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Volumn 39, Issue 7, 2014, Pages 1202-1213

Tau acts as a mediator for Alzheimer's disease-related synaptic deficits

Author keywords

Amyloid beta; Amyloid cascade hypothesis; Dendritic spines; Soluble proteins; Synaptic dysfunction

Indexed keywords

AMYLOID BETA PROTEIN; CALCIUM; PHOSPHOPROTEIN; PRION PROTEIN; PROTEIN KINASE FYN; TAU PROTEIN;

EID: 84898733006     PISSN: 0953816X     EISSN: 14609568     Source Type: Journal    
DOI: 10.1111/ejn.12504     Document Type: Article
Times cited : (44)

References (192)
  • 3
    • 0000293742 scopus 로고
    • Uber eine eigenartige Erkrankung der Hirnrinde
    • Alzheimer, A. (1907) Uber eine eigenartige Erkrankung der Hirnrinde. Allg. Z. Psychiatr., 64, 146-148.
    • (1907) Allg. Z. Psychiatr. , vol.64 , pp. 146-148
    • Alzheimer, A.1
  • 5
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • Andorfer, C., Acker, C.M., Kress, Y., Hof, P.R., 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
  • 6
    • 67349213205 scopus 로고    scopus 로고
    • Synaptic degeneration in Alzheimer's disease
    • Arendt, T. (2009) Synaptic degeneration in Alzheimer's disease. Acta Neuropathol., 118, 167-179.
    • (2009) Acta Neuropathol. , vol.118 , pp. 167-179
    • Arendt, T.1
  • 7
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P.V., Growdon, J.H., Hedley-Whyte, E.T. & Hyman, B.T. (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology, 42, 631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 8
    • 77953675879 scopus 로고    scopus 로고
    • Probing the biology of Alzheimer's disease in mice
    • Ashe, K.H. & Zahs, K.R. (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
  • 9
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • Avila, J., Lucas, J.J., Perez, M. & Hernandez, F. (2004) Role of tau protein in both physiological and pathological conditions. Physiol. Rev., 84, 361-384.
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 10
    • 1542268242 scopus 로고    scopus 로고
    • Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function
    • Bennett, D.A., Schneider, J.A., Wilson, R.S., Bienias, J.L. & Arnold, S.E. (2004) Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function. Arch. Neurol., 61, 378-384.
    • (2004) Arch. Neurol. , vol.61 , pp. 378-384
    • Bennett, D.A.1    Schneider, J.A.2    Wilson, R.S.3    Bienias, J.L.4    Arnold, S.E.5
  • 12
    • 3042558276 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: a drug target for CNS therapies
    • Bhat, R.V., Budd Haeberlein, S.L. & Avila, J. (2004) Glycogen synthase kinase 3: a drug target for CNS therapies. J. Neurochem., 89, 1313-1317.
    • (2004) J. Neurochem. , vol.89 , pp. 1313-1317
    • Bhat, R.V.1    Budd Haeberlein, S.L.2    Avila, J.3
  • 13
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings, L.M., Oddo, S., Green, K.N., McGaugh, J.L. & LaFerla, F.M. (2005) Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron, 45, 675-688.
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 17
    • 38349013141 scopus 로고    scopus 로고
    • Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP x tau transgenic mice
    • Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M.C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M. & Jucker, M. (2007) Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP x tau transgenic mice. Am. J. Pathol., 171, 2012-2020.
    • (2007) Am. J. Pathol. , vol.171 , pp. 2012-2020
    • Bolmont, T.1    Clavaguera, F.2    Meyer-Luehmann, M.3    Herzig, M.C.4    Radde, R.5    Staufenbiel, M.6    Lewis, J.7    Hutton, M.8    Tolnay, M.9    Jucker, M.10
  • 19
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: mechanisms and models
    • Brandt, R., Hundelt, M. & Shahani, N. (2005) Tau alteration and neuronal degeneration in tauopathies: mechanisms and models. Biochim. Biophys. Acta, 1739, 331-354.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 23
    • 80052508278 scopus 로고    scopus 로고
    • The impacts of geometry and binding on CaMKII diffusion and retention in dendritic spines
    • Byrne, M.J., Waxham, M.N. & Kubota, Y. (2011) The impacts of geometry and binding on CaMKII diffusion and retention in dendritic spines. J. Comput. Neurosci., 31, 1-12.
    • (2011) J. Comput. Neurosci. , vol.31 , pp. 1-12
    • Byrne, M.J.1    Waxham, M.N.2    Kubota, Y.3
  • 24
    • 84867600744 scopus 로고    scopus 로고
    • Rational heterodoxy: cholesterol reformation of the amyloid doctrine
    • Castello, M.A. & Soriano, S. (2013) Rational heterodoxy: cholesterol reformation of the amyloid doctrine. Ageing Res. Rev., 12, 282-288.
    • (2013) Ageing Res. Rev. , vol.12 , pp. 282-288
    • Castello, M.A.1    Soriano, S.2
  • 26
    • 0036354603 scopus 로고    scopus 로고
    • Alzheimer amyloid beta-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus
    • Chen, Q.-S., Wei, W.-Z., Shimahara, T. & Xie, C.-W. (2002) Alzheimer amyloid beta-peptide inhibits the late phase of long-term potentiation through calcineurin-dependent mechanisms in the hippocampal dentate gyrus. Neurobiol. Learn. Mem., 77, 354-371.
    • (2002) Neurobiol. Learn. Mem. , vol.77 , pp. 354-371
    • Chen, Q.-S.1    Wei, W.-Z.2    Shimahara, T.3    Xie, C.-W.4
  • 29
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy
    • Cingolani, L.A. & Goda, Y. (2008) Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy. Nat. Rev. Neurosci., 9, 344-356.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 33
    • 84881546833 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
    • Crimins, J.L., Pooler, A., Polydoro, M., Luebke, J.I. & Spires-Jones, T.L. (2013) The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease. Ageing Res. Rev., 12, 757-763.
