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Volumn 4 JUL, Issue , 2013, Pages

The importance of tau phosphorylation for neurodegenerative diseases

Author keywords

Alzheimer's disease; Extracellular; Function; Oligomers; Phosphorylation; Tau

Indexed keywords

ADENYLATE KINASE; AMPA RECEPTOR; CASPASE 3; CYCLIN DEPENDENT KINASE 5; GLYCOGEN SYNTHASE KINASE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; GLYCOGEN SYNTHASE KINASE 3BETA; LITHIUM; MESSENGER RNA; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE FYN; TAU PROTEIN; TIDEGLUSIB;

EID: 84883524853     PISSN: None     EISSN: 16642295     Source Type: Journal    
DOI: 10.3389/fneur.2013.00083     Document Type: Review
Times cited : (317)

References (165)
  • 1
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • doi:10.1126/science.1113694
    • Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science (2005) 309:476-81. doi:10.1126/science.1113694
    • (2005) Science , vol.309 , pp. 476-81
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 2
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • doi:10.1523/JNEUROSCI.0587-07.2007
    • Berger Z, Roder H, Hanna A, Carlson A, Rangachari V, Yue M, et al. Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J Neurosci (2007) 27:3650-62. doi:10.1523/JNEUROSCI.0587-07.2007
    • (2007) J Neurosci , vol.27 , pp. 3650-62
    • Berger, Z.1    Roder, H.2    Hanna, A.3    Carlson, A.4    Rangachari, V.5    Yue, M.6
  • 3
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • doi:10.1016/j.cell.2010.06.036
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, van Eersel J, et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell (2010) 142:387-97. doi:10.1016/j.cell.2010.06.036
    • (2010) Cell , vol.142 , pp. 387-97
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    van Eersel, J.6
  • 4
    • 77952554382 scopus 로고    scopus 로고
    • Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs
    • doi:10.1016/j.expneurol.2009.07.029
    • Rocher AB, Crimins JL, Amatrudo JM, Kinson MS, Todd-Brown MA, Lewis J, et al. Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs. Exp Neurol (2010) 223:385-93. doi:10.1016/j.expneurol.2009.07.029
    • (2010) Exp Neurol , vol.223 , pp. 385-93
    • Rocher, A.B.1    Crimins, J.L.2    Amatrudo, J.M.3    Kinson, M.S.4    Todd-Brown, M.A.5    Lewis, J.6
  • 6
    • 0036264527 scopus 로고    scopus 로고
    • Sporadic Pick's disease: a tauopathy characterized by a spectrum of pathological tau isoforms in gray and white matter
    • doi:10.1002/ana.10222
    • Zhukareva V, Mann D, Pickering-Brown S, Uryu K, Shuck T, Shah K, et al. Sporadic Pick's disease: a tauopathy characterized by a spectrum of pathological tau isoforms in gray and white matter. Ann Neurol (2002) 51(6):730-9. doi:10.1002/ana.10222
    • (2002) Ann Neurol , vol.51 , Issue.6 , pp. 730-9
    • Zhukareva, V.1    Mann, D.2    Pickering-Brown, S.3    Uryu, K.4    Shuck, T.5    Shah, K.6
  • 8
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
    • doi:10.1016/j.molmed.2009.01.003
    • Hanger DP, Anderton BH, Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med (2009) 15:112-9. doi:10.1016/j.molmed.2009.01.003
    • (2009) Trends Mol Med , vol.15 , pp. 112-9
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 9
    • 79960544589 scopus 로고    scopus 로고
    • Advances in tau-based drug discovery
    • doi:10.1517/17460441.2011.586690
    • Noble W, Pooler AM, Hanger DP. Advances in tau-based drug discovery. Expert Opin Drug Discov (2011) 6:797-810. doi:10.1517/17460441.2011.586690
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 797-810
    • Noble, W.1    Pooler, A.M.2    Hanger, D.P.3
  • 10
    • 34548191034 scopus 로고    scopus 로고
    • Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis
    • doi:10.1074/jbc.M703269200
    • Hanger DP, Byers HL, Wray S, Leung KY, Saxton MJ, Seereeram A, et al. Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem (2007) 282:23645-54. doi:10.1074/jbc.M703269200
    • (2007) J Biol Chem , vol.282 , pp. 23645-54
    • Hanger, D.P.1    Byers, H.L.2    Wray, S.3    Leung, K.Y.4    Saxton, M.J.5    Seereeram, A.6
  • 11
    • 0033009603 scopus 로고    scopus 로고
    • Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: tau pathologies with exclusively "exon 10" isoforms
    • doi:10.1046/j.1471-4159.1999.0721243.x
    • Sergeant N, Wattez A, Delacourte A. Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: tau pathologies with exclusively "exon 10" isoforms. J Neurochem (1999) 72:1243-9. doi:10.1046/j.1471-4159.1999.0721243.x
    • (1999) J Neurochem , vol.72 , pp. 1243-9
    • Sergeant, N.1    Wattez, A.2    Delacourte, A.3
  • 12
    • 9144224301 scopus 로고    scopus 로고
    • Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration
    • doi:10.1002/ana.10793
    • Arai T, Ikeda K, Akiyama H, Nonaka T, Hasegawa M, Ishiguro K, et al. Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration. Ann Neurol (2004) 55:72-9. doi:10.1002/ana.10793
    • (2004) Ann Neurol , vol.55 , pp. 72-9
    • Arai, T.1    Ikeda, K.2    Akiyama, H.3    Nonaka, T.4    Hasegawa, M.5    Ishiguro, K.6
  • 13
    • 44649100169 scopus 로고    scopus 로고
    • Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats
    • doi:10.1111/j.1471-4159.2008.05321.x
    • Wray S, Saxton M, Anderton BH, Hanger DP. Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats. J Neurochem (2008) 105:2343-52. doi:10.1111/j.1471-4159.2008.05321.x
    • (2008) J Neurochem , vol.105 , pp. 2343-52
    • Wray, S.1    Saxton, M.2    Anderton, B.H.3    Hanger, D.P.4
  • 14
    • 0025893793 scopus 로고
    • Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated
    • Hanger DP, Brion JP, Gallo JM, Cairns NJ, Luthert PJ, Anderton BH. Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated. Biochem J (1991) 275(Pt 1):99-104.
    • (1991) Biochem J , vol.275 , Issue.PART 1 , pp. 99-104
    • Hanger, D.P.1    Brion, J.P.2    Gallo, J.M.3    Cairns, N.J.4    Luthert, P.J.5    Anderton, B.H.6
  • 15
    • 0028899714 scopus 로고
    • Proline-directed and non-proline-directed phosphorylation of PHF-tau
    • doi:10.1074/jbc.270.2.823
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Yoshida H, Titani K, et al. Proline-directed and non-proline-directed phosphorylation of PHF-tau. J Biol Chem (1995) 270:823-9. doi:10.1074/jbc.270.2.823
    • (1995) J Biol Chem , vol.270 , pp. 823-9
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Yoshida, H.5    Titani, K.6
  • 16
    • 0031741247 scopus 로고    scopus 로고
    • New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
    • doi:10.1046/j.1471-4159.1998.71062465.x
    • Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH. New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. J Neurochem (1998) 71:2465-76. doi:10.1046/j.1471-4159.1998.71062465.x
    • (1998) J Neurochem , vol.71 , pp. 2465-76
    • Hanger, D.P.1    Betts, J.C.2    Loviny, T.L.3    Blackstock, W.P.4    Anderton, B.H.5
  • 17
    • 84878234937 scopus 로고    scopus 로고
    • Prostate-derived Sterile 20-like Kinases (PSKs/TAOKs) Phosphorylate Tau Protein and Are Activated in Tangle-bearing Neurons in Alzheimer Disease
    • doi:10.1074/jbc.M112.448183
    • Tavares IA, Touma D, Lynham S, Troakes C, Schober M, Causevic M, et al. Prostate-derived Sterile 20-like Kinases (PSKs/TAOKs) Phosphorylate Tau Protein and Are Activated in Tangle-bearing Neurons in Alzheimer Disease. J Biol Chem (2013) 288(21):15418-29. doi:10.1074/jbc.M112.448183
    • (2013) J Biol Chem , vol.288 , Issue.21 , pp. 15418-29
    • Tavares, I.A.1    Touma, D.2    Lynham, S.3    Troakes, C.4    Schober, M.5    Causevic, M.6
  • 18
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase
    • doi:10.1016/0304-3940(92)90774-2
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci Lett (1992) 147:58-62. doi:10.1016/0304-3940(92)90774-2
    • (1992) Neurosci Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 19
    • 0028675873 scopus 로고
    • Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells
    • doi:10.1016/S0960-9822(00)00246-3
    • Lovestone S, Reynolds CH, Latimer D, Davis DR, Anderton BH, Gallo JM, et al. Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr Biol (1994) 4:1077-86. doi:10.1016/S0960-9822(00)00246-3
    • (1994) Curr Biol , vol.4 , pp. 1077-86
    • Lovestone, S.1    Reynolds, C.H.2    Latimer, D.3    Davis, D.R.4    Anderton, B.H.5    Gallo, J.M.6
  • 20
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules
    • doi:10.1016/0306-4522(96)00126-1
    • Lovestone S, Hartley CL, Pearce J, Anderton BH. Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: the effects on the organization and stability of microtubules. Neuroscience (1996) 73:1145-57. doi:10.1016/0306-4522(96)00126-1
    • (1996) Neuroscience , vol.73 , pp. 1145-57
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Anderton, B.H.4
  • 21
    • 3142592230 scopus 로고    scopus 로고
    • GSK-3beta inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
    • doi:10.1038/sj.mp.4001483
    • Mudher A, Shepherd D, Newman TA, Mildren P, Jukes JP, Squire A, et al. GSK-3beta inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila. Mol Psychiatry (2004) 9:522-30. doi:10.1038/sj.mp.4001483
    • (2004) Mol Psychiatry , vol.9 , pp. 522-30
    • Mudher, A.1    Shepherd, D.2    Newman, T.A.3    Mildren, P.4    Jukes, J.P.5    Squire, A.6
