.5    Wang, Y.6    Zhou, F.7
  • 171
    • 77950681411 scopus 로고    scopus 로고
    • Reaction rates and mechanism of the ascorbic acid oxidation by molecular oxygen facilitated by Cu(II)-containing amyloid-b complexes and aggregates
    • Jiang D, Li X, Liu L, Yagnik GB, Zhou F (2010) Reaction rates and mechanism of the ascorbic acid oxidation by molecular oxygen facilitated by Cu(II)-containing amyloid-b complexes and aggregates. J Phys Chem B 114:4896-4903
    • (2010) J Phys Chem B , vol.114 , pp. 4896-4903
    • Jiang, D.1    Li, X.2    Liu, L.3    Yagnik, G.B.4    Zhou, F.5
  • 172
    • 3142720638 scopus 로고    scopus 로고
    • Transforming growth factor-b stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitinationmediated degradation
    • Jin YH, Jeon EJ, Li QL, Lee YH, Choi JK, Kim WJ, Lee KY, Bae SC (2004) Transforming growth factor-b stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitinationmediated degradation. J Biol Chem 279:29409-29417
    • (2004) J Biol Chem , vol.279 , pp. 29409-29417
    • Jin, Y.H.1    Jeon, E.J.2    Li, Q.L.3    Lee, Y.H.4    Choi, J.K.5    Kim, W.J.6    Lee, K.Y.7    Bae, S.C.8
  • 174
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers T, Friedhoff P, Biernat J, Mandelkow EM, Mandelkow E (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 399:344-349
    • (1996) FEBS Lett , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 176
    • 0036591863 scopus 로고    scopus 로고
    • Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid b-peptide
    • Kanski J, Aksenova M, Schoneich C, Butterfield DA (2002a) Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid b-peptide. Free Radic Biol Med 32:1205-1211
    • (2002) Free Radic Biol Med , vol.32 , pp. 1205-1211
    • Kanski, J.1    Aksenova, M.2    Schoneich, C.3    ButterfiEld, D.A.4
  • 177
    • 0037117310 scopus 로고    scopus 로고
    • Role of glycine-33 and methionine-35 in Alzheimer's amyloid b-peptide 1-42-associated oxidative stress and neurotoxicity
    • Kanski J, Varadarajan S, Aksenova M, Butterfield DA (2002b) Role of glycine-33 and methionine-35 in Alzheimer's amyloid b-peptide 1-42-associated oxidative stress and neurotoxicity. Biochim Biophys Acta 1586:190-198
    • (2002) Biochim Biophys Acta , vol.1586 , pp. 190-198
    • Kanski, J.1    Varadarajan, S.2    Aksenova, M.3    ButterfiEld, D.A.4
  • 178
    • 0344441249 scopus 로고    scopus 로고
    • Amyloid b peptides and central cholinergic neurons: Functional interrelationship and relevance to Alzheimer's disease pathology
    • Kar S, Quirion R (2004) Amyloid b peptides and central cholinergic neurons: functional interrelationship and relevance to Alzheimer's disease pathology. Prog Brain Res 145:261-274
    • (2004) Prog Brain Res , vol.145 , pp. 261-274
    • Kar, S.1    Quirion, R.2
  • 180
    • 11144356498 scopus 로고    scopus 로고
    • Dimeric amyloid b protein rapidly accumulates in lipid rafts followed by apolipoprotein e and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease
    • Kawarabayashi T, Shoji M, Younkin LH, Wen-Lang L, Dickson DW, Murakami T, Matsubara E, Abe K, Ashe KH, Younkin SG (2004) Dimeric amyloid b protein rapidly accumulates in lipid rafts followed by apolipoprotein E and phosphorylated tau accumulation in the Tg2576 mouse model of Alzheimer's disease. J Neurosci 24:3801-3809
    • (2004) J Neurosci , vol.24 , pp. 3801-3809
    • Kawarabayashi, T.1    Shoji, M.2    Younkin, L.H.3    Wen-Lang, L.4    Dickson, D.W.5    Murakami, T.6    Matsubara, E.7    Abe, K.8    Ashe, K.H.9    Younkin, S.G.10
  • 181
    • 67049136162 scopus 로고    scopus 로고
    • Prefilament tau species as potential targets for immunotherapy for Alzheimer disease and related disorders
    • Kayed R, Jackson GR (2009) Prefilament tau species as potential targets for immunotherapy for Alzheimer disease and related disorders. Curr Opin Immunol 21:359-363
    • (2009) Curr Opin Immunol , vol.21 , pp. 359-363
    • Kayed, R.1    Jackson, G.R.2
  • 183
    • 33748792254 scopus 로고    scopus 로고
    • B-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons
    • Kelly BL, Ferreira A (2006) b-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-D-aspartate receptors in hippocampal neurons. J Biol Chem 281:28079-28089
    • (2006) J Biol Chem , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 184
    • 0030774852 scopus 로고    scopus 로고
    • Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration
    • Kenessey A, Nacharaju P, Ko LW, Yen SH (1997) Degradation of tau by lysosomal enzyme cathepsin D: implication for Alzheimer neurofibrillary degeneration. J Neurochem 69: 2026-2038
    • (1997) J Neurochem , vol.69 , pp. 2026-2038
    • Kenessey, A.1    Nacharaju, P.2    Ko, L.W.3    Yen, S.H.4
  • 185
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian ZS (1985) Diagnosis of Alzheimer's disease. Arch Neurol 42:1097-1105
    • (1985) Arch Neurol , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 188
    • 0033539689 scopus 로고    scopus 로고
    • Ligand-dependent tau filament formation: Implications for Alzheimer's disease progression
    • King ME, Ahuja V, Binder LI, Kuret J (1999) Ligand-dependent tau filament formation: implications for Alzheimer's disease progression. Biochemistry 38:14851-14859
    • (1999) Biochemistry , vol.38 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 189
    • 25644456097 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclin-dependent kinase 5-mediated pathway in a transgenic model of Alzheimer's disease
    • Kitazawa M, Oddo S, Yamasaki TR, Green KN, Laferla FM (2005) Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclin-dependent kinase 5-mediated pathway in a transgenic model of Alzheimer's disease. J Neurosci 25:8843-8853
    • (2005) J Neurosci , vol.25 , pp. 8843-8853
    • Kitazawa, M.1    Oddo, S.2    Yamasaki, T.R.3    Green, K.N.4    Laferla, F.M.5
  • 192
    • 11844300395 scopus 로고    scopus 로고
    • Soluble A b oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain
    • Kokubo H, Kayed R, Glabe CG, Yamaguchi H (2005) Soluble A b oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain. Brain Res 1031:222-228
    • (2005) Brain Res , vol.1031 , pp. 222-228
    • Kokubo, H.1    Kayed, R.2    Glabe, C.G.3    Yamaguchi, H.4
  • 194
    • 6344287664 scopus 로고    scopus 로고
    • Anionic contribution for fibrous maturation of protofibrillar assemblies of the human tau repeat domain in a fluoroalcohol solution
    • Konno T, Oiki S, Hasegawa K, Naiki H (2004) Anionic contribution for fibrous maturation of protofibrillar assemblies of the human tau repeat domain in a fluoroalcohol solution. Biochemistry 43:13613-13620
    • (2004) Biochemistry , vol.43 , pp. 13613-13620
    • Konno, T.1    Oiki, S.2    Hasegawa, K.3    Naiki, H.4
  • 195
    • 34548620157 scopus 로고    scopus 로고
    • Swimming against the tide: Mobility of the microtubule-associated protein tau in neurons
    • Konzack S, Thies E, Marx A, Mandelkow EM, Mandelkow E (2007) Swimming against the tide: mobility of the microtubule-associated protein tau in neurons. J Neurosci 27:9916-9927
    • (2007) J Neurosci , vol.27 , pp. 9916-9927
    • Konzack, S.1    Thies, E.2    Marx, A.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 197