    • (2013) Ageing Res. Rev. , vol.12 , pp. 757-763
    • Crimins, J.L.1    Pooler, A.2    Polydoro, M.3    Luebke, J.I.4    Spires-Jones, T.L.5
  • 36
    • 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, C.A., Mann, D.M., Sumpter, P.Q. & Yates, P.O. (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
  • 39
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity
    • DeKosky, S.T. & Scheff, S.W. (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
  • 43
    • 34547653708 scopus 로고    scopus 로고
    • Acute inhibition of calcineurin restores associative learning and memory in Tg2576 APP transgenic mice
    • Dineley, K.T., Hogan, D., Zhang, W.-R. & Taglialatela, G. (2007) Acute inhibition of calcineurin restores associative learning and memory in Tg2576 APP transgenic mice. Neurobiol. Learn. Mem., 88, 217-224.
    • (2007) Neurobiol. Learn. Mem. , vol.88 , pp. 217-224
    • Dineley, K.T.1    Hogan, D.2    Zhang, W.-R.3    Taglialatela, G.4
  • 44
    • 84876208687 scopus 로고    scopus 로고
    • From soluble aβ to progressive aβ aggregation: could prion-like templated misfolding play a role?
    • Eisele, Y.S. (2013) From soluble aβ to progressive aβ aggregation: could prion-like templated misfolding play a role? Brain Pathol., 23, 333-341.
    • (2013) Brain Pathol. , vol.23 , pp. 333-341
    • Eisele, Y.S.1
  • 45
    • 84980053538 scopus 로고    scopus 로고
    • ER-stress in Alzheimer's disease: turning the scale?
    • Endres, K. & Reinhradt, S. (2013) ER-stress in Alzheimer's disease: turning the scale? Am. J. Neurodegener. Dis., 2, 247-265.
    • (2013) Am. J. Neurodegener. Dis. , vol.2 , pp. 247-265
    • Endres, K.1    Reinhradt, S.2
  • 46
    • 42249113832 scopus 로고    scopus 로고
    • The use of the hippocampal slice preparation in the study of Alzheimer's disease
    • Fitzjohn, S.M., Doherty, A.J. & Collingridge, G.L. (2008) The use of the hippocampal slice preparation in the study of Alzheimer's disease. Eur. J. Pharmacol., 585, 50-59.
    • (2008) Eur. J. Pharmacol. , vol.585 , pp. 50-59
    • Fitzjohn, S.M.1    Doherty, A.J.2    Collingridge, G.L.3
  • 47
    • 84883780939 scopus 로고    scopus 로고
    • Activation of the endoplasmic reticulum stress response by the amyloid-beta 1-40 peptide in brain endothelial cells
    • Fonseca, A.C.R.G., Ferreiro, E., Oliveira, C.R., Cardoso, S.M. & Pereira, C.F. (2013) Activation of the endoplasmic reticulum stress response by the amyloid-beta 1-40 peptide in brain endothelial cells. Biochim. Biophys. Acta, 1832, 2191-2203.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 2191-2203
    • Fonseca, A.C.R.G.1    Ferreiro, E.2    Oliveira, C.R.3    Cardoso, S.M.4    Pereira, C.F.5
  • 48
    • 75049084559 scopus 로고    scopus 로고
    • Changing perspectives regarding late-life dementia
    • Fotuhi, M., Hachinski, V. & Whitehouse, P.J. (2009) Changing perspectives regarding late-life dementia. Nat. Rev. Neurol., 5, 649-658.
    • (2009) Nat. Rev. Neurol. , vol.5 , pp. 649-658
    • Fotuhi, M.1    Hachinski, V.2    Whitehouse, P.J.3
  • 53
    • 77952549757 scopus 로고    scopus 로고
    • Targeting Abeta and tau in Alzheimer's disease, an early interim report
    • Golde, T.E., Petrucelli, L. & Lewis, J. (2010) Targeting Abeta and tau in Alzheimer's disease, an early interim report. Exp. Neurol., 223, 252-266.
    • (2010) Exp. Neurol. , vol.223 , pp. 252-266
    • Golde, T.E.1    Petrucelli, L.2    Lewis, J.3
  • 55
    • 0014036452 scopus 로고
    • The contribution of altered synapses in the senile plaque: an electron microscopic study in Alzheimer's dementia
    • Gonatas, N.K., Anderson, W. & Evangelista, I. (1967) The contribution of altered synapses in the senile plaque: an electron microscopic study in Alzheimer's dementia. J. Neuropath. Exp. Neur., 26, 25-39.
    • (1967) J. Neuropath. Exp. Neur. , vol.26 , pp. 25-39
    • Gonatas, N.K.1    Anderson, W.2    Evangelista, I.3
  • 56
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Götz, J., Probst, A., Spillantini, M.G., Schäfer, T., Jakes, R., Bürki, K. & Goedert, M. (1995) Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. EMBO J., 14, 1304-1313.
    • (1995) EMBO J. , vol.14 , pp. 1304-1313
    • Götz, J.1    Probst, A.2    Spillantini, M.G.3    Schäfer, T.4    Jakes, R.5    Bürki, K.6    Goedert, M.7
  • 57
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils
    • Götz, J., Chen, F., van Dorpe, J. & Nitsch, R.M. (2001) Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils. Science, 293, 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 58
    • 72849144675 scopus 로고    scopus 로고
    • Calcium in the initiation, progression and as an effector of Alzheimer's disease pathology
    • Green, K.N. (2009) Calcium in the initiation, progression and as an effector of Alzheimer's disease pathology. J. Cell Mol. Med., 13, 2787-2799.
    • (2009) J. Cell Mol. Med. , vol.13 , pp. 2787-2799
    • Green, K.N.1
  • 59
    • 72549105935 scopus 로고    scopus 로고
    • Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial
    • Tarenflurbil Phase 3 Study Group
    • Green, R.C., Schneider, L.S., Amato, D.A., Beelen, A.P., Wilcock, G., Swabb, E.A., Zavitz, K.H. & Tarenflurbil Phase 3 Study Group (2009) Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial. JAMA, 302, 2557-2564.
