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Volumn 6, Issue 8, 2011, Pages 797-810

Advances in tau-based drug discovery

Author keywords

Aggregation; Alzheimer's disease; Autophagy; Chaperone; Immunotherapy; Phosphorylation; Tau; Tauopathy; Therapeutic

Indexed keywords

2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; 2 (3 CHLORO 4 HYDROXYANILINO) 3 (2 NITROPHENYL)MALEIMIDE; 3 AMINOPYRAZINYL 2 CARBOXAMIDE; 4 BENZYL 2 METHYL 1,2,4 THIAZOLIDINE 3,5 DIONE; ALSTERPAULLONE; AMINOTHIENOPYRIDAZINE DERIVATIVE; ANTHRAQUINONE DERIVATIVE; AR A 014418; AZD 1080; CYANINE DYE; DAUNORUBICIN; DOXORUBICIN; EPALRESTAT; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; INDIRUBIN; LITHIUM CHLORIDE; MALEIMIDE DERIVATIVE; METHYLENE BLUE; OXINDOLEQUINAZOLINE; PACLITAXEL; PACLITAXEL DERIVATIVE; PAULLONE; PHENOTHIAZINE; PROTEIN SERINE THREONINE KINASE INHIBITOR; REMBER; SRN 003 556; TAU PROTEIN; THIADIAZOLIDINONE; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 79960544589     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2011.586690     Document Type: Review
Times cited : (37)

References (112)
  • 2
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • DOI 10.1038/nrn2194, PII NRN2194
    • Ballatore C, Lee VM, Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimers disease and related disorders. Nat Rev Neurosci 2007;8:663-72 Available from: www.alz.co.uk/dementia [Last accessed 4 April 2011] (Pubitemid 47283144)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.9 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 3
    • 77957927865 scopus 로고    scopus 로고
    • The genetics of Alzheimer disease: Back to the future
    • Bertram L, Lill CM, Tanzi RE. The genetics of Alzheimer disease: back to the future. Neuron 2010;68:270-81
    • (2010) Neuron , vol.68 , pp. 270-81
    • Bertram, L.1    Lill, C.M.2    Tanzi, R.E.3
  • 5
    • 70349558522 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimers disease
    • Harold D, Abraham R, Hollingworth P, et al. Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimers disease. Nat Genet 2009;41:1088-93
    • (2009) Nat Genet , vol.41 , pp. 1088-93
    • Harold, D.1    Abraham, R.2    Hollingworth, P.3
  • 6
    • 78549264026 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimers disease
    • Lambert JC, Heath S, Even G, et al. Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimers disease. Nat Genet 2009;41:1094-9
    • (2009) Nat Genet , vol.41 , pp. 1094-9
    • Lambert, J.C.1    Heath, S.2    Even, G.3
  • 7
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 1998;393:702-5
    • (1998) Nature , vol.393 , pp. 702-5
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 8
    • 65249116483 scopus 로고    scopus 로고
    • Tau mutations in neurodegenerative diseases
    • Wolfe MS. Tau mutations in neurodegenerative diseases. J Biol Chem 2009;284:6021-5
    • (2009) J Biol Chem , vol.284 , pp. 6021-5
    • Wolfe, M.S.1
  • 11
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau - A toxic pas de deux in Alzheimers disease
    • Ittner LM, Gotz J. Amyloid-beta and tau - a toxic pas de deux in Alzheimers disease. Nat Rev Neurosci 2011;12:65-72
    • (2011) Nat Rev Neurosci , vol.12 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 12
    • 66549106850 scopus 로고    scopus 로고
    • Serial PIB and MRI in normal, mild cognitive impairment and Alzheimers disease: Implications for sequence of pathological events in Alzheimers disease
    • Jack CR Jr, Lowe VJ, Weigand SD, et al. Serial PIB and MRI in normal, mild cognitive impairment and Alzheimers disease: implications for sequence of pathological events in Alzheimers disease. Brain 2009;132:1355-65
    • (2009) Brain , vol.132 , pp. 1355-65
