메뉴 건너뛰기




Volumn 76, Issue PART A, 2014, Pages 1-8

A role for tau at the synapse in Alzheimer's disease pathogenesis

Author keywords

Alzheimer's disease; Neurodegeneration; Synapse; Synaptotoxicity; Tau

Indexed keywords

AMYLOID PROTEIN; KINESIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEUROTRANSMITTER RECEPTOR; SYNAPTOPHYSIN; TAU PROTEIN;

EID: 84886509822     PISSN: 00283908     EISSN: 18737064     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2013.09.018     Document Type: Review
Times cited : (142)

References (120)
  • 2
    • 67349213205 scopus 로고    scopus 로고
    • Synaptic degeneration in Alzheimer's disease
    • T. Arendt Synaptic degeneration in Alzheimer's disease Acta Neuropathol. 118 2009 167 179
    • (2009) Acta Neuropathol. , vol.118 , pp. 167-179
    • Arendt, T.1
  • 4
    • 35148870841 scopus 로고    scopus 로고
    • Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment
    • DOI 10.1523/JNEUROSCI.3269-07.2007
    • K.F. Bell, D.A. Bennett, and A.C. Cuello Paradoxical upregulation of glutamatergic presynaptic boutons during mild cognitive impairment J. Neurosci. 27 2007 10810 10817 (Pubitemid 47535872)
    • (2007) Journal of Neuroscience , vol.27 , Issue.40 , pp. 10810-10817
    • Bell, K.F.S.1    Bennett, D.A.2    Cuello, A.C.3
  • 6
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and tau
    • DOI 10.1074/jbc.M505895200
    • K. Bhaskar, S.H. Yen, and G. Lee Disease-related modifications in tau affect the interaction between fyn and tau J. Biol. Chem. 280 2005 35119 35125 (Pubitemid 41532698)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.-H.2    Lee, G.3
  • 7
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice
    • M. Bi, A. Ittner, Y.D. Ke, J. Gotz, and L.M. Ittner Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice PLoS One 6 2011 e26860
    • (2011) PLoS One , vol.6 , pp. 26860
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 8
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • DOI 10.1083/jcb.101.4.1371
    • L.I. Binder, A. Frankfurter, and L.I. Rebhun The distribution of tau in the mammalian central nervous system J. Cell Biol. 101 1985 1371 1378 (Pubitemid 16203754)
    • (1985) Journal of Cell Biology , vol.101 , Issue.4 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 9
    • 79960563632 scopus 로고    scopus 로고
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain
    • A. Boutajangout, J. Ingadottir, P. Davies, and E.M. Sigurdsson Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain J. Neurochem. 118 2011 658 667
    • (2011) J. Neurochem. , vol.118 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 10
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological stageing of Alzheimer-related changes Acta Neuropathol. 82 1991 239 259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 11
    • 0027308924 scopus 로고
    • 396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • DOI 10.1016/0896-6273(93)90057-X
    • G.T. Bramblett, M. Goedert, R. Jakes, S.E. Merrick, J.Q. Trojanowski, and V.M. Lee Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding Neuron 10 1993 1089 1099 (Pubitemid 23194399)
    • (1993) Neuron , vol.10 , Issue.6 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee -, V.M.Y.6
  • 12
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • R. Brandt, J. Leger, and G. Lee Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain J. Cell Biol. 131 1995 1327 1340
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 13
    • 33744964144 scopus 로고    scopus 로고
    • 2+ overload than nonsynaptic mitochondria
    • DOI 10.1074/jbc.M510303200
    • M.R. Brown, P.G. Sullivan, and J.W. Geddes Synaptic mitochondria are more susceptible to Ca2+overload than nonsynaptic mitochondria J. Biol. Chem. 281 2006 11658 11668 (Pubitemid 43855423)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 11658-11668