    • (2009) JAMA , vol.302 , pp. 2557-2564
    • Green, R.C.1    Schneider, L.S.2    Amato, D.A.3    Beelen, A.P.4    Wilcock, G.5    Swabb, E.A.6    Zavitz, K.H.7
  • 60
  • 62
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass, C. & Selkoe, D.J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol., 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 64
    • 79955535364 scopus 로고    scopus 로고
    • Hyperphosphorylated tau in an α-synuclein-overexpressing transgenic model of Parkinson's disease
    • Haggerty, T., Credle, J., Rodriguez, O., Wills, J., Oaks, A.W., Masliah, E. & Sidhu, A. (2011) Hyperphosphorylated tau in an α-synuclein-overexpressing transgenic model of Parkinson's disease. Eur. J. Neurosci., 33, 1598-1610.
    • (2011) Eur. J. Neurosci. , vol.33 , pp. 1598-1610
    • Haggerty, T.1    Credle, J.2    Rodriguez, O.3    Wills, J.4    Oaks, A.W.5    Masliah, E.6    Sidhu, A.7
  • 66
    • 32544435900 scopus 로고    scopus 로고
    • Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: a follow-up study
    • Hansson, O., Zetterberg, H., Buchhave, P., Londos, E., Blennow, K. & Minthon, L. (2006) Association between CSF biomarkers and incipient Alzheimer's disease in patients with mild cognitive impairment: a follow-up study. Lancet Neurol., 5, 228-234.
    • (2006) Lancet Neurol. , vol.5 , pp. 228-234
    • Hansson, O.1    Zetterberg, H.2    Buchhave, P.3    Londos, E.4    Blennow, K.5    Minthon, L.6
  • 67
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy, J. & Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci., 12, 383-388.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 68
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy, J.A. & Higgins, G.A. (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
  • 69
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D.J. (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
  • 70
    • 0028801680 scopus 로고
    • Loss of synaptophysin-like immunoreactivity in the hippocampal formation is an early phenomenon in Alzheimer's disease
    • Heinonen, O., Soininen, H., Sorvari, H., Kosunen, O., Paljärvi, L., Koivisto, E. & Riekkinen, P.J. (1995) Loss of synaptophysin-like immunoreactivity in the hippocampal formation is an early phenomenon in Alzheimer's disease. Neuroscience, 64, 375-384.
    • (1995) Neuroscience , vol.64 , pp. 375-384
    • Heinonen, O.1    Soininen, H.2    Sorvari, H.3    Kosunen, O.4    Paljärvi, L.5    Koivisto, E.6    Riekkinen, P.J.7
  • 71
    • 75949101330 scopus 로고    scopus 로고
    • Oligomeric Abeta in Alzheimer's disease: relationship to plaque and tangle pathology, APOE genotype and cerebral amyloid angiopathy
    • van Helmond, Z., Miners, J.S., Kehoe, P.G. & Love, S. (2010) Oligomeric Abeta in Alzheimer's disease: relationship to plaque and tangle pathology, APOE genotype and cerebral amyloid angiopathy. Brain Pathol., 20, 468-480.
    • (2010) Brain Pathol. , vol.20 , pp. 468-480
    • van Helmond, Z.1    Miners, J.S.2    Kehoe, P.G.3    Love, S.4
  • 72
    • 84874025583 scopus 로고    scopus 로고
    • Synthetic Aβ oligomers (Aβ(1-42) globulomer) modulate presynaptic calcium currents: prevention of Aβ-induced synaptic deficits by calcium channel blockers
    • Hermann, D., Mezler, M., Muller, M.K., Wicke, K., Gross, G., Draguhn, A., Bruehl, C. & Nimmrich, V. (2013) Synthetic Aβ oligomers (Aβ(1-42) globulomer) modulate presynaptic calcium currents: prevention of Aβ-induced synaptic deficits by calcium channel blockers. Eur. J. Pharmacol., 702, 44-55.
    • (2013) Eur. J. Pharmacol. , vol.702 , pp. 44-55
    • Hermann, D.1    Mezler, M.2    Muller, M.K.3    Wicke, K.4    Gross, G.5    Draguhn, A.6    Bruehl, C.7    Nimmrich, V.8
  • 73
    • 80755145989 scopus 로고    scopus 로고
    • Presenilins in synaptic function and disease
    • Ho, A. & Shen, J. (2011) Presenilins in synaptic function and disease. Trends Mol. Med., 17, 617-624.
    • (2011) Trends Mol. Med. , vol.17 , pp. 617-624
    • Ho, A.1    Shen, J.2
  • 78
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F. & Cole, G. (1996) Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science, 274, 99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6    Yang, F.7    Cole, G.8
  • 79
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss
    • Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S. & Malinow, R. (2006) AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron, 52, 831-843.
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 80
    • 84872760710 scopus 로고    scopus 로고
    • Age-dependent alterations in the presynaptic active zone in a Drosophila model of Alzheimer's disease
    • Huang, J.K., Ma, P.L., Ji, S.Y., Zhao, X.L., Tan, J.X., Sun, X.J. & Huang, F.D. (2013) Age-dependent alterations in the presynaptic active zone in a Drosophila model of Alzheimer's disease. Neurobiol. Dis., 51, 161-167.
    • (2013) Neurobiol. Dis. , vol.51 , pp. 161-167
    • Huang, J.K.1    Ma, P.L.2    Ji, S.Y.3    Zhao, X.L.4    Tan, J.X.5    Sun, X.J.6    Huang, F.D.7
  • 81
    • 0031593785 scopus 로고    scopus 로고
    • Neuropathological and neuropsychological changes in "normal" aging: evidence for preclinical alzheimer disease in cognitively normal individuals
    • Hulette, C.M., Welsh-Bohmer, K.A., Murray, M.G., Saunders, A.M., Mash, D.C. & Mcintyre, L.M. (1998) Neuropathological and neuropsychological changes in "normal" aging: evidence for preclinical alzheimer disease in cognitively normal individuals. J. Neuropath. Exp. Neur., 57, 1168.