    • Jack Jr., C.R.1    Lowe, V.J.2    Weigand, S.D.3
  • 13
    • 70949100259 scopus 로고    scopus 로고
    • Mediators of tau phosphorylation in the pathogenesis of Alzheimers disease
    • Hanger DP, Seereeram A, Noble W. Mediators of tau phosphorylation in the pathogenesis of Alzheimers disease. Expert Rev Neurother 2009;9:1647-66
    • (2009) Expert Rev Neurother , vol.9 , pp. 1647-66
    • Hanger, D.P.1    Seereeram, A.2    Noble, W.3
  • 14
    • 0037103844 scopus 로고    scopus 로고
    • Expression patterns of tau mRNA isoforms correlate with susceptible lesions in progressive supranuclear palsy and corticobasal degeneration
    • Takanashi M, Mori H, Arima K, et al. Expression patterns of tau mRNA isoforms correlate with susceptible lesions in progressive supranuclear palsy and corticobasal degeneration. Brain Res Mol Brain Res 2002;104:210-19
    • (2002) Brain Res Mol Brain Res , vol.104 , pp. 210-19
    • Takanashi, M.1    Mori, H.2    Arima, K.3
  • 15
    • 46749113005 scopus 로고    scopus 로고
    • Tau-based treatment strategies in neurodegenerative diseases
    • DOI 10.1016/j.nurt.2008.05.006, PII S1933721308000962
    • Schneider A, Mandelkow E. Tau-based treatment strategies in neurodegenerative diseases. Neurotherapeutics 2008;5:443-57 (Pubitemid 351952490)
    • (2008) Neurotherapeutics , vol.5 , Issue.3 , pp. 443-457
    • Schneider, A.1    Mandelkow, E.2
  • 17
    • 0033520355 scopus 로고    scopus 로고
    • Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies
    • Sontag E, Nunbhakdi-Craig V, Lee G, et al. Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies. J Biol Chem 1999;274:25490-8
    • (1999) J Biol Chem , vol.274 , pp. 25490-8
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3
  • 18
    • 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, PII S0014579396013865
    • Kampers T, Friedhoff P, Biernat J, et al. RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments. FEBS Lett 1996;399:344-9 (Pubitemid 26426879)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 20
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by taus amino-terminal projection domain
    • Brandt R, Leger J, Lee G. Interaction of tau with the neural plasma membrane mediated by taus amino-terminal projection domain. J Cell Biol 1995;131:1327-40
    • (1995) J Cell Biol , vol.131 , pp. 1327-40
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 21
    • 82755189704 scopus 로고    scopus 로고
    • Dynamic association of tau with neuronal membranes is regulated by phosphorylation
    • published online 7 March 2011 doi:10.1016/j. neurobiolaging.2011.01.005
    • Pooler AM, Usardi A, Evans CJ, et al. Dynamic association of tau with neuronal membranes is regulated by phosphorylation. Neurobiol Aging 2011;published online 7 March 2011, doi:10.1016/j. neurobiolaging.2011.01.005
    • (2011) Neurobiol Aging
    • Pooler, A.M.1    Usardi, A.2    Evans, C.J.3
  • 22
    • 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
    • Reynolds CH, Garwood CJ, Wray S, 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
    • (2008) J Biol Chem , vol.283 , pp. 18177-86
    • Reynolds, C.H.1    Garwood, C.J.2    Wray, S.3
  • 23
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimers disease mouse models
    • Ittner LM, Ke YD, Delerue F, et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimers disease mouse models. Cell 2010;142:387-97
    • (2010) Cell , vol.142 , pp. 387-97
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3
  • 25
    • 70349133040 scopus 로고    scopus 로고
    • The microtubule-associated protein tau is also phosphorylated on tyrosine
    • Lebouvier T, Scales TM, Williamson R, et al. The microtubule-associated protein tau is also phosphorylated on tyrosine. J Alzheimers Dis 2009;18:1-9