    • Brown, M.R.1    Sullivan, P.G.2    Geddes, J.W.3
  • 15
    • 0028989895 scopus 로고
    • Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease
    • L.M. Callahan, and P.D. Coleman Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease Neurobiol. Aging 16 1995 311 314
    • (1995) Neurobiol. Aging , vol.16 , pp. 311-314
    • Callahan, L.M.1    Coleman, P.D.2
  • 16
    • 0033025080 scopus 로고    scopus 로고
    • Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles
    • L.M. Callahan, W.A. Vaules, and P.D. Coleman Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles J. Neuropathol. Exp. Neurol. 58 1999 275 287 (Pubitemid 29140968)
    • (1999) Journal of Neuropathology and Experimental Neurology , vol.58 , Issue.3 , pp. 275-287
    • Callahan, L.M.1    Vaules, W.A.2    Coleman, P.D.3
  • 17
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • X. Chai, J.L. Dage, and M. Citron Constitutive secretion of tau protein by an unconventional mechanism Neurobiol. Dis. 48 2012 356 366
    • (2012) Neurobiol. Dis. , vol.48 , pp. 356-366
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 19
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2003.09.001
    • P.D. Coleman, and P.J. Yao Synaptic slaughter in Alzheimer's disease Neurobiol. Aging 24 2003 1023 1027 (Pubitemid 37487880)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 20
    • 84867704094 scopus 로고    scopus 로고
    • The BCM theory of synapse modification at 30: Interaction of theory with experiment
    • L.N. Cooper, and M.F. Bear The BCM theory of synapse modification at 30: interaction of theory with experiment Nat. Rev. Neurosci. 13 2012 798 810
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 798-810
    • Cooper, L.N.1    Bear, M.F.2
  • 21
    • 84881546833 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
    • J.L. Crimins, A. Pooler, M. Polydoro, J.I. Luebke, and T.L. Spires-Jones The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease Ageing Res. Rev. 12 2013 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
  • 22
    • 84878374182 scopus 로고    scopus 로고
    • Electrophysiological changes precede morphological changes to frontal cortical pyramidal neurons in the rTg4510 mouse model of progressive tauopathy
    • J.L. Crimins, A.B. Rocher, and J.I. Luebke Electrophysiological changes precede morphological changes to frontal cortical pyramidal neurons in the rTg4510 mouse model of progressive tauopathy Acta Neuropathol. 124 2012 777 795
    • (2012) Acta Neuropathol. , vol.124 , pp. 777-795
    • Crimins, J.L.1    Rocher, A.B.2    Luebke, J.I.3
  • 23
    • 82355169037 scopus 로고    scopus 로고
    • Homeostatic responses by surviving cortical pyramidal cells in neurodegenerative tauopathy
    • J.L. Crimins, A.B. Rocher, A. Peters, P. Shultz, J. Lewis, and J.I. Luebke Homeostatic responses by surviving cortical pyramidal cells in neurodegenerative tauopathy Acta Neuropathol. 122 2011 551 564
    • (2011) Acta Neuropathol. , vol.122 , pp. 551-564
    • Crimins, J.L.1    Rocher, A.B.2    Peters, A.3    Shultz, P.4    Lewis, J.5    Luebke, J.I.6
  • 25
  • 27
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
    • S.T. DeKosky, and S.W. Scheff Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity Ann. Neurol. 27 1990 457 464 (Pubitemid 20149963)
    • (1990) Annals of Neurology , vol.27 , Issue.5 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 30
    • 23244440196 scopus 로고    scopus 로고
    • The actin cytoskeleton: Integrating form and function at the synapse
    • DOI 10.1146/annurev.neuro.28.061604.135757
    • C. Dillon, and Y. Goda The actin cytoskeleton: integrating form and function at the synapse Annu. Rev. Neurosci. 28 2005 25 55 (Pubitemid 41098898)
    • (2005) Annual Review of Neuroscience , vol.28 , pp. 25-55
    • Dillon, C.1    Goda, Y.2
  • 31
