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Volumn 43, Issue 8, 2012, Pages 645-654

Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome

Author keywords

Alzheimer's disease; Amyloid precursor protein; Down syndrome; Dyrk1A; Rcan; Tau protein

Indexed keywords

AMYLOID PRECURSOR PROTEIN; TAU PROTEIN;

EID: 84871662000     PISSN: 01884409     EISSN: 18735487     Source Type: Journal    
DOI: 10.1016/j.arcmed.2012.10.012     Document Type: Review
Times cited : (54)

References (163)
  • 1
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M., Spillantini M.G., Jakes R., et al. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989, 3:519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3
  • 2
    • 0028153168 scopus 로고
    • Diversity of high-molecular-weight tau proteins in different regions of the nervous system
    • Mavilia C., Couchie D., Nunez J. Diversity of high-molecular-weight tau proteins in different regions of the nervous system. J Neurochem 1994, 63:2300-2306.
    • (1994) J Neurochem , vol.63 , pp. 2300-2306
    • Mavilia, C.1    Couchie, D.2    Nunez, J.3
  • 3
    • 0024641959 scopus 로고
    • Developmentally regulated expression of specific tau sequences
    • Kosik K.S., Orecchio L.D., Bakalis S., et al. Developmentally regulated expression of specific tau sequences. Neuron 1989, 2:1389-1397.
    • (1989) Neuron , vol.2 , pp. 1389-1397
    • Kosik, K.S.1    Orecchio, L.D.2    Bakalis, S.3
  • 4
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M., Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 1990, 9:4225-4230.
    • (1990) EMBO J , vol.9 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 5
    • 0042924434 scopus 로고    scopus 로고
    • Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease
    • Panda D., Samuel J.C., Massie M., et al. Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease. Proc Natl Acad Sci USA 2003, 100:9548-9553.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3
  • 6
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode B.L., Feinstein S.C. Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau. J Cell Biol 1994, 124:769-782.
    • (1994) J Cell Biol , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 7
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee G., Neve R.L., Kosik K.S. The microtubule binding domain of tau protein. Neuron 1989, 2:1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 8
    • 57649134248 scopus 로고    scopus 로고
    • Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome
    • Shi J., Zhang T., Zhou C., et al. Increased dosage of Dyrk1A alters alternative splicing factor (ASF)-regulated alternative splicing of tau in Down syndrome. J Biol Chem 2008, 283:28660-28669.
    • (2008) J Biol Chem , vol.283 , pp. 28660-28669
    • Shi, J.1    Zhang, T.2    Zhou, C.3
  • 9
    • 0036892302 scopus 로고    scopus 로고
    • Tau gene mutations: dissecting the pathogenesis of FTDP-17
    • Ingram E.M., Spillantini M.G. Tau gene mutations: dissecting the pathogenesis of FTDP-17. Trends Mol Med 2002, 8:555-562.
    • (2002) Trends Mol Med , vol.8 , pp. 555-562
    • Ingram, E.M.1    Spillantini, M.G.2
  • 10
    • 33846080979 scopus 로고    scopus 로고
    • The DeltaK280 mutation in MAP tau favors exon 10 skipping in vivo
    • van Swieten J.C., Bronner I.F., Azmani A., et al. The DeltaK280 mutation in MAP tau favors exon 10 skipping in vivo. J Neuropathol Exp Neurol 2007, 66:17-25.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 17-25
    • van Swieten, J.C.1    Bronner, I.F.2    Azmani, A.3
  • 11
    • 27644460461 scopus 로고    scopus 로고
    • Hereditary Pick's disease with the G272V tau mutation shows predominant three-repeat tau pathology
    • Bronner I.F., ter Meulen B.C., Azmani A., et al. Hereditary Pick's disease with the G272V tau mutation shows predominant three-repeat tau pathology. Brain 2005, 128:2645-2653.
    • (2005) Brain , vol.128 , pp. 2645-2653
    • Bronner, I.F.1    ter Meulen, B.C.2    Azmani, A.3
  • 12
    • 0032859650 scopus 로고    scopus 로고
    • Overexpression of four-repeat tau mRNA isoforms in progressive supranuclear palsy but not in Alzheimer's disease
    • Chambers C.B., Lee J.M., Troncoso J.C., et al. Overexpression of four-repeat tau mRNA isoforms in progressive supranuclear palsy but not in Alzheimer's disease. Ann Neurol 1999, 46:325-332.
    • (1999) Ann Neurol , vol.46 , pp. 325-332
    • Chambers, C.B.1    Lee, J.M.2    Troncoso, J.C.3
  • 13
    • 34948883291 scopus 로고    scopus 로고
    • Increase in the relative expression of tau with four microtubule binding repeat regions in frontotemporal lobar degeneration and progressive supranuclear palsy brains
    • Ingelsson M., Ramasamy K., Russ C., et al. Increase in the relative expression of tau with four microtubule binding repeat regions in frontotemporal lobar degeneration and progressive supranuclear palsy brains. Acta Neuropathol 2007, 114:471-479.
    • (2007) Acta Neuropathol , vol.114 , pp. 471-479
    • Ingelsson, M.1    Ramasamy, K.2    Russ, C.3
  • 14
    • 80053167649 scopus 로고    scopus 로고
    • MicroRNA-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy
    • Smith P.Y., Delay C., Girard J., et al. MicroRNA-132 loss is associated with tau exon 10 inclusion in progressive supranuclear palsy. Hum Mol Genet 2011, 20:4016-4024.
    • (2011) Hum Mol Genet , vol.20 , pp. 4016-4024
    • Smith, P.Y.1    Delay, C.2    Girard, J.3
  • 15
    • 0035146717 scopus 로고    scopus 로고
    • Distinct isoforms of tau aggregated in neurons and glial cells in brains of patients with Pick's disease, corticobasal degeneration and progressive supranuclear palsy
    • Arai T., Ikeda K., Akiyama H., et al. Distinct isoforms of tau aggregated in neurons and glial cells in brains of patients with Pick's disease, corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol 2001, 101:167-173.
    • (2001) Acta Neuropathol , vol.101 , pp. 167-173
    • Arai, T.1    Ikeda, K.2    Akiyama, H.3
  • 16
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G., Cole R.D. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem 1984, 259:5301-5305.
    • (1984) J Biol Chem , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 17
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat J., Gustke N., Drewes G., et al. Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 1993, 11:153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3
  • 18
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett G.T., Goedert M., Jakes R., et al. Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron 1993, 10:1089-1099.
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3
  • 19
    • 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., et al. Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation. J Cell Sci 1996, 109:1537-1543.
    • (1996) J Cell Sci , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3
  • 20
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A., Biernat J., von Bergen M., et al. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 1999, 38:3549-3558.
    • (1999) Biochemistry , vol.38 , pp. 3549-3558
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3
  • 21
    • 0037855706 scopus 로고    scopus 로고
    • Tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules
    • Takahashi S., Saito T., Hisanaga S., et al. Tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules. J Biol Chem 2003, 278:10506-10515.
    • (2003) J Biol Chem , vol.278 , pp. 10506-10515
    • Takahashi, S.1    Saito, T.2    Hisanaga, S.3
  • 22
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • Hanger D.P., Anderton B.H., Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 2009, 15:112-119.
