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Volumn 8, Issue 10, 2009, Pages 783-793

Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

Author keywords

[No Author keywords available]

Indexed keywords

2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; ALSTERPAULLONE; AMINOTHIENOPYRIDAZINE; ANILINE; AR A 014418; CHIR 98014; CYCLIN DEPENDENT KINASE 5; DAUNORUBICIN; DOXORUBICIN; EC 102; EXIFONE; GLYCOGEN SYNTHASE KINASE 3; GLYCOSIDASE INHIBITOR; HEAT SHOCK PROTEIN 90 INHIBITOR; HYDRAZIDE DERIVATIVE; METHYLENE BLUE; MICROTUBULE ASSOCIATED PROTEIN 1; N 774; N ACETYL BETA GLUCOSAMINIDASE; OLIGOMER; PACLITAXEL; PROTEIN KINASE INHIBITOR; PYRIDAZINE DERIVATIVE; QUINOXALINE; RAPAMYCIN; RHODANINE; SRN 003 556; TAU PROTEIN; THIAMET G; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 70349638299     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd2959     Document Type: Review
Times cited : (380)

References (137)
  • 1
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V. M. Y. & Trojanowski, J. Q. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nature Rev. Neurosci. 8, 663-672 (2007).
    • (2007) Nature Rev. Neurosci , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 3
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of alzheimers disease
    • Kidd, M. Paired helical filaments in electron microscopy of alzheimers disease. Nature 197, 192-193 (1963).
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 4
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimers disease
    • Arriagada, P. V., Growdon, J. H., Hedleywhyte, E. T. & Hyman, B. T. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimers disease. Neurology 42, 631-639 (1992).
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedleywhyte, E.T.3    Hyman, B.T.4
  • 5
    • 0019935804 scopus 로고
    • Plaques, tangles and dementia - a quantitative study
    • Wilcock, G. K. & Esiri, M. M. Plaques, tangles and dementia - a quantitative study. J. Neurological. Sci. 56, 343-356 (1982).
    • (1982) J. Neurological. Sci , vol.56 , pp. 343-356
    • Wilcock, G.K.1    Esiri, M.M.2
  • 6
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • GomezIsla, T. et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann. Neurol. 41 17-24 (1997).
    • (1997) Ann. Neurol , vol.41 , pp. 17-24
    • GomezIsla, T.1
  • 7
    • 13844255273 scopus 로고    scopus 로고
    • Molecular biology and genetics of Alzheimer's disease
    • George-Hyslop, P. H. & Petit, A. Molecular biology and genetics of Alzheimer's disease. C. R. Biol. 328, 119-130 (2005).
    • (2005) C. R. Biol , vol.328 , pp. 119-130
    • George-Hyslop, P.H.1    Petit, A.2
  • 8
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • Selkoe, D. J. & Schenk, D. Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Ann. Rev. Pharmacol. Toxicol. 43, 545-584 (2003).
    • (2003) Ann. Rev. Pharmacol. Toxicol , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 9
    • 26444581827 scopus 로고    scopus 로고
    • Tau gene mutations and their effects
    • Goedert, M. Tau gene mutations and their effects. Mov. Disord. 20, S45-S52 (2005).
    • (2005) Mov. Disord , vol.20
    • Goedert, M.1
  • 10
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • Goedert, M. & Jakes, R. Mutations causing neurodegenerative tauopathies. Biochim. Biophys. Acta 1739, 240-250 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 11
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models
    • Brandt, R., Hundelt, M. & Shahani, N. Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models. Biochim. Biophys. Acta 1739, 331-354 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 12
    • 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 297 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 13
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D. N., Hyman, A. A., Cobb, M. H. & Kirschner, M. W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3, 1141-1154 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 15
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder, L. I., Frankfurter, A. & Rebhun, L. I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101, 1371-1378 (1985).
    • (1985) J. Cell Biol , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 16
    • 0026488111 scopus 로고
    • Structure and novel exons of the human-tau gene
    • Andreadis, A., Brown, W. M. & Kosik, K. S. Structure and novel exons of the human-tau gene. Biochemistry 31, 10626-10633 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 17
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein-tau - sequences and localization in neurofibrillary tangles of Alzheimers disease
    • Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D. & Crowther, R. A. Multiple isoforms of human microtubule-associated protein-tau - sequences and localization in neurofibrillary tangles of Alzheimers disease. Neuron 3, 519-526 (1989).
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 18
    • 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., Feinstein, S. C. & Wilson, L. Differential regulation of microtubule dynamics by three- and four-repeat tau: Implications for the onset of neurodegenerative disease. Proc. Natl Acad. Sci. USA 100, 9548-9553 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 19
    • 0030887854 scopus 로고    scopus 로고
    • Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments
    • Spillantini, M. G. et al. Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments. Proc. Natl Acad. Sci. USA 94, 4113-4118 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4113-4118
    • Spillantini, M.G.1
  • 20
    • 0033042978 scopus 로고    scopus 로고
    • Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation
    • Dayanandan, R. et al. Mutations in tau reduce its microtubule binding properties in intact cells and affect its phosphorylation. FEBS Lett. 446, 228-232 (1999).
    • (1999) FEBS Lett , vol.446 , pp. 228-232
    • Dayanandan, R.1
  • 21
    • 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. 437, 207-210 (1998).
    • (1998) FEBS Lett , vol.437 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 22
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct Tau isoforms of hereditary FTDP-17
    • Hong, M. et al. Mutation-specific functional impairments in distinct Tau isoforms of hereditary FTDP-17. Science 282, 1914-1917 (1998).
