메뉴 건너뛰기




Volumn 7, Issue 9, 2012, Pages

Model Hirano Bodies Protect against Tau-Independent and Tau-Dependent Cell Death Initiated by the Amyloid Precursor Protein Intracellular Domain

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN C31 FRAGMENT; AMYLOID PRECURSOR PROTEIN INTRACELLULAR DOMAIN C58; CELL PROTEIN; F ACTIN; PROTEIN FE65; PROTEIN P53; PROTEIN TIP60; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 84866508857     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044996     Document Type: Article
Times cited : (17)

References (98)
  • 1
    • 31544481443 scopus 로고    scopus 로고
    • Neuropathology of Alzheimer's disease
    • Mott RT, Hulette CM, (2005) Neuropathology of Alzheimer's disease. Neuroimaging Clin N Am 215: 755-765.
    • (2005) Neuroimaging Clin N Am , vol.215 , pp. 755-765
    • Mott, R.T.1    Hulette, C.M.2
  • 2
    • 0017642031 scopus 로고
    • Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer's disease
    • Gibson PH, Tomlinson BE, (1977) Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer's disease. J Neurol Sci 33: 199-206.
    • (1977) J Neurol Sci , vol.33 , pp. 199-206
    • Gibson, P.H.1    Tomlinson, B.E.2
  • 3
    • 0014351211 scopus 로고
    • Fine structure of the Pick and Hirano bodies in a case of Pick's disease
    • Schochet SS Jr, Lampert PW, Lindenberg R, (1968) Fine structure of the Pick and Hirano bodies in a case of Pick's disease. Acta Neuropathol (Berl) 11: 330-337.
    • (1968) Acta Neuropathol (Berl) , vol.11 , pp. 330-337
    • Schochet Jr., S.S.1    Lampert, P.W.2    Lindenberg, R.3
  • 4
    • 0022257309 scopus 로고
    • Hirano bodies in the perikaryon of the Purkinje cell in a case of Alzheimer's disease
    • Yamamoto T, Hirano A, (1985) Hirano bodies in the perikaryon of the Purkinje cell in a case of Alzheimer's disease. Acta Neuropathol 67: 167-169.
    • (1985) Acta Neuropathol , vol.67 , pp. 167-169
    • Yamamoto, T.1    Hirano, A.2
  • 5
    • 0028286860 scopus 로고
    • Hirano bodies and related neuronal inclusions
    • Hirano A, (1994) Hirano bodies and related neuronal inclusions. Neuropathol Appl Neurobiol 20: 3-11.
    • (1994) Neuropathol Appl Neurobiol , vol.20 , pp. 3-11
    • Hirano, A.1
  • 7
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, et al. (1999) Protofibrillar intermediates of amyloid beta-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
  • 8
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5
  • 9
    • 0036489445 scopus 로고    scopus 로고
    • The relationship between Abeta and memory in the Tg2576 mouse model of Alzheimer's disease
    • Westerman MA, Cooper-Blacketer D, Mariash A, Kotilinek L, Kawarabayashi T, et al. (2002) The relationship between Abeta and memory in the Tg2576 mouse model of Alzheimer's disease. J Neurosci 22: 1858-1867.
    • (2002) J Neurosci , vol.22 , pp. 1858-1867
    • Westerman, M.A.1    Cooper-Blacketer, D.2    Mariash, A.3    Kotilinek, L.4    Kawarabayashi, T.5
  • 10
    • 45549087725 scopus 로고    scopus 로고
    • Place cell firing correlates with memory deficits and amyloid plaque burden in Tg2576 Alzheimer mouse model
    • Cacucci F, Yi M, Wills TJ, Chapman P, O'Keefe J, (2008) Place cell firing correlates with memory deficits and amyloid plaque burden in Tg2576 Alzheimer mouse model. Proc Natl Acad Sci U S A 105: 7863-7868.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 7863-7868
    • Cacucci, F.1    Yi, M.2    Wills, T.J.3    Chapman, P.4    O'Keefe, J.5
  • 11
    • 60349125886 scopus 로고    scopus 로고
    • Reassessing the amyloid cascade hypothesis of Alzheimer's disease
    • Pimplikar SW, (2009) Reassessing the amyloid cascade hypothesis of Alzheimer's disease. Int J Biochem Cell Biol 41: 1261-1268.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1261-1268
    • Pimplikar, S.W.1
  • 12
    • 79955128215 scopus 로고    scopus 로고
    • Biology and pathophysiology of the amyloid precursor protein
    • Zheng H, Koo EH, (2011) Biology and pathophysiology of the amyloid precursor protein. Mol Neurodegener 6: 27.