    • 83455224821 scopus 로고    scopus 로고
    • Tau truncation is a productive posttranslational modification of neurofibrillary degeneration in Alzheimer's disease
    • Kovacech B, Novak M (2010) Tau truncation is a productive posttranslational modification of neurofibrillary degeneration in Alzheimer's disease. Curr Alzheimer Res 7:708-716
    • (2010) Curr Alzheimer Res , vol.7 , pp. 708-716
    • Kovacech, B.1    Novak, M.2
  • 198
    • 24144465828 scopus 로고    scopus 로고
    • Characterization of paired helical filaments by scanning transmission electron microscopy
    • Ksiezak-Reding H, Wall JS (2005) Characterization of paired helical filaments by scanning transmission electron microscopy. Microsc Res Tech 67:126-140
    • (2005) Microsc Res Tech , vol.67 , pp. 126-140
    • Ksiezak-Reding, H.1    Wall, J.S.2
  • 199
    • 0023139520 scopus 로고
    • Two monoclonal antibodies recognize Alzheimer's neurofibrillary tangles, neurofilament, and microtubule-associated proteins
    • Ksiezak-Reding H, Yen SH (1987) Two monoclonal antibodies recognize Alzheimer's neurofibrillary tangles, neurofilament, and microtubule-associated proteins. J Neurochem 48:455-462
    • (1987) J Neurochem , vol.48 , pp. 455-462
    • Ksiezak-Reding, H.1    Yen, S.H.2
  • 200
    • 0025852163 scopus 로고
    • Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association
    • Ksiezak-Reding H, Yen SH (1991) Structural stability of paired helical filaments requires microtubule-binding domains of tau: A model for self-association. Neuron 6:717-728
    • (1991) Neuron , vol.6 , pp. 717-728
    • Ksiezak-Reding, H.1    Yen, S.H.2
  • 201
    • 0023899370 scopus 로고
    • Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1
    • Ksiezak-Reding H, Binder LI, Yen SH (1988) Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1. J Biol Chem 263:7948-7953
    • (1988) J Biol Chem , vol.263 , pp. 7948-7953
    • Ksiezak-Reding, H.1    Binder, L.I.2    Yen, S.H.3
  • 202
    • 0028242639 scopus 로고
    • Tau immunoreactivity and SDS solubility of two populations of paired helical filaments that differ in morphology
    • Ksiezak-Reding H, Morgan K, Dickson DW (1994a) Tau immunoreactivity and SDS solubility of two populations of paired helical filaments that differ in morphology. Brain Res 649:185-196
    • (1994) Brain Res , vol.649 , pp. 185-196
    • Ksiezak-Reding, H.1    Morgan, K.2    Dickson, D.W.3
  • 208
    • 33846633336 scopus 로고    scopus 로고
    • A b oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor PN, Buniel MC, Furlow PW, Clemente AS, Velasco PT, Wood M, Viola KL, Klein WL (2007) A b oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 27:796-807
    • (2007) J Neurosci , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 212
    • 0034925118 scopus 로고    scopus 로고
    • The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: The role of A b 1-42
    • Lauderback CM, Hackett JM, Huang FF, Keller JN, Szweda LI, Markesbery WR, Butterfield DA (2001) The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of A b 1-42. J Neurochem 78:413-416
    • (2001) J Neurochem , vol.78 , pp. 413-416
    • Lauderback, C.M.1    Hackett, J.M.2    Huang, F.F.3    Keller, J.N.4    Szweda, L.I.5    Markesbery, W.R.6    ButterfiEld, D.A.7
  • 213
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee G, Neve RL, Kosik KS (1989) The microtubule binding domain of tau protein. Neuron 2:1615-1624
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 214
    • 0025904444 scopus 로고
    • A68: A major subunit of paired helical filaments and derivatized forms of normal Tau
    • Lee VM, Balin BJ, Otvos L Jr, Trojanowski JQ (1991) A68: A major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251:675-678
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 215
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111(Pt 21):3167-3177
    • (1998) J Cell Sci , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 220
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL (2009) The ubiquitin proteasome system in neuropathology. Acta Neuropathol 118:329-347
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 224
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid b protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li S, Hong S, Shepardson NE, Walsh DM, Shankar GM, Selkoe DJ (2009) Soluble oligomers of amyloid b protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron 62:788-801
    • (2009) Neuron 62 , pp. 788-801
    • Li, S.1    Hong, S.2    Shepardson, N.E.3    Walsh, D.M.4    Shankar, G.M.5    Selkoe, D.J.6
  • 226
    • 0035680685 scopus 로고    scopus 로고
    • FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain
    • Lim F, Hernandez F, Lucas JJ, Gomez-Ramos P, Moran MA, Avila J (2001) FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain. Mol Cell Neurosci 18:702-714
    • (2001) Mol Cell Neurosci , vol.18 , pp. 702-714
    • Lim, F.1    Hernandez, F.2    Lucas, J.J.3    Gomez-Ramos, P.4    Moran, M.A.5    Avila, J.6
  • 227
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid b protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R (2001) Amyloid b protein forms ion channels: implications for Alzheimer's disease pathophysiology. FASEB J 15:2433-2444
    • (2001) FASEB J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 229
    • 70349849851 scopus 로고    scopus 로고
    • Proteasome inhibition increases tau accumulation independent of phosphorylation
    • Liu YH, Wei W, Yin J, Liu GP, Wang Q, Cao FY, Wang JZ (2009) Proteasome inhibition increases tau accumulation independent of phosphorylation. Neurobiol Aging 30:1949-1961
    • (2009) Neurobiol Aging , vol.30 , pp. 1949-1961
    • Liu, Y.H.1    Wei, W.2    Yin, J.3    Liu, G.P.4    Wang, Q.5    Cao, F.Y.6    Wang, J.Z.7
  • 230
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid b-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB (1996) On the nucleation and growth of amyloid b-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 93:1125-1129
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 231
  • 233
    • 0028172886 scopus 로고
    • B-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A, Yankner BA (1994) b-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91:12243-12247
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 235
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • Lovell MA, Xie C, Markesbery WR (2001) Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures. Neurobiol Aging 22:187-194
    • (2001) Neurobiol Aging , vol.22 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 237
    • 0028223015 scopus 로고
    • Clinical and neuropathological criteria for frontotemporal dementia
    • The Lund and Manchester Groups, Lund, Manchester-Groups
    • Lund, Manchester-Groups (1994) Clinical and neuropathological criteria for frontotemporal dementia. The Lund and Manchester Groups. J Neurol Neurosurg Psychiatry 57:416-418
    • (1994) J Neurol Neurosurg Psychiatry , vol.57 , pp. 416-418
  • 238
    • 0346728801 scopus 로고    scopus 로고
    • Long-term potentiation and memory
    • Lynch MA (2004) Long-term potentiation and memory. Physiol Rev 84:87-136
    • (2004) Physiol Rev , vol.84 , pp. 87-136
    • Lynch, M.A.1
  • 241