    • (2009) J Alzheimers Dis , vol.18 , pp. 1-9
    • Lebouvier, T.1    Scales, T.M.2    Williamson, R.3
  • 26
    • 0033596946 scopus 로고    scopus 로고
    • Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments
    • Schneider A, Biernat J, von Bergen M, et al. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 1999;38:3549-58
    • (1999) Biochemistry , vol.38 , pp. 3549-58
    • Schneider, A.1    Biernat, J.2    Von Bergen, M.3
  • 27
    • 79952105548 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein: Implications for Alzheimers disease
    • published online 6 Jan 2011, doi:10.1016/j.neuint.2010.12.023
    • Martin L, Latypova X, Terro F. Post-translational modifications of tau protein: implications for Alzheimers disease. Neurochem Int 2011, published online 6 Jan 2011, doi:10.1016/j.neuint.2010.12.023
    • (2011) Neurochem Int
    • Martin, L.1    Latypova, X.2    Terro, F.3
  • 28
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimers disease and related tauopathies
    • Brunden KR, Trojanowski JQ, Lee VM. Advances in tau-focused drug discovery for Alzheimers disease and related tauopathies. Nat Rev Drug Discov 2009;8:783-93
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 783-93
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 29
    • 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. Alzheimers disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 1996;2:783-7 (Pubitemid 26225094)
    • (1996) Nature Medicine , vol.2 , Issue.7 , pp. 783-787
    • Del C. Alonso, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 30
    • 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, et al. Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses. Neurobiol Aging 2003;24:1079-85 (Pubitemid 37487885)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1079-1085
    • Mandelkow, E.-M.1    Stamer, K.2    Vogel, R.3    Thies, E.4    Mandelkow, E.5
  • 31
    • 51349143580 scopus 로고    scopus 로고
    • Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin
    • Cuchillo-Ibanez I, Seereeram A, Byers HL, et al. Phosphorylation of tau regulates its axonal transport by controlling its binding to kinesin. FASEB J 2008;22:3186-95
    • (2008) FASEB J , vol.22 , pp. 3186-95
    • Cuchillo-Ibanez, I.1    Seereeram, A.2    Byers, H.L.3
  • 35
    • 20044367108 scopus 로고    scopus 로고
    • Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
    • DOI 10.1523/JNEUROSCI.4637-04.2005
    • Andorfer C, Acker CM, Kress Y, et al. Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 2005;25:5446-54 (Pubitemid 40770926)
    • (2005) Journal of Neuroscience , vol.25 , Issue.22 , pp. 5446-5454
    • Andorfer, C.1    Acker, C.M.2    Kress, Y.3    Hof, P.R.4    Duff, K.5    Davies, P.6
  • 36
    • 78650251838 scopus 로고    scopus 로고
    • Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration
    • Hoover BR, Reed MN, Su J, et al. Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration. Neuron 2010;68:1067-81
    • (2010) Neuron , vol.68 , pp. 1067-81
    • Hoover, B.R.1    Reed, M.N.2    Su, J.3
  • 39
    • 0033798031 scopus 로고    scopus 로고
    • Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25
    • Leost M, Schultz C, Link A, et al. Paullones are potent inhibitors of glycogen synthase kinase-3beta and cyclin-dependent kinase 5/p25. Eur J Biochem 2000;267:5983-94
    • (2000) Eur J Biochem , vol.267 , pp. 5983-94
    • Leost, M.1    Schultz, C.2    Link, A.3
  • 40
    • 0037075791 scopus 로고    scopus 로고
    • First non-ATP competitive glycogen synthase kinase 3 β (GSK-3β) inhibitors: Thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimer's disease
    • DOI 10.1021/jm011020u