    • (2011) Mol Neurodegener , vol.6 , pp. 27
    • Zheng, H.1    Koo, E.H.2
  • 13
    • 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
  • 16
    • 84857642949 scopus 로고    scopus 로고
    • The toxic aß oliogmer and Alzheimer's disease: an emperor in need of clothes
    • Benilova I, Karran E, De Strooper B, (2012) The toxic aß oliogmer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 15: 349-357.
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 17
    • 0023987430 scopus 로고
    • Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease
    • Dyrks T, Weidemann A, Multhaup G, Salbaum JM, Lemaire HG, et al. (1988) Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease. EMBO J 7: 949-957.
    • (1988) EMBO J , vol.7 , pp. 949-957
    • Dyrks, T.1    Weidemann, A.2    Multhaup, G.3    Salbaum, J.M.4    Lemaire, H.G.5
  • 18
    • 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
  • 19
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A, Salbaum JM, Masters CL, et al. (1987) The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325: 733-736.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5
  • 20
    • 33749177143 scopus 로고    scopus 로고
    • A hundred years of Alzheimer's disease research
    • Hardy J, (2006) A hundred years of Alzheimer's disease research. Neuron 52: 3-13.
    • (2006) Neuron , vol.52 , pp. 3-13
    • Hardy, J.1
  • 21
    • 48349085043 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease
    • Muller T, Meyer HE, Egensperger R, Marcus K, (2008) The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease. Prog Neurobiol 85: 393-406.
    • (2008) Prog Neurobiol , vol.85 , pp. 393-406
    • Muller, T.1    Meyer, H.E.2    Egensperger, R.3    Marcus, K.4
  • 22
    • 83555176204 scopus 로고    scopus 로고
    • Nuclear signalling by membrane protein intracellular domains: The AICD enigma
    • Beckett C, Nalivaeva NN, Belyaev ND, Turner AJ, (2012) Nuclear signalling by membrane protein intracellular domains: The AICD enigma. Cell Signal 24: 402-409.
    • (2012) Cell Signal , vol.24 , pp. 402-409
    • Beckett, C.1    Nalivaeva, N.N.2    Belyaev, N.D.3    Turner, A.J.4
  • 23
    • 84655166492 scopus 로고    scopus 로고
    • The physiology of the ß-amyloid precursor protein intracellular domain AICD
    • Pardossi-Piquard R, Checler F, (2012) The physiology of the ß-amyloid precursor protein intracellular domain AICD. J Neurochem 120(Suppl. 1): 109-124.
    • (2012) J Neurochem , vol.120 , pp. 109-124
    • Pardossi-Piquard, R.1    Checler, F.2
  • 24
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ, (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 83: 4044-4048.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 25
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, et al. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261: 6084-6089.
    • (1986) J Biol Chem , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4    Zaidi, M.S.5
  • 26
    • 72049099376 scopus 로고    scopus 로고
    • Clinical, pathological, and genetic characteristics of frontotemporal dementia and parkinsonism linked to chromosome 17 with mutations in the MAPT and PGRN
    • Tsuboi Y, (2009) Clinical, pathological, and genetic characteristics of frontotemporal dementia and parkinsonism linked to chromosome 17 with mutations in the MAPT and PGRN. Brain Nerve 61: 1285-1291.
    • (2009) Brain Nerve , vol.61 , pp. 1285-1291
    • Tsuboi, Y.1
  • 27
    • 84862833600 scopus 로고    scopus 로고
    • Tau in Alzheimer Disease and related tauopathies
    • C.-X G
    • Iqbal K, Liu F, C.-X G, Grundke-Iqbal I, (2010) Tau in Alzheimer Disease and related tauopathies. Curr Alzheimer Res 7: 656-664.