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1
  • 23
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S. et al. Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias. Biochemistry 39, 11714-11721 (2000).
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1
  • 24
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin, T. C. et al. In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants. Biochemistry 39, 6136-6144 (2000).
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1
  • 25
    • 49149091448 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju, P. et al. Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. J. Neuropathol. Exp. Neurol. 58, 545 (1999).
    • (1999) J. Neuropathol. Exp. Neurol , vol.58 , pp. 545
    • Nacharaju, P.1
  • 27
    • 70349648031 scopus 로고    scopus 로고
    • Tau phosphorylation and tau assembly
    • Avila, J. Tau and tauopathies: Tau phosphorylation and tau assembly. FEBS J. 273, 23 (2006).
    • (2006) FEBS J , vol.273 , pp. 23
    • Avila1    Tau, J.2    tauopathies3
  • 28
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A. & Hof, P. R. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res. Rev. 33, 95-130 (2000).
    • (2000) Brain Res. Rev , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 29
    • 0030813929 scopus 로고    scopus 로고
    • Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons (NT2N cells)
    • Merrick, S. E., Trojanowski, J. Q. & Lee, V. M. Y. Selective destruction of stable microtubules and axons by inhibitors of protein serine/threonine phosphatases in cultured human neurons (NT2N cells). J. Neurosci. 17, 5726-5737 (1997).
    • (1997) J. Neurosci , vol.17 , pp. 5726-5737
    • Merrick, S.E.1    Trojanowski, J.Q.2    Lee, V.M.Y.3
  • 30
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation
    • Wagner, U., Utton, M., Gallo, J. M. & Miller, C. C. J. Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation. J. Cell Sci. 109, 1537-1543 (1996).
    • (1996) J. Cell Sci , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.M.3    Miller, C.C.J.4
  • 31
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • Alonso, A. D., GrundkeIqbal, I. & Iqbal, K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nature Med. 2, 783-787 (1996).
    • (1996) Nature Med , vol.2 , pp. 783-787
    • Alonso, A.D.1    GrundkeIqbal, I.2    Iqbal, K.3
  • 32
    • 2342607166 scopus 로고
    • Abnormally phosphorylated tau from Alzheimer disease brain depolymerizes microtubules
    • S
    • Alonso, A. D., GrundkeIqbal, I. & Iqbal, K. Abnormally phosphorylated tau from Alzheimer disease brain depolymerizes microtubules. Neurobiol. Aging 15, S37 (1994).
    • (1994) Neurobiol. Aging , vol.15 , pp. 37
    • Alonso, A.D.1    GrundkeIqbal, I.2    Iqbal, K.3
  • 33
    • 9644273963 scopus 로고    scopus 로고
    • Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro
    • Necula, M. & Kuret, J. Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro. J. Biol. Chem. 279, 49694-49703 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 49694-49703
    • Necula, M.1    Kuret, J.2
  • 34
    • 0035851175 scopus 로고    scopus 로고
    • Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice
    • Kins, S. et al. Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice. J. Biol. Chem. 276, 38193-38200 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 38193-38200
    • Kins, S.1
  • 35
    • 3242739968 scopus 로고    scopus 로고
    • Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W. & Gong, C. X. O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease. Proc. Natl Acad. Sci. USA 101, 10804-10809 (2004).
    • Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W. & Gong, C. X. O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease. Proc. Natl Acad. Sci. USA 101, 10804-10809 (2004).
  • 36
    • 0037454755 scopus 로고    scopus 로고
    • Evidence of a balance between phosphorylation and O-GlcNAc glycosylation of Tau proteins - a role in nuclear localization
    • Lefebvre, T. et al. Evidence of a balance between phosphorylation and O-GlcNAc glycosylation of Tau proteins - a role in nuclear localization. Biochim. Biophys. Acta 1619, 167-176 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1619 , pp. 167-176
    • Lefebvre, T.1
  • 37
    • 12144288564 scopus 로고    scopus 로고
    • Phosphorylation of tau by fyn: Implications for Alzheimer's disease
    • Lee, G. et al. Phosphorylation of tau by fyn: Implications for Alzheimer's disease. J. Neurosci. 24, 2304-2312 (2004).
    • (2004) J. Neurosci , vol.24 , pp. 2304-2312
    • Lee, G.1
  • 38
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • Gong, C. X., Liu, F., Grundke-Iqbal, I. & Iqbal, K. Post-translational modifications of tau protein in Alzheimer's disease. J. Neural Transm. 112, 813-838 (2005).
    • (2005) J. Neural Transm , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 39
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates β-amyloid-induced neurodegeneration
    • Park, S. Y. & Ferreira, A. The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates β-amyloid-induced neurodegeneration. J. Neurosci. 25, 5365-5375 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 40
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin, T. C. et al. Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl Acad. Sci. USA 100, 10032-10037 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1
  • 41
    • 0038152836 scopus 로고    scopus 로고
    • Anionic micelles and vesicles induce tau fibrillization in vitro
    • Chirita, C. N., Necula, M. & Kuret, J. Anionic micelles and vesicles induce tau fibrillization in vitro. J. Biol. Chem. 278, 25644-25650 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 25644-25650
    • Chirita, C.N.1    Necula, M.2    Kuret, J.3
  • 42
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson, D. M. & Binder, L. I. Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. Am. J. Pathol. 150, 2181-2195 (1997).