  • 22
    • 21044449225 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo
    • doi:10.1073/pnas.0500466102
    • Noble W, Planel E, Zehr C, Olm V, Meyerson J, Suleman F, et al. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc Natl Acad Sci U S A (2005) 102(19):6990-5. doi:10.1073/pnas.0500466102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.19 , pp. 6990-5
    • Noble, W.1    Planel, E.2    Zehr, C.3    Olm, V.4    Meyerson, J.5    Suleman, F.6
  • 23
    • 0027757042 scopus 로고
    • Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5
    • doi:10.1016/0014-5793(93)80849-P
    • Baumann K, Mandelkow EM, Biernat J, Piwnica-Worms H, Mandelkow E. Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5. FEBS Lett (1993) 336:417-24. doi:10.1016/0014-5793(93)80849-P
    • (1993) FEBS Lett , vol.336 , pp. 417-24
    • Baumann, K.1    Mandelkow, E.M.2    Biernat, J.3    Piwnica-Worms, H.4    Mandelkow, E.5
  • 24
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • doi:10.1016/S0896-6273(03)00627-5
    • Cruz JC, Tseng HC, Goldman JA, Shih H, Tsai LH. Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles. Neuron (2003) 40:471-83. doi:10.1016/S0896-6273(03)00627-5
    • (2003) Neuron , vol.40 , pp. 471-83
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.H.5
  • 25
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • doi:10.1016/S0896-6273(03)00259-9
    • Noble W, Olm V, Takata K, Casey E, Mary O, Meyerson J, et al. Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron (2003) 38:555-65. doi:10.1016/S0896-6273(03)00259-9
    • (2003) Neuron , vol.38 , pp. 555-65
    • Noble, W.1    Olm, V.2    Takata, K.3    Casey, E.4    Mary, O.5    Meyerson, J.6
  • 26
    • 79952135798 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid beta-peptide exposure
    • doi:10.1042/BJ20101485
    • Thornton C, Bright NJ, Sastre M, Muckett PJ, Carling D. AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid beta-peptide exposure. Biochem J (2011) 434:503-12. doi:10.1042/BJ20101485
    • (2011) Biochem J , vol.434 , pp. 503-12
    • Thornton, C.1    Bright, N.J.2    Sastre, M.3    Muckett, P.J.4    Carling, D.5
  • 27
    • 84876078566 scopus 로고    scopus 로고
    • The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Abeta oligomers through tau phosphorylation
    • doi:10.1016/j.neuron.2013.02.003
    • Mairet-Coello G, Courchet J, Pieraut S, Courchet V, Maximov A, Polleux F. The CAMKK2-AMPK kinase pathway mediates the synaptotoxic effects of Abeta oligomers through tau phosphorylation. Neuron (2013) 78:94-108. doi:10.1016/j.neuron.2013.02.003
    • (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
  • 28
    • 84871759268 scopus 로고    scopus 로고
    • Phospho-dependent ubiquitination and degradation of PAR-1 regulates synaptic morphology and tau-mediated Abeta toxicity in Drosophila
    • doi:10.1038/ncomms2278
    • Lee S, Wang JW, Yu W, Lu B. Phospho-dependent ubiquitination and degradation of PAR-1 regulates synaptic morphology and tau-mediated Abeta toxicity in Drosophila. Nat Commun (2012) 3:1312. doi:10.1038/ncomms2278
    • (2012) Nat Commun , vol.3 , pp. 1312
    • Lee, S.1    Wang, J.W.2    Yu, W.3    Lu, B.4
  • 29
    • 0028937631 scopus 로고
    • Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark) A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262.
    • Drewes G, Trinczek B, Illenberger S, Biernat J, Schmitt-Ulms G, Meyer HE, et al. Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J Biol Chem (1995) 270:7679-88.
    • (1995) J Biol Chem , vol.270 , pp. 7679-88
    • Drewes, G.1    Trinczek, B.2    Illenberger, S.3    Biernat, J.4    Schmitt-Ulms, G.5    Meyer, H.E.6
  • 30
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek B, Biernat J, Baumann K, Mandelkow EM, Mandelkow E. Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol Biol Cell (1995) 6:1887-902.
    • (1995) Mol Biol Cell , vol.6 , pp. 1887-902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 31
    • 0033803750 scopus 로고    scopus 로고
    • PKA phosphorylations on tau: developmental studies in the mouse
    • doi:10.1159/000017454
    • Andorfer CA, Davies P. PKA phosphorylations on tau: developmental studies in the mouse. Dev Neurosci (2000) 22:303-9. doi:10.1159/000017454
    • (2000) Dev Neurosci , vol.22 , pp. 303-9
    • Andorfer, C.A.1    Davies, P.2
  • 32
    • 84876270805 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor, protein kinase A (PKA) and c-Jun N-terminal kinase (JNK) signaling pathways mediate tau pathology in Alzheimer disease models
    • doi:10.1074/jbc.M112.415141
    • Wang D, Fu Q, Zhou Y, Xu B, Shi Q, Igwe B, et al. Beta2 adrenergic receptor, protein kinase A (PKA) and c-Jun N-terminal kinase (JNK) signaling pathways mediate tau pathology in Alzheimer disease models. J Biol Chem (2013) 288:10298-307. doi:10.1074/jbc.M112.415141
    • (2013) J Biol Chem , vol.288 , pp. 10298-307
    • Wang, D.1    Fu, Q.2    Zhou, Y.3    Xu, B.4    Shi, Q.5    Igwe, B.6
  • 33
    • 84856955428 scopus 로고    scopus 로고
    • Altered regulation of tau phosphorylation in a mouse model of down syndrome aging
    • doi:10.1016/j.neurobiolaging.2011.06.025
    • Sheppard O, Plattner F, Rubin A, Slender A, Linehan JM, Brandner S, et al. Altered regulation of tau phosphorylation in a mouse model of down syndrome aging. Neurobiol Aging (2012) 33(828):e831-44. doi:10.1016/j.neurobiolaging.2011.06.025
    • (2012) Neurobiol Aging , vol.33 , Issue.828
    • Sheppard, O.1    Plattner, F.2    Rubin, A.3    Slender, A.4    Linehan, J.M.5    Brandner, S.6
  • 34
    • 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 YL, Cohen P, Becker W, Jakes R, Goedert M, Wang X, 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) 355:609-15.
    • (2001) Biochem J , vol.355 , pp. 609-15
    • Woods, Y.L.1    Cohen, P.2    Becker, W.3    Jakes, R.4    Goedert, M.5    Wang, X.6
  • 35
    • 0036138048 scopus 로고    scopus 로고
    • Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-beta peptide exposure: involvement of Src family protein kinases
    • Williamson R, Scales T, Clark BR, Gibb G, Reynolds CH, Kellie S, et al. Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-beta peptide exposure: involvement of Src family protein kinases. J Neurosci (2002) 22:10-20.
    • (2002) J Neurosci , vol.22 , pp. 10-20
    • Williamson, R.1    Scales, T.2    Clark, B.R.3    Gibb, G.4    Reynolds, C.H.5    Kellie, S.6
  • 36
    • 12144288564 scopus 로고    scopus 로고
    • Phosphorylation of tau by fyn: implications for Alzheimer's disease
    • doi:10.1523/JNEUROSCI.4162-03.2004
    • Lee G, Thangavel R, Sharma VM, Litersky JM, Bhaskar K, Fang SM, et al. Phosphorylation of tau by fyn: implications for Alzheimer's disease. J Neurosci (2004) 24:2304-12. doi:10.1523/JNEUROSCI.4162-03.2004
    • (2004) J Neurosci , vol.24 , pp. 2304-12
    • Lee, G.1    Thangavel, R.2    Sharma, V.M.3    Litersky, J.M.4    Bhaskar, K.5    Fang, S.M.6
  • 37
    • 79958765866 scopus 로고    scopus 로고
    • c-Abl tyrosine kinase modulates tau pathology and Cdk5 phosphorylation in AD transgenic mice
    • doi:10.1016/j.neurobiolaging.2009.07.007
    • Cancino GI, Perez de Arce K, Castro PU, Toledo EM, Von Bernhardi R, Alvarez AR. c-Abl tyrosine kinase modulates tau pathology and Cdk5 phosphorylation in AD transgenic mice. Neurobiol Aging (2011) 32:1249-61. doi:10.1016/j.neurobiolaging.2009.07.007
    • (2011) Neurobiol Aging , vol.32 , pp. 1249-61
    • Cancino, G.I.1    Perez de Arce, K.2    Castro, P.U.3    Toledo, E.M.4    Von Bernhardi, R.5    Alvarez, A.R.6
  • 38
    • 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
    • doi:10.1523/JNEUROSCI.1487-05.2005
    • Derkinderen P, Scales TM, Hanger DP, Leung KY, Byers HL, Ward MA, 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) 25:6584-93. doi:10.1523/JNEUROSCI.1487-05.2005
    • (2005) J Neurosci , vol.25 , pp. 6584-93
    • Derkinderen, P.1    Scales, T.M.2    Hanger, D.P.3    Leung, K.Y.4    Byers, H.L.5    Ward, M.A.6
  • 40
    • 27644478606 scopus 로고    scopus 로고
    • Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
    • doi:10.1111/j.1460-9568.2005.04391.x
    • Liu F, Grundke-Iqbal I, Iqbal K, Gong CX. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci (2005) 22:1942-50. doi:10.1111/j.1460-9568.2005.04391.x
    • (2005) Eur J Neurosci , vol.22 , pp. 1942-50
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Gong, C.X.4
  • 41
    • 43249114144 scopus 로고    scopus 로고
    • Membrane-bound beta-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism
    • doi:10.1096/fj.07-9766com
    • Williamson R, Usardi A, Hanger DP, Anderton BH. Membrane-bound beta-amyloid oligomers are recruited into lipid rafts by a fyn-dependent mechanism. FASEB J (2008) 22:1552-9. doi:10.1096/fj.07-9766com
    • (2008) FASEB J , vol.22 , pp. 1552-9
    • Williamson, R.1    Usardi, A.2    Hanger, D.P.3    Anderton, B.H.4
  • 42
    • 84891149958 scopus 로고    scopus 로고
    • Clusterin regulates beta-amyloid toxicity via Dickkopf-1-driven induction of the wnt-PCP-JNK pathway
    • doi:10.1038/mp.2012.163. [Epub ahead of print]
    • Killick R, Ribe EM, Al-Shawi R, Malik B, Hooper C, Fernandes C, et al. Clusterin regulates beta-amyloid toxicity via Dickkopf-1-driven induction of the wnt-PCP-JNK pathway. Mol Psychiatry (2012). doi:10.1038/mp.2012.163. [Epub ahead of print].