    • (1998) J. Neuropath. Exp. Neur. , vol.57 , pp. 1168
    • Hulette, C.M.1    Welsh-Bohmer, K.A.2    Murray, M.G.3    Saunders, A.M.4    Mash, D.C.5    Mcintyre, L.M.6
  • 82
    • 84883174947 scopus 로고    scopus 로고
    • Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies
    • Irwin, D.J., Lee, V.M.Y. & Trojanowski, J.Q. (2013) Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies. Nat. Rev. Neurosci., 14, 626-636.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 626-636
    • Irwin, D.J.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 88
    • 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
  • 90
    • 84874629526 scopus 로고    scopus 로고
    • Metabotropic NMDA receptor function is required for β-amyloid-induced synaptic depression
    • Kessels, H.W., Nabavi, S. & Malinow, R. (2013) Metabotropic NMDA receptor function is required for β-amyloid-induced synaptic depression. Proc. Natl. Acad. Sci. USA, 110, 4033-4038.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 4033-4038
    • Kessels, H.W.1    Nabavi, S.2    Malinow, R.3
  • 91
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins, S., Crameri, A., Evans, D.R., Hemmings, B.A., Nitsch, R.M. & Götz, J. (2001) Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem., 276, 38193-38200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38193-38200
    • Kins, S.1    Crameri, A.2    Evans, D.R.3    Hemmings, B.A.4    Nitsch, R.M.5    Götz, J.6
  • 93
    • 77955919696 scopus 로고    scopus 로고
    • ADDLs and the signaling web that leads to Alzheimer's disease
    • Krafft, G.A. & Klein, W.L. (2010) ADDLs and the signaling web that leads to Alzheimer's disease. Neuropharmacology, 59, 230-242.
    • (2010) Neuropharmacology , vol.59 , pp. 230-242
    • Krafft, G.A.1    Klein, W.L.2
  • 94
    • 47749113650 scopus 로고    scopus 로고
    • Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks
    • Kuchibhotla, K.V., Goldman, S.T., Lattarulo, C.R., Wu, H.-Y., Hyman, B.T. & Bacskai, B.J. (2008) Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron, 59, 214-225.
    • (2008) Neuron , vol.59 , pp. 214-225
    • Kuchibhotla, K.V.1    Goldman, S.T.2    Lattarulo, C.R.3    Wu, H.-Y.4    Hyman, B.T.5    Bacskai, B.J.6
  • 95
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor, P.N., Buniel, M.C., Furlow, P.W., Clemente, A.S., Velasco, P.T., Wood, M., Viola, K.L. & Klein, W.L. (2007) Abeta 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
  • 96
    • 10344254833 scopus 로고    scopus 로고
    • Mixed dementia: emerging concepts and therapeutic implications
    • Langa, K.M., Foster, N.L. & Larson, E.B. (2004) Mixed dementia: emerging concepts and therapeutic implications. JAMA, 292, 2901-2908.
    • (2004) JAMA , vol.292 , pp. 2901-2908
    • Langa, K.M.1    Foster, N.L.2    Larson, E.B.3
  • 97
    • 0043095312 scopus 로고    scopus 로고
    • Dendritic spine loss in the hippocampus of young PDAPP and Tg2576 mice and its prevention by the ApoE2 genotype
    • Lanz, T.A., Carter, D.B. & Merchant, K.M. (2003) Dendritic spine loss in the hippocampus of young PDAPP and Tg2576 mice and its prevention by the ApoE2 genotype. Neurobiol. Dis., 13, 246-253.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 246-253
    • Lanz, T.A.1    Carter, D.B.2    Merchant, K.M.3
  • 98
    • 84655162704 scopus 로고    scopus 로고
    • Soluble Aβ oligomer production and toxicity
    • Larson, M.E. & Lesné, S.E. (2012) Soluble Aβ oligomer production and toxicity. J. Neurochem., 120(Suppl 1), 125-139.
    • (2012) J. Neurochem. , vol.120 , Issue.SUPPL 1 , pp. 125-139
    • Larson, M.E.1    Lesné, S.E.2
  • 100
    • 84889570015 scopus 로고    scopus 로고
    • Cellular prion protein as a therapeutic target in Alzheimer's disease
    • Laurén, J. (2014) Cellular prion protein as a therapeutic target in Alzheimer's disease. J. Alzheimers Dis., 38, 227-244.
    • (2014) J. Alzheimers Dis. , vol.38 , pp. 227-244
    • Laurén, J.1
  • 101
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Laurén, J., Gimbel, D.A., Nygaard, H.B., Gilbert, J.W. & Strittmatter, S.M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature, 457, 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 102
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • Lee, S.-J.R., Escobedo-Lozoya, Y., Szatmari, E.M. & Yasuda, R. (2009) Activation of CaMKII in single dendritic spines during long-term potentiation. Nature, 458, 299-304.
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.-J.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 107
    • 79955769953 scopus 로고    scopus 로고
    • Soluble Aβ oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors
    • Li, S., Jin, M., Koeglsperger, T., Shepardson, N., Shankar, G. & Selkoe, D. (2011) Soluble Aβ oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors. J. Neurosci., 31, 6627-6638.
    • (2011) J. Neurosci. , vol.31 , pp. 6627-6638
    • Li, S.1    Jin, M.2    Koeglsperger, T.3    Shepardson, N.4    Shankar, G.5    Selkoe, D.6
  • 108
    • 84861192034 scopus 로고    scopus 로고
    • AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation
    • Li, X.H., Lv, B.L., Xie, J.Z., Liu, J., Zhou, X.W. & Wang, J.Z. (2012) AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation. Neurobiol. Aging, 33, 1-11.
    • (2012) Neurobiol. Aging , vol.33 , pp. 1-11
    • Li, X.H.1    Lv, B.L.2    Xie, J.Z.3    Liu, J.4    Zhou, X.W.5    Wang, J.Z.6
  • 109
  • 111
    • 84876078566 scopus 로고    scopus 로고
    • The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Aβ oligomers through tau phosphorylation
    • Mairet-Coello, G., Courchet, J., Pieraut, S., Courchet, V., Maximov, A. & Polleux, F. (2013) The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Aβ oligomers through tau phosphorylation. Neuron, 78, 94-408.
    • (2013) Neuron , vol.78 , pp. 94-408
    • Mairet-Coello, G.1    Courchet, J.2    Pieraut, S.3    Courchet, V.4    Maximov, A.5    Polleux, F.6
  • 112
    • 5344241223 scopus 로고    scopus 로고
    • LTP and LTD: an embarrassment of riches
    • Malenka, R.C. & Bear, M.F. (2004) LTP and LTD: an embarrassment of riches. Neuron, 44, 5-21.