    • (1997) Am. J. Pathol , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 43
    • 70349637413 scopus 로고    scopus 로고
    • Effect of tramiprosate in patients with mild-to-moderate Alzheimer's disease: Exploratory analyses of the MRI sub-group of the Alphase study
    • Gauthier, S. et al. Effect of tramiprosate in patients with mild-to-moderate Alzheimer's disease: Exploratory analyses of the MRI sub-group of the Alphase study. J. Nutr. Health Aging 13, 550-557 (2009).
    • (2009) J. Nutr. Health Aging , vol.13 , pp. 550-557
    • Gauthier, S.1
  • 44
    • 70349642619 scopus 로고    scopus 로고
    • Safety and efficacy of tarenflurbil in subjects with mild Alzheimer's disease: Results from an 18 month multicenter phase 3 trial
    • Green, R. C., Schneider, L. S., Hendrix, S., Zavitz, K. & Swabb, E. Safety and efficacy of tarenflurbil in subjects with mild Alzheimer's disease: Results from an 18 month multicenter phase 3 trial. Eur. J. Neurol. 15, 412 (2008).
    • (2008) Eur. J. Neurol , vol.15 , pp. 412
    • Green, R.C.1    Schneider, L.S.2    Hendrix, S.3    Zavitz, K.4    Swabb, E.5
  • 45
    • 0030240325 scopus 로고    scopus 로고
    • Reduction of acetylated α-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease
    • Hempen, B. & Brion, J. P. Reduction of acetylated α-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease. J. Neuropathol. Exp. Neurol. 55, 964-972 (1996).
    • (1996) J. Neuropathol. Exp. Neurol , vol.55 , pp. 964-972
    • Hempen, B.1    Brion, J.P.2
  • 46
    • 0036293375 scopus 로고    scopus 로고
    • Intracellular deposition, microtubule destabilization, and transport failure: An "early" pathogenic cascade leading to synaptic decline
    • Bendiske, J., Caba, E., Brown, Q. B. & Bahr, B. A. Intracellular deposition, microtubule destabilization, and transport failure: An "early" pathogenic cascade leading to synaptic decline. J. Neuropathol. Exp. Neurol. 61, 640-650 (2002).
    • (2002) J. Neuropathol. Exp. Neurol , vol.61 , pp. 640-650
    • Bendiske, J.1    Caba, E.2    Brown, Q.B.3    Bahr, B.A.4
  • 47
    • 0033230886 scopus 로고    scopus 로고
    • Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform
    • Ishihara, T. et al. Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron 24, 751-762 (1999).
    • (1999) Neuron , vol.24 , pp. 751-762
    • Ishihara, T.1
  • 48
    • 0242600546 scopus 로고    scopus 로고
    • Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation
    • Cash, A. D. et al. Microtubule reduction in Alzheimer's disease and aging is independent of tau filament formation. Am. J. Pathol. 162, 1623-1627 (2003).
    • (2003) Am. J. Pathol , vol.162 , pp. 1623-1627
    • Cash, A.D.1
  • 49
    • 39549117998 scopus 로고    scopus 로고
    • Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice
    • Yuan, A., Kumar, A., Peterhoff, C., Duff, K. & Nixon, R. A. Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. J. Neurosci. 28, 1682-1687 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 1682-1687
    • Yuan, A.1    Kumar, A.2    Peterhoff, C.3    Duff, K.4    Nixon, R.A.5
  • 50
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model
    • Roberson, E. D. et al. Reducing endogenous tau ameliorates amyloid β-induced deficits in an Alzheimer's disease mouse model. Science 316, 750-754 (2007).
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1
  • 51
    • 0028301455 scopus 로고
    • Altered microtubule organization in small-caliber axons of mice lacking tau protein
    • Harada, A. et al. Altered microtubule organization in small-caliber axons of mice lacking tau protein. Nature 369, 488-491 (1994).
    • (1994) Nature , vol.369 , pp. 488-491
    • Harada, A.1
  • 52
    • 0035067021 scopus 로고    scopus 로고
    • Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice
    • Dawson, H. N. et al. Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice. J. Cell Sci. 114 1179-1187 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 1179-1187
    • Dawson, H.N.1
  • 53
    • 0033969771 scopus 로고    scopus 로고
    • Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice
    • Ikegami, S., Harada, A. & Hirokawa, N. Muscle weakness, hyperactivity, and impairment in fear conditioning in tau-deficient mice. Neurosci. Lett. 279, 129-132 (2000).
    • (2000) Neurosci. Lett , vol.279 , pp. 129-132
    • Ikegami, S.1    Harada, A.2    Hirokawa, N.3
  • 54
    • 19944429064 scopus 로고    scopus 로고
    • Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model
    • Zhang, B. et al. Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model. Proc. Natl Acad. Sci. USA 102, 227-231 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 227-231
    • Zhang, B.1
  • 55
    • 13444287985 scopus 로고    scopus 로고
    • The femtomolar-acting NAP interacts with microtubules: Novel aspects of astrocyte protection
    • Gozes, I. & Divinski, I. The femtomolar-acting NAP interacts with microtubules: Novel aspects of astrocyte protection. J. Alzheimers Dis. 6, S37-S41 (2004).
    • (2004) J. Alzheimers Dis , vol.6
    • Gozes, I.1    Divinski, I.2
  • 56
    • 34248354279 scopus 로고    scopus 로고
    • Intranasal NAP administration reduces accumulation of amyloid peptide and tau hyperphosphorylation in a transgenic mouse model of Alzheimer's disease at early pathological stage
    • Matsuoka, Y. et al. Intranasal NAP administration reduces accumulation of amyloid peptide and tau hyperphosphorylation in a transgenic mouse model of Alzheimer's disease at early pathological stage. J. Mol. Neurosci. 31, 165-170 (2007).