    • (2010) Curr Alzheimer Res , vol.7 , pp. 656-664
    • Iqbal, K.1    Liu, F.2    Grundke-Iqbal, I.3
  • 28
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, et al. (2007) Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 316: 750-754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5
  • 29
    • 77957737750 scopus 로고    scopus 로고
    • Tau reduction prevents Abeta-induced defects in axonal transport
    • Vossel KA, Zhang K, Brodbeck J, Daub AC, Sharma P, et al. (2010) Tau reduction prevents Abeta-induced defects in axonal transport. Science 330: 198-200.
    • (2010) Science , vol.330 , pp. 198-200
    • Vossel, K.A.1    Zhang, K.2    Brodbeck, J.3    Daub, A.C.4    Sharma, P.5
  • 30
    • 79951818085 scopus 로고    scopus 로고
    • Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic tau mutant
    • Sydow A, Van der Jeugd A, Zheng F, Ahmed T, Balschun D, et al. (2011) Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic tau mutant. J Neurosci 31: 2511-2525.
    • (2011) J Neurosci , vol.31 , pp. 2511-2525
    • Sydow, A.1    van der Jeugd, A.2    Zheng, F.3    Ahmed, T.4    Balschun, D.5
  • 31
    • 0015271474 scopus 로고
    • A study of rod-like structures (Hirano bodies) in 240 normal and pathological brains
    • Ogata J, Budzilovich GN, Cravioto H, (1972) A study of rod-like structures (Hirano bodies) in 240 normal and pathological brains. Acta Neuropathol 21: 61-67.
    • (1972) Acta Neuropathol , vol.21 , pp. 61-67
    • Ogata, J.1    Budzilovich, G.N.2    Cravioto, H.3
  • 32
    • 0016805913 scopus 로고
    • Unusual, rod-shaped cytoplasmic inclusions (Hirano bodies) in a cerebellar hemangioblastoma
    • Fu Y, Ward J, Young HF, (1975) Unusual, rod-shaped cytoplasmic inclusions (Hirano bodies) in a cerebellar hemangioblastoma. Acta Neuropathol 31: 129-135.
    • (1975) Acta Neuropathol , vol.31 , pp. 129-135
    • Fu, Y.1    Ward, J.2    Young, H.F.3
  • 33
    • 0022448777 scopus 로고
    • The structure analysis of Hirano bodies by digital processing on electron micrographs
    • Mori H, Tomonaga M, Baba N, Kanaya K, (1986) The structure analysis of Hirano bodies by digital processing on electron micrographs. Acta Neuropathol 71: 32-37.
    • (1986) Acta Neuropathol , vol.71 , pp. 32-37
    • Mori, H.1    Tomonaga, M.2    Baba, N.3    Kanaya, K.4
  • 36
    • 0028286861 scopus 로고
    • Hirano bodies and chronic alcoholism
    • Laas R, Hagel C, (1994) Hirano bodies and chronic alcoholism. Neuropathol Appl Neurobiol 20: 12-21.
    • (1994) Neuropathol Appl Neurobiol , vol.20 , pp. 12-21
    • Laas, R.1    Hagel, C.2
  • 38
    • 0023132179 scopus 로고
    • Hirano body filaments contain actin and actin-associated proteins
    • Galloway PG, Perry G, Gambetti P, (1987) Hirano body filaments contain actin and actin-associated proteins. J Neuropathol Exp Neurol 46: 185-199.
    • (1987) J Neuropathol Exp Neurol , vol.46 , pp. 185-199
    • Galloway, P.G.1    Perry, G.2    Gambetti, P.3
  • 39
    • 0020540685 scopus 로고
    • The association of actin with Hirano bodies
    • Goldman JE, (1983) The association of actin with Hirano bodies. J Neuropathol Exp Neurol 42: 146-152.
    • (1983) J Neuropathol Exp Neurol , vol.42 , pp. 146-152
    • Goldman, J.E.1
  • 41
    • 0026022118 scopus 로고
    • Elucidation of three-dimensional ultrastructure of Hirano bodies by the quick-freeze, deep-etch and replica method
    • Izumiyama N, Ohtsubo K, Tachikawa T, Nakamura H, (1991) Elucidation of three-dimensional ultrastructure of Hirano bodies by the quick-freeze, deep-etch and replica method. Acta Neuropathol 81: 248-254.
    • (1991) Acta Neuropathol , vol.81 , pp. 248-254
    • Izumiyama, N.1    Ohtsubo, K.2    Tachikawa, T.3    Nakamura, H.4
  • 42
    • 0036573221 scopus 로고    scopus 로고
    • Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin cross-linking protein
    • Maselli AG, Davis R, Furukawa R, Fechheimer M, (2002) Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin cross-linking protein. J Cell Sci 115: 1939-1952.