    • (2012) Mol Psychiatry
    • Killick, R.1    Ribe, E.M.2    Al-Shawi, R.3    Malik, B.4    Hooper, C.5    Fernandes, C.6
  • 43
    • 84865966647 scopus 로고    scopus 로고
    • JNK3 perpetuates metabolic stress induced by Abeta peptides
    • doi:10.1016/j.neuron.2012.06.024
    • Yoon SO, Park DJ, Ryu JC, Ozer HG, Tep C, Shin YJ, et al. JNK3 perpetuates metabolic stress induced by Abeta peptides. Neuron (2012) 75:824-37. doi:10.1016/j.neuron.2012.06.024
    • (2012) Neuron , vol.75 , pp. 824-37
    • Yoon, S.O.1    Park, D.J.2    Ryu, J.C.3    Ozer, H.G.4    Tep, C.5    Shin, Y.J.6
  • 44
    • 37049027122 scopus 로고    scopus 로고
    • Tau phosphorylation sites work in concert to promote neurotoxicity in vivo
    • doi:10.1091/mbc.E07-04-0327
    • Steinhilb ML, Dias-Santagata D, Fulga TA, Felch DL, Feany MB. Tau phosphorylation sites work in concert to promote neurotoxicity in vivo. Mol Biol Cell (2007) 18(12):5060-8. doi:10.1091/mbc.E07-04-0327
    • (2007) Mol Biol Cell , vol.18 , Issue.12 , pp. 5060-8
    • Steinhilb, M.L.1    Dias-Santagata, D.2    Fulga, T.A.3    Felch, D.L.4    Feany, M.B.5
  • 45
    • 79954437580 scopus 로고    scopus 로고
    • Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody
    • doi:10.1007/s00726-010-0705-1
    • Yuzwa SA, Yadav AK, Skorobogatko Y, Clark T, Vosseller K, Vocadlo DJ. Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody. Amino Acids (2011) 40:857-68. doi:10.1007/s00726-010-0705-1
    • (2011) Amino Acids , vol.40 , pp. 857-68
    • Yuzwa, S.A.1    Yadav, A.K.2    Skorobogatko, Y.3    Clark, T.4    Vosseller, K.5    Vocadlo, D.J.6
  • 46
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: implications for Alzheimer's disease
    • doi:10.1016/j.neuint.2010.12.023
    • Martin L, Latypova X, Terro F. Post-translational modifications of tau protein: implications for Alzheimer's disease. Neurochem Int (2011) 58:458-71. doi:10.1016/j.neuint.2010.12.023
    • (2011) Neurochem Int , vol.58 , pp. 458-71
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 47
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • doi:10.1172/JCI20640
    • Rissman RA, Poon WW, Blurton-Jones M, Oddo S, Torp R, Vitek MP, et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J Clin Invest (2004) 114:121-30. doi:10.1172/JCI20640
    • (2004) J Clin Invest , vol.114 , pp. 121-30
    • Rissman, R.A.1    Poon, W.W.2    Blurton-Jones, M.3    Oddo, S.4    Torp, R.5    Vitek, M.P.6
  • 48
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • doi:10.1523/JNEUROSCI.1125-05.2005
    • Park SY, Ferreira A. The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci (2005) 25:5365-75. doi:10.1523/JNEUROSCI.1125-05.2005
    • (2005) J Neurosci , vol.25 , pp. 5365-75
    • Park, S.Y.1    Ferreira, A.2
  • 50
    • 79960735446 scopus 로고    scopus 로고
    • Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathies
    • doi:10.2119/molmed.2010.00220
    • Ferreira A, Bigio EH. Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathies. Mol Med (2011) 17:676-85. doi:10.2119/molmed.2010.00220
    • (2011) Mol Med , vol.17 , pp. 676-85
    • Ferreira, A.1    Bigio, E.H.2
  • 52
    • 11144227267 scopus 로고    scopus 로고
    • Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis
    • doi:10.1074/jbc.M408186200
    • Rametti A, Esclaire F, Yardin C, Terro F. Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis. J Biol Chem (2004) 279:54518-28. doi:10.1074/jbc.M408186200
    • (2004) J Biol Chem , vol.279 , pp. 54518-28
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3    Terro, F.4
  • 53
    • 33646080573 scopus 로고    scopus 로고
    • Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo
    • doi:10.1111/j.1471-4159.2006.03784.x
    • Guillozet-Bongaarts AL, Cahill ME, Cryns VL, Reynolds MR, Berry RW, Binder LI. Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo. J Neurochem (2006) 97:1005-14. doi:10.1111/j.1471-4159.2006.03784.x
    • (2006) J Neurochem , vol.97 , pp. 1005-14
    • Guillozet-Bongaarts, A.L.1    Cahill, M.E.2    Cryns, V.L.3    Reynolds, M.R.4    Berry, R.W.5    Binder, L.I.6
  • 54
    • 79959945013 scopus 로고    scopus 로고
    • Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture
    • doi:10.1038/cddis.2011.50
    • Garwood CJ, Pooler AM, Atherton J, Hanger DP, Noble W. Astrocytes are important mediators of Abeta-induced neurotoxicity and tau phosphorylation in primary culture. Cell Death Dis (2011) 2:e167. doi:10.1038/cddis.2011.50
    • (2011) Cell Death Dis , vol.2
    • Garwood, C.J.1    Pooler, A.M.2    Atherton, J.3    Hanger, D.P.4    Noble, W.5
  • 55
    • 11144228296 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ
    • doi:10.1074/jbc.M403364200
    • Cho JH, Johnson GV. Glycogen synthase kinase 3 beta induces caspase-cleaved tau aggregation in situ. J Biol Chem (2004) 279:54716-23. doi:10.1074/jbc.M403364200
    • (2004) J Biol Chem , vol.279 , pp. 54716-23
    • Cho, J.H.1    Johnson, G.V.2
  • 56
    • 20044381844 scopus 로고    scopus 로고
    • Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease
    • doi:10.1016/j.neurobiolaging.2004.09.019
    • Guillozet-Bongaarts AL, Garcia-Sierra F, Reynolds MR, Horowitz PM, Fu Y, Wang T, et al. Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol Aging (2005) 26:1015-22. doi:10.1016/j.neurobiolaging.2004.09.019
    • (2005) Neurobiol Aging , vol.26 , pp. 1015-22
    • Guillozet-Bongaarts, A.L.1    Garcia-Sierra, F.2    Reynolds, M.R.3    Horowitz, P.M.4    Fu, Y.5    Wang, T.6
  • 57
    • 13644268449 scopus 로고    scopus 로고
    • Changed conformation of mutant tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of tau-4R/2N transgenic mice
    • doi:10.1074/jbc.M409876200
    • Terwel D, Lasrado R, Snauwaert J, Vandeweert E, Van Haesendonck C, Borghgraef P, et al. Changed conformation of mutant tau-P301L underlies the moribund tauopathy, absent in progressive, nonlethal axonopathy of tau-4R/2N transgenic mice. J Biol Chem (2005) 280(5):3963-73. doi:10.1074/jbc.M409876200
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3963-73
    • Terwel, D.1    Lasrado, R.2    Snauwaert, J.3    Vandeweert, E.4    Van Haesendonck, C.5    Borghgraef, P.6
  • 58
    • 36448936747 scopus 로고    scopus 로고
    • Kinase activities increase during the development of tauopathy in htau mice
    • doi:10.1111/j.1471-4159.2007.04930.x
    • Kelleher I, Garwood C, Hanger DP, Anderton BH, Noble W. Kinase activities increase during the development of tauopathy in htau mice. J Neurochem (2007) 103:2256-67. doi:10.1111/j.1471-4159.2007.04930.x
    • (2007) J Neurochem , vol.103 , pp. 2256-67
    • Kelleher, I.1    Garwood, C.2    Hanger, D.P.3    Anderton, B.H.4    Noble, W.5
  • 61
    • 84855368532 scopus 로고    scopus 로고
    • NMNAT suppresses tau-induced neurodegeneration by promoting clearance of hyperphosphorylated tau oligomers in a Drosophila model of tauopathy
    • doi:10.1093/hmg/ddr449
    • Ali YO, Ruan K, Zhai RG. NMNAT suppresses tau-induced neurodegeneration by promoting clearance of hyperphosphorylated tau oligomers in a Drosophila model of tauopathy. Hum Mol Genet (2012) 21:237-50. doi:10.1093/hmg/ddr449
    • (2012) Hum Mol Genet , vol.21 , pp. 237-50
    • Ali, Y.O.1    Ruan, K.2    Zhai, R.G.3
  • 62
    • 34249862316 scopus 로고    scopus 로고
    • The role of tau phosphorylation and cleavage in neuronal cell death
    • doi:10.2741/2097
    • Chun W, Johnson GV. The role of tau phosphorylation and cleavage in neuronal cell death. Front Biosci (2007) 12:733-56. doi:10.2741/2097
    • (2007) Front Biosci , vol.12 , pp. 733-56
    • Chun, W.1    Johnson, G.V.2
  • 63
    • 84867519558 scopus 로고    scopus 로고
    • Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with alpha-synuclein at the single molecule level
    • doi:10.1186/1750-1326-7-35
    • Nubling G, Bader B, Levin J, Hildebrandt J, Kretzschmar H, Giese A. Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with alpha-synuclein at the single molecule level. Mol Neurodegener (2012) 7:35. doi:10.1186/1750-1326-7-35
    • (2012) Mol Neurodegener , vol.7 , pp. 35
    • Nubling, G.1    Bader, B.2    Levin, J.3    Hildebrandt, J.4    Kretzschmar, H.5    Giese, A.6
  • 64
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • doi:10.1073/pnas.1630428100
    • Gamblin TC, Chen F, Zambrano A, Abraha A, Lagalwar S, Guillozet AL, et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci U S A (2003) 100(17):10032-7. doi:10.1073/pnas.1630428100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.17 , pp. 10032-7
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3    Abraha, A.4    Lagalwar, S.5    Guillozet, A.L.6
  • 65
    • 84867571146 scopus 로고    scopus 로고
    • Extensive p-tau pathology and SDS-stable p-tau oligomers in Alzheimer's cortical synapses
    • doi:10.1111/j.1750-3639.2012.00598.x
    • Henkins KM, Sokolow S, Miller CA, Vinters HV, Poon WW, Cornwell LB, et al. Extensive p-tau pathology and SDS-stable p-tau oligomers in Alzheimer's cortical synapses. Brain Pathol (2012) 22:826-33. doi:10.1111/j.1750-3639.2012.00598.x
    • (2012) Brain Pathol , vol.22 , pp. 826-33
    • Henkins, K.M.1    Sokolow, S.2    Miller, C.A.3    Vinters, H.V.4    Poon, W.W.5    Cornwell, L.B.6
  • 66
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • doi:10.1101/cshperspect.a006247
    • Mandelkow EM, Mandelkow E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb Perspect Med (2012) 2:a006247. doi:10.1101/cshperspect.a006247