    • (2004) Neuron , vol.44 , pp. 5-21
    • Malenka, R.C.1    Bear, M.F.2
  • 113
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • Masliah, E., Terry, R.D., DeTeresa, R.M. & Hansen, L.A. (1989) Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease. Neurosci. Lett., 103, 234-239.
    • (1989) Neurosci. Lett. , vol.103 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 115
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki, M., Honkura, N., Ellis-Davies, G.C.R. & 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.R.3    Kasai, H.4
  • 116
    • 84887863225 scopus 로고    scopus 로고
    • Lysosome and calcium dysregulation in Alzheimer's disease: partners in crime
    • McBrayer, M. & Nixon, R.A. (2013) Lysosome and calcium dysregulation in Alzheimer's disease: partners in crime. Biochem. Soc. Trans., 41, 1495-1502.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1495-1502
    • McBrayer, M.1    Nixon, R.A.2
  • 117
    • 84885456046 scopus 로고    scopus 로고
    • The amyloid cascade-inflammatory hypothesis of Alzheimer disease: implications for therapy
    • McGeer, P.L. & McGeer, E.G. (2013) The amyloid cascade-inflammatory hypothesis of Alzheimer disease: implications for therapy. Acta. Neuropathol., 126, 479-497.
    • (2013) Acta. Neuropathol. , vol.126 , pp. 479-497
    • McGeer, P.L.1    McGeer, E.G.2
  • 119
    • 84863914431 scopus 로고    scopus 로고
    • Differential modulation of drug-induced structural and functional plasticity of dendritic spines
    • Miller, E.C., Zhang, L., Dummer, B.W., Cariveau, D.R., Loh, H.H., Law, P.Y. & Liao, D. (2012) Differential modulation of drug-induced structural and functional plasticity of dendritic spines. Mol. Pharmacol., 82, 333-343.
    • (2012) Mol. Pharmacol. , vol.82 , pp. 333-343
    • Miller, E.C.1    Zhang, L.2    Dummer, B.W.3    Cariveau, D.R.4    Loh, H.H.5    Law, P.Y.6    Liao, D.7
  • 120
    • 84898719221 scopus 로고    scopus 로고
    • Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer-induced AMPA glutamate receptor signaling deficits
    • doi: 10.1111/ejn.12507. [Epub ahead of print].
    • Miller, E.C., Teravskis, P., Dummer, B.W., Zhao, X., Huganir, R.L. & Liao, D. (2014) Tau phosphorylation and tau mislocalization mediate soluble Aβ oligomer-induced AMPA glutamate receptor signaling deficits. Eur. J. Neurosci., doi: 10.1111/ejn.12507. [Epub ahead of print].
    • (2014) Eur. J. Neurosci
    • Miller, E.C.1    Teravskis, P.2    Dummer, B.W.3    Zhao, X.4    Huganir, R.L.5    Liao, D.6
  • 122
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation
    • Mucke, L., Masliah, E., Yu, G.Q., Mallory, M., Rockenstein, E.M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K. & McConlogue, L. (2000) High-level neuronal expression of abeta 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J. Neurosci., 20, 4050-4058.
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6    Hu, K.7    Kholodenko, D.8    Johnson-Wood, K.9    McConlogue, L.10
  • 123
    • 0028176087 scopus 로고
    • Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression
    • Mulkey, R.M., Endo, S., Shenolikar, S. & Malenka, R.C. (1994) Involvement of a calcineurin/inhibitor-1 phosphatase cascade in hippocampal long-term depression. Nature, 369, 486-488.
    • (1994) Nature , vol.369 , pp. 486-488
    • Mulkey, R.M.1    Endo, S.2    Shenolikar, S.3    Malenka, R.C.4
  • 124
    • 0038117796 scopus 로고    scopus 로고
    • Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline
    • Näslund, J., Haroutunian, V., Mohs, R., Davis, K.L., Davies, P., Greengard, P. & Buxbaum, J.D. (2000) Correlation between elevated levels of amyloid beta-peptide in the brain and cognitive decline. JAMA, 283, 1571-1577.
    • (2000) JAMA , vol.283 , pp. 1571-1577
    • Näslund, J.1    Haroutunian, V.2    Mohs, R.3    Davis, K.L.4    Davies, P.5    Greengard, P.6    Buxbaum, J.D.7
  • 126
    • 84878425040 scopus 로고    scopus 로고
    • Newly developed glycogen synthase kinase-3 (GSK-3) inhibitors protect neuronal cells death in amyloid-beta induced cell model and in a transgenic mouse model of Alzheimer's disease
    • Noh, M.-Y., Chun, K., Kang, B.Y., Kim, H., Park, J.-S., Lee, H.-C., Kim, Y.-H., Ku, S. & Kim, S.H. (2013) Newly developed glycogen synthase kinase-3 (GSK-3) inhibitors protect neuronal cells death in amyloid-beta induced cell model and in a transgenic mouse model of Alzheimer's disease. Biochem. Bioph. Res. Co., 435, 274-281.
    • (2013) Biochem. Bioph. Res. Co. , vol.435 , pp. 274-281
    • Noh, M.-Y.1    Chun, K.2    Kang, B.Y.3    Kim, H.4    Park, J.-S.5    Lee, H.-C.6    Kim, Y.-H.7    Ku, S.8    Kim, S.H.9
  • 127
    • 0022723508 scopus 로고
    • One of the antigenic determinants of paired helical filaments is related to tau protein
    • Nukina, N. & Ihara, Y. (1986) One of the antigenic determinants of paired helical filaments is related to tau protein. J. Biochem., 99, 1541-1544.
    • (1986) J. Biochem. , vol.99 , pp. 1541-1544
    • Nukina, N.1    Ihara, Y.2
  • 128
    • 84874608863 scopus 로고    scopus 로고
    • Alzheimer disease: a tale of two prions
    • Nussbaum, J.M., Seward, M.E. & Bloom, G.S. (2013) Alzheimer disease: a tale of two prions. Prion, 7, 14-19.