    • 33244456786 scopus 로고    scopus 로고
    • Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
    • Maeda S, Sahara N, Saito Y, Murayama S, Ikai A, Takashima A (2006) Increased levels of granular tau oligomers: an early sign of brain aging and Alzheimer's disease. Neurosci Res 54:197-201
    • (2006) Neurosci Res , vol.54 , pp. 197-201
    • Maeda, S.1    Sahara, N.2    Saito, Y.3    Murayama, S.4    Ikai, A.5    Takashima, A.6
  • 243
    • 0032555385 scopus 로고    scopus 로고
    • Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes
    • Mailliot C, Sergeant N, Bussiere T, Caillet-Boudin ML, Delacourte A, Buee L (1998) Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes. FEBS Lett 433:201-204
    • (1998) FEBS Lett , vol.433 , pp. 201-204
    • Mailliot, C.1    Sergeant, N.2    Bussiere, T.3    Caillet-Boudin, M.L.4    Delacourte, A.5    Buee, L.6
  • 244
    • 30544447666 scopus 로고    scopus 로고
    • B-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid b: A feedforward mechanism for Alzheimer's disease
    • Maloney M.T., Minamide L.S., Kinley A.W., Boyle J.A., Bamburg J.R. (2005) B-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid b: A feedforward mechanism for Alzheimer's disease. J Neurosci 25:11313-11321
    • (2005) J Neurosci , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 245
    • 30544447666 scopus 로고    scopus 로고
    • B-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid b: A feedforward mechanism for Alzheimer's disease
    • Maloney MT, Minamide LS, Kinley AW, Boyle JA, Bamburg JR (2005) b-Secretase-cleaved amyloid precursor protein accumulates at actin inclusions induced in neurons by stress or amyloid b: A feedforward mechanism for Alzheimer's disease. J Neurosci 25:11313-11321
    • (2005) J Neurosci , vol.25 , pp. 11313-11321
    • Maloney, M.T.1    Minamide, L.S.2    Kinley, A.W.3    Boyle, J.A.4    Bamburg, J.R.5
  • 246
    • 33646152108 scopus 로고    scopus 로고
    • Mitochondria are a direct site of A b accumulation in Alzheimer's disease neurons: Implications for free radical generation and oxidative damage in disease progression
    • Manczak M, Anekonda TS, Henson E, Park BS, Quinn J, Reddy PH (2006) Mitochondria are a direct site of A b accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression. Hum Mol Genet 15:1437-1449
    • (2006) Hum Mol Genet , vol.15 , pp. 1437-1449
    • Manczak, M.1    Anekonda, T.S.2    Henson, E.3    Park, B.S.4    Quinn, J.5    Reddy, P.H.6
  • 247
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow EM, Stamer K, Vogel R, Thies E, Mandelkow E (2003) Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 24:1079-1085
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 248
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow EM, Thies E, Trinczek B, Biernat J, Mandelkow E (2004) MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J Cell Biol 167:99-110
    • (2004) J Cell Biol , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 249
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid b-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark RJ, Pang Z, Geddes JW, Uchida K, Mattson MP (1997) Amyloid b-peptide impairs glucose transport in hippocampal and cortical neurons: involvement of membrane lipid peroxidation. J Neurosci 17:1046-1054
    • (1997) J Neurosci , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 250
    • 0031980065 scopus 로고    scopus 로고
    • Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease
    • Markesbery WR, Lovell MA (1998) Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease. Neurobiol Aging 19:33-36
    • (1998) Neurobiol Aging , vol.19 , pp. 33-36
    • Markesbery, W.R.1    Lovell, M.A.2
  • 252
    • 0025154917 scopus 로고
    • Increased immunoreactivity of brain spectrin in Alzheimer disease: A marker for synapse loss?
    • Masliah E, Iimoto DS, Saitoh T, Hansen LA, Terry RD (1990) Increased immunoreactivity of brain spectrin in Alzheimer disease: A marker for synapse loss? Brain Res 531:36-44
    • (1990) Brain Res , vol.531 , pp. 36-44
    • Masliah, E.1    Iimoto, D.S.2    Saitoh, T.3    Hansen, L.A.4    Terry, R.D.5
  • 255
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki M, Honkura N, Ellis-Davies GC, Kasai H (2004) Structural basis of long-term potentiation in single dendritic spines. Nature 429:761-766
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 256
    • 0030797336 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau
    • Mattson MP, Fu W, Waeg G, Uchida K (1997) 4-Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. Neuroreport 8:2275-2281
    • (1997) Neuroreport , vol.8 , pp. 2275-2281
    • Mattson, M.P.1    Fu, W.2    Waeg, G.3    Uchida, K.4
  • 257
    • 0032526423 scopus 로고    scopus 로고
    • B-Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP1 monocytes
    • Mcdonald DR, Bamberger ME, Combs CK, Landreth GE (1998) b-Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP1 monocytes. J Neurosci 18:4451-4460
    • (1998) J Neurosci , vol.18 , pp. 4451-4460
    • McDonald, D.R.1    Bamberger, M.E.2    Combs, C.K.3    Landreth, G.E.4
  • 258
    • 0025773225 scopus 로고
    • Neuritic pathology and dementia in Alzheimer's disease
    • Mckee AC, Kosik KS, Kowall NW (1991) Neuritic pathology and dementia in Alzheimer's disease. Ann Neurol 30:156-165
    • (1991) Ann Neurol , vol.30 , pp. 156-165
    • McKee, A.C.1    Kosik, K.S.2    Kowall, N.W.3
  • 259
    • 0027320508 scopus 로고
    • Interlaboratory histopathologic assessment of Alzheimer neuropathology: Different methodologies yield comparable diagnostic results
    • Mckeel DW Jr, Ball MJ, Price JL, Smith DS, Miller JP, Berg L, Morris JC (1993) Interlaboratory histopathologic assessment of Alzheimer neuropathology: different methodologies yield comparable diagnostic results. Alzheimer Dis Assoc Disord 7:136-151
    • (1993) Alzheimer Dis Assoc Disord , vol.7 , pp. 136-151
    • Mckeel, D.W.1    Ball, M.J.2    Price, J.L.3    Smith, D.S.4    Miller, J.P.5    Berg, L.6    Morris, J.C.7
  • 260
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-b peptides with glycosaminoglycans effects on fibril nucleation and growth
    • Mclaurin J, Franklin T, Zhang X, Deng J, Fraser PE (1999) Interactions of Alzheimer amyloid-b peptides with glycosaminoglycans effects on fibril nucleation and growth. Eur J Biochem 266:1101-1110
    • (1999) Eur J Biochem , vol.266 , pp. 1101-1110
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 262
    • 0033614920 scopus 로고    scopus 로고
    • Spatial attention and neglect: Parietal, frontal and cingulate contributions to the mental representation and attentional targeting of salient extrapersonal events
    • Mesulam MM (1999) Spatial attention and neglect: parietal, frontal and cingulate contributions to the mental representation and attentional targeting of salient extrapersonal events. Philos Trans R Soc Lond B Biol Sci 354:1325-1346
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 1325-1346
    • Mesulam, M.M.1
  • 266
    • 0027936091 scopus 로고
    • Corticobasal degeneration: A disease with widespread appearance of abnormal tau and neurofibrillary tangles, and its relation to progressive supranuclear palsy