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 67
    • 84859580519 scopus 로고    scopus 로고
    • Tau and tauopathies
    • doi:10.1016/B978-0-12-385883-2.00004-7
    • Lee G,Leugers CJ. Tau and tauopathies. Prog Mol Biol Transl Sci (2012) 107:263-93. doi:10.1016/B978-0-12-385883-2.00004-7
    • (2012) Prog Mol Biol Transl Sci , vol.107 , pp. 263-93
    • Lee, G.1    Leugers, C.J.2
  • 68
    • 0035811050 scopus 로고    scopus 로고
    • Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments
    • doi:10.1073/pnas.121119298
    • Alonso A, Zaidi T, Novak M, Grundke-Iqbal I, Iqbal K. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci U S A (2001) 98(12):6923-8. doi:10.1073/pnas.121119298
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.12 , pp. 6923-8
    • Alonso, A.1    Zaidi, T.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 69
    • 22244443877 scopus 로고    scopus 로고
    • Hyperphosphorylation-induced self assembly of murine tau: a comparison with human tau
    • doi:10.1007/s00702-004-0241-9
    • Chohan MO, Haque N, Alonso A, El-Akkad E, Grundke-Iqbal I, Grover A, et al. Hyperphosphorylation-induced self assembly of murine tau: a comparison with human tau. J Neural Transm (2005) 112:1035-47. doi:10.1007/s00702-004-0241-9
    • (2005) J Neural Transm , vol.112 , pp. 1035-47
    • Chohan, M.O.1    Haque, N.2    Alonso, A.3    El-Akkad, E.4    Grundke-Iqbal, I.5    Grover, A.6
  • 70
    • 0031633953 scopus 로고    scopus 로고
    • Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles
    • doi:10.1007/978-3-7091-6467-9_15
    • Iqbal K, Alonso AC, Gong CX, Khatoon S, Pei JJ, Wang JZ, et al. Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles. J Neural Transm Suppl (1998) 53:169-80. doi:10.1007/978-3-7091-6467-9_15
    • (1998) J Neural Transm Suppl , vol.53 , pp. 169-80
    • Iqbal, K.1    Alonso, A.C.2    Gong, C.X.3    Khatoon, S.4    Pei, J.J.5    Wang, J.Z.6
  • 71
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • doi:10.1093/emboj/20.1.27
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R, Avila J. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J (2001) 20:27-39. doi:10.1093/emboj/20.1.27
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 72
    • 33745449875 scopus 로고    scopus 로고
    • An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice
    • doi:10.1073/pnas.0602913103
    • Le Corre S, Klafki HW, Plesnila N, Hubinger G, Obermeier A, Sahagun H, et al. An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice. Proc Natl Acad Sci U S A (2006) 103:9673-8. doi:10.1073/pnas.0602913103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9673-8
    • Le Corre, S.1    Klafki, H.W.2    Plesnila, N.3    Hubinger, G.4    Obermeier, A.5    Sahagun, H.6
  • 73
    • 84871744906 scopus 로고    scopus 로고
    • Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo
    • doi:10.1523/JNEUROSCI.3593-12.2013
    • Sundaram JR, Poore CP, Sulaimee NH, Pareek T, Asad AB, Rajkumar R, et al. Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo. J Neurosci (2013) 33:334-43. doi:10.1523/JNEUROSCI.3593-12.2013
    • (2013) J Neurosci , vol.33 , pp. 334-43
    • Sundaram, J.R.1    Poore, C.P.2    Sulaimee, N.H.3    Pareek, T.4    Asad, A.B.5    Rajkumar, R.6
  • 74
    • 84858153335 scopus 로고    scopus 로고
    • Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: implications of autophagy promotion
    • doi:10.1016/j.nbd.2011.12.050
    • Shimada K, Motoi Y, Ishiguro K, Kambe T, Matsumoto SE, Itaya M, et al. Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: implications of autophagy promotion. Neurobiol Dis (2012) 46:101-8. doi:10.1016/j.nbd.2011.12.050
    • (2012) Neurobiol Dis , vol.46 , pp. 101-8
    • Shimada, K.1    Motoi, Y.2    Ishiguro, K.3    Kambe, T.4    Matsumoto, S.E.5    Itaya, M.6
  • 75
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • doi:10.1021/bi981874p
    • Schneider A, Biernat J, Von Bergen M, Mandelkow E, Mandelkow EM. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry (1999) 38:3549-58. doi:10.1021/bi981874p
    • (1999) Biochemistry , vol.38 , pp. 3549-58
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 76
    • 0042679510 scopus 로고    scopus 로고
    • Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice
    • doi:10.1016/S0002-9440(10)63444-X
    • Kins S, Kurosinski P, Nitsch RM, Götz J. Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice. Am J Pathol (2003) 163(3):833-43. doi:10.1016/S0002-9440(10)63444-X
    • (2003) Am J Pathol , vol.163 , Issue.3 , pp. 833-43
    • Kins, S.1    Kurosinski, P.2    Nitsch, R.M.3    Götz, J.4
  • 77
    • 79955566269 scopus 로고    scopus 로고
    • Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta
    • doi:10.1073/pnas.1018777108
    • Louis JV, Martens E, Borghgraef P, Lambrecht C, Sents W, Longin S, et al. Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta. Proc Natl Acad Sci U S A (2011) 108(17):6957-62. doi:10.1073/pnas.1018777108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.17 , pp. 6957-62
    • Louis, J.V.1    Martens, E.2    Borghgraef, P.3    Lambrecht, C.4    Sents, W.5    Longin, S.6
  • 78
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • doi:10.1126/science.1062097
    • Götz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science (2001) 293(5534):1491-5. doi:10.1126/science.1062097
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-5
    • Götz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 80
    • 49149109927 scopus 로고    scopus 로고
    • Is tau aggregation toxic or protective?
    • Congdon EE, Duff KE. Is tau aggregation toxic or protective?. J Alzheimers Dis (2008) 14:453-7.
    • (2008) J Alzheimers Dis , vol.14 , pp. 453-7
    • Congdon, E.E.1    Duff, K.E.2
  • 81
    • 0028838142 scopus 로고
    • Sorting mechanisms of tau and MAP2 in neurons: suppressed axonal transit of MAP2 and locally regulated microtubule binding
    • doi:10.1016/0896-6273(95)90298-8
    • Kanai Y, Hirokawa N. Sorting mechanisms of tau and MAP2 in neurons: suppressed axonal transit of MAP2 and locally regulated microtubule binding. Neuron (1995) 14:421-32. doi:10.1016/0896-6273(95)90298-8
    • (1995) Neuron , vol.14 , pp. 421-32
    • Kanai, Y.1    Hirokawa, N.2
  • 82
    • 0036798495 scopus 로고    scopus 로고
    • Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules
    • doi:10.1242/jcs.00058
    • Aronov S, Aranda G, Behar L, Ginzburg I. Visualization of translated tau protein in the axons of neuronal P19 cells and characterization of tau RNP granules. J Cell Sci (2002) 115:3817-27. doi:10.1242/jcs.00058
    • (2002) J Cell Sci , vol.115 , pp. 3817-27
    • Aronov, S.1    Aranda, G.2    Behar, L.3    Ginzburg, I.4
  • 83
    • 82455208974 scopus 로고    scopus 로고
    • Novel diffusion barrier for axonal retention of tau in neurons and its failure in neurodegeneration
    • doi:10.1038/emboj.2011.376
    • Li X, Kumar Y, Zempel H, Mandelkow EM, Biernat J, Mandelkow E. Novel diffusion barrier for axonal retention of tau in neurons and its failure in neurodegeneration. EMBO J (2011) 30:4825-37. doi:10.1038/emboj.2011.376
    • (2011) EMBO J , vol.30 , pp. 4825-37
    • Li, X.1    Kumar, Y.2    Zempel, H.3    Mandelkow, E.M.4    Biernat, J.5    Mandelkow, E.6
  • 84
    • 70350455151 scopus 로고    scopus 로고
    • Specification of neuronal polarity regulated by local translation of CRMP2 and tau via the mTOR-p70S6K pathway
    • doi:10.1074/jbc.M109.008177
    • Morita T, Sobue K. Specification of neuronal polarity regulated by local translation of CRMP2 and tau via the mTOR-p70S6K pathway. J Biol Chem (2009) 284:27734-45. doi:10.1074/jbc.M109.008177
    • (2009) J Biol Chem , vol.284 , pp. 27734-45
    • Morita, T.1    Sobue, K.2
  • 85
    • 0030028366 scopus 로고    scopus 로고
    • Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons
    • doi:10.1083/jcb.132.4.667
    • Hirokawa N, Funakoshi T, Sato-Harada R, Kanai Y. Selective stabilization of tau in axons and microtubule-associated protein 2C in cell bodies and dendrites contributes to polarized localization of cytoskeletal proteins in mature neurons. J Cell Biol (1996) 132:667-79. doi:10.1083/jcb.132.4.667
    • (1996) J Cell Biol , vol.132 , pp. 667-79
    • Hirokawa, N.1    Funakoshi, T.2    Sato-Harada, R.3    Kanai, Y.4
  • 86
    • 0041803006 scopus 로고    scopus 로고
    • Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms
    • doi:10.1046/j.1471-4159.2003.01879.x
    • Andorfer C, Kress Y, Espinoza M, de Silva R, Tucker KL, Barde YA, et al. Hyperphosphorylation and aggregation of tau in mice expressing normal human tau isoforms. J Neurochem (2003) 86:582-90. doi:10.1046/j.1471-4159.2003.01879.x
    • (2003) J Neurochem , vol.86 , pp. 582-90
    • Andorfer, C.1    Kress, Y.2    Espinoza, M.3    de Silva, R.4    Tucker, K.L.5    Barde, Y.A.6
  • 87
    • 80054904670 scopus 로고    scopus 로고
    • Stages of the pathologic process in Alzheimer disease: age categories from 1 to 100 years
    • doi:10.1097/NEN.0b013e318232a379
    • Braak H, Thal DR, Ghebremedhin E, Del Tredici K. Stages of the pathologic process in Alzheimer disease: age categories from 1 to 100 years. J Neuropathol Exp Neurol (2011) 70:960-9. doi:10.1097/NEN.0b013e318232a379
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 960-9
    • Braak, H.1    Thal, D.R.2    Ghebremedhin, E.3    Del Tredici, K.4
  • 88
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites Differential impact on microtubule binding.