    • (2013) Prion , vol.7 , pp. 14-19
    • Nussbaum, J.M.1    Seward, M.E.2    Bloom, G.S.3
  • 129
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B.P. & LaFerla, F.M. (2003) Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging, 24, 1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 130
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo, S., Billings, L., Kesslak, J.P., Cribbs, D.H. & LaFerla, F.M. (2004) Abeta 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
  • 131
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • Oddo, S., Vasilevko, V., Caccamo, A., Kitazawa, M., Cribbs, D.H. & LaFerla, F.M. (2006) Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J. Biol. Chem., 281, 39413-39423.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 133
    • 33750582958 scopus 로고    scopus 로고
    • Alpha1-antichymotrypsin, an inflammatory protein overexpressed in Alzheimer's disease brain, induces tau phosphorylation in neurons
    • Padmanabhan, J., Levy, M., Dickson, D.W. & Potter, H. (2006) Alpha1-antichymotrypsin, an inflammatory protein overexpressed in Alzheimer's disease brain, induces tau phosphorylation in neurons. Brain, 129, 3020-3034.
    • (2006) Brain , vol.129 , pp. 3020-3034
    • Padmanabhan, J.1    Levy, M.2    Dickson, D.W.3    Potter, H.4
  • 134
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of tau in the central nervous system
    • Papasozomenos, S.C. & Binder, L.I. (1987) Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motil. Cytoskel., 8, 210-226.
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 135
    • 79960894827 scopus 로고    scopus 로고
    • Signalling pathways underlying structural plasticity of dendritic spines
    • Patterson, M. & Yasuda, R. (2011) Signalling pathways underlying structural plasticity of dendritic spines. Brit. J. Pharmacol., 163, 1626-1638.
    • (2011) Brit. J. Pharmacol. , vol.163 , pp. 1626-1638
    • Patterson, M.1    Yasuda, R.2
  • 136
    • 79952401018 scopus 로고    scopus 로고
    • Reduced spine density in specific regions of CA1 pyramidal neurons in two transgenic mouse models of Alzheimer's disease
    • Perez-Cruz, C., Nolte, M.W., van Gaalen, M.M., Rustay, N.R., Termont, A., Tanghe, A., Kirchhoff, F. & Ebert, U. (2011) Reduced spine density in specific regions of CA1 pyramidal neurons in two transgenic mouse models of Alzheimer's disease. J. Neurosci., 31, 3926-3934.
    • (2011) J. Neurosci. , vol.31 , pp. 3926-3934
    • Perez-Cruz, C.1    Nolte, M.W.2    van Gaalen, M.M.3    Rustay, N.R.4    Termont, A.5    Tanghe, A.6    Kirchhoff, F.7    Ebert, U.8
  • 137
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides
    • Phiel, C.J., Wilson, C.A., Lee, V.M. & Klein, P.S. (2003) GSK-3alpha regulates production of Alzheimer's disease amyloid-beta peptides. Nature, 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 140
    • 71849116135 scopus 로고    scopus 로고
    • Non-motor features of Parkinson's disease: depression and dementia
    • Reichmann, H., Schneider, C. & Löhle, M. (2009) Non-motor features of Parkinson's disease: depression and dementia. Parkinsonism Relat. D., 15(Suppl 3), S87-S92.
    • (2009) Parkinsonism Relat. D. , vol.15 , Issue.SUPPL 3
    • Reichmann, H.1    Schneider, C.2    Löhle, M.3
  • 141
    • 84859755505 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid cascade hypothesis: a critical review
    • Reitz, C. (2012) Alzheimer's disease and the amyloid cascade hypothesis: a critical review. Int. J. Alzheimers Dis., 2012, 369808.
    • (2012) Int. J. Alzheimers Dis. , vol.2012 , pp. 369808
    • Reitz, C.1
  • 144
    • 80053646630 scopus 로고    scopus 로고
    • Early onset amyloid lesions lead to severe neuritic abnormalities and local, but not global neuron loss in APPPS1 transgenic mice
    • 2324e1-2324e6
    • Rupp, N.J., Wegenast-Braun, B.M., Radde, R., Calhoun, M.E. & Jucker, M. (2011) Early onset amyloid lesions lead to severe neuritic abnormalities and local, but not global neuron loss in APPPS1 transgenic mice. Neurobiol. Aging, 32, 2324.e1-2324.e6.
    • (2011) Neurobiol. Aging , vol.32
    • Rupp, N.J.1    Wegenast-Braun, B.M.2    Radde, R.3    Calhoun, M.E.4    Jucker, M.5
  • 145
    • 84865054611 scopus 로고    scopus 로고
    • Amyloid-β acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2
    • Russell, C.L., Semerdjieva, S., Empson, R.M., Austen, B.M., Beesley, P.W. & Alifragis, P. (2012) Amyloid-β acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2. PLoS One, 7, e403201.
    • (2012) PLoS One , vol.7
    • Russell, C.L.1    Semerdjieva, S.2    Empson, R.M.3    Austen, B.M.4    Beesley, P.W.5    Alifragis, P.6
  • 147
    • 33746652117 scopus 로고    scopus 로고
    • Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits
    • Schindowski, K., Bretteville, A., Leroy, K., Bégard, S., Brion, J.-P., Hamdane, M. & Buée, L. (2006) Alzheimer's disease-like tau neuropathology leads to memory deficits and loss of functional synapses in a novel mutated tau transgenic mouse without any motor deficits. Am. J. Pathol., 169, 599-616.
    • (2006) Am. J. Pathol. , vol.169 , pp. 599-616
    • Schindowski, K.1    Bretteville, A.2    Leroy, K.3    Bégard, S.4    Brion, J.-P.5    Hamdane, M.6    Buée, L.7
  • 148
    • 70350464483 scopus 로고    scopus 로고
    • High blood pressure and microinfarcts: a link between vascular risk factors, dementia, and clinical Alzheimer's disease
    • Schneider, J.A. (2009) High blood pressure and microinfarcts: a link between vascular risk factors, dementia, and clinical Alzheimer's disease. J. Am. Geriatr. Soc., 57, 2146-2147.