    • (2002) J Cell Sci , vol.115 , pp. 1939-1952
    • Maselli, A.G.1    Davis, R.2    Furukawa, R.3    Fechheimer, M.4
  • 43
    • 38349002996 scopus 로고    scopus 로고
    • A cell culture model for investigation of Hirano bodies
    • Davis RC, Furukawa R, Fechheimer M, (2008) A cell culture model for investigation of Hirano bodies. Acta Neuropathol 115: 205-217.
    • (2008) Acta Neuropathol , vol.115 , pp. 205-217
    • Davis, R.C.1    Furukawa, R.2    Fechheimer, M.3
  • 45
    • 0027498295 scopus 로고
    • Hirano bodies accumulate C-terminal sequences of beta-amyloid precursor protein (beta-APP) epitopes
    • Munoz DG, Wang D, Greenberg BD, (1993) Hirano bodies accumulate C-terminal sequences of beta-amyloid precursor protein (beta-APP) epitopes. J Neuropathol Exp Neurol 52: 14-21.
    • (1993) J Neuropathol Exp Neurol , vol.52 , pp. 14-21
    • Munoz, D.G.1    Wang, D.2    Greenberg, B.D.3
  • 46
    • 0042232060 scopus 로고    scopus 로고
    • Formation of Hirano bodies induced by expression of an actin cross-linking protein with a gain of function mutation
    • Maselli AG, Furukawa R, Thomson SAM, Davis RC, Fechheimer M, (2003) Formation of Hirano bodies induced by expression of an actin cross-linking protein with a gain of function mutation. Eucaryot Cell 2: 778-787.
    • (2003) Eucaryot Cell , vol.2 , pp. 778-787
    • Maselli, A.G.1    Furukawa, R.2    Thomson, S.A.M.3    Davis, R.C.4    Fechheimer, M.5
  • 47
    • 80053654938 scopus 로고    scopus 로고
    • Association of AICD and Fe65 with Hirano bodies reduces transcriptional activation and initiation of apoptosis
    • Ha S, Furukawa R, Fechheimer M, (2011) Association of AICD and Fe65 with Hirano bodies reduces transcriptional activation and initiation of apoptosis. Neurobiol Aging 32: 2287-2298.
    • (2011) Neurobiol Aging , vol.32 , pp. 2287-2298
    • Ha, S.1    Furukawa, R.2    Fechheimer, M.3
  • 48
    • 0142179222 scopus 로고    scopus 로고
    • Caspase cleavage of the amyloid precursor protein modulates amyloid beta-protein toxicity
    • Lu DC, Soriano S, Bredesen DE, Koo EH, (2003) Caspase cleavage of the amyloid precursor protein modulates amyloid beta-protein toxicity. J Neurochem 87: 733-741.
    • (2003) J Neurochem , vol.87 , pp. 733-741
    • Lu, D.C.1    Soriano, S.2    Bredesen, D.E.3    Koo, E.H.4
  • 49
    • 20844450734 scopus 로고    scopus 로고
    • Development of a high throughput drug screening assay for the detection of changes in tau levels - proof of concept with HSP90 inhibitors
    • Dickey CA, Eriksen J, Kamal A, Burrows F, Kasibhatla S, et al. (2005) Development of a high throughput drug screening assay for the detection of changes in tau levels - proof of concept with HSP90 inhibitors. Curr Alzheimer Res 2: 231-238.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 231-238
    • Dickey, C.A.1    Eriksen, J.2    Kamal, A.3    Burrows, F.4    Kasibhatla, S.5
  • 50
    • 62849084327 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of tau mutants reveals specific phosphorylation pattern likely linked to early tau conformational changes
    • Bretteville A, Ando K, Ghestem A, Loyens A, Begard S, et al. (2009) Two-dimensional electrophoresis of tau mutants reveals specific phosphorylation pattern likely linked to early tau conformational changes. PLoS One 4: e4843.