    • Mori H, Nishimura M, Namba Y, Oda M (1994) Corticobasal degeneration: A disease with widespread appearance of abnormal tau and neurofibrillary tangles, and its relation to progressive supranuclear palsy. Acta Neuropathol 88:113-121
    • (1994) Acta Neuropathol , vol.88 , pp. 113-121
    • Mori, H.1    Nishimura, M.2    Namba, Y.3    Oda, M.4
  • 269
    • 0025909840 scopus 로고
    • Clinical diagnosis and course of Alzheimer's disease
    • Morris JC, Rubin EH (1991) Clinical diagnosis and course of Alzheimer's disease. Psychiatr Clin North Am 14:223-236
    • (1991) Psychiatr Clin North Am , vol.14 , pp. 223-236
    • Morris, J.C.1    Rubin, E.H.2
  • 270
    • 0033028074 scopus 로고    scopus 로고
    • Neurons may live for decades with neurofibrillary tangles
    • Morsch R, Simon W, Coleman PD (1999) Neurons may live for decades with neurofibrillary tangles. J Neuropathol Exp Neurol 58:188-197
    • (1999) J Neuropathol Exp Neurol , vol.58 , pp. 188-197
    • Morsch, R.1    Simon, W.2    Coleman, P.D.3
  • 272
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • Murrell J, Farlow M, Ghetti B, Benson MD (1991) A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Science 254:97-99
    • (1991) Science , vol.254 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 273
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju P, Lewis J, Easson C, Yen S, Hackett J, Hutton M, Yen SH (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett 447:195-199
    • (1999) FEBS Lett , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 274
    • 0037066072 scopus 로고    scopus 로고
    • Intracellular accumulation of b-amyloid(1-42) in neurons is facilitated by the a 7 nicotinic acetylcholine receptor in Alzheimer's disease
    • Nagele RG, D'andrea MR, Anderson WJ, Wang HY (2002) Intracellular accumulation of b-amyloid(1-42) in neurons is facilitated by the a 7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 110:199-211
    • (2002) Neuroscience , vol.110 , pp. 199-211
    • Nagele, R.G.1    D'Andrea, M.R.2    Anderson, W.J.3    Wang, H.Y.4
  • 277
  • 278
    • 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 (2005) Cyanine dye N744 inhibits tau fibrillization by blocking filament extension: implications for the treatment of tauopathic neurodegenerative diseases. Biochemistry 44:10227-10237
    • (2005) Biochemistry , vol.44 , pp. 10227-10237
    • Necula, M.1    Chirita, C.N.2    Kuret, J.3
  • 280
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • Neve RL, Harris P, Kosik KS, Kurnit DM, Donlon TA (1986) Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res 387:271-280
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 281
    • 62549147038 scopus 로고    scopus 로고
    • The E693 D mutation in amyloid precursor protein increases intracellular accumulation of amyloid b oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells
    • Nishitsuji K, Tomiyama T, Ishibashi K, Ito K, Teraoka R, Lambert MP, Klein WL, Mori H (2009) The E693 D mutation in amyloid precursor protein increases intracellular accumulation of amyloid b oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 174:957-969
    • (2009) Am J Pathol , vol.174 , pp. 957-969
    • Nishitsuji, K.1    Tomiyama, T.2    Ishibashi, K.3    Ito, K.4    Teraoka, R.5    Lambert, M.P.6    Klein, W.L.7    Mori, H.8
  • 282
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by a-, b-and g-secretases
    • Nunan J, Small DH (2000) Regulation of APP cleavage by a-, b-and g-secretases. FEBS Lett 483:6-10
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 284
    • 70449629657 scopus 로고    scopus 로고
    • Cellular prion protein mediates the toxicity of b-amyloid oligomers: Implications for Alzheimer disease
    • Nygaard HB, Strittmatter SM (2009) Cellular prion protein mediates the toxicity of b-amyloid oligomers: implications for Alzheimer disease. Arch Neurol 66:1325-1328
    • (2009) Arch Neurol , vol.66 , pp. 1325-1328
    • Nygaard, H.B.1    Strittmatter, S.M.2
  • 286
    • 4043167747 scopus 로고    scopus 로고
    • A b 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 (2004) A b immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 43:321-332
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    Laferla, F.M.5
  • 287
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates b-amyloid-induced neurodegeneration
    • Park SY, Ferreira A (2005) The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates b-amyloid-induced neurodegeneration. J Neurosci 25:5365-5375
    • (2005) J Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 288
    • 0343831898 scopus 로고    scopus 로고
    • In vitro assembly of tau protein: Mapping the regions involved in filament formation
    • Perez M, Arrasate M, Montejo De Garcini E, Munoz V, Avila J (2001) In vitro assembly of tau protein: mapping the regions involved in filament formation. Biochemistry 40:5983-5991
    • (2001) Biochemistry , vol.40 , pp. 5983-5991
    • Perez, M.1    Arrasate, M.2    De Montejo Garcini, E.3    Munoz, V.4    Avila, J.5
  • 289
    • 0025992417 scopus 로고
    • In vitro aging of b-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike CJ, Walencewicz AJ, Glabe CG, Cotman CW (1991) In vitro aging of b-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res 563:311-314
    • (1991) Brain Res , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 292
    • 0022976136 scopus 로고
    • Filamentous aggregates in Pick's disease, progressive supranuclear palsy, and Alzheimer's disease share antigenic determinants with microtubule-associated protein, tau
    • Pollock NJ, Mirra SS, Binder LI, Hansen LA, Wood JG (1986) Filamentous aggregates in Pick's disease, progressive supranuclear palsy, and Alzheimer's disease share antigenic determinants with microtubule-associated protein, tau. Lancet 2:1211
    • (1986) Lancet , vol.2 , pp. 1211
    • Pollock, N.J.1    Mirra, S.S.2    Binder, L.I.3    Hansen, L.A.4    Wood, J.G.5
  • 293
    • 69449093036 scopus 로고    scopus 로고
    • Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology
    • Polydoro M, Acker CM, Duff K, Castillo PE, Davies P (2009) Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology. J Neurosci 29:10741-10749
    • (2009) J Neurosci , vol.29 , pp. 10741-10749
    • Polydoro, M.1    Acker, C.M.2    Duff, K.3    Castillo, P.E.4    Davies, P.5
  • 295
    • 0032989712 scopus 로고    scopus 로고
    • Tangles and plaques in nondemented aging and "preclinical" Alzheimer's disease
    • Price JL, Morris JC (1999) Tangles and plaques in nondemented aging and "preclinical" Alzheimer's disease. Ann Neurol 45:358-368
    • (1999) Ann Neurol , vol.45 , pp. 358-368
    • Price, J.L.1    Morris, J.C.2
  • 296
    • 67650556426 scopus 로고    scopus 로고
    • Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: Implications for the pathogenesis of Alzheimer disease
    • Quintanilla RA, Matthews-Roberson TA, Dolan PJ, Johnson GV (2009) Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease. J Biol Chem 284:18754-18766
    • (2009) J Biol Chem , vol.284 , pp. 18754-18766
    • Quintanilla, R.A.1    Matthews-Roberson, T.A.2    Dolan, P.J.3    Johnson, G.V.4
  • 297
    • 39749196738 scopus 로고    scopus 로고
    • Why is the amyloid b peptide of Alzheimer's disease neurotoxic?