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 23
    • 10944228450 scopus 로고    scopus 로고
    • Tau and src family tyrosine kinases
    • Lee G. Tau and src family tyrosine kinases. Biochim Biophys Acta 2005, 1739:323-330.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 323-330
    • Lee, G.1
  • 24
    • 0034067992 scopus 로고    scopus 로고
    • Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta
    • Reynolds C.H., Betts J.C., Blackstock W.P., et al. Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. J Neurochem 2000, 74:1587-1595.
    • (2000) J Neurochem , vol.74 , pp. 1587-1595
    • Reynolds, C.H.1    Betts, J.C.2    Blackstock, W.P.3
  • 25
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: physiological and pathological consequences
    • Stoothoff W.H., Johnson G.V. Tau phosphorylation: physiological and pathological consequences. Biochim Biophys Acta 2005, 1739:280-297.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 26
    • 0031007546 scopus 로고    scopus 로고
    • Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration
    • Billingsley M.L., Kincaid R.L. Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J 1997, 323:577-591.
    • (1997) Biochem J , vol.323 , pp. 577-591
    • Billingsley, M.L.1    Kincaid, R.L.2
  • 27
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso A.C., Zaidi T., Grundke-Iqbal I., et al. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci USA 1994, 91:5562-5566.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3
  • 28
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso A.C., Grundke-Iqbal I., Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 1996, 2:783-787.
    • (1996) Nat Med , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 29
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • Alonso A., Zaidi T., Novak M., et al. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci USA 2001, 98:6923-6928.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6923-6928
    • Alonso, A.1    Zaidi, T.2    Novak, M.3
  • 30
    • 33646922314 scopus 로고    scopus 로고
    • Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3
    • Engel T., Hernandez F., Avila J., et al. Full reversal of Alzheimer's disease-like phenotype in a mouse model with conditional overexpression of glycogen synthase kinase-3. J Neurosci 2006, 26:5083-5090.
    • (2006) J Neurosci , vol.26 , pp. 5083-5090
    • Engel, T.1    Hernandez, F.2    Avila, J.3
  • 31
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F., Angelo M., Giese K.P. The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J Biol Chem 2006, 281:25457-25465.
    • (2006) J Biol Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 32
    • 34547653872 scopus 로고    scopus 로고
    • Tau phosphorylation by GSK-3beta promotes tangle-like filament morphology
    • Rankin C.A., Sun Q., Gamblin T.C. Tau phosphorylation by GSK-3beta promotes tangle-like filament morphology. Mol Neurodegener 2007, 2:12.
    • (2007) Mol Neurodegener , vol.2 , pp. 12
    • Rankin, C.A.1    Sun, Q.2    Gamblin, T.C.3
  • 33
    • 0032578024 scopus 로고    scopus 로고
    • Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
    • Pei J.J., Grundke-Iqbal I., Iqbal K., et al. Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res 1998, 797:267-277.
    • (1998) Brain Res , vol.797 , pp. 267-277
    • Pei, J.J.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 34
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • Cruz J.C., Tseng H.C., Goldman J.A., et al. Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron 2003, 40:471-483.
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3
  • 35
    • 33644849088 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta
    • Li T., Hawkes C., Qureshi H.Y., et al. Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3beta. Biochemistry 2006, 45:3134-3145.
    • (2006) Biochemistry , vol.45 , pp. 3134-3145
    • Li, T.1    Hawkes, C.2    Qureshi, H.Y.3
  • 36
    • 80052795886 scopus 로고    scopus 로고
    • Potentiation of tau aggregation by cdk5 and GSK3β
    • Lee S., Hall G.F., Shea T.B. Potentiation of tau aggregation by cdk5 and GSK3β. J Alzheimers Dis 2011, 26:355-364.
    • (2011) J Alzheimers Dis , vol.26 , pp. 355-364
    • Lee, S.1    Hall, G.F.2    Shea, T.B.3
  • 37
    • 22244475384 scopus 로고    scopus 로고
    • Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase
    • Derkinderen P., Scales T.M., Hanger D.P., et al. Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J Neurosci 2005, 25:6584-6593.
    • (2005) J Neurosci , vol.25 , pp. 6584-6593
    • Derkinderen, P.1    Scales, T.M.2    Hanger, D.P.3
  • 38
    • 79960566233 scopus 로고    scopus 로고
    • AMP-activated protein kinase. A potential player in Alzheimer's disease
    • Salminen A., Kaarniranta K., Haapasalo A., et al. AMP-activated protein kinase. A potential player in Alzheimer's disease. J Neurochem 2011, 118:460-474.
    • (2011) J Neurochem , vol.118 , pp. 460-474
    • Salminen, A.1    Kaarniranta, K.2    Haapasalo, A.3
  • 39
    • 77049126656 scopus 로고    scopus 로고
    • Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase
    • Tremblay M.A., Acker C.M., Davies P. Tau phosphorylated at tyrosine 394 is found in Alzheimer's disease tangles and can be a product of the Abl-related kinase. Arg. J Alzheimers Dis 2010, 19:721-733.
    • (2010) Arg. J Alzheimers Dis , vol.19 , pp. 721-733
    • Tremblay, M.A.1    Acker, C.M.2    Davies, P.3
  • 40
    • 79251556232 scopus 로고    scopus 로고
    • Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-beta peptide degradation
    • Vingtdeux V., Chandakkar P., Zhao H., et al. Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-beta peptide degradation. FASEB J 2011, 25:219-231.
    • (2011) FASEB J , vol.25 , pp. 219-231
    • Vingtdeux, V.1    Chandakkar, P.2    Zhao, H.3
  • 41
    • 26944433068 scopus 로고    scopus 로고
    • Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models
    • Ferrer I., Barrachina M., Puig B., et al. Constitutive Dyrk1A is abnormally expressed in Alzheimer disease, Down syndrome, Pick disease, and related transgenic models. Neurobiol Dis 2005, 20:392-400.
    • (2005) Neurobiol Dis , vol.20 , pp. 392-400
    • Ferrer, I.1    Barrachina, M.2    Puig, B.3
  • 42
    • 51349109221 scopus 로고    scopus 로고
    • Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome
    • Liu F., Liang Z., Wegiel J., et al. Overexpression of Dyrk1A contributes to neurofibrillary degeneration in Down syndrome. FASEB J 2008, 22:3224-3233.
    • (2008) FASEB J , vol.22 , pp. 3224-3233
    • Liu, F.1    Liang, Z.2    Wegiel, J.3
  • 43
    • 36849075621 scopus 로고    scopus 로고
    • DYRK1A-mediated hyperphosphorylation of Tau. A functional link between Down syndrome and Alzheimer disease
    • Ryoo S.R., Jeong H.K., Radnaabazar C., et al. DYRK1A-mediated hyperphosphorylation of Tau. A functional link between Down syndrome and Alzheimer disease. J Biol Chem 2007, 282:34850-34857.
    • (2007) J Biol Chem , vol.282 , pp. 34850-34857
    • Ryoo, S.R.1    Jeong, H.K.2    Radnaabazar, C.3
  • 44
    • 51849158177 scopus 로고    scopus 로고
    • The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome
    • Wegiel J., Dowjat K., Kaczmarski W., et al. The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome. Acta Neuropathol 2008, 116:391-407.