    • (2009) PLoS One , vol.4
    • Bretteville, A.1    Ando, K.2    Ghestem, A.3    Loyens, A.4    Begard, S.5
  • 51
    • 0018143832 scopus 로고
    • Light and electron microscopic observations on the relationship between Hirano bodies, neuron and glial perikarya in the human hippocampus
    • Gibson PH, (1978) Light and electron microscopic observations on the relationship between Hirano bodies, neuron and glial perikarya in the human hippocampus. Acta Neuropathol (Berl) 42: 165-171.
    • (1978) Acta Neuropathol (Berl) , vol.42 , pp. 165-171
    • Gibson, P.H.1
  • 52
    • 79959945013 scopus 로고    scopus 로고
    • Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture
    • Garwood CJ, Pooler AM, Atherton J, Hanger DP, Noble W, (2011) Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture. Cell Death Dis 2: e167.
    • (2011) Cell Death Dis , vol.2
    • Garwood, C.J.1    Pooler, A.M.2    Atherton, J.3    Hanger, D.P.4    Noble, W.5
  • 53
    • 0037047434 scopus 로고    scopus 로고
    • The gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells
    • Kinoshita A, Whelan CM, Berezovska O, Hyman BT, (2002) The gamma secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells. J Biol Chem 277: 28530-28536.
    • (2002) J Biol Chem , vol.277 , pp. 28530-28536
    • Kinoshita, A.1    Whelan, C.M.2    Berezovska, O.3    Hyman, B.T.4
  • 54
    • 0037111833 scopus 로고    scopus 로고
    • Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease
    • Fath T, Eldenmüller J, Brandt R, (2002) Tau-mediated cytotoxicity in a pseudohyperphosphorylation model of Alzheimer's disease. J Neurosci 22: 9733-9741.
    • (2002) J Neurosci , vol.22 , pp. 9733-9741
    • Fath, T.1    Eldenmüller, J.2    Brandt, R.3
  • 55
    • 0035425347 scopus 로고    scopus 로고
    • Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein
    • Eidenmüller J, Fath T, Maas T, Pool M, Sontag E, et al. (2001) Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein. Biochem J 357: 759-767.
    • (2001) Biochem J , vol.357 , pp. 759-767
    • Eidenmüller, J.1    Fath, T.2    Maas, T.3    Pool, M.4    Sontag, E.5
  • 56
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation
    • Cao X, Südhof TC, (2004) Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation. J Biol Chem 279: 24601-14611.
    • (2004) J Biol Chem , vol.279 , pp. 14611-24601
    • Cao, X.1    Südhof, T.C.2
  • 57
    • 33745632662 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease
    • Alves da Costa C, Sunyach C, Pardossi-Piquard R, Sevalle J, Vincent B, et al. (2006) Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease. J Neurosci 26: 6377-6385.
    • (2006) J Neurosci , vol.26 , pp. 6377-6385
    • Alves da Costa, C.1    Sunyach, C.2    Pardossi-Piquard, R.3    Sevalle, J.4    Vincent, B.5
  • 58
    • 33845668241 scopus 로고    scopus 로고
    • Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis
    • Tang Y, Luo J, Zhang W, Gu W, (2006) Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. Mol Cell 24: 827-839.
    • (2006) Mol Cell , vol.24 , pp. 827-839
    • Tang, Y.1    Luo, J.2    Zhang, W.3    Gu, W.4
  • 59
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, et al. (2006) Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol Cell 24: 841-851.
    • (2006) Mol Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Marmorstein, R.5
  • 60
    • 67749103995 scopus 로고    scopus 로고
    • Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53
    • Sykes SM, Stanek TJ, Frank A, Murphy ME, McMahon SB, (2009) Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53. J Biol Chem 284: 20197-20205.
    • (2009) J Biol Chem , vol.284 , pp. 20197-20205
    • Sykes, S.M.1    Stanek, T.J.2    Frank, A.3    Murphy, M.E.4    McMahon, S.B.5
  • 61
    • 0033543728 scopus 로고    scopus 로고
    • A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy
    • Komarov PG, Komarova EA, Kondratov RV, Christov-Tselkov K, Coon JS, et al. (1999) A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Science 285: 1733-1737.
    • (1999) Science , vol.285 , pp. 1733-1737
    • Komarov, P.G.1    Komarova, E.A.2    Kondratov, R.V.3    Christov-Tselkov, K.4    Coon, J.S.5
  • 62
    • 82955220477 scopus 로고    scopus 로고
    • Alzheimer's disease: Pathological mechanisms and recent insights
    • Niedowicz DM, Nelson PT, Murphy MP, (2011) Alzheimer's disease: Pathological mechanisms and recent insights. Curr Neuropharm 9: 674-684.