    • Rauk A (2008) Why is the amyloid b peptide of Alzheimer's disease neurotoxic? Dalton Trans 1273-1282
    • (2008) Dalton Trans 1273-1282
    • Rauk, A.1
  • 298
    • 70350153272 scopus 로고    scopus 로고
    • The chemistry of Alzheimer's disease
    • Rauk A (2009) The chemistry of Alzheimer's disease. Chem Soc Rev 38:2698-2715
    • (2009) Chem Soc Rev , vol.38 , pp. 2698-2715
    • Rauk, A.1
  • 299
    • 0014167665 scopus 로고
    • Corticodentatonigral degeneration with neuronal achromasia: A progressive disorder of late adult life
    • Rebeiz JJ, Kolodny EH, Richardson EP Jr (1967) Corticodentatonigral degeneration with neuronal achromasia: A progressive disorder of late adult life. Trans Am Neurol Assoc 92:23-26
    • (1967) Trans Am Neurol Assoc , vol.92 , pp. 23-26
    • Rebeiz, J.J.1    Kolodny, E.H.2    Richardson, E.P.3
  • 300
    • 0014225976 scopus 로고
    • Corticodentatonigral degeneration with neuronal achromasia
    • Rebeiz JJ, Kolodny EH, Richardson EP Jr (1968) Corticodentatonigral degeneration with neuronal achromasia. Arch Neurol 18:20-33
    • (1968) Arch Neurol , vol.18 , pp. 20-33
    • Rebeiz, J.J.1    Kolodny, E.H.2    Richardson, E.P.3
  • 301
    • 17844378691 scopus 로고    scopus 로고
    • Differential loss of synaptic proteins in Alzheimer's disease: Implications for synaptic dysfunction
    • discussion 73-80
    • Reddy PH, Mani G, Park BS, Jacques J, Murdoch G, Whetsell W Jr, Kaye J, Manczak M (2005) Differential loss of synaptic proteins in Alzheimer's disease: implications for synaptic dysfunction. J Alzheimers Dis 7:103-117, discussion 73-80
    • (2005) J Alzheimers Dis , vol.7 , pp. 103-117
    • Reddy, P.H.1    Mani, G.2    Park, B.S.3    Jacques, J.4    Murdoch, G.5    Whetsell, W.6    Kaye, J.7    Manczak, M.8
  • 304
    • 13444287877 scopus 로고    scopus 로고
    • Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: Implications for Alzheimer's disease
    • Reynolds MR, Berry RW, Binder LI (2005) Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry 44:1690-1700
    • (2005) Biochemistry , vol.44 , pp. 1690-1700
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 306
    • 34250854596 scopus 로고    scopus 로고
    • Nitration in neurodegeneration: Deciphering the "Hows" "nYs"
    • Reynolds MR, Berry RW, Binder LI (2007) Nitration in neurodegeneration: deciphering the "Hows" "nYs". Biochemistry 46:7325-7336
    • (2007) Biochemistry , vol.46 , pp. 7325-7336
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 309
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • Robakis NK, Ramakrishna N, Wolfe G, Wisniewski HM (1987) Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides. Proc Natl Acad Sci USA 84:4190-4194
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 311
    • 80355142815 scopus 로고    scopus 로고
    • SDS-PAGE/immunoblot detection of A b multimers in human cortical tissue homogenates using antigen-epitope retrieval
    • pii: 1916
    • Rosen RF, Tomidokoro Y, Ghiso JA, Walker LC (2010) SDS-PAGE/immunoblot detection of A b multimers in human cortical tissue homogenates using antigen-epitope retrieval. J Vis Exp. 38, pii: 1916. doi:10.3791/1916
    • (2010) J Vis Exp , vol.38
    • Rosen, R.F.1    Tomidokoro, Y.2    Ghiso, J.A.3    Walker, L.C.4
  • 312
    • 44949259180 scopus 로고    scopus 로고
    • Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis
    • Rosenberg KJ, Ross JL, Feinstein HE, Feinstein SC, Israelachvili J (2008) Complementary dimerization of microtubule-associated tau protein: implications for microtubule bundling and tau-mediated pathogenesis. Proc Natl Acad Sci USA 105:7445-7450
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7445-7450
    • Rosenberg, K.J.1    Ross, J.L.2    Feinstein, H.E.3    Feinstein, S.C.4    Israelachvili, J.5
  • 315
    • 77950893260 scopus 로고    scopus 로고
    • Inhibition of AMPA receptor trafficking at hippocampal synapses by b-amyloid oligomers: The mitochondrial contribution
    • Rui Y, Gu J, Yu K, Hartzell HC, Zheng JQ (2010) Inhibition of AMPA receptor trafficking at hippocampal synapses by b-amyloid oligomers: the mitochondrial contribution. Mol Brain 3:10
    • (2010) Mol Brain , vol.3 , pp. 10
    • Rui, Y.1    Gu, J.2    Yu, K.3    Hartzell, H.C.4    Zheng, J.Q.5
  • 319
    • 20444428693 scopus 로고    scopus 로고
    • Effect of quinones on microtubule polymerization: A link between oxidative stress and cytoskeletal alterations in Alzheimer's disease
    • Santa-Maria I, Smith MA, Perry G, Hernandez F, Avila J, Moreno FJ (2005) Effect of quinones on microtubule polymerization: A link between oxidative stress and cytoskeletal alterations in Alzheimer's disease. Biochim Biophys Acta 1740:472-480
    • (2005) Biochim Biophys Acta , vol.1740 , pp. 472-480
    • Santa-Maria, I.1    Smith, M.A.2    Perry, G.3    Hernandez, F.4    Avila, J.5    Moreno, F.J.6
  • 320
    • 36348989570 scopus 로고    scopus 로고
    • Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-b-peptide aggregation
    • Santa-Maria I, Hernandez F, Moreno FJ, Avila J (2007) Taurine, an inducer for tau polymerization and a weak inhibitor for amyloid-b-peptide aggregation. Neurosci Lett 429:91-94
    • (2007) Neurosci Lett , vol.429 , pp. 91-94
    • Santa-Maria, I.1    Hernandez, F.2    Moreno, F.J.3    Avila, J.4
  • 322
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A, Biernat J, Von Bergen M, Mandelkow E, Mandelkow EM (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38:3549-3558
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 323
    • 0036098268 scopus 로고    scopus 로고
    • Cu(II)-catalyzed oxidation of b-amyloid peptide targets His13 and His14 over His6: Detection of 2-Oxo-histidine by HPLC-MS/MS
    • Schoneich C, Williams TD (2002) Cu(II)-catalyzed oxidation of b-amyloid peptide targets His13 and His14 over His6: detection of 2-Oxo-histidine by HPLC-MS/MS. Chem Res Toxicol 15:717-722
    • (2002) Chem Res Toxicol , vol.15 , pp. 717-722
    • Schoneich, C.1    Williams, T.D.2
  • 324
    • 0037119947 scopus 로고    scopus 로고
    • Single-molecule investigation of the interference between kinesin, tau and MAP2c
    • Seitz A, Kojima H, Oiwa K, Mandelkow EM, Song YH, Mandelkow E (2002) Single-molecule investigation of the interference between kinesin, tau and MAP2c. EMBO J 21:4896-4905
    • (2002) EMBO J , vol.21 , pp. 4896-4905
    • Seitz, A.1    Kojima, H.2    Oiwa, K.3    Mandelkow, E.M.4    Song, Y.H.5    Mandelkow, E.6
  • 325
    • 33644827036 scopus 로고    scopus 로고
    • Activation of N-methyl-D-aspartate receptor induces a shift of drebrin distribution: Disappearance from dendritic spines and appearance in dendritic shafts
    • Sekino Y, Tanaka S, Hanamura K, Yamazaki H, Sasagawa Y, Xue Y, Hayashi K, Shirao T (2006) Activation of N-methyl-D-aspartate receptor induces a shift of drebrin distribution: disappearance from dendritic spines and appearance in dendritic shafts. Mol Cell Neurosci 31:493-504
    • (2006) Mol Cell Neurosci , vol.31 , pp. 493-504
    • Sekino, Y.1    Tanaka, S.2    Hanamura, K.3    Yamazaki, H.4    Sasagawa, Y.5    Xue, Y.6    Hayashi, K.7    Shirao, T.8
  • 326
    • 0024314702 scopus 로고