    • (2007) J. Mol. Neurosci , vol.31 , pp. 165-170
    • Matsuoka, Y.1
  • 57
    • 41149175575 scopus 로고    scopus 로고
    • A neuronal microtubule-interacting agent, NAPVSIPQ, reduces tau pathology and enhances cognitive function in a mouse model of Alzheimer's disease
    • Matsuoka, Y. et al. A neuronal microtubule-interacting agent, NAPVSIPQ, reduces tau pathology and enhances cognitive function in a mouse model of Alzheimer's disease. J. Pharmacol. Exp. Ther. 325, 146-153 (2008).
    • (2008) J. Pharmacol. Exp. Ther , vol.325 , pp. 146-153
    • Matsuoka, Y.1
  • 58
    • 34250159077 scopus 로고    scopus 로고
    • Paclitaxel C-10 carbamates: Potential candidates for the treatment of neurodegenerative tauopathies
    • Ballatore, C. et al. Paclitaxel C-10 carbamates: Potential candidates for the treatment of neurodegenerative tauopathies. Bioorg. Med. Chem. Lett. 17, 3642-3646 (2007).
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 3642-3646
    • Ballatore, C.1
  • 59
    • 0036841686 scopus 로고    scopus 로고
    • Transport of paclitaxel (Taxol) across the blood-brain barrier in vitro and in vivo
    • Fellner, S. et al. Transport of paclitaxel (Taxol) across the blood-brain barrier in vitro and in vivo. J. Clin. Invest. 110, 1309-1318 (2002).
    • (2002) J. Clin. Invest , vol.110 , pp. 1309-1318
    • Fellner, S.1
  • 60
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimers disease paired helical filament tau
    • Matsuo, E. S. et al. Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimers disease paired helical filament tau. Neuron 13, 989-1002 (1994).
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1
  • 61
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the Alzheimers disease brain
    • Hasegawa, M. et al. Protein sequence and mass spectrometric analyses of tau in the Alzheimers disease brain. J. Biol. Chem. 267, 17047-17054 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 17047-17054
    • Hasegawa, M.1
  • 62
    • 61849088424 scopus 로고    scopus 로고
    • Tau phos phory lation: The therapeutic challenge for neuro degenerative disease
    • Hanger, D. P., Anderton, B. H. & Noble, W. Tau phos phory lation: The therapeutic challenge for neuro degenerative disease. Trends Mol. Med. 15, 112-119 (2009).
    • (2009) Trends Mol. Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 63
    • 0032530145 scopus 로고    scopus 로고
    • Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules
    • Sengupta, A. et al. Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. Arch. Biochem. Biophys. 357, 299-309 (1998).
    • (1998) Arch. Biochem. Biophys , vol.357 , pp. 299-309
    • Sengupta, A.1
  • 64
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • Alonso, A. D., Mederlyova, A., Novak, M., Grundke-Iqbal, I. & Iqbal, K. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J. Biol. Chem. 279, 34873-34881 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 34873-34881
    • Alonso, A.D.1    Mederlyova, A.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 65
    • 53749089884 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau from microtubules S262 and S214 protects it against aggregation into Alzheimer paired helical filaments
    • S
    • Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E. & Mandelkow, E. M. Phosphorylation that detaches tau from microtubules S262 and S214 protects it against aggregation into Alzheimer paired helical filaments. J. Neurochem. 73, S26 (1999).
    • (1999) J. Neurochem , vol.73 , pp. 26
    • Schneider, A.1    Biernat, J.2    von Bergen, M.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 66
    • 62849094732 scopus 로고    scopus 로고
    • Selectivity and therapeutic inhibition of kinases: To be or not to be?
    • Ghoreschi, K., Laurence, A. & O'Shea, J. J. Selectivity and therapeutic inhibition of kinases: To be or not to be? Nature Immunol. 10 356-360 (2009).
    • (2009) Nature Immunol , vol.10 , pp. 356-360
    • Ghoreschi, K.1    Laurence, A.2    O'Shea, J.J.3
  • 67
    • 34447503455 scopus 로고    scopus 로고
    • Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
    • Mazanetz, M. P. & Fischer, P. M. Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nature Rev. Drug Discov. 6, 464-479 (2007).
    • (2007) Nature Rev. Drug Discov , vol.6 , pp. 464-479
    • Mazanetz, M.P.1    Fischer, P.M.2
  • 68
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease
    • Gong, C. X. & Iqbal, K. Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease. Curr. Med. Chem. 15, 2321-2328 (2008).
    • (2008) Curr. Med. Chem , vol.15 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 69
    • 0031045216 scopus 로고    scopus 로고
    • Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
    • Imahori, K. & Uchida, T. Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. J. Biochem. 121, 179-188 (1997).
    • (1997) J. Biochem , vol.121 , pp. 179-188
    • Imahori, K.1    Uchida, T.2
  • 70
    • 0030635495 scopus 로고    scopus 로고
    • Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain
    • Pei, J. J. et al. Distribution, levels, and activity of glycogen synthase kinase-3 in the Alzheimer disease brain. J. Neuropathol. Exp. Neurol. 56, 70-78 (1997).