    • doi:10.1074/jbc.M206236200
    • Cho JH, Johnson GV. Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J Biol Chem (2003) 278:187-93. doi:10.1074/jbc.M206236200
    • (2003) J Biol Chem , vol.278 , pp. 187-93
    • Cho, J.H.1    Johnson, G.V.2
  • 89
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • doi:10.1038/21650
    • Lu PJ, Wulf G, Zhou XZ, Davies P, Lu KP. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature (1999) 399:784-8. doi:10.1038/21650
    • (1999) Nature , vol.399 , pp. 784-8
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 90
    • 0033638180 scopus 로고    scopus 로고
    • Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins
    • doi:10.1016/S1097-2765(05)00083-3
    • Zhou XZ, Kops O, Werner A, Lu PJ, Shen M, Stoller G, et al. Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and tau proteins. Mol Cell (2000) 6(4):873-83. doi:10.1016/S1097-2765(05)00083-3
    • (2000) Mol Cell , vol.6 , Issue.4 , pp. 873-83
    • Zhou, X.Z.1    Kops, O.2    Werner, A.3    Lu, P.J.4    Shen, M.5    Stoller, G.6
  • 91
    • 79959534777 scopus 로고    scopus 로고
    • Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau
    • doi:10.1371/journal.pone.0021521
    • Landrieu I, Smet-Nocca C, Amniai L, Louis JV, Wieruszeski JM, Goris J, et al. Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau. PLoS One (2011) 6(6):e21521. doi:10.1371/journal.pone.0021521
    • (2011) PLoS One , vol.6 , Issue.6
    • Landrieu, I.1    Smet-Nocca, C.2    Amniai, L.3    Louis, J.V.4    Wieruszeski, J.M.5    Goris, J.6
  • 92
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • doi:10.1038/nm0796-783
    • Alonso AC, Grundke-Iqbal I, Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med (1996) 2:783-7. doi:10.1038/nm0796-783
    • (1996) Nat Med , vol.2 , pp. 783-7
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 93
    • 33745024475 scopus 로고    scopus 로고
    • Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity
    • doi:10.1073/pnas.0603214103
    • Alonso Adel C, Li B, Grundke-Iqbal I, Iqbal K. Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity. Proc Natl Acad Sci U S A (2006) 103(23):8864-9. doi:10.1073/pnas.0603214103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.23 , pp. 8864-9
    • Alonso Adel, C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 94
    • 84864395349 scopus 로고    scopus 로고
    • Brain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathies
    • doi:10.1042/BST20120010
    • Brunden KR, Ballatore C, Lee VM, Smith AB III, Trojanowski JQ. Brain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathies. Biochem Soc Trans (2012) 40:661-6. doi:10.1042/BST20120010
    • (2012) Biochem Soc Trans , vol.40 , pp. 661-6
    • Brunden, K.R.1    Ballatore, C.2    Lee, V.M.3    Smith, A.B.4    Trojanowski, J.Q.5
  • 95
    • 84863230105 scopus 로고    scopus 로고
    • The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • doi:10.1523/JNEUROSCI.4922-11.2012
    • Zhang B, Carroll J, Trojanowski JQ, Yao Y, Iba M, Potuzak JS, et al. The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci (2012) 32:3601-11. doi:10.1523/JNEUROSCI.4922-11.2012
    • (2012) J Neurosci , vol.32 , pp. 3601-11
    • Zhang, B.1    Carroll, J.2    Trojanowski, J.Q.3    Yao, Y.4    Iba, M.5    Potuzak, J.S.6
  • 96
    • 27844470590 scopus 로고    scopus 로고
    • Molecular motors implicated in the axonal transport of tau and alpha-synuclein
    • doi:10.1242/jcs.02558
    • Utton MA, Noble WJ, Hill JE, Anderton BH, Hanger DP. Molecular motors implicated in the axonal transport of tau and alpha-synuclein. J Cell Sci (2005) 118:4645-54. doi:10.1242/jcs.02558
    • (2005) J Cell Sci , vol.118 , pp. 4645-54
    • Utton, M.A.1    Noble, W.J.2    Hill, J.E.3    Anderton, B.H.4    Hanger, D.P.5
  • 97
    • 51349143580 scopus 로고    scopus 로고
    • Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin
    • doi:10.1096/fj.08-109181
    • Cuchillo-Ibanez I, Seereeram A, Byers HL, Leung KY, Ward MA, Anderton BH, et al. Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin. FASEB J (2008) 22:3186-95. doi:10.1096/fj.08-109181
    • (2008) FASEB J , vol.22 , pp. 3186-95
    • Cuchillo-Ibanez, I.1    Seereeram, A.2    Byers, H.L.3    Leung, K.Y.4    Ward, M.A.5    Anderton, B.H.6
  • 99
    • 39749165656 scopus 로고    scopus 로고
    • Differential regulation of dynein and kinesin motor proteins by tau
    • doi:10.1126/science.1152993
    • Dixit R, Ross JL, Goldman YE, Holzbaur EL. Differential regulation of dynein and kinesin motor proteins by tau. Science (2008) 319:1086-9. doi:10.1126/science.1152993
    • (2008) Science , vol.319 , pp. 1086-9
    • Dixit, R.1    Ross, J.L.2    Goldman, Y.E.3    Holzbaur, E.L.4
  • 100
    • 84856954738 scopus 로고    scopus 로고
    • Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport
    • doi:10.1016/j.neurobiolaging.2011.06.006
    • Kanaan NM, Morfini G, Pigino G, Lapointe NE, Andreadis A, Song Y, et al. Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport. Neurobiol Aging (2012) 33(826):e815-30. doi:10.1016/j.neurobiolaging.2011.06.006
    • (2012) Neurobiol Aging , vol.33 , Issue.826
    • Kanaan, N.M.1    Morfini, G.2    Pigino, G.3    Lapointe, N.E.4    Andreadis, A.5    Song, Y.6
  • 101
    • 57349172663 scopus 로고    scopus 로고
    • Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
    • doi:10.1073/pnas.0808084105
    • Ittner LM, Fath T, Ke YD, Bi M, van Eersel J, Li KM, et al. Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. Proc Natl Acad Sci U S A (2008) 105:15997-6002. doi:10.1073/pnas.0808084105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15997-6002
    • Ittner, L.M.1    Fath, T.2    Ke, Y.D.3    Bi, M.4    van Eersel, J.5    Li, K.M.6
  • 102
    • 68949105821 scopus 로고    scopus 로고
    • Phosphorylated tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease
    • doi:10.1074/jbc.M109.014472
    • Ittner LM, Ke YD, Gotz J. Phosphorylated tau interacts with c-Jun N-terminal kinase-interacting protein 1 (JIP1) in Alzheimer disease. J Biol Chem (2009) 284:20909-16. doi:10.1074/jbc.M109.014472
    • (2009) J Biol Chem , vol.284 , pp. 20909-16
    • Ittner, L.M.1    Ke, Y.D.2    Gotz, J.3
  • 103
    • 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
    • Mandelkow EM, Stamer K, Vogel R, Thies E, Mandelkow E. Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging (2003) 24:1079-85. doi:10.1016/j.neurobiolaging.2003.04.007
    • (2003) Neurobiol Aging , vol.24 , pp. 1079-85
    • Mandelkow, E.M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 104
    • 48249102303 scopus 로고    scopus 로고
    • Role of axonal transport in neurodegenerative diseases
    • doi:10.1146/annurev.neuro.31.061307.090711
    • De Vos KJ, Grierson AJ, Ackerley S, Miller CC. Role of axonal transport in neurodegenerative diseases. Annu Rev Neurosci (2008) 31:151-73. doi:10.1146/annurev.neuro.31.061307.090711
    • (2008) Annu Rev Neurosci , vol.31 , pp. 151-73
    • De Vos, K.J.1    Grierson, A.J.2    Ackerley, S.3    Miller, C.C.4
  • 105
    • 84866150232 scopus 로고    scopus 로고
    • Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1
    • doi:10.1371/journal.pgen.1002918
    • Iijima-Ando K, Sekiya M, Maruko-Otake A, Ohtake Y, Suzuki E, Lu B, et al. Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1. PLoS Genet (2012) 8:e1002918. doi:10.1371/journal.pgen.1002918
    • (2012) PLoS Genet , vol.8
    • Iijima-Ando, K.1    Sekiya, M.2    Maruko-Otake, A.3    Ohtake, Y.4    Suzuki, E.5    Lu, B.6
  • 106
    • 77958459087 scopus 로고    scopus 로고
    • Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies
    • doi:10.1093/hmg/ddq363
    • Falzone TL, Gunawardena S, McCleary D, Reis GF, Goldstein LS. Kinesin-1 transport reductions enhance human tau hyperphosphorylation, aggregation and neurodegeneration in animal models of tauopathies. Hum Mol Genet (2010) 19:4399-408. doi:10.1093/hmg/ddq363
    • (2010) Hum Mol Genet , vol.19 , pp. 4399-408
    • Falzone, T.L.1    Gunawardena, S.2    McCleary, D.3    Reis, G.F.4    Goldstein, L.S.5
  • 107
    • 84859598872 scopus 로고    scopus 로고
    • Biology of mitochondria in neurodegenerative diseases
    • doi:10.1016/B978-0-12-385883-2.00005-9