    • (2009) J. Am. Geriatr. Soc. , vol.57 , pp. 2146-2147
    • Schneider, J.A.1
  • 149
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D.J. (2002) Alzheimer's disease is a synaptic failure. Science, 298, 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 150
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar, G.M., Bloodgood, B.L., Townsend, M., Walsh, D.M., Selkoe, D.J. & Sabatini, B.L. (2007) Natural oligomers of the Alzheimer amyloid-beta 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
  • 152
    • 84896729483 scopus 로고    scopus 로고
    • Function and dysfunction of presenilin
    • Shen, J. (2013) Function and dysfunction of presenilin. Neurodegener. Dis., 13, 61-63.
    • (2013) Neurodegener. Dis. , vol.13 , pp. 61-63
    • Shen, J.1
  • 155
    • 84871649258 scopus 로고    scopus 로고
    • Deregulated Cdk5 activity is involved in inducing Alzheimer's disease
    • Shukla, V., Skuntz, S. & Pant, H.C. (2012) Deregulated Cdk5 activity is involved in inducing Alzheimer's disease. Arch. Med. Res., 43, 435-439.
    • (2012) Arch. Med. Res. , vol.43 , pp. 435-439
    • Shukla, V.1    Skuntz, S.2    Pant, H.C.3
  • 157
    • 33646519920 scopus 로고    scopus 로고
    • Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • Spires, T.L., Orne, J.D., SantaCruz, K., Pitstick, R., Carlson, G.A., Ashe, K.H. & Hyman, B.T. (2006) Region-specific 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
  • 159
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death
    • Stadelmann, C., Deckwerth, T.L., Srinivasan, A., Bancher, C., Brück, W., Jellinger, K. & Lassmann, H. (1999) Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease. Evidence for apoptotic cell death. Am. J. Pathol., 155, 1459-1466.
    • (1999) Am. J. Pathol. , vol.155 , pp. 1459-1466
    • Stadelmann, C.1    Deckwerth, T.L.2    Srinivasan, A.3    Bancher, C.4    Brück, W.5    Jellinger, K.6    Lassmann, H.7
  • 160
    • 80053254091 scopus 로고    scopus 로고
    • Synaptic and extrasynaptic NMDA receptors differentially modulate neuronal COX-2 function, lipid peroxidation, and neuroprotection
    • Stark, D.T. & Bazan, N.G. (2011) Synaptic and extrasynaptic NMDA receptors differentially modulate neuronal COX-2 function, lipid peroxidation, and neuroprotection. J. Neurosci., 31, 13710-13721.
    • (2011) J. Neurosci. , vol.31 , pp. 13710-13721
    • Stark, D.T.1    Bazan, N.G.2
  • 163
    • 84863880556 scopus 로고    scopus 로고
    • Cognitive impairment in patients with Parkinson's disease: diagnosis, biomarkers, and treatment
    • Svenningsson, P., Westman, E., Ballard, C. & Aarsland, D. (2012) Cognitive impairment in patients with Parkinson's disease: diagnosis, biomarkers, and treatment. Lancet Neurol., 11, 697-707.
    • (2012) Lancet Neurol. , vol.11 , pp. 697-707
    • Svenningsson, P.1    Westman, E.2    Ballard, C.3    Aarsland, D.4
  • 164
    • 77956224679 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis
    • Swerdlow, R.H., Burns, J.M. & Khan, S.M. (2010) The Alzheimer's disease mitochondrial cascade hypothesis. J. Alzheimers Dis., 20, S265-S279.
    • (2010) J. Alzheimers Dis. , vol.20
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 165
    • 84903304968 scopus 로고    scopus 로고
    • The Alzheimer's disease mitochondrial cascade hypothesis: progress and perspectives
    • doi: 10.1016/j.bbadis.2013.09.010. [Epub ahead of print].
    • Swerdlow, R.H., Burns, J.M. & Khan, S.M. (2013) The Alzheimer's disease mitochondrial cascade hypothesis: progress and perspectives. Biochim. Biophys. Acta, doi: 10.1016/j.bbadis.2013.09.010. [Epub ahead of print].
    • (2013) Biochim. Biophys. Acta
    • Swerdlow, R.H.1    Burns, J.M.2    Khan, S.M.3
  • 166
    • 0030872413 scopus 로고    scopus 로고
    • Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease
    • Sze, C.I., Troncoso, J.C., Kawas, C., Mouton, P., Price, D.L. & Martin, L.J. (1997) Loss of the presynaptic vesicle protein synaptophysin in hippocampus correlates with cognitive decline in Alzheimer disease. J. Neuropath. Exp. Neur., 56, 933-944.
    • (1997) J. Neuropath. Exp. Neur. , 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
  • 167
    • 62649147319 scopus 로고    scopus 로고
    • Intermediate- and long-term recognition memory deficits in Tg2576 mice are reversed with acute calcineurin inhibition
    • Taglialatela, G., Hogan, D., Zhang, W.-R. & Dineley, K.T. (2009) Intermediate- and long-term recognition memory deficits in Tg2576 mice are reversed with acute calcineurin inhibition. Behav. Brain Res., 200, 95-99.
    • (2009) Behav. Brain Res. , vol.200 , pp. 95-99
    • Taglialatela, G.1    Hogan, D.2    Zhang, W.-R.3    Dineley, K.T.4
  • 168
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta
    • Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K. & Imahori, K. (1996) Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta. Neurosci. Lett., 203, 33-36.
    • (1996) Neurosci. Lett. , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 169
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
    • Tanzi, R.E. & Bertram, L. (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell, 120, 545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 170
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment
    • Terry, R.D., Masliah, E., Salmon, D.P., Butters, N., DeTeresa, R., Hill, R., Hansen, L.A. & 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
  • 172
    • 84874585213 scopus 로고    scopus 로고
    • Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
    • Um, J.W. & Strittmatter, S.M. (2013) Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease. Prion, 7, 37-41.
    • (2013) Prion , vol.7 , pp. 37-41
    • Um, J.W.1    Strittmatter, S.M.2
  • 176
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation
    • Wagner, U., Utton, M., Gallo, J.M. & Miller, C.C. (1996) Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation. J. Cell Sci., 109(Pt 6), 1537-1543.
    • (1996) J. Cell Sci. , vol.109 , Issue.PT 6 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3    Miller, C.C.4
  • 177
    • 0029995590 scopus 로고    scopus 로고
    • Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1
    • Wang, J.Z., Grundke-Iqbal, I. & Iqbal, K. (1996) Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1. Mol. Brain Res., 38, 200-208.