    • Martinez A, Alonso M, Castro A, et al. First non-ATP competitive glycogen synthase kinase 3 beta (GSK- 3beta) inhibitors: thiadiazolidinones (TDZD) as potential drugs for the treatment of Alzheimers disease. J Med Chem 2002;45:1292-9 (Pubitemid 34263565)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.6 , pp. 1292-1299
    • Martinez, A.1    Alonso, M.2    Castro, A.3    Perez, C.4    Moreno, F.J.5
  • 41
    • 0033776383 scopus 로고    scopus 로고
    • Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription
    • Coghlan MP, Culbert AA, Cross DA, et al. Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription. Chem Biol 2000;7:793-803
    • (2000) Chem Biol , vol.7 , pp. 793-803
    • Coghlan, M.P.1    Culbert, A.A.2    Cross, D.A.3
  • 43
    • 0034805180 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 by competition for magnesium
    • DOI 10.1006/bbrc.2000.4169
    • Ryves WJ, Harwood AJ. Lithium inhibits glycogen synthase kinase-3 by competition for magnesium. Biochem Biophys Res Commun 2001;280:720-5 (Pubitemid 32924489)
    • (2001) Biochemical and Biophysical Research Communications , vol.280 , Issue.3 , pp. 720-725
    • Ryves, W.J.1    Harwood, A.J.2
  • 44
    • 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
    • DOI 10.1111/j.1471-4159.2006.04139.x
    • Engel T, Goni-Oliver P, Lucas JJ, et al. Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert. J Neurochem 2006;99:1445-55 (Pubitemid 44924224)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.6 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 45
    • 77049116286 scopus 로고    scopus 로고
    • Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology
    • Leroy K, Ando K, Heraud C, et al. Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology. J Alzheimers Dis 2010;19:705-19
    • (2010) J Alzheimers Dis , vol.19 , pp. 705-19
    • Leroy, K.1    Ando, K.2    Heraud, C.3
  • 47
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • DOI 10.1038/nature01640
    • Phiel CJ, Wilson CA, Lee VM, Klein PS. GSK-3alpha regulates production of Alzheimers disease amyloid-beta peptides. Nature 2003;423:435-9 (Pubitemid 36626994)
    • (2003) Nature , vol.423 , Issue.6938 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.-Y.3    Klein, P.S.4
  • 48
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in Alzheimers disease: A randomized, single-blind, placebo-controlled, multicenter 10-week study
    • Hampel H, Ewers M, Burger K, et al. Lithium trial in Alzheimers disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. J Clin Psychiatry 2009;70:922-31
    • (2009) J Clin Psychiatry , vol.70 , pp. 922-31
    • Hampel, H.1    Ewers, M.2    Burger, K.3
  • 50
    • 58349114277 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3beta downregulates total tau proteins in cultured neurons and its reversal by the blockade of protein phosphatase-2A
    • Martin L, Magnaudeix A, Esclaire F, et al. Inhibition of glycogen synthase kinase-3beta downregulates total tau proteins in cultured neurons and its reversal by the blockade of protein phosphatase-2A. Brain Res 2009;1252:66-75
    • (2009) Brain Res , vol.1252 , pp. 66-75
    • Martin, L.1    Magnaudeix, A.2    Esclaire, F.3
  • 52
    • 77957340852 scopus 로고    scopus 로고
    • Phosphorylation alters tau distribution and elongates life span in Drosophila
    • Yeh PA, Chang CJ, Tu PH, et al. Phosphorylation alters tau distribution and elongates life span in Drosophila. J Alzheimers Dis 2010;21:543-56
    • (2010) J Alzheimers Dis , vol.21 , pp. 543-56
    • Yeh, P.A.1    Chang, C.J.2    Tu, P.H.3
  • 53
    • 54249140068 scopus 로고    scopus 로고
    • GSK-3 inhibitors a ray of hope for the treatment of Alzheimers disease?