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • DOI 10.1126/science.1152993
    • R. Dixit, J.L. Ross, Y.E. Goldman, and E.L. Holzbaur Differential regulation of dynein and kinesin motor proteins by tau Science 319 2008 1086 1089 (Pubitemid 351300789)
    • (2008) Science , vol.319 , Issue.5866 , pp. 1086-1089
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.F.4
  • 32
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • D.N. Drechsel, A.A. Hyman, M.H. Cobb, and M.W. Kirschner Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau Mol. Biol. Cell 3 1992 1141 1154 (Pubitemid 23088964)
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.10 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 33
    • 84878586555 scopus 로고    scopus 로고
    • Why size matters - Balancing mitochondrial dynamics in Alzheimer's disease
    • B. Duboff, M. Feany, and J. Gotz Why size matters - balancing mitochondrial dynamics in Alzheimer's disease Trends Neurosci. 36 2013 325 335
    • (2013) Trends Neurosci. , vol.36 , pp. 325-335
    • Duboff, B.1    Feany, M.2    Gotz, J.3
  • 34
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • B. DuBoff, J. Gotz, and M.B. Feany Tau promotes neurodegeneration via DRP1 mislocalization in vivo Neuron 75 2012 618 632
    • (2012) Neuron , vol.75 , pp. 618-632
    • Duboff, B.1    Gotz, J.2    Feany, M.B.3
  • 36
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • C. Duyckaerts, B. Delatour, and M.C. Potier Classification and basic pathology of Alzheimer disease Acta Neuropathol. 118 2009 5 36
    • (2009) Acta Neuropathol. , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 40
    • 77950940279 scopus 로고    scopus 로고
    • Drosophila models of human tauopathies indicate that tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein
    • S. Feuillette, L. Miguel, T. Frebourg, D. Campion, and M. Lecourtois Drosophila models of human tauopathies indicate that tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein J. Neurochem. 113 2010 895 903
    • (2010) J. Neurochem. , vol.113 , pp. 895-903
    • Feuillette, S.1    Miguel, L.2    Frebourg, T.3    Campion, D.4    Lecourtois, M.5
  • 42
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • DOI 10.1038/ncb1528, PII NCB1528
    • T.A. Fulga, I. Elson-Schwab, V. Khurana, M.L. Steinhilb, T.L. Spires, B.T. Hyman, and M.B. Feany Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo Nat. Cell Biol. 9 2007 139 148 (Pubitemid 46420856)
    • (2007) Nature Cell Biology , vol.9 , Issue.2 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhilb, M.L.4    Spires, T.L.5    Hyman, B.T.6    Feany, M.B.7
  • 46
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
    • A. Gomez-Ramos, M. Diaz-Hernandez, A. Rubio, M.T. Miras-Portugal, and J. Avila Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells Mol. Cell Neurosci. 37 2008 673 681
    • (2008) Mol. Cell Neurosci. , vol.37 , pp. 673-681
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 47
    • 77955328980 scopus 로고    scopus 로고
    • Fyn-tau-amyloid: A toxic triad
    • C. Haass, and E. Mandelkow Fyn-tau-amyloid: a toxic triad Cell 142 2010 356 358
    • (2010) Cell , vol.142 , pp. 356-358
    • Haass, C.1    Mandelkow, E.2
  • 48
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • D.P. Hanger, B.H. Anderton, and W. Noble Tau phosphorylation: the therapeutic challenge for neurodegenerative disease Trends Mol. Med. 15 2009 112 119
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 50
    • 84866681445 scopus 로고    scopus 로고
    • Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits
    • J.A. Harris, A. Koyama, S. Maeda, K. Ho, N. Devidze, D.B. Dubal, G.Q. Yu, E. Masliah, and L. Mucke Human P301L-mutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits PLoS One 7 2012 e45881
    • (2012) PLoS One , vol.7 , pp. 45881