    • Martin LJ. Biology of mitochondria in neurodegenerative diseases. Prog Mol Biol Transl Sci (2012) 107:355-415. doi:10.1016/B978-0-12-385883-2.00005-9
    • (2012) Prog Mol Biol Transl Sci , vol.107 , pp. 355-415
    • Martin, L.J.1
  • 108
    • 80053289984 scopus 로고    scopus 로고
    • Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain
    • doi:10.1016/j.ajpath.2011.07.004
    • Kopeikina KJ, Carlson GA, Pitstick R, Ludvigson AE, Peters A, Luebke JI, et al. Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain. Am J Pathol (2011) 179:2071-82. doi:10.1016/j.ajpath.2011.07.004
    • (2011) Am J Pathol , vol.179 , pp. 2071-82
    • Kopeikina, K.J.1    Carlson, G.A.2    Pitstick, R.3    Ludvigson, A.E.4    Peters, A.5    Luebke, J.I.6
  • 109
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease
    • doi:10.1083/jcb.143.3.777
    • Ebneth A, Godemann R, Stamer K, Illenberger S, Trinczek B, Mandelkow E. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J Cell Biol (1998) 143:777-94. doi:10.1083/jcb.143.3.777
    • (1998) J Cell Biol , vol.143 , pp. 777-94
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 110
    • 84857073309 scopus 로고    scopus 로고
    • Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease
    • doi:10.1523/JNEUROSCI.5927-11.2012
    • Shahpasand K, Uemura I, Saito T, Asano T, Hata K, Shibata K, et al. Regulation of mitochondrial transport and inter-microtubule spacing by tau phosphorylation at the sites hyperphosphorylated in Alzheimer's disease. J Neurosci (2012) 32:2430-41. doi:10.1523/JNEUROSCI.5927-11.2012
    • (2012) J Neurosci , vol.32 , pp. 2430-41
    • Shahpasand, K.1    Uemura, I.2    Saito, T.3    Asano, T.4    Hata, K.5    Shibata, K.6
  • 111
    • 84861130196 scopus 로고    scopus 로고
    • Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage
    • doi:10.1093/hmg/dds072
    • Manczak M, Reddy PH. Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage. Hum Mol Genet (2012) 21:2538-47. doi:10.1093/hmg/dds072
    • (2012) Hum Mol Genet , vol.21 , pp. 2538-47
    • Manczak, M.1    Reddy, P.H.2
  • 112
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • doi:10.1016/j.neuron.2012.06.026
    • DuBoff B, Götz J, Feany MB. Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron (2012) 75(4):618-32. doi:10.1016/j.neuron.2012.06.026
    • (2012) Neuron , vol.75 , Issue.4 , pp. 618-32
    • DuBoff, B.1    Götz, J.2    Feany, M.B.3
  • 113
    • 84878586555 scopus 로고    scopus 로고
    • Why size matters - balancing mitochondrial dynamics in Alzheimer's disease.
    • doi:10.1016/j.tins.2013.03.002
    • DuBoff B, Feany M, Gotz J. Why size matters - balancing mitochondrial dynamics in Alzheimer's disease. Trends Neurosci (2013). doi:10.1016/j.tins.2013.03.002
    • (2013) Trends Neurosci
    • DuBoff, B.1    Feany, M.2    Gotz, J.3
  • 114
    • 33750553861 scopus 로고    scopus 로고
    • Tau interacts with Golgi membranes and mediates their association with microtubules
    • doi:10.1002/cm.20157
    • Farah CA, Perreault S, Liazoghli D, Desjardins M, Anton A, Lauzon M, et al. Tau interacts with Golgi membranes and mediates their association with microtubules. Cell Motil Cytoskeleton (2006) 63:710-24. doi:10.1002/cm.20157
    • (2006) Cell Motil Cytoskeleton , vol.63 , pp. 710-24
    • Farah, C.A.1    Perreault, S.2    Liazoghli, D.3    Desjardins, M.4    Anton, A.5    Lauzon, M.6
  • 115
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • doi:10.1083/jcb.131.5.1327
    • Brandt R, Leger J, Lee G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J Cell Biol (1995) 131:1327-40. doi:10.1083/jcb.131.5.1327
    • (1995) J Cell Biol , vol.131 , pp. 1327-40
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 116
    • 82755189704 scopus 로고    scopus 로고
    • Dynamic association of tau with neuronal membranes is regulated by phosphorylation
    • doi:10.1016/j.neurobiolaging.2011.01.005
    • Pooler AM, Usardi A, Evans CJ, Philpott KL, Noble W, Hanger DP. Dynamic association of tau with neuronal membranes is regulated by phosphorylation. Neurobiol Aging (2012) 33(431):e427-38. doi:10.1016/j.neurobiolaging.2011.01.005
    • (2012) Neurobiol Aging , vol.33 , Issue.431
    • Pooler, A.M.1    Usardi, A.2    Evans, C.J.3    Philpott, K.L.4    Noble, W.5    Hanger, D.P.6
  • 117
    • 0040141570 scopus 로고    scopus 로고
    • Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
    • doi:10.1074/jbc.M000389200
    • Maas T, Eidenmuller J, Brandt R. Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments. J Biol Chem (2000) 275:15733-40. doi:10.1074/jbc.M000389200
    • (2000) J Biol Chem , vol.275 , pp. 15733-40
    • Maas, T.1    Eidenmuller, J.2    Brandt, R.3
  • 118
    • 77955941947 scopus 로고    scopus 로고
    • Functional implications of the association of tau with the plasma membrane
    • doi:10.1042/BST0381012
    • Pooler AM, Hanger DP. Functional implications of the association of tau with the plasma membrane. Biochem Soc Trans (2010) 38:1012-5. doi:10.1042/BST0381012
    • (2010) Biochem Soc Trans , vol.38 , pp. 1012-5
    • Pooler, A.M.1    Hanger, D.P.2
  • 119
    • 17544393297 scopus 로고    scopus 로고
    • Tau dephosphorylation at tau-1 site correlates with its association to cell membrane
    • doi:10.1023/A:1007583214722
    • Arrasate M, Perez M, Avila J. Tau dephosphorylation at tau-1 site correlates with its association to cell membrane. Neurochem Res (2000) 25:43-50. doi:10.1023/A:1007583214722
    • (2000) Neurochem Res , vol.25 , pp. 43-50
    • Arrasate, M.1    Perez, M.2    Avila, J.3
  • 120
    • 0033922393 scopus 로고    scopus 로고
    • Phosphorylation of tau alters its association with the plasma membrane
    • doi:10.1023/A:1007075115574
    • Ekinci FJ, Shea TB. Phosphorylation of tau alters its association with the plasma membrane. Cell Mol Neurobiol (2000) 20:497-508. doi:10.1023/A:1007075115574
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 497-508
    • Ekinci, F.J.1    Shea, T.B.2
  • 121
    • 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
    • doi:10.1111/j.1742-4658
    • Usardi A, Pooler AM, Seereeram A, Reynolds CH, Derkinderen P, Anderton B, et al. Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau. FEBS J (2011) 278:2927-37. doi:10.1111/j.1742-4658
    • (2011) FEBS J , vol.278 , pp. 2927-37
    • Usardi, A.1    Pooler, A.M.2    Seereeram, A.3    Reynolds, C.H.4    Derkinderen, P.5    Anderton, B.6
  • 122
    • 49649119504 scopus 로고    scopus 로고
    • Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases
    • doi:10.1074/jbc.M709715200
    • Reynolds CH, Garwood CJ, Wray S, Price C, Kellie S, Perera T, et al. Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases. J Biol Chem (2008) 283:18177-86. doi:10.1074/jbc.M709715200
    • (2008) J Biol Chem , vol.283 , pp. 18177-86
    • Reynolds, C.H.1    Garwood, C.J.2    Wray, S.3    Price, C.4    Kellie, S.5    Perera, T.6
  • 123
    • 0035139540 scopus 로고    scopus 로고
    • Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy
    • doi:10.1016/S0002-9440(10)63962-4
    • Hall GF, Lee VM, Lee G, Yao J. Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy. Am J Pathol (2001) 158:235-46. doi:10.1016/S0002-9440(10)63962-4
    • (2001) Am J Pathol , vol.158 , pp. 235-46
    • Hall, G.F.1    Lee, V.M.2    Lee, G.3    Yao, J.4
  • 124
    • 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
    • Katsuse O, Lin WL, Lewis J, Hutton ML, Dickson DW. Neurofibrillary tangle-related synaptic alterations of spinal motor neurons of P301L tau transgenic mice. Neurosci Lett (2006) 409:95-9. doi:10.1016/j.neulet.2006.09.021
    • (2006) Neurosci Lett , vol.409 , pp. 95-9
    • Katsuse, O.1    Lin, W.L.2    Lewis, J.3    Hutton, M.L.4    Dickson, D.W.5
  • 125
    • 35748954923 scopus 로고    scopus 로고
    • The beta-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy
    • doi:10.1074/jbc.M705282200
    • Eckermann K, Mocanu MM, Khlistunova I, Biernat J, Nissen A, Hofmann A, et al. The beta-propensity of tau determines aggregation and synaptic loss in inducible mouse models of tauopathy. J Biol Chem (2007) 282:31755-65. doi:10.1074/jbc.M705282200
    • (2007) J Biol Chem , vol.282 , pp. 31755-65
    • Eckermann, K.1    Mocanu, M.M.2    Khlistunova, I.3    Biernat, J.4    Nissen, A.5    Hofmann, A.6