    • Amyloid b protein precursor and the pathogenesis of Alzheimer's disease
    • Selkoe DJ (1989) Amyloid b protein precursor and the pathogenesis of Alzheimer's disease. Cell 58:611-612
    • (1989) Cell , vol.58 , pp. 611-612
    • Selkoe, D.J.1
  • 327
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • Selkoe DJ (1997) Alzheimer's disease: genotypes, phenotypes, and treatments. Science 275:630-631
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 328
    • 0030748399 scopus 로고    scopus 로고
    • Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases
    • Sergeant N, David JP, Lefranc D, Vermersch P, Wattez A, Delacourte A (1997) Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases. FEBS Lett 412:578-582
    • (1997) FEBS Lett , vol.412 , pp. 578-582
    • Sergeant, N.1    David, J.P.2    Lefranc, D.3    Vermersch, P.4    Wattez, A.5    Delacourte, A.6
  • 330
    • 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 (2007) Natural oligomers of the Alzheimer amyloid-b protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27:2866-2875
    • (2007) J Neurosci , vol.27 , 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
  • 332
    • 70349973683 scopus 로고    scopus 로고
    • Biochemical and immunohistochemical analysis of an Alzheimer's disease mouse model reveals the presence of multiple cerebral A b assembly forms throughout life
    • Shankar GM, Leissring MA, Adame A, Sun X, Spooner E, Masliah E, Selkoe DJ, Lemere CA, Walsh DM (2009) Biochemical and immunohistochemical analysis of an Alzheimer's disease mouse model reveals the presence of multiple cerebral A b assembly forms throughout life. Neurobiol Dis 36:293-302
    • (2009) Neurobiol Dis , vol.36 , pp. 293-302
    • Shankar, G.M.1    Leissring, M.A.2    Adame, A.3    Sun, X.4    Spooner, E.5    Masliah, E.6    Selkoe, D.J.7    Lemere, C.A.8    Walsh, D.M.9
  • 333
    • 34047166439 scopus 로고    scopus 로고
    • Tau impacts on growth-factor-stimulated actin remodeling
    • Sharma VM, Litersky JM, Bhaskar K, Lee G (2007) Tau impacts on growth-factor-stimulated actin remodeling. J Cell Sci 120:748-757
    • (2007) J Cell Sci , vol.120 , pp. 748-757
    • Sharma, V.M.1    Litersky, J.M.2    Bhaskar, K.3    Lee, G.4
  • 335
    • 0025786986 scopus 로고
    • Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and Alzheimer's disease brain tissues
    • Shin RW, Iwaki T, Kitamoto T, Tateishi J (1991) Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and Alzheimer's disease brain tissues. Lab Invest 64:693-702
    • (1991) Lab Invest , vol.64 , pp. 693-702
    • Shin, R.W.1    Iwaki, T.2    Kitamoto, T.3    Tateishi, J.4
  • 336
    • 34547147090 scopus 로고    scopus 로고
    • The redox chemistry of the Alzheimer's disease amyloid b peptide
    • Smith DG, Cappai R, Barnham KJ (2007) The redox chemistry of the Alzheimer's disease amyloid b peptide. Biochim Biophys Acta 1768:1976-1990
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1976-1990
    • Smith, D.G.1    Cappai, R.2    Barnham, K.J.3
  • 338
    • 33751516396 scopus 로고    scopus 로고
    • Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure
    • Sokolov Y, Kozak JA, Kayed R, Chanturiya A, Glabe C, Hall JE (2006) Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure. J Gen Physiol 128:637-647
    • (2006) J Gen Physiol , vol.128 , pp. 637-647
    • Sokolov, Y.1    Kozak, J.A.2    Kayed, R.3    Chanturiya, A.4    Glabe, C.5    Hall, J.E.6
  • 339
    • 61349164312 scopus 로고    scopus 로고
    • B Amyloid oligomers and fibrils stimulate differential activation of primary microglia
    • Sondag CM, Dhawan G, Combs CK (2009) b Amyloid oligomers and fibrils stimulate differential activation of primary microglia. J Neuroinflammation 6:1
    • (2009) J NeuroinflAmmation , vol.6 , pp. 1
    • Sondag, C.M.1    Dhawan, G.2    Combs, C.K.3
  • 340
    • 33646519920 scopus 로고    scopus 로고
    • Regionspecific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • Spires TL, Orne JD, Santacruz K, Pitstick R, Carlson GA, Ashe KH, Hyman BT (2006) Regionspecific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy. Am J Pathol 168:1598-1607
    • (2006) Am J Pathol , vol.168 , pp. 1598-1607
    • Spires, T.L.1    Orne, J.D.2    Santacruz, K.3    Pitstick, R.4    Carlson, G.A.5    Ashe, K.H.6    Hyman, B.T.7
  • 344
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K, Vogel R, Thies E, Mandelkow E, Mandelkow EM (2002) Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J Cell Biol 156:1051-1063
    • (2002) J Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 345
    • 75549116708 scopus 로고
    • Progressive supranuclear palsy. A heterogeneous degeneration involving the brain stem, basal ganglia and cerebellum with vertical gaze and pseudobulbar palsy, nuchal dystonia and dementia
    • Steele JC, Richardson JC, Olszewski J (1964) Progressive supranuclear palsy. A heterogeneous degeneration involving the brain stem, basal ganglia and cerebellum with vertical gaze and pseudobulbar palsy, nuchal dystonia and dementia. Arch Neurol 10:333-359
    • (1964) Arch Neurol , vol.10 , pp. 333-359
    • Steele, J.C.1    Richardson, J.C.2    Olszewski, J.3
  • 346
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff WH, Johnson GV (2005) Tau phosphorylation: physiological and pathological consequences. Biochim Biophys Acta 1739:280-297
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 347
    • 0030872413 scopus 로고    scopus 로고
    • Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease
    • Sze CI, Troncoso JC, Kawas C, Mouton P, Price DL, Martin LJ (1997) Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J Neuropathol Exp Neurol 56:933-944
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 933-944
    • Sze, C.I.1    Troncoso, J.C.2    Kawas, C.3    Mouton, P.4    Price, D.L.5    Martin, L.J.6
  • 349
  • 350
    • 33745228920 scopus 로고    scopus 로고
    • The various aggregation states of b-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression
    • Tamagno E, Bardini P, Guglielmotto M, Danni O, Tabaton M (2006) The various aggregation states of b-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression. Free Radic Biol Med 41:202-212
    • (2006) Free Radic Biol Med , vol.41 , pp. 202-212
    • Tamagno, E.1    Bardini, P.2    Guglielmotto, M.3    Danni, O.4    Tabaton, M.5
  • 352
    • 2342442848 scopus 로고    scopus 로고
    • The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid b-peptide from liposomes prepared from brain membrane-like lipids
    • Tashima Y, Oe R, Lee S, Sugihara G, Chambers EJ, Takahashi M, Yamada T (2004) The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid b-peptide from liposomes prepared from brain membrane-like lipids. J Biol Chem 279:17587-17595
    • (2004) J Biol Chem , vol.279 , pp. 17587-17595
    • Tashima, Y.1    Oe, R.2    Lee, S.3    Sugihara, G.4    Chambers, E.J.5    Takahashi, M.6    Yamada, T.7
  • 353
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP, Butters N, Deteresa R, Hill R, Hansen LA, Katzman R (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann Neurol 30:572-580
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 354
    • 33947307791 scopus 로고    scopus 로고
    • Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1
    • Thies E, Mandelkow EM (2007) Missorting of tau in neurons causes degeneration of synapses that can be rescued by the kinase MARK2/Par-1. J Neurosci 27:2896-2907
    • (2007) J Neurosci , vol.27 , pp. 2896-2907
    • Thies, E.1    Mandelkow, E.M.2
  • 357
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid b-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ (2006) Effects of secreted oligomers of amyloid b-protein on hippocampal synaptic plasticity: A potent role for trimers. J Physiol 572:477-492
    • (2006) J Physiol , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 358
    • 0028644131 scopus 로고
    • Phosphorylation of neuronal cytoskeletal proteins in Alzheimer's disease and Lewy body dementias
    • Trojanowski JQ, Lee VM (1994) Phosphorylation of neuronal cytoskeletal proteins in Alzheimer's disease and Lewy body dementias. Ann N Y Acad Sci 747:92-109
    • (1994) Ann N y Acad Sci , vol.747 , pp. 92-109
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 361
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A b (1-42) and A b (25-35)
    • Varadarajan S, Kanski J, Aksenova M, Lauderback C, Butterfield DA (2001) Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's A b (1-42) and A b (25-35). J Am Chem Soc 123:5625-5631
    • (2001) J Am Chem Soc , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    ButterfiEld, D.A.5
  • 363
    • 72849109858 scopus 로고    scopus 로고
    • NSAIDs prevent, but do not reverse, neuronal cell cycle reentry in a mouse model of Alzheimer disease
    • Varvel NH, Bhaskar K, Kounnas MZ, Wagner SL, Yang Y, Lamb BT, Herrup K (2009) NSAIDs prevent, but do not reverse, neuronal cell cycle reentry in a mouse model of Alzheimer disease. J Clin Invest 119:3692-3702
    • (2009) J Clin Invest , vol.119 , pp. 3692-3702
    • Varvel, N.H.1    Bhaskar, K.2    Kounnas, M.Z.3    Wagner, S.L.4    Yang, Y.5    Lamb, B.T.6    Herrup, K.7
  • 365
    • 23744482703 scopus 로고    scopus 로고
    • Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates
    • Vega IE, Cui L, Propst JA, Hutton ML, Lee G, Yen SH (2005) Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res Mol Brain Res 138:135-144
    • (2005) Brain Res Mol Brain Res , vol.138 , pp. 135-144
    • Vega, I.E.1    Cui, L.2    Propst, J.A.3    Hutton, M.L.4    Lee, G.5    Yen, S.H.6
  • 366
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid b-peptide in cell plasma membrane and implications for Alzheimer's disease
    • Verdier Y, Penke B (2004) Binding sites of amyloid b-peptide in cell plasma membrane and implications for Alzheimer's disease. Curr Protein Pept Sci 5:19-31
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 367
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid b-peptide interactions with neuronal and glial cell plasma membrane: Binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarandi M, Penke B (2004) Amyloid b-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J Pept Sci 10:229-248
    • (2004) J Pept Sci , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarandi, M.2    Penke, B.3
  • 369
  • 370
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ( 306 VQIVYK 311 ) forming b structure
    • Von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ( 306 VQIVYK 311 ) forming b structure. Proc Natl Acad Sci USA 97:5129-5134
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 371
    • 34248190279 scopus 로고    scopus 로고
    • A b oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ (2007) A b oligomers-a decade of discovery. J Neurochem 101:1172-1184
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 372
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid b-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB (1997) Amyloid b-protein fibrillogenesis. Detection of a protofibrillar intermediate. J Biol Chem 272:22364-22372
    • (1997) J Biol Chem , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 374
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid b-protein begins intracellularly in cells derived from human brain
    • Walsh DM, Tseng BP, Rydel RE, Podlisny MB, Selkoe DJ (2000) The oligomerization of amyloid b-protein begins intracellularly in cells derived from human brain. Biochemistry 39: 10831-10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 377
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble brain A b distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J, Dickson DW, Trojanowski JQ, Lee VM (1999) The levels of soluble versus insoluble brain A b distinguish Alzheimer's disease from normal and pathologic aging. Exp Neurol 158:328-337
    • (1999) Exp Neurol , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 378
    • 0034006944 scopus 로고    scopus 로고
    • B-Amyloid(1-42) binds to a 7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • Wang HY, Lee DH, D'andrea MR, Peterson PA, Shank RP, Reitz AB (2000) b-Amyloid(1-42) binds to a 7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J Biol Chem 275:5626-5632
    • (2000) J Biol Chem , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.2    D'Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 380
    • 0042357192 scopus 로고    scopus 로고
    • A 7 Nicotinic acetylcholine receptors mediate b-amyloid peptide-induced tau protein phosphorylation
    • Wang HY, Li W, Benedetti NJ, Lee DH (2003) a 7 Nicotinic acetylcholine receptors mediate b-amyloid peptide-induced tau protein phosphorylation. J Biol Chem 278:31547-31553
    • (2003) J Biol Chem , vol.278 , pp. 31547-31553
    • Wang, H.Y.1    Li, W.2    Benedetti, N.J.3    Lee, D.H.4
  • 381
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid b-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogenactivated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q, Walsh DM, Rowan MJ, Selkoe DJ, Anwyl R (2004) Block of long-term potentiation by naturally secreted and synthetic amyloid b-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogenactivated protein kinase as well as metabotropic glutamate receptor type 5. J Neurosci 24:3370-3378
    • (2004) J Neurosci , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 382
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
    • Wang JZ, Grundke-Iqbal I, Iqbal K (2007a) Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur J Neurosci 25:59-68
    • (2007) Eur J Neurosci , vol.25 , pp. 59-68
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 383
    • 34547203592 scopus 로고    scopus 로고
    • Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model
    • Wang YP, Biernat J, Pickhardt M, Mandelkow E, Mandelkow EM (2007b) Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model. Proc Natl Acad Sci U S A 104:10252-10257
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10252-10257
    • Wang, Y.P.1    Biernat, J.2    Pickhardt, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 385
    • 76549123596 scopus 로고    scopus 로고
    • Amyloid-b-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons
    • Wang X, Perry G, Smith MA, Zhu X (2010) Amyloid-b-derived diffusible ligands cause impaired axonal transport of mitochondria in neurons. Neurodegener Dis 7:56-59