    • Harris, J.A.1    Koyama, A.2    Maeda, S.3    Ho, K.4    Devidze, N.5    Dubal, D.B.6    Yu, G.Q.7    Masliah, E.8    Mucke, L.9
  • 54
    • 77957254409 scopus 로고    scopus 로고
    • Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease
    • K. Iijima, A. Gatt, and K. Iijima-Ando Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease Hum. Mol. Genet. 19 2010 2947 2957
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2947-2957
    • Iijima, K.1    Gatt, A.2    Iijima-Ando, K.3
  • 55
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • DOI 10.1016/S0304-3940(99)00964-7, PII S0304394099009647
    • S. Ikegami, A. Harada, and N. Hirokawa Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice Neurosci. Lett. 279 2000 129 132 (Pubitemid 30069810)
    • (2000) Neuroscience Letters , vol.279 , Issue.3 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 56
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease
    • L.M. Ittner, and J. Gotz Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease Nat. Rev. Neurosci. 12 2011 65 72
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 58
    • 84871982184 scopus 로고    scopus 로고
    • Synaptic vesicle exocytosis in hippocampal synaptosomes correlates directly with total mitochondrial volume
    • M.V. Ivannikov, M. Sugimori, and R.R. Llinas Synaptic vesicle exocytosis in hippocampal synaptosomes correlates directly with total mitochondrial volume J. Mol. Neurosci. 49 2013 223 230
    • (2013) J. Mol. Neurosci. , vol.49 , pp. 223-230
    • Ivannikov, M.V.1    Sugimori, M.2    Llinas, R.R.3
  • 59
    • 33750404114 scopus 로고    scopus 로고
    • Neurofibrillary tangle-related synaptic alterations of spinal motor neurons of P301L tau transgenic mice
    • DOI 10.1016/j.neulet.2006.09.021, PII S0304394006009608
    • O. Katsuse, W.L. Lin, J. Lewis, M.L. Hutton, and D.W. Dickson Neurofibrillary tangle-related synaptic alterations of spinal motor neurons of P301L tau transgenic mice Neurosci. Lett. 409 2006 95 99 (Pubitemid 44637252)
    • (2006) Neuroscience Letters , vol.409 , Issue.2 , pp. 95-99
    • Katsuse, O.1    Lin, W.-L.2    Lewis, J.3    Hutton, M.L.4    Dickson, D.W.5
  • 61
    • 77049123465 scopus 로고    scopus 로고
    • Interneuronal transfer of human tau between Lamprey central neurons in situ
    • W. Kim, S. Lee, C. Jung, A. Ahmed, G. Lee, and G.F. Hall Interneuronal transfer of human tau between Lamprey central neurons in situ J. Alzheimers Dis. 19 2010 647 664
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 647-664
    • Kim, W.1    Lee, S.2    Jung, C.3    Ahmed, A.4    Lee, G.5    Hall, G.F.6
  • 64
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • H.C. Kornau, L.T. Schenker, M.B. Kennedy, and P.H. Seeburg Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95 Science 269 1995 1737 1740
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 68
    • 84864976166 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer disease: The challenge of adverse effects
    • Y.H. Liu, B. Giunta, H.D. Zhou, J. Tan, and Y.J. Wang Immunotherapy for Alzheimer disease: the challenge of adverse effects Nat. Rev. Neurol. 8 2012 465 469
    • (2012) Nat. Rev. Neurol. , vol.8 , pp. 465-469
    • Liu, Y.H.1    Giunta, B.2    Zhou, H.D.3    Tan, J.4    Wang, Y.J.5
  • 70
    • 84876078566 scopus 로고    scopus 로고
    • The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of abeta oligomers through tau phosphorylation
    • G. Mairet-Coello, J. Courchet, S. Pieraut, V. Courchet, A. Maximov, and F. Polleux The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of abeta oligomers through tau phosphorylation Neuron 78 2013 94 108
    • (2013) Neuron , vol.78 , pp. 94-108
    • Mairet-Coello, G.1    Courchet, J.2    Pieraut, S.3    Courchet, V.4    Maximov, A.5    Polleux, F.6
  • 72
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • DOI 10.1016/j.neurobiolaging.2003.04.007