    • Martinez A, Perez DI. GSK-3 inhibitors: a ray of hope for the treatment of Alzheimers disease? J Alzheimers Dis 2008;15:181-91
    • (2008) J Alzheimers Dis , vol.15 , pp. 181-91
    • Martinez, A.1    Perez, D.I.2
  • 54
    • 70349331692 scopus 로고    scopus 로고
    • Alpha-Synuclein contributes to GSK-3beta-catalyzed Tau phosphorylation in Parkinsons disease models
    • Duka T, Duka V, Joyce JN, Sidhu A. Alpha-Synuclein contributes to GSK-3beta-catalyzed Tau phosphorylation in Parkinsons disease models. FASEB J 2009;23:2820-30
    • (2009) FASEB J , vol.23 , pp. 2820-30
    • Duka, T.1    Duka, V.2    Joyce, J.N.3    Sidhu, A.4
  • 55
    • 68149150844 scopus 로고    scopus 로고
    • A novel GSK-3beta inhibitor reduces Alzheimers pathology and rescues neuronal loss in vivo
    • Sereno L, Coma M, Rodriguez M, et al. A novel GSK-3beta inhibitor reduces Alzheimers pathology and rescues neuronal loss in vivo. Neurobiol Dis 2009;35:359-67
    • (2009) Neurobiol Dis , vol.35 , pp. 359-67
    • Sereno, L.1    Coma, M.2    Rodriguez, M.3
  • 56
    • 58149479354 scopus 로고    scopus 로고
    • GSK3 inhibitors show benefits in an Alzheimers disease (AD) model of neurodegeneration but adverse effects in control animals
    • Hu S, Begum AN, Jones MR, et al. GSK3 inhibitors show benefits in an Alzheimers disease (AD) model of neurodegeneration but adverse effects in control animals. Neurobiol Dis 2009;33:193-206
    • (2009) Neurobiol Dis , vol.33 , pp. 193-206
    • Hu, S.1    Begum, A.N.2    Jones, M.R.3
  • 57
    • 19244367909 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35: Implications for Alzheimer's disease
    • DOI 10.1074/jbc.M311512200
    • Hernandez F, Perez M, Lucas JJ, et al. Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimers disease. J Biol Chem 2004;279:3801-6 Available from: http://www.astrazeneca. com/article/511390.aspx [Last accessed 26 February 2011] (Pubitemid 38140625)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3801-3806
    • Hernandez, F.1    Perez, M.2    Lucas, J.J.3    Mata, A.M.4    Bhat, R.5    Avila, J.6
  • 59
    • 77950937605 scopus 로고    scopus 로고
    • Crosstalk between Cdk5 and GSK3beta: Implications for Alzheimers disease
    • Engmann O, Giese KP. Crosstalk between Cdk5 and GSK3beta: implications for Alzheimers disease. Front Mol Neurosci 2009;2:2
    • (2009) Front Mol Neurosci , vol.2 , pp. 2
    • Engmann, O.1    Giese, K.P.2
  • 61
    • 0035823496 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse
    • Planel E, Yasutake K, Fujita SC, Ishiguro K. Inhibition of protein phosphatase 2A overrides tau protein kinase I/glycogen synthase kinase 3 beta and cyclin-dependent kinase 5 inhibition and results in tau hyperphosphorylation in the hippocampus of starved mouse. J Biol Chem 2001;276:34298-306
    • (2001) J Biol Chem , vol.276 , pp. 34298-306
    • Planel, E.1    Yasutake, K.2    Fujita, S.C.3    Ishiguro, K.4
  • 62
    • 2442465965 scopus 로고    scopus 로고
    • Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration
    • DOI 10.1016/j.febslet.2004.04.047, PII S0014579304004727
    • Li L, Sengupta A, Haque N, et al. Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration. FEBS Lett 2004;566:261-9 (Pubitemid 38625969)
    • (2004) FEBS Letters , vol.566 , Issue.1-3 , pp. 261-269
    • Li, L.1    Sengupta, A.2    Haque, N.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 63
    • 79960483325 scopus 로고    scopus 로고
    • Last accessed 26 February 2011
    • Available from: http://www. signumbiosciences.com/pipeline.html [Last accessed 26 February 2011]
  • 64
    • 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
  • 65
    • 68849086671 scopus 로고    scopus 로고
    • Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening
    • Crowe A, Huang W, Ballatore C, et al. Identification of aminothienopyridazine inhibitors of tau assembly by quantitative high-throughput screening. Biochemistry 2009;48:7732-45
    • (2009) Biochemistry , vol.48 , pp. 7732-45
    • Crowe, A.1    Huang, W.2    Ballatore, C.3
  • 69
    • 65249128503 scopus 로고    scopus 로고