    • (2011) Curr Neuropharm , vol.9 , pp. 674-684
    • Niedowicz, D.M.1    Nelson, P.T.2    Murphy, M.P.3
  • 63
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics
    • Karran E, Mercken M, De Strooper B, (2011) The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov 10: 698-712.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 64
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly WT, Zheng JB, Guenette SY, Selkoe DJ, (2001) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 276: 40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 65
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurons in culture
    • Cupers P, Orlans I, Craessarts K, Annaert W, De Strooper B, (2001) The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurons in culture. J Neurochem 78: 1168-1178.
    • (2001) J Neurochem , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessarts, K.3    Annaert, W.4    De Strooper, B.5
  • 66
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann A, Eggert S, Reinhard FBM, Vogel M, Paliga K, et al. (2002) A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41: 2825-2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.M.3    Vogel, M.4    Paliga, K.5
  • 67
    • 36849084471 scopus 로고    scopus 로고
    • Amyloid ß-protein precursor juxtamembrain domain regulates specificty of γ-secretase-dependent cleavages
    • Ren Z, Schenk D, Basi GS, Shapiro IP, (2007) Amyloid ß-protein precursor juxtamembrain domain regulates specificty of γ-secretase-dependent cleavages. J Biol Chem 48: 35350-33560.
    • (2007) J Biol Chem , vol.48 , pp. 33560-35350
    • Ren, Z.1    Schenk, D.2    Basi, G.S.3    Shapiro, I.P.4
  • 68
    • 33645559774 scopus 로고    scopus 로고
    • The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase
    • Yamasaki A, Eimer S, Okochi M, Smialowska A, Kaether C, et al. (2006) The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase. J Neurosci 26: 3821-3828.
    • (2006) J Neurosci , vol.26 , pp. 3821-3828
    • Yamasaki, A.1    Eimer, S.2    Okochi, M.3    Smialowska, A.4    Kaether, C.5
  • 69
    • 84655160766 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's ß-amyloid precursor protein
    • Zhang H, Ma Q, Zhang Y-w, Xu H, (2012) Proteolytic processing of the Alzheimer's ß-amyloid precursor protein. J Neurochen 120: 9-21.
    • (2012) J Neurochen , vol.120 , pp. 9-21
    • Zhang, H.1    Ma, Q.2    Zhang, Y.-w.3    Xu, H.4
  • 70
    • 75649135280 scopus 로고    scopus 로고
    • Neuropathology of Alzheimer's disease
    • Perl DP, (2010) Neuropathology of Alzheimer's disease. Mt Sinai J Med 77: 32-42.
    • (2010) Mt Sinai J Med , vol.77 , pp. 32-42
    • Perl, D.P.1
  • 72
    • 0034488295 scopus 로고    scopus 로고
    • Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor
    • Passer B, Pellegrini L, Russo C, Siegel RM, Lenardo MJ, et al. (2000) Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor. J Alzheimers Dis 2: 289-301.
    • (2000) J Alzheimers Dis , vol.2 , pp. 289-301
    • Passer, B.1    Pellegrini, L.2    Russo, C.3    Siegel, R.M.4    Lenardo, M.J.5
  • 73
    • 33646862834 scopus 로고    scopus 로고
    • Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration
    • Chang KA, Kim HS, Ha TY, Ha JW, Shin KY, et al. (2006) Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration. Mol Biol Cell 26: 4327-4338.
    • (2006) Mol Biol Cell , vol.26 , pp. 4327-4338
    • Chang, K.A.1    Kim, H.S.2    Ha, T.Y.3    Ha, J.W.4    Shin, K.Y.5
  • 74
    • 78649460670 scopus 로고    scopus 로고
    • Possible roles of amyloid intracellular domain of amyloid precusor protein
    • Chang K-A, Suh Y-H, (2010) Possible roles of amyloid intracellular domain of amyloid precusor protein. BMB Rep 43: 656-663.
    • (2010) BMB Rep , vol.43 , pp. 656-663
    • Chang, K.-A.1    Suh, Y.-H.2
  • 75
    • 84858199215 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain-Fe65 multiprotein complexes: As challenge to the amyloid hypothesis for Alzheimer's disease?