    • E.M. Mandelkow, K. Stamer, R. Vogel, E. Thies, and E. Mandelkow Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses Neurobiol. Aging 24 2003 1079 1085 (Pubitemid 37487885)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1079-1085
    • Mandelkow, E.-M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 73
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • DOI 10.1016/0304-3940(89)90582-X
    • E. Masliah, R.D. Terry, R.M. DeTeresa, and L.A. Hansen Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease Neurosci. Lett. 103 1989 234 239 (Pubitemid 19201259)
    • (1989) Neuroscience Letters , vol.103 , Issue.2 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 74
    • 73549117464 scopus 로고    scopus 로고
    • Excitatory amino acid involvement in dendritic spine formation, maintenance and remodelling
    • R.A. McKinney Excitatory amino acid involvement in dendritic spine formation, maintenance and remodelling J. Physiol. 588 2010 107 116
    • (2010) J. Physiol. , vol.588 , pp. 107-116
    • McKinney, R.A.1
  • 75
    • 84866361333 scopus 로고    scopus 로고
    • Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D-aspartate receptor-dependent tau phosphorylation
    • S. Mondragon-Rodriguez, E. Trillaud-Doppia, A. Dudilot, C. Bourgeois, M. Lauzon, N. Leclerc, and J. Boehm Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D-aspartate receptor-dependent tau phosphorylation J. Biol. Chem. 287 2012 32040 32053
    • (2012) J. Biol. Chem. , vol.287 , pp. 32040-32053
    • Mondragon-Rodriguez, S.1    Trillaud-Doppia, E.2    Dudilot, A.3    Bourgeois, C.4    Lauzon, M.5    Leclerc, N.6    Boehm, J.7
  • 80
    • 70149098692 scopus 로고    scopus 로고
    • Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau
    • S. Perreault, O. Bousquet, M. Lauzon, J. Paiement, and N. Leclerc Increased association between rough endoplasmic reticulum membranes and mitochondria in transgenic mice that express P301L tau J. Neuropathol. Exp. Neurol. 68 2009 503 514
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 503-514
    • Perreault, S.1    Bousquet, O.2    Lauzon, M.3    Paiement, J.4    Leclerc, N.5
  • 82
    • 69449093036 scopus 로고    scopus 로고
    • Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology
    • M. Polydoro, C.M. Acker, K. Duff, P.E. Castillo, and P. Davies Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology J. Neurosci. 29 2009 10741 10749
    • (2009) J. Neurosci. , vol.29 , pp. 10741-10749
    • Polydoro, M.1    Acker, C.M.2    Duff, K.3    Castillo, P.E.4    Davies, P.5
  • 83
    • 77955941947 scopus 로고    scopus 로고
    • Functional implications of the association of tau with the plasma membrane
    • A.M. Pooler, and D.P. Hanger Functional implications of the association of tau with the plasma membrane Biochem. Soc. Trans. 38 2010 1012 1015
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1012-1015
    • Pooler, A.M.1    Hanger, D.P.2
  • 84
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • A.M. Pooler, E.C. Phillips, D.H. Lau, W. Noble, and D.P. Hanger Physiological release of endogenous tau is stimulated by neuronal activity EMBO Rep. 14 2013 389 394
    • (2013) EMBO Rep. , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 87
    • 80052846665 scopus 로고    scopus 로고
    • Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
    • P.H. Reddy Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease Brain Res. 1415 2011 136 148
    • (2011) Brain Res. , vol.1415 , pp. 136-148
    • Reddy, P.H.1
  • 89
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • DOI 10.1126/science.1141736
    • E.D. Roberson, K. Scearce-Levie, J.J. Palop, F. Yan, I.H. Cheng, T. Wu, H. Gerstein, G.Q. Yu, and L. Mucke Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model Science 316 2007 750 754 (Pubitemid 46717684)
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.-Q.8    Mucke, L.9