    • (2008) Acta Neuropathol , vol.116 , pp. 391-407
    • Wegiel, J.1    Dowjat, K.2    Kaczmarski, W.3
  • 45
    • 78650679575 scopus 로고    scopus 로고
    • Link between DYRK1A overexpression and several-fold enhancement of neurofibrillary degeneration with 3-repeat tau protein in Down syndrome
    • Wegiel J., Kaczmarski W., Barua M., et al. Link between DYRK1A overexpression and several-fold enhancement of neurofibrillary degeneration with 3-repeat tau protein in Down syndrome. J Neuropathol Exp Neurol 2011, 70:36-50.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 36-50
    • Wegiel, J.1    Kaczmarski, W.2    Barua, M.3
  • 46
    • 0022438889 scopus 로고
    • Biochemical characterization of an immune serum which specifically marks neurons in neurofibrillary degeneration in Alzheimer's disease
    • Delacourte A., Défossez A. Biochemical characterization of an immune serum which specifically marks neurons in neurofibrillary degeneration in Alzheimer's disease. CR Acad Sci III 1986, 303:439-444.
    • (1986) CR Acad Sci III , vol.303 , pp. 439-444
    • Delacourte, A.1    Défossez, A.2
  • 47
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I., Iqbal K., Tung Y.C., et al. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci USA 1986, 83:4913-4917.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3
  • 48
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik K.S., Joachim C.L., Selkoe D.J. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 1986, 83:4044-4048.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 49
    • 0022723508 scopus 로고
    • One of the antigenic determinants of paired helical filaments is related to tau protein
    • Nukina N., Ihara Y. One of the antigenic determinants of paired helical filaments is related to tau protein. J Biochem 1986, 99:1541-1544.
    • (1986) J Biochem , vol.99 , pp. 1541-1544
    • Nukina, N.1    Ihara, Y.2
  • 50
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)
    • Wood J.G., Mirra S.S., Pollock N.J., et al. Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc Natl Acad Sci USA 1986, 83:4040-4043.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3
  • 51
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Ihara Y., Nukina N., Miura R., et al. Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease. J Biochem 1986, 99:1807-1810.
    • (1986) J Biochem , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3
  • 52
    • 0022550260 scopus 로고
    • Defective brain microtubule assembly in Alzheimer's disease
    • Iqbal K., Grundke-Iqbal I., Zaidi T., et al. Defective brain microtubule assembly in Alzheimer's disease. Lancet 1986, 2:421-426.
    • (1986) Lancet , vol.2 , pp. 421-426
    • Iqbal, K.1    Grundke-Iqbal, I.2    Zaidi, T.3
  • 53
    • 0023635030 scopus 로고
    • Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders
    • Joachim C.L., Morris J.H., Kosik K.S., et al. Tau antisera recognize neurofibrillary tangles in a range of neurodegenerative disorders. Ann Neurol 1987, 22:514-520.
    • (1987) Ann Neurol , vol.22 , pp. 514-520
    • Joachim, C.L.1    Morris, J.H.2    Kosik, K.S.3
  • 54
    • 0024589232 scopus 로고
    • Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam
    • Shankar S.K., Yanagihara R., Garruto R.M., et al. Immunocytochemical characterization of neurofibrillary tangles in amyotrophic lateral sclerosis and parkinsonism-dementia of Guam. Ann Neurol 1989, 25:146-151.
    • (1989) Ann Neurol , vol.25 , pp. 146-151
    • Shankar, S.K.1    Yanagihara, R.2    Garruto, R.M.3
  • 55
    • 0028929548 scopus 로고
    • Neurofibrillary tangles in Niemann-Pick disease type C
    • Love S., Bridges L.R., Case C.P. Neurofibrillary tangles in Niemann-Pick disease type C. Brain 1995, 118:119-129.
    • (1995) Brain , vol.118 , pp. 119-129
    • Love, S.1    Bridges, L.R.2    Case, C.P.3
  • 56
    • 42249085980 scopus 로고    scopus 로고
    • Refining frontotemporal dementia with parkinsonism linked to chromosome 17: introducing FTDP-17 (MAPT) and FTDP-17 (PGRN)
    • Boeve B.F., Hutton M. Refining frontotemporal dementia with parkinsonism linked to chromosome 17: introducing FTDP-17 (MAPT) and FTDP-17 (PGRN). Arch Neurol 2008, 65:460-464.
    • (2008) Arch Neurol , vol.65 , pp. 460-464
    • Boeve, B.F.1    Hutton, M.2
  • 57
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • Goedert M., Jakes R. Mutations causing neurodegenerative tauopathies. Biochim Biophys Acta 2005, 1739:240-250.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 58
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong M., Zhukareva V., Vogelsberg-Ragaglia V., et al. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 1998, 282:1914-1917.
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1    Zhukareva, V.2    Vogelsberg-Ragaglia, V.3
  • 59
    • 0342368837 scopus 로고    scopus 로고
    • The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules
    • Pérez M., Lim F., Arrasate M., et al. The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules. J Neurochem 2000, 4:2583-2589.
    • (2000) J Neurochem , vol.4 , pp. 2583-2589
    • Pérez, M.1    Lim, F.2    Arrasate, M.3
  • 60
    • 0032561415 scopus 로고    scopus 로고
    • Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly
    • Hasegawa M., Smith M.J., Goedert M. Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly. FEBS Lett 1998, 437:207-210.
    • (1998) FEBS Lett , vol.437 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 61
    • 33744952341 scopus 로고    scopus 로고
    • FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells
    • Bunker J.M., Kamath K., Wilson L., et al. FTDP-17 mutations compromise the ability of tau to regulate microtubule dynamics in cells. J Biol Chem 2006, 281:11856-11863.
    • (2006) J Biol Chem , vol.281 , pp. 11856-11863
    • Bunker, J.M.1    Kamath, K.2    Wilson, L.3
  • 62
    • 61349120799 scopus 로고    scopus 로고
    • FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an alternative core model for normal and pathological Tau action
    • LeBoeuf A.C., Levy S.F., Gaylord M., et al. FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an alternative core model for normal and pathological Tau action. J Biol Chem 2008, 283:36406-36415.
    • (2008) J Biol Chem , vol.283 , pp. 36406-36415
    • LeBoeuf, A.C.1    Levy, S.F.2    Gaylord, M.3
  • 63
    • 67649388412 scopus 로고    scopus 로고
    • Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro
    • Han D., Qureshi H.Y., Lu Y., et al. Familial FTDP-17 missense mutations inhibit microtubule assembly-promoting activity of tau by increasing phosphorylation at Ser202 in vitro. J Biol Chem 2009, 284:13422-13433.
    • (2009) J Biol Chem , vol.284 , pp. 13422-13433
    • Han, D.1    Qureshi, H.Y.2    Lu, Y.3
  • 64
    • 0033850080 scopus 로고    scopus 로고
    • Abnormal tau-containing filaments in neurodegenerative diseases
    • Crowther R.A., Goedert M. Abnormal tau-containing filaments in neurodegenerative diseases. J Struct Biol 2000, 130:271-279.