    • Borquez DA, Gonzalez-Billault C, (2012) The amyloid precursor protein intracellular domain-Fe65 multiprotein complexes: As challenge to the amyloid hypothesis for Alzheimer's disease? Int J Alzheimers Dis 2012: 353145-353155.
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 353145-353155
    • Borquez, D.A.1    Gonzalez-Billault, C.2
  • 76
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Südhof TC, (2001) A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293: 115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 77
    • 64549152034 scopus 로고    scopus 로고
    • FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4
    • Kajiwara Y, Akram A, Katsel P, Haroutunian V, Schmeidler J, et al. (2009) FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4. PLoS One 4: e5071.
    • (2009) PLoS One , vol.4
    • Kajiwara, Y.1    Akram, A.2    Katsel, P.3    Haroutunian, V.4    Schmeidler, J.5
  • 78
    • 70450235497 scopus 로고    scopus 로고
    • Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain
    • Ghosal K, Vogt DL, Liang M, Shen Y, Lamb BT, et al. (2009) Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain. Proc Natl Acad Sci U S A 106: 18367-18372.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18367-18372
    • Ghosal, K.1    Vogt, D.L.2    Liang, M.3    Shen, Y.4    Lamb, B.T.5
  • 79
    • 51349120462 scopus 로고    scopus 로고
    • Intracellular domain of amyloid precursor protein induces neuron-specific apoptosis
    • Nakayama K, Ohkawara T, Hiratochi M, Koh C-S, Nagase H, (2008) Intracellular domain of amyloid precursor protein induces neuron-specific apoptosis. Neurosci Lett 444: 127-131.
    • (2008) Neurosci Lett , vol.444 , pp. 127-131
    • Nakayama, K.1    Ohkawara, T.2    Hiratochi, M.3    Koh, C.-S.4    Nagase, H.5
  • 80
    • 0034107524 scopus 로고    scopus 로고
    • A second cytotoxic proteolytic peptide derived from amyloid ß-protein precursor
    • Lu DC, Rabizadeh S, Chandra S, Shayya RF, Ellerby LM, et al. (2000) A second cytotoxic proteolytic peptide derived from amyloid ß-protein precursor. Nature Medicine 6: 397-404.
    • (2000) Nature Medicine , vol.6 , pp. 397-404
    • Lu, D.C.1    Rabizadeh, S.2    Chandra, S.3    Shayya, R.F.4    Ellerby, L.M.5
  • 81
    • 0345602771 scopus 로고    scopus 로고
    • Amyloid beta protein toxicity mediated by the formation of amyloid-beta protein precursor complexes
    • Lu DC, Shaked GM, Masliah E, Bredesen DE, Koo EH, (2003) Amyloid beta protein toxicity mediated by the formation of amyloid-beta protein precursor complexes. Ann Neurol 54: 781-789.
    • (2003) Ann Neurol , vol.54 , pp. 781-789
    • Lu, D.C.1    Shaked, G.M.2    Masliah, E.3    Bredesen, D.E.4    Koo, E.H.5
  • 82
    • 77955637621 scopus 로고    scopus 로고
    • APP intracellular domain impairs adult neurogenesis in transgenic mice by inducing neuroinflammation
    • Ghosal K, Stathopoulos A, Pimplikar SW, (2010) APP intracellular domain impairs adult neurogenesis in transgenic mice by inducing neuroinflammation. PLoS One 5: e11866.
    • (2010) PLoS One , vol.5
    • Ghosal, K.1    Stathopoulos, A.2    Pimplikar, S.W.3
  • 83
    • 80053633517 scopus 로고    scopus 로고
    • Aging and excitotoxic stress exacerbate neural circuit reorganization in amyloid precursor protein intracellular domain transgenic mice
    • Ghosal K, Pimplikar SW (2011) Aging and excitotoxic stress exacerbate neural circuit reorganization in amyloid precursor protein intracellular domain transgenic mice. Neurobiol Aging 32: 2320 2321-2329.
    • (2011) Neurobiol Aging , vol.32
    • Ghosal, K.1    Pimplikar, S.W.2
  • 84
    • 79960133399 scopus 로고    scopus 로고
    • Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain
    • Vogt DL, Thomas D, Galvan V, Bredesen DE, Lamb BT, et al. (2011) Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain. Neurobiol Aging 32: 1725-1729.