  • 92
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • S. Saman, W. Kim, M. Raya, Y. Visnick, S. Miro, B. Jackson, A.C. McKee, V.E. Alvarez, N.C. Lee, and G.F. Hall Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease J. Biol. Chem. 287 2012 3842 3849
    • (2012) J. Biol. Chem. , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Jackson, B.6    McKee, A.C.7    Alvarez, V.E.8    Lee, N.C.9    Hall, G.F.10
  • 94
    • 84859230759 scopus 로고    scopus 로고
    • Tau's role in the developing brain: Implications for intellectual disability
    • T. Sapir, M. Frotscher, T. Levy, E.M. Mandelkow, and O. Reiner Tau's role in the developing brain: implications for intellectual disability Hum. Mol. Genet. 21 2012 1681 1692
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1681-1692
    • Sapir, T.1    Frotscher, M.2    Levy, T.3    Mandelkow, E.M.4    Reiner, O.5
  • 96
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • DOI 10.1126/science.1074069
    • D.J. Selkoe Alzheimer's disease is a synaptic failure Science 298 2002 789 791 (Pubitemid 35231524)
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 98
    • 84857073309 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease
    • K. Shahpasand, I. Uemura, T. Saito, T. Asano, K. Hata, K. Shibata, Y. Toyoshima, M. Hasegawa, and S. Hisanaga Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease J. Neurosci. 32 2012 2430 2441
    • (2012) J. Neurosci. , vol.32 , pp. 2430-2441
    • Shahpasand, K.1    Uemura, I.2    Saito, T.3    Asano, T.4    Hata, K.5    Shibata, K.6    Toyoshima, Y.7    Hasegawa, M.8    Hisanaga, S.9
  • 101
    • 84876850027 scopus 로고    scopus 로고
    • Pathogenesis of abeta oligomers in synaptic failure
    • S. Sivanesan, A. Tan, and J. Rajadas Pathogenesis of abeta oligomers in synaptic failure Curr. Alzheimer Res. 10 2013 316 323
    • (2013) Curr. Alzheimer Res. , vol.10 , pp. 316-323
    • Sivanesan, S.1    Tan, A.2    Rajadas, J.3
  • 102
    • 77955924937 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • B. Solomon, and D. Frenkel Immunotherapy for Alzheimer's disease Neuropharmacology 59 2010 303 309
    • (2010) Neuropharmacology , vol.59 , pp. 303-309
    • Solomon, B.1    Frenkel, D.2
  • 103
    • 78650914558 scopus 로고    scopus 로고
    • Tubulin-independent tau in Alzheimer's disease and cancer: Implications for disease pathogenesis and treatment
    • S. Souter, and G. Lee Tubulin-independent tau in Alzheimer's disease and cancer: implications for disease pathogenesis and treatment Curr. Alzheimer Res. 7 2010 697 707
    • (2010) Curr. Alzheimer Res. , vol.7 , pp. 697-707
    • Souter, S.1    Lee, G.2
  • 104
    • 33646519920 scopus 로고    scopus 로고
    • Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy
    • T.L. Spires, J.D. Orne, K. SantaCruz, R. Pitstick, G.A. Carlson, K.H. Ashe, and B.T. Hyman Region-specific dissociation of neuronal loss and neurofibrillary pathology in a mouse model of tauopathy Am. J. Pathol. 168 2006 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
  • 106
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • DOI 10.1083/jcb.200108057
    • K. Stamer, R. Vogel, E. Thies, E. Mandelkow, and E.M. Mandelkow Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress J. Cell Biol. 156 2002 1051 1063 (Pubitemid 34839854)
    • (2002) Journal of Cell Biology , vol.156 , Issue.6 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.-M.5
  • 107
    • 84881611195 scopus 로고    scopus 로고
    • Motile axonal mitochondria contribute to the variability of presynaptic strength
    • T. Sun, H. Qiao, P.Y. Pan, Y. Chen, and Z.H. Sheng Motile axonal mitochondria contribute to the variability of presynaptic strength Cell Rep. 4 2013 413 419
    • (2013) Cell Rep. , vol.4 , pp. 413-419
    • Sun, T.1    Qiao, H.2    Pan, P.Y.3    Chen, Y.4    Sheng, Z.H.5
  • 110