    • (2000) J Struct Biol , vol.130 , pp. 271-279
    • Crowther, R.A.1    Goedert, M.2
  • 65
    • 0037219399 scopus 로고    scopus 로고
    • Filamentous tau in oligodendrocytes and astrocytes of transgenic mice expressing the human tau isoform with the P301L mutation
    • Lin W.L., Lewis J., Yen S.H., et al. Filamentous tau in oligodendrocytes and astrocytes of transgenic mice expressing the human tau isoform with the P301L mutation. Am J Pathol 2003, 162:213-218.
    • (2003) Am J Pathol , vol.162 , pp. 213-218
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3
  • 66
    • 26844479213 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant (N279K) human tau show mutation dependent cognitive deficits without neurofibrillary tangle formation
    • Taniguchi T., Doe N., Matsuyama S., et al. Transgenic mice expressing mutant (N279K) human tau show mutation dependent cognitive deficits without neurofibrillary tangle formation. FEBS Lett 2005, 579:5704-5712.
    • (2005) FEBS Lett , vol.579 , pp. 5704-5712
    • Taniguchi, T.1    Doe, N.2    Matsuyama, S.3
  • 67
    • 34548145867 scopus 로고    scopus 로고
    • The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model
    • Dawson H.N., Cantillana V., Chen L., et al. The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model. J Neurosci 2007, 27:9155-9168.
    • (2007) J Neurosci , vol.27 , pp. 9155-9168
    • Dawson, H.N.1    Cantillana, V.2    Chen, L.3
  • 68
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 69
    • 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., et al. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 1992, 42:631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3
  • 70
    • 0028090656 scopus 로고
    • Abnormally phosphorylated tau protein in Alzheimer's disease: heterogeneity of individual regional distribution and relationship to clinical severity
    • Holzer M., Holzapfel H.P., Zedlick D., et al. Abnormally phosphorylated tau protein in Alzheimer's disease: heterogeneity of individual regional distribution and relationship to clinical severity. Neuroscience 1994, 63:499-516.
    • (1994) Neuroscience , vol.63 , pp. 499-516
    • Holzer, M.1    Holzapfel, H.P.2    Zedlick, D.3
  • 71
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • Dickson D.W., Crystal H.A., Bevona C., et al. Correlations of synaptic and pathological markers with cognition of the elderly. Neurobiol Aging 1995, 16:285-298.
    • (1995) Neurobiol Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1    Crystal, H.A.2    Bevona, C.3
  • 72
    • 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., et al. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol Aging 2003, 24:1063-1070.
    • (2003) Neurobiol Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3
  • 73
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 74
    • 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. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 75
    • 0026595567 scopus 로고
    • Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs
    • Burdick D., Soreghan B., Kwon M., et al. Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs. J Biol Chem 1992, 267:546-554.
    • (1992) J Biol Chem , vol.267 , pp. 546-554
    • Burdick, D.1    Soreghan, B.2    Kwon, M.3
  • 76
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., Berger E.P., Lansbury P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 77
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan G., Kirkitadze M.D., Lomakin A., et al. Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci USA 2003, 100:330-335.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3
  • 78
    • 33645520634 scopus 로고    scopus 로고
    • Early-onset behavioral and synaptic deficits in a mouse model of Alzheimer's disease
    • Jacobsen J.S., Wu C.C., Redwine J.M., et al. Early-onset behavioral and synaptic deficits in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 2006, 103:5161-5166.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5161-5166
    • Jacobsen, J.S.1    Wu, C.C.2    Redwine, J.M.3
  • 79
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S., Koh M.T., Kotilinek L., et al. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 2006, 440:352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 80
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior
    • Selkoe D.J. Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior. Behav Brain Res 2008, 192:106-113.
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 81
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar G.M., Li S., Mehta T.H., et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 2008, 14:837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3
  • 82
    • 84865305651 scopus 로고    scopus 로고
    • Postsynaptic dysfunction is associated with spatial and object recognition memory loss in a natural model of Alzheimer's disease
    • Ardiles A.O., Tapia-Rojas C.C., Mandal M., et al. Postsynaptic dysfunction is associated with spatial and object recognition memory loss in a natural model of Alzheimer's disease. Proc Natl Acad Sci USA 2012, 109:13835-13840.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13835-13840
    • Ardiles, A.O.1    Tapia-Rojas, C.C.2    Mandal, M.3
  • 83
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J., Gimbel D.A., Nygaard H.B., et al. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009, 457:1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3
  • 84
    • 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., et al. 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 2010, 285:7619-7632.
    • (2010) J Biol Chem , vol.285 , pp. 7619-7632
    • Zhao, W.Q.1    Santini, F.2    Breese, R.3
  • 85
    • 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., et al. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 2007, 27:796-807.
    • (2007) J Neurosci , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3
  • 86
    • 77953658771 scopus 로고    scopus 로고
    • Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5
    • Renner M., Lacor P.N., Velasco P.T., et al. Deleterious effects of amyloid beta oligomers acting as an extracellular scaffold for mGluR5. Neuron 2010, 66:739-754.
    • (2010) Neuron , vol.66 , pp. 739-754
    • Renner, M.1    Lacor, P.N.2    Velasco, P.T.3
  • 87
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction
    • Mucke L., Selkoe D.J. Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction. Cold Spring Harb Perspect Med 2012, 2:a006338.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Mucke, L.1    Selkoe, D.J.2
  • 88
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J., Dickson D.W., Lin W.L., et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 2001, 293:1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 89
    • 27744435409 scopus 로고    scopus 로고
    • Accelerated amyloid deposition, neurofibrillary degeneration and neuronal loss in double mutant APP/tau transgenic mice
    • Ribe E.M., Perez M., Puig B., et al. Accelerated amyloid deposition, neurofibrillary degeneration and neuronal loss in double mutant APP/tau transgenic mice. Neurobiol Dis 2005, 20:814-822.
    • (2005) Neurobiol Dis , vol.20 , pp. 814-822
    • Ribe, E.M.1    Perez, M.2    Puig, B.3
  • 90
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus
    • Vogelsberg-Ragaglia V., Schuck T., Trojanowski J.Q., et al. PP2A mRNA expression is quantitatively decreased in Alzheimer's disease hippocampus. Exp Neurol 2001, 168:402-412.
    • (2001) Exp Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3
  • 91
    • 0036771832 scopus 로고    scopus 로고
    • AbetaPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576
    • Otth C., Concha I.I., Arendt T., et al. AbetaPP induces cdk5-dependent tau hyperphosphorylation in transgenic mice Tg2576. J Alzheimers Dis 2002, 4:417-430.
    • (2002) J Alzheimers Dis , vol.4 , pp. 417-430
    • Otth, C.1    Concha, I.I.2    Arendt, T.3
  • 92
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    • Hoshi M., Sato M., Matsumoto S., et al. Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta. Proc Natl Acad Sci USA 2003, 100:6370-6375.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3
  • 93
    • 0037110601 scopus 로고    scopus 로고
    • Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures
    • Zheng W.H., Bastianetto S., Mennicken F., et al. Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures. Neuroscience 2002, 115:201-211.