    • (1996) Mol. Brain Res. , vol.38 , pp. 200-208
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 178
    • 0032566623 scopus 로고    scopus 로고
    • Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase
    • Wang, J.Z., Wu, Q., Smith, A., Grundke-Iqbal, I. & Iqbal, K. (1998) Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. FEBS Lett., 436, 28-34.
    • (1998) FEBS Lett. , vol.436 , pp. 28-34
    • Wang, J.Z.1    Wu, Q.2    Smith, A.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 179
    • 84872551783 scopus 로고    scopus 로고
    • Abnormal hyperphosphorylation of tau: sites, regulation, and molecular mechanism of neurofibrillary degeneration
    • Wang, J.-Z., Xia, Y.-Y., Grundke-Iqbal, I. & Iqbal, K. (2013) Abnormal hyperphosphorylation of tau: sites, regulation, and molecular mechanism of neurofibrillary degeneration. J. Alzheimers Dis., 33(Suppl 1), S123-S139.
    • (2013) J. Alzheimers Dis. , vol.33 , Issue.SUPPL 1
    • Wang, J.-Z.1    Xia, Y.-Y.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 181
    • 39549115445 scopus 로고    scopus 로고
    • Progression of amyloid pathology to Alzheimer's disease pathology in an amyloid precursor protein transgenic mouse model by removal of nitric oxide synthase 2
    • Wilcock, D.M., Lewis, M.R., Van Nostrand, W.E., Davis, J., Previti, M.L., Gharkholonarehe, N., Vitek, M.P. & Colton, C.A. (2008) Progression of amyloid pathology to Alzheimer's disease pathology in an amyloid precursor protein transgenic mouse model by removal of nitric oxide synthase 2. J. Neurosci., 28, 1537-1545.
    • (2008) J. Neurosci. , vol.28 , pp. 1537-1545
    • Wilcock, D.M.1    Lewis, M.R.2    Van Nostrand, W.E.3    Davis, J.4    Previti, M.L.5    Gharkholonarehe, N.6    Vitek, M.P.7    Colton, C.A.8
  • 182
    • 84898059466 scopus 로고    scopus 로고
    • Tau-aggregation inhibitor therapy for Alzheimer's disease
    • doi: 10.1016/j.bcp.2013.12.008. [Epub ahead of print].
    • Wischik, C.M., Harrington, C.R. & Storey, J.M. (2013) Tau-aggregation inhibitor therapy for Alzheimer's disease. Biochem. Pharmacol., doi: 10.1016/j.bcp.2013.12.008. [Epub ahead of print].
    • (2013) Biochem. Pharmacol.
    • Wischik, C.M.1    Harrington, C.R.2    Storey, J.M.3
  • 185
  • 186
    • 84892690719 scopus 로고    scopus 로고
    • Axonal transport rates in vivo are unaltered in Htau mice
    • Yuan, A., Kumar, A., Sasaki, T., Duff, K. & Nixon, R.A. (2013) Axonal transport rates in vivo are unaltered in Htau mice. J. Alzheimers Dis., 37, 579-586.
    • (2013) J. Alzheimers Dis. , vol.37 , pp. 579-586
    • Yuan, A.1    Kumar, A.2    Sasaki, T.3    Duff, K.4    Nixon, R.A.5
  • 187
    • 77955278262 scopus 로고    scopus 로고
    • 'Too much good news' - are Alzheimer mouse models trying to tell us how to prevent, not cure, Alzheimer's disease?
    • Zahs, K.R. & Ashe, K.H. (2010) 'Too much good news' - are Alzheimer mouse models trying to tell us how to prevent, not cure, Alzheimer's disease? Trends Neurosci., 33, 381-389.
    • (2010) Trends Neurosci. , vol.33 , pp. 381-389
    • Zahs, K.R.1    Ashe, K.H.2
  • 188
    • 84883578547 scopus 로고    scopus 로고
    • β-Amyloid oligomers in aging and Alzheimer's disease
    • Zahs, K.R. & Ashe, K.H. (2013) β-Amyloid oligomers in aging and Alzheimer's disease. Front. Aging Neurosci., 5, 28.
    • (2013) Front. Aging Neurosci. , vol.5 , pp. 28
    • Zahs, K.R.1    Ashe, K.H.2
  • 190
    • 77956587739 scopus 로고    scopus 로고
    • 2+ elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines
    • 2+ elevation, missorting of endogenous tau into dendrites, tau phosphorylation, and destruction of microtubules and spines. J. Neurosci., 30, 11938-11950.
    • (2010) J. Neurosci. , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 191
    • 84887828122 scopus 로고    scopus 로고
    • Amyloid-β oligomers induce synaptic damage via tau-dependent microtubule severing by TTLL6 and spastin
    • Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E. & Mandelkow, E.M. (2013) Amyloid-β oligomers induce synaptic damage via tau-dependent microtubule severing by TTLL6 and spastin. EMBO J., 32, 2920-2937.
    • (2013) EMBO J. , vol.32 , pp. 2920-2937
    • Zempel, H.1    Luedtke, J.2    Kumar, Y.3    Biernat, J.4    Dawson, H.5    Mandelkow, E.6    Mandelkow, E.M.7
  • 192
    • 77951246736 scopus 로고    scopus 로고
    • Inhibition of calcineurin-mediated endocytosis and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors prevents amyloid beta oligomer-induced synaptic disruption
    • Zhao, W.-Q., Santini, F., Breese, R., Ross, D., Zhang, X.D., Stone, D.J., Ferrer, M., Townsend, M., Wolfe, A.L., Seager, M.A., Kinney, G.G., Shughrue, P.J. & Ray, W.J. (2010) Inhibition of calcineurin-mediated endocytosis and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors prevents amyloid beta oligomer-induced synaptic disruption. J. Biol. Chem., 285, 7619-7632.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7619-7632
    • Zhao, W.-Q.1    Santini, F.2    Breese, R.3    Ross, D.4    Zhang, X.D.5    Stone, D.J.6    Ferrer, M.7    Townsend, M.8    Wolfe, A.L.9    Seager, M.A.10    Kinney, G.G.11    Shughrue, P.J.12    Ray, W.J.13


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