    • (1997) J. Neuropathol. Exp. Neurol , vol.56 , pp. 70-78
    • Pei, J.J.1
  • 71
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice
    • Lucas, J. J. et al. Decreased nuclear β-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3β conditional transgenic mice. EMBO J. 20, 27-39 (2001).
    • (2001) EMBO J , vol.20 , pp. 27-39
    • Lucas, J.J.1
  • 72
    • 1642363745 scopus 로고    scopus 로고
    • Spatial learning deficit in transgenic mice that conditionally over-express GSK-3β in the brain but do not form tau filaments
    • Hernandez, F., Borrell, J., Guaza, C., Avila, J. & Lucas, J. J. Spatial learning deficit in transgenic mice that conditionally over-express GSK-3β in the brain but do not form tau filaments. J. Neurochem. 83, 1529-1533 (2002).
    • (2002) J. Neurochem , vol.83 , pp. 1529-1533
    • Hernandez, F.1    Borrell, J.2    Guaza, C.3    Avila, J.4    Lucas, J.J.5
  • 73
    • 0032988741 scopus 로고    scopus 로고
    • Elevated neuronal Cdc2-like kinase activity in the Alzheimer disease brain
    • Lee, K. Y. et al. Elevated neuronal Cdc2-like kinase activity in the Alzheimer disease brain. Neurosci. Res. 34, 21-29 (1999).
    • (1999) Neurosci. Res , vol.34 , pp. 21-29
    • Lee, K.Y.1
  • 74
    • 0037125209 scopus 로고    scopus 로고
    • A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains
    • Tseng, H. C., Zhou, Y., Shen, Y. & Tsai, L. H. A survey of Cdk5 activator p35 and p25 levels in Alzheimer's disease brains. FEBS Lett. 523, 58-62 (2002).
    • (2002) FEBS Lett , vol.523 , pp. 58-62
    • Tseng, H.C.1    Zhou, Y.2    Shen, Y.3    Tsai, L.H.4
  • 75
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK)I glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II
    • Yamaguchi, H. et al. Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK)I glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol. 92, 232-241 (1996).
    • (1996) Acta Neuropathol , vol.92 , pp. 232-241
    • Yamaguchi, H.1
  • 76
    • 0036275991 scopus 로고    scopus 로고
    • Colocalization and fluorescence resonance energy transfer between cdk5 and AT8 suggests a close association in pre-neurofibrillary tangles and neurofibrillary tangles
    • Augustinack, J. C., Sanders, J. L., Tsai, L. H. & Hyman, B. T. Colocalization and fluorescence resonance energy transfer between cdk5 and AT8 suggests a close association in pre-neurofibrillary tangles and neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 61, 557-564 (2002).
    • (2002) J. Neuropathol. Exp. Neurol , vol.61 , pp. 557-564
    • Augustinack, J.C.1    Sanders, J.L.2    Tsai, L.H.3    Hyman, B.T.4
  • 77
    • 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. et al. Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration. Brain Res. 797, 267-277 (1998).
    • (1998) Brain Res , vol.797 , pp. 267-277
    • Pei, J.J.1
  • 78
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • Noble, W. et al. Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron 38, 555-565 (2003).
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1
  • 79
    • 33749826587 scopus 로고    scopus 로고
    • P25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid β in vivo
    • Cruz, J. C. et al. P25/cyclin-dependent kinase 5 induces production and intraneuronal accumulation of amyloid β in vivo. J. Neurosci. 26, 10536-10541 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 10536-10541
    • Cruz, J.C.1
  • 80
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • Phiel, C. J., Wilson, C. A., Lee, V. M. Y. & Klein, P. S. GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature 423, 435-439 (2003).
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.Y.3    Klein, P.S.4
  • 81
    • 0030887531 scopus 로고    scopus 로고
    • Effect of increased glycogen synthase kinase-3 activity upon the maturation of the amyloid precursor protein in transfected cells
    • Aplin, A. E., Jacobsen, J. S., Anderton, B. H. & Gallo, J. M. Effect of increased glycogen synthase kinase-3 activity upon the maturation of the amyloid precursor protein in transfected cells. Neuroreport 8 639-643 (1997).
    • (1997) Neuroreport , vol.8 , pp. 639-643
    • Aplin, A.E.1    Jacobsen, J.S.2    Anderton, B.H.3    Gallo, J.M.4
  • 82
    • 33847214486 scopus 로고    scopus 로고
    • Neuroprotective effects of regulators of the glycogen synthase kinase-3β signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation
    • Rockenstein, E. et al. Neuroprotective effects of regulators of the glycogen synthase kinase-3β signaling pathway in a transgenic model of Alzheimer's disease are associated with reduced amyloid precursor protein phosphorylation. J. Neurosci. 27, 1981-1991 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 1981-1991
    • Rockenstein, E.1
  • 83
    • 40449087334 scopus 로고    scopus 로고
    • Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3β mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing
    • Wen, Y. et al. Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3β mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing. J. Neurosci. 28, 2624-2632 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 2624-2632
    • Wen, Y.1
  • 84
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E. M. & Mandelkow, E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89, 297-308 (1997).
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 85
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study
    • Chin, J. Y. et al. Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: A fluorescence resonance energy transfer study. J. Neuropathol. Exp. Neurol. 59, 966-971 (2000).
    • (2000) J. Neuropathol. Exp. Neurol , vol.59 , pp. 966-971
    • Chin, J.Y.1
  • 86
    • 1542358895 scopus 로고    scopus 로고
    • PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila
    • Nishimura, I., Yang, Y. F. & Lu, B. W. PAR-1 kinase plays an initiator role in a temporally ordered phosphorylation process that confers tau toxicity in Drosophila. Cell 116, 671-682 (2004).