    • (2002) Neuroscience , vol.115 , pp. 201-211
    • Zheng, W.H.1    Bastianetto, S.2    Mennicken, F.3
  • 94
    • 67650729973 scopus 로고    scopus 로고
    • Beta-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: suppression by omega-3 fatty acids and curcumin
    • Ma Q.L., Yang F., Rosario E.R., et al. Beta-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: suppression by omega-3 fatty acids and curcumin. J Neurosci 2009, 29:9078-9089.
    • (2009) J Neurosci , vol.29 , pp. 9078-9089
    • Ma, Q.L.1    Yang, F.2    Rosario, E.R.3
  • 95
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J., Chen F., van Dorpe J., et al. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 2001, 293:1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3
  • 96
    • 78651506630 scopus 로고    scopus 로고
    • Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease
    • Roberson E.D., Halabisky B., Yoo J.W., et al. Amyloid-beta/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease. J Neurosci 2011, 31:700-711.
    • (2011) J Neurosci , vol.31 , pp. 700-711
    • Roberson, E.D.1    Halabisky, B.2    Yoo, J.W.3
  • 97
    • 0037070606 scopus 로고    scopus 로고
    • Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II
    • Rank K.B., Pauley A.M., Bhattacharya K., et al. Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II. FEBS Lett 2002, 514:263-268.
    • (2002) FEBS Lett , vol.514 , pp. 263-268
    • Rank, K.B.1    Pauley, A.M.2    Bhattacharya, K.3
  • 98
    • 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., et al. Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem 2006, 281:39413-39423.
    • (2006) J Biol Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3
  • 99
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • Roberson E.D., Scearce-Levie K., Palop J.J., et al. Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model. Science 2007, 316:750-754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3
  • 100
    • 0038561176 scopus 로고    scopus 로고
    • Elements of a neurobiological theory of the hippocampus: the role of activity-dependent synaptic plasticity in memory
    • Morris R.G., Moser E.I., Riedel G., et al. Elements of a neurobiological theory of the hippocampus: the role of activity-dependent synaptic plasticity in memory. Philos Trans R Soc Lond B Biol Sci 2003, 358:773-786.
    • (2003) Philos Trans R Soc Lond B Biol Sci , vol.358 , pp. 773-786
    • Morris, R.G.1    Moser, E.I.2    Riedel, G.3
  • 101
    • 79551510136 scopus 로고    scopus 로고
    • Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation
    • Shipton O.A., Leitz J.R., Dworzak J., et al. Tau protein is required for amyloid {beta}-induced impairment of hippocampal long-term potentiation. J Neurosci 2011, 31:1688-1692.
    • (2011) J Neurosci , vol.31 , pp. 1688-1692
    • Shipton, O.A.1    Leitz, J.R.2    Dworzak, J.3
  • 102
    • 69449093036 scopus 로고    scopus 로고
    • Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology
    • Polydoro M., Acker C.M., Dukk K., et al. Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology. J Neurosci 2009, 29:10741-10749.
    • (2009) J Neurosci , vol.29 , pp. 10741-10749
    • Polydoro, M.1    Acker, C.M.2    Dukk, K.3
  • 103
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of Tau in the central nervous system
    • Papasozomenos S.C., Binder L.I. Phosphorylation determines two distinct species of Tau in the central nervous system. Cell Motil Cytoskeleton 1987, 8:210-226.
    • (1987) Cell Motil Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 104
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover B.R., Reed M.N., Su J., et al. Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 2010, 68:1067-1081.
    • (2010) Neuron , vol.68 , pp. 1067-1081
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3
  • 105
    • 0345276565 scopus 로고    scopus 로고
    • Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses
    • Mandelkow E.M., Stamer K., Vogel R., et al. Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 2003, 24:1079-1085.
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-1085
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3
  • 106
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • Ittner L.M., Ke Y.D., Delerue F., et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 2010, 142:387-397.
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3
  • 107
    • 78649498235 scopus 로고    scopus 로고
    • Multiple events lead to dendritic spine loss in triple transgenic Alzheimer's disease mice
    • Bittner T., Fuhrmann M., Burgold S., et al. Multiple events lead to dendritic spine loss in triple transgenic Alzheimer's disease mice. PLoS ONE 2010, 5:e15477.
    • (2010) PLoS ONE , vol.5
    • Bittner, T.1    Fuhrmann, M.2    Burgold, S.3
  • 108
    • 77956587739 scopus 로고    scopus 로고
    • + elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • + elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J Neurosci 2010, 30:11938-11950.
    • (2010) J Neurosci , vol.30 , pp. 11938-11950
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3
  • 109
    • 48249102303 scopus 로고    scopus 로고
    • Role of axonal transport in neurodegenerative diseases
    • De Vos K.J., Grierson A.J., Ackerley S., et al. Role of axonal transport in neurodegenerative diseases. Annu Rev Neurosci 2008, 31:151-173.
    • (2008) Annu Rev Neurosci , vol.31 , pp. 151-173
    • De Vos, K.J.1    Grierson, A.J.2    Ackerley, S.3
  • 110
    • 65249161745 scopus 로고    scopus 로고
    • Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid beta
    • Pigino G., Morfini G., Atagi Y., et al. Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid beta. Proc Natl Acad Sci USA 2009, 106:5907-5912.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5907-5912
    • Pigino, G.1    Morfini, G.2    Atagi, Y.3
  • 111
    • 78650545423 scopus 로고    scopus 로고
    • Deficits in axonal transport precede ALS symptoms in vivo
    • Bilsland L.G., Sahai E., Kelly G., et al. Deficits in axonal transport precede ALS symptoms in vivo. Proc Natl Acad Sci USA 2010, 107:20523-20528.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20523-20528
    • Bilsland, L.G.1    Sahai, E.2    Kelly, G.3
  • 112
    • 0028845388 scopus 로고
    • Role of microtubule-associated proteins in the control of microtubule assembly
    • Maccioni R.B., Cambiazo V. Role of microtubule-associated proteins in the control of microtubule assembly. Physiol Rev 1995, 75:835-864.
    • (1995) Physiol Rev , vol.75 , pp. 835-864
    • Maccioni, R.B.1    Cambiazo, V.2
  • 113
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J., Lorenzo A., Yeh J., et al. Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 1995, 14:879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3
  • 114
    • 0031012497 scopus 로고    scopus 로고
    • Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau
    • Alonso A.D., Grundke-Iqbal I., Barra H.S., et al. Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. Proc Natl Acad Sci USA 1997, 94:298-303.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 298-303
    • Alonso, A.D.1    Grundke-Iqbal, I.2    Barra, H.S.3
  • 115
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid
    • King M.E., Kan H.M., Baas P.W., et al. Tau-dependent microtubule disassembly initiated by prefibrillar beta-amyloid. J Cell Biol 2006, 175:541-546.
    • (2006) J Cell Biol , vol.175 , pp. 541-546
    • King, M.E.1    Kan, H.M.2    Baas, P.W.3
  • 116
    • 77954466407 scopus 로고    scopus 로고
    • Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons
    • Decker H., Lo K.Y., Unger S.M., et al. Amyloid-beta peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3beta in primary cultured hippocampal neurons. J Neurosci 2010, 30:9166-9171.
    • (2010) J Neurosci , vol.30 , pp. 9166-9171
    • Decker, H.1    Lo, K.Y.2    Unger, S.M.3
  • 117
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., et al. Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 1992, 12:376-389.