  • 126
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • doi:10.1016/j.ajpath.2012.06.033
    • Tai HC, Serrano-Pozo A, Hashimoto T, Frosch MP, Spires-Jones TL, Hyman BT. The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am J Pathol (2012) 181:1426-35. doi:10.1016/j.ajpath.2012.06.033
    • (2012) Am J Pathol , vol.181 , pp. 1426-35
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 127
    • 77956587739 scopus 로고    scopus 로고
    • Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines
    • doi:10.1523/JNEUROSCI.2357-10.2010
    • Zempel H, Thies E, Mandelkow E, Mandelkow EM. Abeta oligomers cause localized Ca(2+) elevation, missorting of endogenous Tau into dendrites, Tau phosphorylation, and destruction of microtubules and spines. J Neurosci (2010) 30:11938-50. doi:10.1523/JNEUROSCI.2357-10.2010
    • (2010) J Neurosci , vol.30 , pp. 11938-50
    • Zempel, H.1    Thies, E.2    Mandelkow, E.3    Mandelkow, E.M.4
  • 128
    • 84860214055 scopus 로고    scopus 로고
    • Linking amyloid-beta and tau: amyloid-beta induced synaptic dysfunction via local wreckage of the neuronal cytoskeleton
    • doi:10.1159/000332816
    • Zempel H, Mandelkow EM. Linking amyloid-beta and tau: amyloid-beta induced synaptic dysfunction via local wreckage of the neuronal cytoskeleton. Neurodegener Dis (2012) 10:64-72. doi:10.1159/000332816
    • (2012) Neurodegener Dis , vol.10 , pp. 64-72
    • Zempel, H.1    Mandelkow, E.M.2
  • 129
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • doi:10.1016/j.neuron.2010.11.030
    • Hoover BR, Reed MN, Su J, Penrod RD, Kotilinek LA, Grant MK, et al. Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron (2010) 68:1067-81. doi:10.1016/j.neuron.2010.11.030
    • (2010) Neuron , vol.68 , pp. 1067-81
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3    Penrod, R.D.4    Kotilinek, L.A.5    Grant, M.K.6
  • 130
    • 84881546833 scopus 로고    scopus 로고
    • The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease
    • doi:10.1016/j.arr.2013.03.002. [Epub ahead of print]
    • Crimins JL, Pooler A, Polydoro M, Luebke JI, Spires-Jones TL. The intersection of amyloid beta and tau in glutamatergic synaptic dysfunction and collapse in Alzheimer's disease. Ageing Res Rev (2013) doi:10.1016/j.arr.2013.03.002. [Epub ahead of print].
    • (2013) Ageing Res Rev
    • Crimins, J.L.1    Pooler, A.2    Polydoro, M.3    Luebke, J.I.4    Spires-Jones, T.L.5
  • 131
    • 33846259727 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition is integral to long-term potentiation
    • doi:10.1111/j.1460-9568.2006.05245.x
    • Hooper C, Markevich V, Plattner F, Killick R, Schofield E, Engel T, et al. Glycogen synthase kinase-3 inhibition is integral to long-term potentiation. Eur J Neurosci (2007) 25:81-6. doi:10.1111/j.1460-9568.2006.05245.x
    • (2007) Eur J Neurosci , vol.25 , pp. 81-6
    • Hooper, C.1    Markevich, V.2    Plattner, F.3    Killick, R.4    Schofield, E.5    Engel, T.6
  • 132
    • 0025096279 scopus 로고
    • Identification of nuclear tau isoforms in human neuroblastoma cells
    • doi:10.1073/pnas.87.21.8422
    • Loomis PA, Howard TH, Castleberry RP, Binder LI. Identification of nuclear tau isoforms in human neuroblastoma cells. Proc Natl Acad Sci U S A (1990) 87:8422-6. doi:10.1073/pnas.87.21.8422
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8422-6
    • Loomis, P.A.1    Howard, T.H.2    Castleberry, R.P.3    Binder, L.I.4
  • 133
    • 11244331892 scopus 로고    scopus 로고
    • Neuronal tau induces DNA conformational changes observed by atomic force microscopy
    • Qu MH, Li H, Tian R, Nie CL, Liu Y, Han BS, et al. Neuronal tau induces DNA conformational changes observed by atomic force microscopy. Neuroreport (2004) 15:2723-7.
    • (2004) Neuroreport , vol.15 , pp. 2723-7
    • Qu, M.H.1    Li, H.2    Tian, R.3    Nie, C.L.4    Liu, Y.5    Han, B.S.6
  • 134
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • doi:10.1016/S0014-5793(96)01386-5
    • Kampers T, Friedhoff P, Biernat J, Mandelkow EM, Mandelkow E. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett (1996) 399:344-9. doi:10.1016/S0014-5793(96)01386-5
    • (1996) FEBS Lett , vol.399 , pp. 344-9
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 135
    • 14244251724 scopus 로고    scopus 로고
    • Tau protein binds single-stranded DNA sequence specifically - the proof obtained in vitro with non-equilibrium capillary electrophoresis of equilibrium mixtures
    • doi:10.1016/j.febslet.2005.01.032
    • Krylova SM, Musheev M, Nutiu R, Li Y, Lee G, Krylov SN. Tau protein binds single-stranded DNA sequence specifically - the proof obtained in vitro with non-equilibrium capillary electrophoresis of equilibrium mixtures. FEBS Lett (2005) 579:1371-5. doi:10.1016/j.febslet.2005.01.032
    • (2005) FEBS Lett , vol.579 , pp. 1371-5
    • Krylova, S.M.1    Musheev, M.2    Nutiu, R.3    Li, Y.4    Lee, G.5    Krylov, S.N.6
  • 136
    • 27944444956 scopus 로고    scopus 로고
    • Human protein tau represses DNA replication in vitro
    • doi:10.1016/j.bbagen.2005.08.014
    • Li W, Wang XS, Qu MH, Liu Y, He RQ. Human protein tau represses DNA replication in vitro. Biochim Biophys Acta (2005) 1726:280-6. doi:10.1016/j.bbagen.2005.08.014
    • (2005) Biochim Biophys Acta , vol.1726 , pp. 280-6
    • Li, W.1    Wang, X.S.2    Qu, M.H.3    Liu, Y.4    He, R.Q.5
  • 137
    • 79953003312 scopus 로고    scopus 로고
    • Nuclear tau, a key player in neuronal DNA protection
    • doi:10.1074/jbc.M110.199976
    • Sultan A, Nesslany F, Violet M, Begard S, Loyens A, Talahari S, et al. Nuclear tau, a key player in neuronal DNA protection. J Biol Chem (2011) 286:4566-75. doi:10.1074/jbc.M110.199976
    • (2011) J Biol Chem , vol.286 , pp. 4566-75
    • Sultan, A.1    Nesslany, F.2    Violet, M.3    Begard, S.4    Loyens, A.5    Talahari, S.6
  • 138
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice
    • doi:10.1523/JNEUROSCI.2569-11.2011
    • Yamada K, Cirrito JR, Stewart FR, Jiang H, Finn MB, Holmes BB, et al. In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. J Neurosci (2011) 31(37):13110-7. doi:10.1523/JNEUROSCI.2569-11.2011
    • (2011) J Neurosci , vol.31 , Issue.37 , pp. 13110-7
    • Yamada, K.1    Cirrito, J.R.2    Stewart, F.R.3    Jiang, H.4    Finn, M.B.5    Holmes, B.B.6
  • 139
    • 84857275902 scopus 로고    scopus 로고
    • Propagation of tau pathology in a model of early Alzheimer's disease
    • doi:10.1016/j.neuron.2011.11.033
    • de Calignon A, Polydoro M, Suarez-Calvet M, William C, Adamowicz DH, Kopeikina KJ, et al. Propagation of tau pathology in a model of early Alzheimer's disease. Neuron (2012) 73:685-97. doi:10.1016/j.neuron.2011.11.033
    • (2012) Neuron , vol.73 , pp. 685-97
    • de Calignon, A.1    Polydoro, M.2    Suarez-Calvet, M.3    William, C.4    Adamowicz, D.H.5    Kopeikina, K.J.6
  • 140
    • 84856454190 scopus 로고    scopus 로고
    • Trans-synaptic spread of tau pathology in vivo
    • doi:10.1371/journal.pone.0031302
    • Liu L, Drouet V, Wu JW, Witter MP, Small SA, Clelland C, et al. Trans-synaptic spread of tau pathology in vivo. PLoS One (2012) 7:e31302. doi:10.1371/journal.pone.0031302
    • (2012) PLoS One , vol.7
    • Liu, L.1    Drouet, V.2    Wu, J.W.3    Witter, M.P.4    Small, S.A.5    Clelland, C.6
  • 141
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • doi:10.1074/jbc.M808759200
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem (2009) 284:12845-52. doi:10.1074/jbc.M808759200
    • (2009) J Biol Chem , vol.284 , pp. 12845-52
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 142
    • 84872714502 scopus 로고    scopus 로고
    • Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons
    • doi:10.1074/jbc.M112.394528
    • Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, et al. Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J Biol Chem (2013) 288:1856-70. doi:10.1074/jbc.M112.394528
    • (2013) J Biol Chem , vol.288 , pp. 1856-70
    • Wu, J.W.1    Herman, M.2    Liu, L.3    Simoes, S.4    Acker, C.M.5    Figueroa, H.6
  • 145
    • 84864935106 scopus 로고    scopus 로고
    • Constitutive secretion of tau protein by an unconventional mechanism