    • (2004) Cell , vol.116 , pp. 671-682
    • Nishimura, I.1    Yang, Y.F.2    Lu, B.W.3
  • 87
    • 46749128127 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic
    • Medina, M. & Castro, A. Glycogen synthase kinase-3 (GSK-3) inhibitors reach the clinic. Curr. Opin. Drug Discov. Dev. 11, 533-543 (2008).
    • (2008) Curr. Opin. Drug Discov. Dev , vol.11 , pp. 533-543
    • Medina, M.1    Castro, A.2
  • 89
    • 0036854327 scopus 로고    scopus 로고
    • Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity
    • Biernat, J. et al. Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity. Mol. Biol. Cell 13, 4013-4028 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4013-4028
    • Biernat, J.1
  • 90
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow, E. M., Thies, E., Trinczek, B., Biernat, J. & Mandelkow, E. MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J. Cell Biol. 167, 99-110 (2004).
    • (2004) J. Cell Biol , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 91
    • 33646198145 scopus 로고    scopus 로고
    • Tau therapeutic strategies for the treatment of Alzheimer's disease
    • Churcher, I. Tau therapeutic strategies for the treatment of Alzheimer's disease. Curr. Top. Med. Chem. 6, 579-595 (2006).
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 579-595
    • Churcher, I.1
  • 93
    • 21044449225 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo
    • Noble, W. et al. Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc. Natl Acad. Sci. USA 102, 6990-6995 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6990-6995
    • Noble, W.1
  • 94
    • 0242720372 scopus 로고    scopus 로고
    • Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model
    • Perez, M., Hernandez, F., Lim, F., Diaz-Nido, J. & Avila, J. Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model. J. Alzheimers Dis. 5, 301-308 (2003).
    • (2003) J. Alzheimers Dis , vol.5 , pp. 301-308
    • Perez, M.1    Hernandez, F.2    Lim, F.3    Diaz-Nido, J.4    Avila, J.5
  • 95
    • 70349646409 scopus 로고    scopus 로고
    • Effect of chronic lithium treatment on an animal model of tauopathies
    • S
    • Nakashima, H. et al. Effect of chronic lithium treatment on an animal model of tauopathies. Neurobiol. Aging 25, S595 (2004).
    • (2004) Neurobiol. Aging , vol.25 , pp. 595
    • Nakashima, H.1
  • 96
    • 33845530335 scopus 로고    scopus 로고
    • Chronic lithium administration to FTDP-17 tau and GSK-3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert
    • Engel, T., Goni-Oliver, P., Lucas, J. J., Avila, J. & Hernandez, F. Chronic lithium administration to FTDP-17 tau and GSK-3β overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert. J. Neurochem. 99, 1445-1455 (2006).
    • (2006) J. Neurochem , vol.99 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 97
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not Aβ or working memory deficits in a transgenic model with both plaques and tangles
    • Caccamo, A., Oddo, S., Tran, L. X. & LaFerla, F. M. Lithium reduces tau phosphorylation but not Aβ or working memory deficits in a transgenic model with both plaques and tangles. Am. J. Pathol. 170, 1669-1675 (2007).
    • (2007) Am. J. Pathol , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    LaFerla, F.M.4
  • 98
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in Alzheimer's disease: A randomized, single-blind, placebo-controlled multicenter 10-week study
    • Hampel, H. et al. Lithium trial in Alzheimer's disease: A randomized, single-blind, placebo-controlled multicenter 10-week study. J. Clin. Psychiatry 70, 922-931 (2009).
    • (2009) J. Clin. Psychiatry , vol.70 , pp. 922-931
    • Hampel, H.1
  • 99
    • 33745449875 scopus 로고    scopus 로고
    • An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice
    • Le Corre, S. et al. An inhibitor of tau hyperphosphorylation prevents severe motor impairments in tau transgenic mice. Proc. Natl Acad. Sci. USA 103, 9673-9678 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9673-9678
    • Le Corre, S.1
  • 100
    • 36048983139 scopus 로고    scopus 로고
    • Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation
    • Selenica, M. L. et al. Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylation. Brit. J. Pharmacol. 152, 959-979 (2007).
    • (2007) Brit. J. Pharmacol , vol.152 , pp. 959-979
    • Selenica, M.L.1
  • 101
    • 47649117312 scopus 로고    scopus 로고
    • Fischer, P. M. Turning down tau phosphorylation. Nature Chem. Biol. 4, 448-449 (2008).
    • Fischer, P. M. Turning down tau phosphorylation. Nature Chem. Biol. 4, 448-449 (2008).
  • 102
    • 47649114560 scopus 로고    scopus 로고
    • A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
    • Yuzwa, S. A. et al. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nature Chem. Biol. 4, 483-490 (2008).
    • (2008) Nature Chem. Biol , vol.4 , pp. 483-490
    • Yuzwa, S.A.1
  • 103
    • 0031439109 scopus 로고    scopus 로고
    • Alzheimer-like changes in microtubule-associated protein tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation
    • Hasegawa, M., Crowther, R. A., Jakes, B. & Goedert, M. Alzheimer-like changes in microtubule-associated protein tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation. J. Biol. Chem. 272, 33118-33124 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 33118-33124
    • Hasegawa, M.1    Crowther, R.A.2    Jakes, B.3    Goedert, M.4
  • 105
    • 70349638396 scopus 로고    scopus 로고
    • Staff, R. T. et al. Tau aggregation inhibitor (TAI) therapy with rember arrests the trajectory of rCBF decline in brain regions affected by tau pathology in mild to moderate Alzheimer's disease. Alzheimers Dement. 4, T775 (2008).