    • (1992) J Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3
  • 118
    • 0037197836 scopus 로고    scopus 로고
    • Tau is essential to beta-amyloid-induced neurotoxicity
    • Rapoport M., Dawson H.N., Binder L.I., et al. Tau is essential to beta-amyloid-induced neurotoxicity. Proc Natl Acad Sci USA 2002, 99:6364-6369.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6364-6369
    • Rapoport, M.1    Dawson, H.N.2    Binder, L.I.3
  • 119
    • 70949090395 scopus 로고    scopus 로고
    • Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau
    • Tackenberg C., Brandt R. Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau. J Neurosci 2009, 29:14439-14450.
    • (2009) J Neurosci , vol.29 , pp. 14439-14450
    • Tackenberg, C.1    Brandt, R.2
  • 120
    • 77957737750 scopus 로고    scopus 로고
    • Tau reduction prevents Abeta-induced defects in axonal transport
    • Vossel K.A., Zhang K., Brodbeck J., et al. Tau reduction prevents Abeta-induced defects in axonal transport. Science 2010, 330:198.
    • (2010) Science , vol.330 , pp. 198
    • Vossel, K.A.1    Zhang, K.2    Brodbeck, J.3
  • 121
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
    • Wang J.Z., Grundke-Iqbal I., Iqbal K. Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur J Neurosci 2007, 25:59-68.
    • (2007) Eur J Neurosci , vol.25 , pp. 59-68
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 122
    • 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. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov 2011, 10:698-712.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 123
    • 0022547120 scopus 로고
    • Developmental genetics
    • Epstein C.J. Developmental genetics. Experientia 1986, 42:1117-1128.
    • (1986) Experientia , vol.42 , pp. 1117-1128
    • Epstein, C.J.1
  • 124
    • 0023064453 scopus 로고
    • Abnormalities in the interferon response and immune systems in Down syndrome: studies in human trisomy 21 and mouse trisomy 16
    • Epstein C.J., Weil J., Epstein L.B. Abnormalities in the interferon response and immune systems in Down syndrome: studies in human trisomy 21 and mouse trisomy 16. Prog Clin Biol Res 1987, 246:191-208.
    • (1987) Prog Clin Biol Res , vol.246 , pp. 191-208
    • Epstein, C.J.1    Weil, J.2    Epstein, L.B.3
  • 126
    • 0030089789 scopus 로고    scopus 로고
    • The neuropsychology of mental retardation
    • Pulsifer M.B. The neuropsychology of mental retardation. J Int Neuropsychol Soc 1996, 2:159-176.
    • (1996) J Int Neuropsychol Soc , vol.2 , pp. 159-176
    • Pulsifer, M.B.1
  • 127
    • 0034682403 scopus 로고    scopus 로고
    • Chromosome 21 mapping and sequencing consortium. The DNA sequence of human chromosome 21
    • Hattori M., Fujiyama A., Taylor T.D., et al. Chromosome 21 mapping and sequencing consortium. The DNA sequence of human chromosome 21. Nature 2000, 405:311-319.
    • (2000) Nature , vol.405 , pp. 311-319
    • Hattori, M.1    Fujiyama, A.2    Taylor, T.D.3
  • 129
    • 0024498840 scopus 로고
    • Neurophysiological abnormalities in cultured dorsal root ganglion neurons from the trisomy-16 mouse fetus, a model for Down syndrome
    • Ault B., Caviedes P., Rapoport S.I. Neurophysiological abnormalities in cultured dorsal root ganglion neurons from the trisomy-16 mouse fetus, a model for Down syndrome. Brain Res 1989, 485:165-170.
    • (1989) Brain Res , vol.485 , pp. 165-170
    • Ault, B.1    Caviedes, P.2    Rapoport, S.I.3
  • 130
    • 1542614438 scopus 로고    scopus 로고
    • The MNB/DYRK1A protein kinase: genetic and biochemical properties
    • Galceran J., de Graaf K., Tejedor F.J., et al. The MNB/DYRK1A protein kinase: genetic and biochemical properties. J Neural Transm Suppl 2003, 67:139-148.
    • (2003) J Neural Transm Suppl , vol.67 , pp. 139-148
    • Galceran, J.1    de Graaf, K.2    Tejedor, F.J.3
  • 131
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Woods Y.L., Cohen P., Becker W., et al. The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem J 2001, 355:609-615.
    • (2001) Biochem J , vol.355 , pp. 609-615
    • Woods, Y.L.1    Cohen, P.2    Becker, W.3
  • 132
    • 33846533244 scopus 로고    scopus 로고
    • The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease
    • Kimura R., Kamino K., Yamamoto M., et al. The DYRK1A gene, encoded in chromosome 21 Down syndrome critical region, bridges between beta-amyloid production and tau phosphorylation in Alzheimer disease. Hum Mol Genet 2007, 16:15-23.
    • (2007) Hum Mol Genet , vol.16 , pp. 15-23
    • Kimura, R.1    Kamino, K.2    Yamamoto, M.3
  • 133
    • 80051737020 scopus 로고    scopus 로고
    • Regulation of the alternative splicing of tau exon 10 by SC35 and Dyrk1A
    • Qian W., Liang H., Shi J., et al. Regulation of the alternative splicing of tau exon 10 by SC35 and Dyrk1A. Nucleic Acids Res 2011, 39:6161-6171.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6161-6171
    • Qian, W.1    Liang, H.2    Shi, J.3
  • 134
    • 84865756788 scopus 로고    scopus 로고
    • Dual-specificity-tyrosine-phosphorylated and regulated kinase 1A (Dyrk1A) modulates serine-arginine rich protein 55 (SRp55)-promoted tau exon 10 inclusion
    • Yin X., Jin N., Gu J., et al. Dual-specificity-tyrosine-phosphorylated and regulated kinase 1A (Dyrk1A) modulates serine-arginine rich protein 55 (SRp55)-promoted tau exon 10 inclusion. J Biol Chem 2012, 287:30497-30506.
    • (2012) J Biol Chem , vol.287 , pp. 30497-30506
    • Yin, X.1    Jin, N.2    Gu, J.3
  • 135
    • 0028904871 scopus 로고
    • Transient adaptation of oxidative stress in mammalian cells
    • Wiese A.G., Pacifici R.E., Davies K.J. Transient adaptation of oxidative stress in mammalian cells. Arch Biochem Biophys 1995, 318:231-240.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 231-240
    • Wiese, A.G.1    Pacifici, R.E.2    Davies, K.J.3
  • 136
    • 0031172775 scopus 로고    scopus 로고
    • Hamster adapt78 mRNA is a Down syndrome critical region homologue that is inducible by oxidative stress
    • Crawford D.R., Leahy K.P., Abramova N., et al. Hamster adapt78 mRNA is a Down syndrome critical region homologue that is inducible by oxidative stress. Arch Biochem Biophys 1997, 342:6-12.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 6-12
    • Crawford, D.R.1    Leahy, K.P.2    Abramova, N.3
  • 137
    • 0028856422 scopus 로고
    • A new human gene from the Down syndrome critical region encodes a proline-rich protein highly expressed in fetal brain and heart
    • Fuentes J.J., Pritchard M.A., Planas A.M., et al. A new human gene from the Down syndrome critical region encodes a proline-rich protein highly expressed in fetal brain and heart. Hum Mol Genet 1995, 4:1935-1944.