    • (2010) Neurodegener Dis , vol.7 , pp. 56-59
    • Wang, X.1    Perry, G.2    Smith, M.A.3    Zhu, X.4
  • 386
    • 4544300178 scopus 로고    scopus 로고
    • Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo
    • Watanabe A, Hong WK, Dohmae N, Takio K, Morishima-Kawashima M, Ihara Y (2004) Molecular aging of tau: disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. J Neurochem 90:1302-1311
    • (2004) J Neurochem , vol.90 , pp. 1302-1311
    • Watanabe, A.1    Hong, W.K.2    Dohmae, N.3    Takio, K.4    Morishima-Kawashima, M.5    Ihara, Y.6
  • 387
    • 49749097123 scopus 로고    scopus 로고
    • Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation
    • Wei Y, Qu MH, Wang XS, Chen L, Wang DL, Liu Y, Hua Q, He RQ (2008) Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation. PLoS One 3:e2600
    • (2008) PLoS One , vol.3 , pp. e2600
    • Wei, Y.1    Qu, M.H.2    Wang, X.S.3    Chen, L.4    Wang, D.L.5    Liu, Y.6    Hua, Q.7    He, R.Q.8
  • 388
    • 77950276918 scopus 로고    scopus 로고
    • Structural diversity of dimers of the Alzheimer amyloid-b (25-35) peptide and polymorphism of the resulting fibrils
    • Wei G, Jewett AI, Shea JE (2010) Structural diversity of dimers of the Alzheimer amyloid-b (25-35) peptide and polymorphism of the resulting fibrils. Phys Chem Chem Phys 12:3622-3629
    • (2010) Phys Chem Chem Phys , vol.12 , pp. 3622-3629
    • Wei, G.1    Jewett, A.I.2    Shea, J.E.3
  • 390
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid b-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • Whalen BM, Selkoe DJ, Hartley DM (2005) Small non-fibrillar assemblies of amyloid b-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiol Dis 20:254-266
    • (2005) Neurobiol Dis , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 394
    • 18944407388 scopus 로고    scopus 로고
    • Nucleationdependent polymerization is an essential component of amyloid-mediated neuronal cell death
    • Wogulis M, Wright S, Cunningham D, Chilcote T, Powell K, Rydel RE (2005) Nucleationdependent polymerization is an essential component of amyloid-mediated neuronal cell death. J Neurosci 25:1071-1080
    • (2005) J Neurosci , vol.25 , pp. 1071-1080
    • Wogulis, M.1    Wright, S.2    Cunningham, D.3    Chilcote, T.4    Powell, K.5    Rydel, R.E.6
  • 395
  • 396
    • 0021113184 scopus 로고
    • Molecular flexibility in microtubule proteins: Proton nuclear magnetic resonance characterization
    • Woody RW, Clark DC, Roberts GC, Martin SR, Bayley PM (1983) Molecular flexibility in microtubule proteins: proton nuclear magnetic resonance characterization. Biochemistry 22:2186-2192
    • (1983) Biochemistry , vol.22 , pp. 2186-2192
    • Woody, R.W.1    Clark, D.C.2    Roberts, G.C.3    Martin, S.R.4    Bayley, P.M.5
  • 397
    • 24744463641 scopus 로고    scopus 로고
    • Apoptotic signals within the basal forebrain cholinergic neurons in Alzheimer's disease
    • Wu CK, Thal L, Pizzo D, Hansen L, Masliah E, Geula C (2005) Apoptotic signals within the basal forebrain cholinergic neurons in Alzheimer's disease. Exp Neurol 195:484-496
    • (2005) Exp Neurol , vol.195 , pp. 484-496
    • Wu, C.K.1    Thal, L.2    Pizzo, D.3    Hansen, L.4    Masliah, E.5    Geula, C.6
  • 398
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid b-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia W, Zhang J, Kholodenko D, Citron M, Podlisny MB, Teplow DB, Haass C, Seubert P, Koo EH, Selkoe DJ (1997) Enhanced production and oligomerization of the 42-residue amyloid b-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J Biol Chem 272:7977-7982
    • (1997) J Biol Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haass, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 399
    • 60549107033 scopus 로고    scopus 로고
    • A specific enzymelinked immunosorbent assay for measuring b-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease
    • Xia W, Yang T, Shankar G, Smith IM, Shen Y, Walsh DM, Selkoe DJ (2009) A specific enzymelinked immunosorbent assay for measuring b-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease. Arch Neurol 66:190-199
    • (2009) Arch Neurol , vol.66 , pp. 190-199
    • Xia, W.1    Yang, T.2    Shankar, G.3    Smith, I.M.4    Shen, Y.5    Walsh, D.M.6    Selkoe, D.J.7
  • 403
    • 0344241479 scopus 로고    scopus 로고
    • Neuronal cell death is preceded by cell cycle events at all stages of Alzheimer's disease
    • Yang Y, Mufson EJ, Herrup K (2003) Neuronal cell death is preceded by cell cycle events at all stages of Alzheimer's disease. J Neurosci 23:2557-2563
    • (2003) J Neurosci , vol.23 , pp. 2557-2563
    • Yang, Y.1    Mufson, E.J.2    Herrup, K.3
  • 404
    • 32544459388 scopus 로고    scopus 로고
    • Ectopic cell cycle events link human Alzheimer's disease and amyloid precursor protein transgenic mouse models
    • Yang Y, Varvel NH, Lamb BT, Herrup K (2006) Ectopic cell cycle events link human Alzheimer's disease and amyloid precursor protein transgenic mouse models. J Neurosci 26:775-784
    • (2006) J Neurosci , vol.26 , pp. 775-784
    • Yang, Y.1    Varvel, N.H.2    Lamb, B.T.3    Herrup, K.4
  • 405
    • 3543060658 scopus 로고    scopus 로고
    • Amyloid b-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-D-aspartate (NMDA) versus non-NMDA receptor/channel activation
    • Ye C, Walsh DM, Selkoe DJ, Hartley DM (2004) Amyloid b-protein induced electrophysiological changes are dependent on aggregation state: N-methyl-D-aspartate (NMDA) versus non-NMDA receptor/channel activation. Neurosci Lett 366:320-325
    • (2004) Neurosci Lett , vol.366 , pp. 320-325
    • Ye, C.1    Walsh, D.M.2    Selkoe, D.J.3    Hartley, D.M.4
  • 406
    • 0032704956 scopus 로고    scopus 로고
    • FTDP-17 tau mutations decrease the susceptibility of tau to calpain i digestion
    • Yen S, Easson C, Nacharaju P, Hutton M, Yen SH (1999) FTDP-17 tau mutations decrease the susceptibility of tau to calpain I digestion. FEBS Lett 461:91-95
    • (1999) FEBS Lett , vol.461 , pp. 91-95
    • Yen, S.1    Easson, C.2    Nacharaju, P.3    Hutton, M.4    Yen, S.H.5
  • 407
    • 29344434456 scopus 로고    scopus 로고
    • C-terminal truncation modulates both nucleation and extension phases of tau fibrillization
    • Yin H, Kuret J (2006) C-terminal truncation modulates both nucleation and extension phases of tau fibrillization. FEBS Lett 580:211-215
    • (2006) FEBS Lett , vol.580 , pp. 211-215
    • Yin, H.1    Kuret, J.2
  • 409
    • 17644393495 scopus 로고    scopus 로고
    • Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity
    • Zhang YJ, Xu YF, Chen XQ, Wang XC, Wang JZ (2005) Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity. FEBS Lett 579:2421-2427
    • (2005) FEBS Lett , vol.579 , pp. 2421-2427
    • Zhang, Y.J.1    Xu, Y.F.2    Chen, X.Q.3    Wang, X.C.4    Wang, J.Z.5
  • 412
    • 3042546220 scopus 로고    scopus 로고
    • Reversal and consolidation of activity-induced synaptic modifications
    • Zhou Q, Poo MM (2004) Reversal and consolidation of activity-induced synaptic modifications. Trends Neurosci 27:378-383
    • (2004) Trends Neurosci , vol.27 , pp. 378-383
    • Zhou, Q.1    Poo, M.M.2


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