    • Staff, R. T. et al. Tau aggregation inhibitor (TAI) therapy with rember arrests the trajectory of rCBF decline in brain regions affected by tau pathology in mild to moderate Alzheimer's disease. Alzheimers Dement. 4, T775 (2008).
  • 106
    • 1542327644 scopus 로고    scopus 로고
    • Ligand-dependent inhibition and reversal of tau filament formation
    • Chirita, C., Necula, M. & Kuret, J. Ligand-dependent inhibition and reversal of tau filament formation. Biochemistry 43, 2879-2887 (2004).
    • (2004) Biochemistry , vol.43 , pp. 2879-2887
    • Chirita, C.1    Necula, M.2    Kuret, J.3
  • 107
    • 34548023741 scopus 로고    scopus 로고
    • Potency of a tar fibrillization inhibitor is influenced by its aggregation state
    • Congdon, E. E., Necula, M., Blackstone, R. D. & Kuret, J. Potency of a tar fibrillization inhibitor is influenced by its aggregation state. Arch. Biochem. Biophys. 465, 127-135 (2007).
    • (2007) Arch. Biochem. Biophys , vol.465 , pp. 127-135
    • Congdon, E.E.1    Necula, M.2    Blackstone, R.D.3    Kuret, J.4
  • 108
    • 13544251748 scopus 로고    scopus 로고
    • Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells
    • Pickhardt, M. et al. Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells. J. Biol. Chem. 280, 3628-3635 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 3628-3635
    • Pickhardt, M.1
  • 109
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova, I. et al. Inducible expression of tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs. J. Biol. Chem. 281, 1205-1214 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1
  • 110
    • 34347378629 scopus 로고    scopus 로고
    • Screening for inhibitors of tau protein aggregation into Alzheimer paired helical filaments: A ligand based approach results in successful scaffold hopping
    • Larbig, G., Pickhardt, M., Lloyd, D. G., Schmidt, B. & Mandelkow, E. Screening for inhibitors of tau protein aggregation into Alzheimer paired helical filaments: A ligand based approach results in successful scaffold hopping. Curr. Alzheimer Res. 4, 315-323 (2007).
    • (2007) Curr. Alzheimer Res , vol.4 , pp. 315-323
    • Larbig, G.1    Pickhardt, M.2    Lloyd, D.G.3    Schmidt, B.4    Mandelkow, E.5
  • 111
    • 34548502687 scopus 로고    scopus 로고
    • Phenylthiazolyl-hydrazide and its derivatives are potent inhibitors of tau aggregation and toxicity in vitro and in cells
    • Pickhardt, M. et al. Phenylthiazolyl-hydrazide and its derivatives are potent inhibitors of tau aggregation and toxicity in vitro and in cells. Biochemistry 46, 10016-10023 (2007).
    • (2007) Biochemistry , vol.46 , pp. 10016-10023
    • Pickhardt, M.1
  • 112
    • 37349128195 scopus 로고    scopus 로고
    • Rhodanine-based tau aggregation inhibitors in cell models of tauopathy
    • Bulic, B. et al. Rhodanine-based tau aggregation inhibitors in cell models of tauopathy. Angew. Chem. Int. Ed. Engl. 46, 9215-9219 (2007).
    • (2007) Angew. Chem. Int. Ed. Engl , vol.46 , pp. 9215-9219
    • Bulic, B.1
  • 113
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • Taniguchi, S. et al. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem. 280, 7614-7623 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 7614-7623
    • Taniguchi, S.1
  • 114
    • 34248142548 scopus 로고    scopus 로고
    • High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation
    • Crowe, A., Ballatore, C., Hyde, E., Trojanowski, J. Q. & Lee, V. M. Y. High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation. Biochem. Biophys. Res. Commun. 358, 1-6 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.358 , pp. 1-6
    • Crowe, A.1    Ballatore, C.2    Hyde, E.3    Trojanowski, J.Q.4    Lee, V.M.Y.5
  • 115
    • 68849086671 scopus 로고    scopus 로고
    • The identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening
    • Crowe, A. et al. The identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening. Biochemistry 48, 7732-7745 (2009).
    • (2009) Biochemistry , vol.48 , pp. 7732-7745
    • Crowe, A.1
  • 116
    • 39349094523 scopus 로고    scopus 로고
    • Feng, B. Y. et al. Small-molecule aggregates inhibit amyloid polymerization. Nature Chem. Biol. 4, 197-199 (2008).
    • Feng, B. Y. et al. Small-molecule aggregates inhibit amyloid polymerization. Nature Chem. Biol. 4, 197-199 (2008).
  • 117
    • 46649101161 scopus 로고    scopus 로고
    • Nucleation-dependent tau filament formation: The importance of dimerization and an estimation of elementary rate constants
    • Congdon, E. E. et al. Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants. J. Biol. Chem. 283, 13806-13816 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 13806-13816
    • Congdon, E.E.1
  • 118
    • 0022395021 scopus 로고
    • Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assemblypromoting factors
    • Drubin, D. G., Feinsteni, S. C., Shooter, E. M. & Kirschner, M. W. Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assemblypromoting factors. J. Cell Biol. 101, 1799-1807 (1985).