    • (1995) Hum Mol Genet , vol.4 , pp. 1935-1944
    • Fuentes, J.J.1    Pritchard, M.A.2    Planas, A.M.3
  • 138
    • 0034234543 scopus 로고    scopus 로고
    • DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways
    • Fuentes J.J., Genescà L., Kingsbury T.J., et al. DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways. Hum Mol Genet 2000, 9:1681-1690.
    • (2000) Hum Mol Genet , vol.9 , pp. 1681-1690
    • Fuentes, J.J.1    Genescà, L.2    Kingsbury, T.J.3
  • 139
    • 0035914413 scopus 로고    scopus 로고
    • Chronic overexpression of the calcineurin inhibitory gene DSCR1 (Adapt78) is associated with Alzheimer's disease
    • Ermak G., Morgan T.E., Davies K.J. Chronic overexpression of the calcineurin inhibitory gene DSCR1 (Adapt78) is associated with Alzheimer's disease. J Biol Chem 2001, 276:38787-38794.
    • (2001) J Biol Chem , vol.276 , pp. 38787-38794
    • Ermak, G.1    Morgan, T.E.2    Davies, K.J.3
  • 140
    • 24644499539 scopus 로고    scopus 로고
    • Expression of calcipressin1, an inhibitor of the phosphatase calcineurin, is altered with aging and Alzheimer's disease
    • Cook C.N., Hejna M.J., Magnuson D.J., et al. Expression of calcipressin1, an inhibitor of the phosphatase calcineurin, is altered with aging and Alzheimer's disease. J Alzheimers Dis 2005, 8:63-73.
    • (2005) J Alzheimers Dis , vol.8 , pp. 63-73
    • Cook, C.N.1    Hejna, M.J.2    Magnuson, D.J.3
  • 141
    • 33947193463 scopus 로고    scopus 로고
    • RCAN1-1L is overexpressed in neurons of Alzheimer's disease patients
    • Harris C.D., Ermak G., Davies K.J. RCAN1-1L is overexpressed in neurons of Alzheimer's disease patients. FEBS J 2007, 274:1715-1724.
    • (2007) FEBS J , vol.274 , pp. 1715-1724
    • Harris, C.D.1    Ermak, G.2    Davies, K.J.3
  • 142
    • 0029798880 scopus 로고    scopus 로고
    • Reduction of calcineurin enzymatic activity in Alzheimer's disease: correlation with neuropathologic changes
    • Ladner C.J., Czech J., Maurice J., et al. Reduction of calcineurin enzymatic activity in Alzheimer's disease: correlation with neuropathologic changes. J Neuropathol Exp Neurol 1996, 55:924-931.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 924-931
    • Ladner, C.J.1    Czech, J.2    Maurice, J.3
  • 143
    • 0030945154 scopus 로고    scopus 로고
    • Cytoskeletal changes in the brains of mice lacking calcineurin A alpha
    • Kayyali U.S., Zhang W., Yee A.G., et al. Cytoskeletal changes in the brains of mice lacking calcineurin A alpha. J Neurochem 1997, 68:1668-1678.
    • (1997) J Neurochem , vol.68 , pp. 1668-1678
    • Kayyali, U.S.1    Zhang, W.2    Yee, A.G.3
  • 144
    • 33646258512 scopus 로고    scopus 로고
    • RCAN1 (DSCR1 or Adapt78) stimulates expression of GSK-3beta
    • Ermak G., Harris C.D., Battocchio D., et al. RCAN1 (DSCR1 or Adapt78) stimulates expression of GSK-3beta. FEBS J 2006, 273:2100-2109.
    • (2006) FEBS J , vol.273 , pp. 2100-2109
    • Ermak, G.1    Harris, C.D.2    Battocchio, D.3
  • 145
    • 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., et al. Cellular phosphorylation of tau by GSK-3 beta influences tau binding to microtubules and microtubule organisation. J Cell Sci 1996, 109:1537-1543.
    • (1996) J Cell Sci , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3
  • 146
    • 0026569335 scopus 로고
    • Dysregulation of gene expression in mouse trisomy 16, an animal model of Down syndrome
    • Holtzman D.M., Bayney R.M., Li Y.W., et al. Dysregulation of gene expression in mouse trisomy 16, an animal model of Down syndrome. EMBO J 1992, 11:619-627.
    • (1992) EMBO J , vol.11 , pp. 619-627
    • Holtzman, D.M.1    Bayney, R.M.2    Li, Y.W.3
  • 147
    • 0041632362 scopus 로고    scopus 로고
    • App gene dosage modulates endosomal abnormalities of Alzheimer's disease in a segmental trisomy 16 mouse model of Down syndrome
    • Cataldo A.M., Petanceska S., Peterhoff C.M., et al. App gene dosage modulates endosomal abnormalities of Alzheimer's disease in a segmental trisomy 16 mouse model of Down syndrome. J Neurosci 2003, 23:6788-6792.
    • (2003) J Neurosci , vol.23 , pp. 6788-6792
    • Cataldo, A.M.1    Petanceska, S.2    Peterhoff, C.M.3
  • 148
    • 77955089472 scopus 로고    scopus 로고
    • Convergence of amyloid-beta and tau pathologies on mitochondria in vivo
    • Eckert A., Schulz K.L., Rhein V., et al. Convergence of amyloid-beta and tau pathologies on mitochondria in vivo. Mol Neurobiol 2010, 41:107-114.
    • (2010) Mol Neurobiol , vol.41 , pp. 107-114
    • Eckert, A.1    Schulz, K.L.2    Rhein, V.3
  • 149
    • 42149164312 scopus 로고    scopus 로고
    • Processing of amyloid precursor protein and amyloid peptide neurotoxicity
    • Nathalie P., Jean-Noël O. Processing of amyloid precursor protein and amyloid peptide neurotoxicity. Curr Alzheimer Res 2008, 5:92-99.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 92-99
    • Nathalie, P.1    Jean-Noël, O.2
  • 150
    • 84876406070 scopus 로고    scopus 로고
    • Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
    • Jul 10. [Epub ahead of print]
    • Selenica M.L., Brownlow M., Jimenez J.P., et al. Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy. Neurodegener Dis 2012, Jul 10. [Epub ahead of print].
    • (2012) Neurodegener Dis
    • Selenica, M.L.1    Brownlow, M.2    Jimenez, J.P.3
  • 151
    • 39749196069 scopus 로고    scopus 로고
    • Dual-specificity tyrosine(Y)-phosphorylation regulated kinase 1A-mediated phosphorylation of amyloid precursor protein: evidence for a functional link between Down syndrome and Alzheimer's disease
    • Ryoo S.R., Cho H.J., Lee H.W., et al. Dual-specificity tyrosine(Y)-phosphorylation regulated kinase 1A-mediated phosphorylation of amyloid precursor protein: evidence for a functional link between Down syndrome and Alzheimer's disease. J Neurochem 2008, 104:1333-1344.