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • H.C. Tai, A. Serrano-Pozo, T. Hashimoto, M.P. Frosch, T.L. Spires-Jones, and B.T. Hyman The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system Am. J. Pathol. 181 2012 1426 1435
    • (2012) Am. J. Pathol. , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 111
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • R.D. Terry, E. Masliah, D.P. Salmon, N. Butters, R. DeTeresa, R. Hill, L.A. Hansen, and R. Katzman Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment Ann. Neurol. 30 1991 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
  • 112
    • 83655192092 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by the tyrosine kinase Fyn
    • C.H. Trepanier, M.F. Jackson, and J.F. MacDonald Regulation of NMDA receptors by the tyrosine kinase Fyn FEBS J. 279 2012 12 19
    • (2012) FEBS J. , vol.279 , pp. 12-19
    • Trepanier, C.H.1    Jackson, M.F.2    Macdonald, J.F.3
  • 113
    • 79961025441 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau
    • A. Usardi, A.M. Pooler, A. Seereeram, C.H. Reynolds, P. Derkinderen, B. Anderton, D.P. Hanger, W. Noble, and R. Williamson Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau FEBS J. 278 2011 2927 2937
    • (2011) FEBS J. , vol.278 , pp. 2927-2937
    • Usardi, A.1    Pooler, A.M.2    Seereeram, A.3    Reynolds, C.H.4    Derkinderen, P.5    Anderton, B.6    Hanger, D.P.7    Noble, W.8    Williamson, R.9
  • 114
    • 27844470590 scopus 로고    scopus 로고
    • Molecular motors implicated in the axonal transport of tau and α-synuclein
    • DOI 10.1242/jcs.02558
    • M.A. Utton, W.J. Noble, J.E. Hill, B.H. Anderton, and D.P. Hanger Molecular motors implicated in the axonal transport of tau and alpha-synuclein J. Cell Sci. 118 2005 4645 4654 (Pubitemid 41646375)
    • (2005) Journal of Cell Science , vol.118 , Issue.20 , pp. 4645-4654
    • Utton, M.A.1    Noble, W.J.2    Hill, J.E.3    Anderton, B.H.4
  • 116
    • 83455181308 scopus 로고    scopus 로고
    • Synaptic mitochondria in synaptic transmission and organization of vesicle pools in health and disease
    • M. Vos, E. Lauwers, and P. Verstreken Synaptic mitochondria in synaptic transmission and organization of vesicle pools in health and disease Front Synaptic Neurosci. 2 2010 139
    • (2010) Front Synaptic Neurosci. , vol.2 , pp. 139
    • Vos, M.1    Lauwers, E.2    Verstreken, P.3
  • 117
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • X. Wang, B. Su, H.G. Lee, X. Li, G. Perry, M.A. Smith, and X. Zhu Impaired balance of mitochondrial fission and fusion in Alzheimer's disease J. Neurosci. 29 2009 9090 9103
    • (2009) J. Neurosci. , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 118
    • 0037343844 scopus 로고    scopus 로고
    • Defects in expression of genes related to synaptic vesicle trafficking in frontal cortex of Alzheimer's disease
    • DOI 10.1016/S0969-9961(02)00009-8
    • P.J. Yao, M. Zhu, E.I. Pyun, A.I. Brooks, S. Therianos, V.E. Meyers, and P.D. Coleman Defects in expression of genes related to synaptic vesicle trafficking in frontal cortex of Alzheimer's disease Neurobiol. Dis. 12 2003 97 109 (Pubitemid 36355860)
    • (2003) Neurobiology of Disease , vol.12 , Issue.2 , pp. 97-109
    • Yao, P.J.1    Zhu, M.2    Pyun, E.I.3    Brooks, A.I.4    Therianos, S.5    Meyers, V.E.6    Coleman, P.D.7
  • 119
    • 84879968745 scopus 로고    scopus 로고
    • Developing therapeutic antibodies for neurodegenerative disease
    • Y.J. Yu, and R.J. Watts Developing therapeutic antibodies for neurodegenerative disease Neurotherapeutics 10 2013 459 472
    • (2013) Neurotherapeutics , vol.10 , pp. 459-472
    • Yu, Y.J.1    Watts, R.J.2
  • 120
    • 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 2010 11938 11950
    • (2010) J. Neurosci. , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.