    • (1985) J. Cell Biol , vol.101 , pp. 1799-1807
    • Drubin, D.G.1    Feinsteni, S.C.2    Shooter, E.M.3    Kirschner, M.W.4
  • 119
    • 49149083015 scopus 로고    scopus 로고
    • Evidence that non-fibrillar tau causes pathology linked to neurodegeneration and behavioral impairments
    • Brunden, K., Trojanowski, J. Q. & Lee, V. M. Y. Evidence that non-fibrillar tau causes pathology linked to neurodegeneration and behavioral impairments. J. Alzheimers Dis. 14, 393-399 (2008).
    • (2008) J. Alzheimers Dis , vol.14 , pp. 393-399
    • Brunden, K.1    Trojanowski, J.Q.2    Lee, V.M.Y.3
  • 120
    • 0141493680 scopus 로고    scopus 로고
    • The roles of the ubiquitin-proteasome and autophagy-lysosome pathways in Huntington's disease and related conditions
    • Ravikumar, B., Sarkar, S., Berger, Z. & Rubinsztein, D. C. The roles of the ubiquitin-proteasome and autophagy-lysosome pathways in Huntington's disease and related conditions. Clin. Neurosci. Res. 3, 141-148 (2003).
    • (2003) Clin. Neurosci. Res , vol.3 , pp. 141-148
    • Ravikumar, B.1    Sarkar, S.2    Berger, Z.3    Rubinsztein, D.C.4
  • 121
    • 33747881231 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disease: Friend, foe or turncoat?
    • Nixon, R. A. Autophagy in neurodegenerative disease: Friend, foe or turncoat? Trends Neurosci. 29, 528-535 (2006).
    • (2006) Trends Neurosci , vol.29 , pp. 528-535
    • Nixon, R.A.1
  • 122
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: An immuno-electron microscopy study
    • Nixon, R. A. et al. Extensive involvement of autophagy in Alzheimer disease: An immuno-electron microscopy study. J. Neuropathol. Exp. Neurol. 64, 113-122 (2005).
    • (2005) J. Neuropathol. Exp. Neurol , vol.64 , pp. 113-122
    • Nixon, R.A.1
  • 123
    • 0025736490 scopus 로고
    • Expression of heat-shock proteins in Alzheimers disease
    • Hamos, J. E. et al. Expression of heat-shock proteins in Alzheimers disease. Neurology 41, 345-350 (1991).
    • (1991) Neurology , vol.41 , pp. 345-350
    • Hamos, J.E.1
  • 124
    • 0026091893 scopus 로고
    • Increased synthesis and accumulation of heat-shock 70 proteins in Alzheimers disease
    • Perez, N. et al. Increased synthesis and accumulation of heat-shock 70 proteins in Alzheimers disease. Mol. Brain Res. 11, 249-254 (1991).
    • (1991) Mol. Brain Res , vol.11 , pp. 249-254
    • Perez, N.1
  • 125
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck, S., Nitsch, R., Grune, T. & Ullrich, O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 85, 115-122 (2003).
    • (2003) J. Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 126
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller, J. N., Hanni, K. B. & Markesbery, W. R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75, 436-439 (2000).
    • (2000) J. Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 127
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • Dickey, C. A. et al. The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J. Clin. Invest. 117, 648-658 (2007).
    • (2007) J. Clin. Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1
  • 128
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of HSP90
    • Zhang, H. & Burrows, F. Targeting multiple signal transduction pathways through inhibition of HSP90. J. Mol. Med. 82, 488-499 (2004).
    • (2004) J. Mol. Med , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 129
    • 33646246733 scopus 로고    scopus 로고
    • HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites
    • Dickey, C. A. et al. HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites. Faseb J. 20, 753-755 (2006).
    • (2006) Faseb J , vol.20 , pp. 753-755
    • Dickey, C.A.1
  • 130
    • 34547183507 scopus 로고    scopus 로고
    • Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
    • Luo, W. J. et al. Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc. Natl Acad. Sci. USA 104, 9511-9516 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 9511-9516
    • Luo, W.J.1
  • 131
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A. et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425, 407-410 (2003).
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1
  • 132
    • 33751034682 scopus 로고    scopus 로고
    • Aggregate-prone proteins are cleared from the cytosol by autophagy: Therapeutic implications
    • Williams, A. et al. Aggregate-prone proteins are cleared from the cytosol by autophagy: Therapeutic implications. Curr. Top. Dev. Biol. 76, 89-101 (2006).
    • (2006) Curr. Top. Dev. Biol , vol.76 , pp. 89-101
    • Williams, A.1
  • 133
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • Berger, Z. et al. Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum. Mol. Genet. 15, 433-442 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 433-442
    • Berger, Z.1
  • 134
    • 41149085729 scopus 로고    scopus 로고
    • Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
    • Hamano, T. et al. Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Eur. J. Neurosci. 27, 1119-1130 (2008).
    • (2008) Eur. J. Neurosci , vol.27 , pp. 1119-1130
    • Hamano, T.1
  • 135
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • Sarkar, S. et al. Lithium induces autophagy by inhibiting inositol monophosphatase. J. Cell Biol. 170, 1101-1111 (2005).
    • (2005) J. Cell Biol , vol.170 , pp. 1101-1111
    • Sarkar, S.1
  • 136
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • SantaCruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • SantaCruz, K.1
  • 137
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff, P., Schneider, A., Mandelkow, E. M. & Mandelkow, E. Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry 37, 10223-10230 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4


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