    • (2008) J Neurochem , vol.104 , pp. 1333-1344
    • Ryoo, S.R.1    Cho, H.J.2    Lee, H.W.3
  • 152
    • 0142123260 scopus 로고    scopus 로고
    • APP processing is regulated by cytoplasmic phosphorylation
    • Lee M.S., Kao S.C., Lemere C.A., et al. APP processing is regulated by cytoplasmic phosphorylation. J Cell Biol 2003, 163:83-95.
    • (2003) J Cell Biol , vol.163 , pp. 83-95
    • Lee, M.S.1    Kao, S.C.2    Lemere, C.A.3
  • 153
    • 81555234239 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of amyloid precursor protein at threonine 668 leads to its altered processing and association with centrosomes
    • Judge M., Hornbeck L., Potter H., et al. Mitosis-specific phosphorylation of amyloid precursor protein at threonine 668 leads to its altered processing and association with centrosomes. Mol Neurodegener 2011, 6:80.
    • (2011) Mol Neurodegener , vol.6 , pp. 80
    • Judge, M.1    Hornbeck, L.2    Potter, H.3
  • 154
    • 84455173610 scopus 로고    scopus 로고
    • Amyloid-β toxicity and tau hyperphosphorylation are linked via RCAN1 in Alzheimer's disease
    • Lloret A., Badia M.C., Giraldo E., et al. Amyloid-β toxicity and tau hyperphosphorylation are linked via RCAN1 in Alzheimer's disease. J Alzheimers Dis 2011, 27:701-709.
    • (2011) J Alzheimers Dis , vol.27 , pp. 701-709
    • Lloret, A.1    Badia, M.C.2    Giraldo, E.3
  • 155
    • 0033525018 scopus 로고    scopus 로고
    • Calcium signals in cell lines derived from the cerebral cortex of normal and trisomy 16 mice
    • Cárdenas A.M., Rodríguez M.P., Cortés M.P., et al. Calcium signals in cell lines derived from the cerebral cortex of normal and trisomy 16 mice. Neuroreport 1999, 10:363-369.
    • (1999) Neuroreport , vol.10 , pp. 363-369
    • Cárdenas, A.M.1    Rodríguez, M.P.2    Cortés, M.P.3
  • 156
    • 33645024791 scopus 로고    scopus 로고
    • Neuronal dysfunction in Down syndrome: contribution of neuronal models in cell culture
    • Saud K., Arriagada C., Cárdenas A.M., et al. Neuronal dysfunction in Down syndrome: contribution of neuronal models in cell culture. J Physiol Paris 2006, 99:201-210.
    • (2006) J Physiol Paris , vol.99 , pp. 201-210
    • Saud, K.1    Arriagada, C.2    Cárdenas, A.M.3
  • 157
    • 33750464821 scopus 로고    scopus 로고
    • Knockdown of amyloid precursor protein normalizes cholinergic function in a cell line derived from the cerebral cortex of a trisomy 16 mouse: an animal model of down syndrome
    • Opazo P., Saud K., de Saint Pierre M., et al. Knockdown of amyloid precursor protein normalizes cholinergic function in a cell line derived from the cerebral cortex of a trisomy 16 mouse: an animal model of down syndrome. J Neurosci Res 2006, 84:1303-1310.
    • (2006) J Neurosci Res , vol.84 , pp. 1303-1310
    • Opazo, P.1    Saud, K.2    de Saint Pierre, M.3
  • 158
    • 37549007249 scopus 로고    scopus 로고
    • Effect of the knockdown of amyloid precursor protein on intracellular calcium increases in a neuronal cell line derived from the cerebral cortex of a trisomy 16 mouse
    • Rojas G., Cárdenas A.M., Fernández-Olivares P., et al. Effect of the knockdown of amyloid precursor protein on intracellular calcium increases in a neuronal cell line derived from the cerebral cortex of a trisomy 16 mouse. Exp Neurol 2008, 209:234-242.
    • (2008) Exp Neurol , vol.209 , pp. 234-242
    • Rojas, G.1    Cárdenas, A.M.2    Fernández-Olivares, P.3
  • 159
    • 84871651244 scopus 로고    scopus 로고
    • RCAN1 overexpression results in enhanced voltage-gated calcium currents via impairment of inactivation in a neuronal cell line derived from cerebral cortex of Ts16 mice, an animal model of Down Syndrome
    • Acuña M., Noriega J., Perez-Nuñez R., et al. RCAN1 overexpression results in enhanced voltage-gated calcium currents via impairment of inactivation in a neuronal cell line derived from cerebral cortex of Ts16 mice, an animal model of Down Syndrome. Soc Neurosci Abstr 2011, 152.14.
    • (2011) Soc Neurosci Abstr
    • Acuña, M.1    Noriega, J.2    Perez-Nuñez, R.3
  • 160
    • 84871650250 scopus 로고    scopus 로고
    • Knockdown of Rcan1 and Dyrk1A ameliorate the cholinergic dysfunction in cell lines derived from the cerebral cortex of a Ts16 mouse, a model of Down syndrome: possible role of VaChT and CHT1 proteins as targets
    • Noriega J., Acuña M., Perez-Nuñez R., et al. Knockdown of Rcan1 and Dyrk1A ameliorate the cholinergic dysfunction in cell lines derived from the cerebral cortex of a Ts16 mouse, a model of Down syndrome: possible role of VaChT and CHT1 proteins as targets. Soc Neurosci Abstr 2011, 152.15.
    • (2011) Soc Neurosci Abstr
    • Noriega, J.1    Acuña, M.2    Perez-Nuñez, R.3
  • 161
    • 84861665526 scopus 로고    scopus 로고
    • The impact of cerebrospinal fluid biomarkers on the diagnosis of Alzheimer's disease
    • Engelborghs S., Le Bastard N. The impact of cerebrospinal fluid biomarkers on the diagnosis of Alzheimer's disease. Mol Diagn Ther 2012, 16:135-141.
    • (2012) Mol Diagn Ther , vol.16 , pp. 135-141
    • Engelborghs, S.1    Le Bastard, N.2
  • 162
    • 84856008210 scopus 로고    scopus 로고
    • Standardization of preanalytical aspects of cerebrospinal fluid biomarker testing for Alzheimer's disease diagnosis: a consensus paper from the Alzheimer's Biomarkers Standardization Initiative
    • Vanderstichele H., Bibl M., Engelborghs S., et al. Standardization of preanalytical aspects of cerebrospinal fluid biomarker testing for Alzheimer's disease diagnosis: a consensus paper from the Alzheimer's Biomarkers Standardization Initiative. Alzheimers Dement 2012, 8:65-73.
    • (2012) Alzheimers Dement , vol.8 , pp. 65-73
    • Vanderstichele, H.1    Bibl, M.2    Engelborghs, S.3
  • 163
    • 84655169783 scopus 로고    scopus 로고
    • Discovery of potent small molecule inhibitors of DYRK1A by structure-based virtual screening and bioassay
    • Wang D., Wang F., Tan Y., et al. Discovery of potent small molecule inhibitors of DYRK1A by structure-based virtual screening and bioassay. Bioorg Med Chem Lett 2012, 22:168-171.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 168-171
    • Wang, D.1    Wang, F.2    Tan, Y.3


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