    • doi:10.1016/j.nbd.2012.05.021
    • Chai X, Dage JL, Citron M. Constitutive secretion of tau protein by an unconventional mechanism. Neurobiol Dis (2012) 48:356-66. doi:10.1016/j.nbd.2012.05.021
    • (2012) Neurobiol Dis , vol.48 , pp. 356-66
    • Chai, X.1    Dage, J.L.2    Citron, M.3
  • 146
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • doi:10.1038/embor.2013.15
    • Pooler AM, Phillips EC, Lau DH, Noble W, Hanger DP. Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep (2013) 14:389-94. doi:10.1038/embor.2013.15
    • (2013) EMBO Rep , vol.14 , pp. 389-94
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 147
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
    • doi:10.1016/j.mcn.2007.12.010
    • Gomez-Ramos A, Diaz-Hernandez M, Rubio A, Miras-Portugal MT, Avila J. Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Mol Cell Neurosci (2008) 37:673-81. doi:10.1016/j.mcn.2007.12.010
    • (2008) Mol Cell Neurosci , vol.37 , pp. 673-81
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 148
    • 68849123079 scopus 로고    scopus 로고
    • Accumulation of tau induced in neurites by microglial proinflammatory mediators
    • doi:10.1096/fj.08-123877
    • Gorlovoy P, Larionov S, Pham TT, Neumann H. Accumulation of tau induced in neurites by microglial proinflammatory mediators. FASEB J (2009) 23:2502-13. doi:10.1096/fj.08-123877
    • (2009) FASEB J , vol.23 , pp. 2502-13
    • Gorlovoy, P.1    Larionov, S.2    Pham, T.T.3    Neumann, H.4
  • 149
  • 150
  • 151
    • 84878769054 scopus 로고    scopus 로고
    • Therapeutic strategies for tau mediated neurodegeneration
    • doi:10.1136/jnnp-2012-303144
    • Yoshiyama Y, Lee VM, Trojanowski JQ. Therapeutic strategies for tau mediated neurodegeneration. J Neurol Neurosurg Psychiatry (2013) 84(7):784-95. doi:10.1136/jnnp-2012-303144
    • (2013) J Neurol Neurosurg Psychiatry , vol.84 , Issue.7 , pp. 784-95
    • Yoshiyama, Y.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 152
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles
    • doi:10.2353/ajpath.2007.061178
    • Caccamo A, Oddo S, Tran LX, Laferla FM. Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles. Am J Pathol (2007) 170:1669-75. doi:10.2353/ajpath.2007.061178
    • (2007) Am J Pathol , vol.170 , pp. 1669-75
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    Laferla, F.M.4
  • 154
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study
    • doi:10.4088/JCP.08m04606
    • Hampel H, Ewers M, Burger K, Annas P, Mortberg A, Bogstedt A, et al. Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. J Clin Psychiatry (2009) 70:922-31. doi:10.4088/JCP.08m04606
    • (2009) J Clin Psychiatry , vol.70 , pp. 922-31
    • Hampel, H.1    Ewers, M.2    Burger, K.3    Annas, P.4    Mortberg, A.5    Bogstedt, A.6
  • 155
    • 79955546563 scopus 로고    scopus 로고
    • Disease-modifying properties of long-term lithium treatment for amnestic mild cognitive impairment: randomised controlled trial
    • doi:10.1192/bjp.bp.110.080044
    • Forlenza OV, Diniz BS, Radanovic M, Santos FS, Talib LL, Gattaz WF. Disease-modifying properties of long-term lithium treatment for amnestic mild cognitive impairment: randomised controlled trial. Br J Psychiatry (2011) 198:351-6. doi:10.1192/bjp.bp.110.080044
    • (2011) Br J Psychiatry , vol.198 , pp. 351-6
    • Forlenza, O.V.1    Diniz, B.S.2    Radanovic, M.3    Santos, F.S.4    Talib, L.L.5    Gattaz, W.F.6
  • 156
    • 68149150844 scopus 로고    scopus 로고
    • A novel GSK-3beta inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo
    • doi:10.1016/j.nbd.2009.05.025
    • Sereno L, Coma M, Rodriguez M, Sanchez-Ferrer P, Sanchez MB, Gich I, et al. A novel GSK-3beta inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo. Neurobiol Dis (2009) 35:359-67. doi:10.1016/j.nbd.2009.05.025
    • (2009) Neurobiol Dis , vol.35 , pp. 359-67
    • Sereno, L.1    Coma, M.2    Rodriguez, M.3    Sanchez-Ferrer, P.4    Sanchez, M.B.5    Gich, I.6
  • 157
    • 84872470005 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease with the GSK-3 inhibitor tideglusib: a pilot study
    • doi:10.3233/JAD-2012-120805
    • Del Ser T, Steinwachs KC, Gertz HJ, Andres MV, Gomez-Carrillo B, Medina M, et al. Treatment of Alzheimer's disease with the GSK-3 inhibitor tideglusib: a pilot study. J Alzheimers Dis (2013) 33:205-15. doi:10.3233/JAD-2012-120805
    • (2013) J Alzheimers Dis , vol.33 , pp. 205-15
    • Del Ser, T.1    Steinwachs, K.C.2    Gertz, H.J.3    Andres, M.V.4    Gomez-Carrillo, B.5    Medina, M.6
  • 158
    • 84875192776 scopus 로고    scopus 로고
    • Protein kinase inhibitors against malignant lymphoma
    • doi:10.1517/14656566.2013.780031
    • D'Cruz OJ, Uckun FM. Protein kinase inhibitors against malignant lymphoma. Expert Opin Pharmacother (2013) 14:707-21. doi:10.1517/14656566.2013.780031
    • (2013) Expert Opin Pharmacother , vol.14 , pp. 707-21
    • D'Cruz, O.J.1    Uckun, F.M.2
  • 159
    • 0037147232 scopus 로고    scopus 로고
    • A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2
    • doi:10.1074/jbc.M209335200
    • Wang H, Brautigan DL. A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2. J Biol Chem (2002) 277:49605-12. doi:10.1074/jbc.M209335200
    • (2002) J Biol Chem , vol.277 , pp. 49605-12
    • Wang, H.1    Brautigan, D.L.2
  • 160
    • 84859607330 scopus 로고    scopus 로고
    • Lemur tyrosine kinase-2 signalling regulates kinesin-1 light chain-2 phosphorylation and binding of Smad2 cargo
    • doi:10.1038/onc.2011.437
    • Manser C, Guillot F, Vagnoni A, Davies J, Lau KF, McLoughlin DM, et al. Lemur tyrosine kinase-2 signalling regulates kinesin-1 light chain-2 phosphorylation and binding of Smad2 cargo. Oncogene (2012) 31:2773-82. doi:10.1038/onc.2011.437
    • (2012) Oncogene , vol.31 , pp. 2773-82
    • Manser, C.1    Guillot, F.2    Vagnoni, A.3    Davies, J.4    Lau, K.F.5    McLoughlin, D.M.6
  • 161
    • 84859597153 scopus 로고    scopus 로고
    • Cdk5/p35 phosphorylates lemur tyrosine kinase-2 to regulate protein phosphatase-1C phosphorylation and activity
    • doi:10.1111/j.1471-4159.2012.07650.x
    • Manser C, Vagnoni A, Guillot F, Davies J, Miller CC. Cdk5/p35 phosphorylates lemur tyrosine kinase-2 to regulate protein phosphatase-1C phosphorylation and activity. J Neurochem (2012) 121:343-8. doi:10.1111/j.1471-4159.2012.07650.x
    • (2012) J Neurochem , vol.121 , pp. 343-8
    • Manser, C.1    Vagnoni, A.2    Guillot, F.3    Davies, J.4    Miller, C.C.5
  • 162
    • 3042634127 scopus 로고    scopus 로고
    • A novel CDK5-dependent pathway for regulating GSK3 activity and kinesin-driven motility in neurons
    • doi:10.1038/sj.emboj.7600237
    • Morfini G, Szebenyi G, Brown H, Pant HC, Pigino G, Deboer S, et al. A novel CDK5-dependent pathway for regulating GSK3 activity and kinesin-driven motility in neurons. EMBO J (2004) 23:2235-45. doi:10.1038/sj.emboj.7600237
    • (2004) EMBO J , vol.23 , pp. 2235-45
    • Morfini, G.1    Szebenyi, G.2    Brown, H.3    Pant, H.C.4    Pigino, G.5    Deboer, S.6
  • 163
    • 78449292337 scopus 로고    scopus 로고
    • Regulation of GSK3 isoforms by phosphatases PP1 and PP2A
    • doi:10.1007/s11010-010-0544-0
    • Hernandez F, Langa E, Cuadros R, Avila J, Villanueva N. Regulation of GSK3 isoforms by phosphatases PP1 and PP2A. Mol Cell Biochem (2010) 344:211-5. doi:10.1007/s11010-010-0544-0
    • (2010) Mol Cell Biochem , vol.344 , pp. 211-5
    • Hernandez, F.1    Langa, E.2    Cuadros, R.3    Avila, J.4    Villanueva, N.5
  • 164
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • doi:10.1146/annurev-biochem-090308-173656
    • Dar AC, Shokat KM. The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Annu Rev Biochem (2011) 80:769-95. doi:10.1146/annurev-biochem-090308-173656
    • (2011) Annu Rev Biochem , vol.80 , pp. 769-95
    • Dar, A.C.1    Shokat, K.M.2
  • 165
    • 78649982418 scopus 로고    scopus 로고
    • Searching for biomarkers in neurodegeneration
    • doi:10.1038/nm1210-1371b
    • Lovestone S. Searching for biomarkers in neurodegeneration. Nat Med (2010) 16:1371-2. doi:10.1038/nm1210-1371b
    • (2010) Nat Med , vol.16 , pp. 1371-2
    • Lovestone, S.1


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