    • (2011) Neurobiol Aging , vol.32 , pp. 1725-1729
    • Vogt, D.L.1    Thomas, D.2    Galvan, V.3    Bredesen, D.E.4    Lamb, B.T.5
  • 85
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production
    • Moehlmann T, Winkler E, Xia X, Edbauer D, Murrell J, et al. (2002) Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Abeta 42 production. Proc Natl Acad Sci USA 99: 8025-8030.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8025-8030
    • Moehlmann, T.1    Winkler, E.2    Xia, X.3    Edbauer, D.4    Murrell, J.5
  • 86
    • 67649534694 scopus 로고    scopus 로고
    • Presenilin-dependent regulated intramembrane proteolysis and gamma-secretase activity
    • McCarthy JV, Twomey C, Wujek P, (2009) Presenilin-dependent regulated intramembrane proteolysis and gamma-secretase activity. Cell Mol Life Sci 66: 1534-1555.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1534-1555
    • McCarthy, J.V.1    Twomey, C.2    Wujek, P.3
  • 87
    • 27544442991 scopus 로고    scopus 로고
    • Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain
    • Ryan KA, Pimplikar SW, (2005) Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. J Cell Biol 171: 327-335.
    • (2005) J Cell Biol , vol.171 , pp. 327-335
    • Ryan, K.A.1    Pimplikar, S.W.2
  • 88
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • Cho JH, Johnson GV, (2004) Primed phosphylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) 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
  • 89
    • 33845926113 scopus 로고    scopus 로고
    • Characterization of two VQIXXK motifs for tau fibrillization in vitro
    • Li W, Lee VM, (2006) Characterization of two VQIXXK motifs for tau fibrillization in vitro. Biochemistry 45: 15692-15701.
    • (2006) Biochemistry , vol.45 , pp. 15692-15701
    • Li, W.1    Lee, V.M.2
  • 91
    • 9644257211 scopus 로고    scopus 로고
    • Tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain
    • Liu SJ, Zhang JY, Li HL, Fang ZY, Wang Q, et al. (2004) Tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain. J Biol Chem 279: 50078-50088.
    • (2004) J Biol Chem , vol.279 , pp. 50078-50088
    • Liu, S.J.1    Zhang, J.Y.2    Li, H.L.3    Fang, Z.Y.4    Wang, Q.5
  • 92
    • 33745236883 scopus 로고    scopus 로고
    • Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices
    • Shahani N, Subramaniam S, Wolf T, Tackenberg C, Brandt R, (2006) Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices. Neurobiol Dis 26: 6103-6114.
    • (2006) Neurobiol Dis , vol.26 , pp. 6103-6114
    • Shahani, N.1    Subramaniam, S.2    Wolf, T.3    Tackenberg, C.4    Brandt, R.5
  • 93
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, et al. (2010) Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67: 953-966.
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3    Schroeder, S.4    Haroutunian, V.5
  • 94
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-ß/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • Roberson ED, Halabisky B, Yoo JW, Yao J, Chin J, et al. (2011) Amyloid-ß/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. J Neurosci 31: 700-711.
    • (2011) J Neurosci , vol.31 , pp. 700-711
    • Roberson, E.D.1    Halabisky, B.2    Yoo, J.W.3    Yao, J.4    Chin, J.5
  • 95
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • Cohen TJ, Guo JL, Hurtado DE, Kwong LK, Mills IP, et al. (2011) The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun 2: 252.
    • (2011) Nat Commun , vol.2 , pp. 252
    • Cohen, T.J.1    Guo, J.L.2    Hurtado, D.E.3    Kwong, L.K.4    Mills, I.P.5
  • 96
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga TA, Elson-Schwab I, Khurana V, Steinhib ML, Spires TL, et al. (2007) Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 9: 139-148.
    • (2007) Nat Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhib, M.L.4    Spires, T.L.5
  • 98
    • 58149389727 scopus 로고    scopus 로고
    • Autophagy contributes to degradation of Hirano bodies
    • Kim DH, Davis RC, Furukawa R, Fechheimer M, (2009) Autophagy contributes to degradation of Hirano bodies. Autophagy 5: 44-51.
    • (2009) Autophagy , vol.5 , pp. 44-51
    • Kim, D.H.1    Davis, R.C.2    Furukawa, R.3    Fechheimer, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.