    • Challenges in the conduct of disease-modifying trials in AD: Practical experience from a phase 2 trial of Tau-aggregation inhibitor therapy
    • Wischik C, Staff R. Challenges in the conduct of disease-modifying trials in AD: practical experience from a phase 2 trial of Tau-aggregation inhibitor therapy. J Nutr Health Aging 2009;13:367-9
    • (2009) J Nutr Health Aging , vol.13 , pp. 367-9
    • Wischik, C.1    Staff, R.2
  • 70
    • 77958566761 scopus 로고    scopus 로고
    • Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
    • OLeary JC III, Li Q, Marinec P, et al. Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden. Mol Neurodegener 2010;5:45
    • (2010) Mol Neurodegener , vol.5 , pp. 45
    • OLeary III, J.C.1    Li, Q.2    Marinec, P.3
  • 71
    • 66749176089 scopus 로고    scopus 로고
    • Structure-activity relationship of cyanine tau aggregation inhibitors
    • Chang E, Congdon EE, Honson NS, et al. Structure-activity relationship of cyanine tau aggregation inhibitors. J Med Chem 2009;52:3539-47
    • (2009) J Med Chem , vol.52 , pp. 3539-47
    • Chang, E.1    Congdon, E.E.2    Honson, N.S.3
  • 72
    • 68949116305 scopus 로고    scopus 로고
    • Inhibition of tau polymerization with a cyanine dye in two distinct model systems
    • Congdon EE, Figueroa YH, Wang L, et al. Inhibition of tau polymerization with a cyanine dye in two distinct model systems. J Biol Chem 2009;284:20830-9
    • (2009) J Biol Chem , vol.284 , pp. 20830-9
    • Congdon, E.E.1    Figueroa, Y.H.2    Wang, L.3
  • 73
    • 1542327644 scopus 로고    scopus 로고
    • Ligand-dependent inhibition and reversal of tau filament formation
    • DOI 10.1021/bi036094h
    • Chirita C, Necula M, Kuret J. Ligand-dependent inhibition and reversal of tau filament formation. Biochemistry 2004;43:2879-87 (Pubitemid 38327819)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2879-2887
    • Chirita, C.1    Necula, M.2    Kuret, J.3
  • 74
    • 77952081276 scopus 로고    scopus 로고
    • Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation
    • Ballatore C, Brunden KR, Piscitelli F, et al. Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation. J Med Chem 2010;53:3739-47
    • (2010) J Med Chem , vol.53 , pp. 3739-47
    • Ballatore, C.1    Brunden, K.R.2    Piscitelli, F.3
  • 76
    • 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, Biernat J, Wang Y, 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 2006;281:1205-14
    • (2006) J Biol Chem , vol.281 , pp. 1205-14
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3
  • 78
    • 33746456027 scopus 로고    scopus 로고
    • Long-term clinical effects of epalrestat, an aldose reductase inhibitor, on diabetic peripheral neuropathy: The 3-year, multicenter, comparative aldose reductase inhibitor-diabetes complications trial
    • DOI 10.2337/dc05-2370
    • Hotta N, Akanuma Y, Kawamori R, et al. Long-term clinical effects of epalrestat, an aldose reductase inhibitor, on diabetic peripheral neuropathy: the 3-year, multicenter, comparative Aldose Reductase Inhibitor-Diabetes Complications Trial. Diabetes Care 2006;29:1538-44 (Pubitemid 44127578)
    • (2006) Diabetes Care , vol.29 , Issue.7 , pp. 1538-1544
    • Hotta, N.1    Akanuma, Y.2    Kawamori, R.3    Matsuoka, K.4    Oka, Y.5    Shichiri, M.6    Toyota, T.7    Nakashima, M.8    Yoshimura, I.9    Sakamoto, N.10    Shigeta, Y.11
  • 79
    • 61349145507 scopus 로고    scopus 로고
    • Development of tau aggregation inhibitors for Alzheimers disease
    • Bulic B, Pickhardt M, Schmidt B, et al. Development of tau aggregation inhibitors for Alzheimers disease. Angew Chem Int Ed Engl 2009;48:1740-52
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 1740-52
    • Bulic, B.1    Pickhardt, M.2    Schmidt, B.3
  • 80
    • 78649767505 scopus 로고    scopus 로고
    • Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimers disease
    • published online 5 Nov 2010, doi:10.1016/j.pneurobio.2010.10.006
    • Salminen A, Ojala J, Kaarniranta K, et al. Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimers disease. Prog Neurobiol 2010;published online 5 Nov 2010, doi:10.1016/j.pneurobio.2010.10.006
    • (2010) Prog Neurobiol
    • Salminen, A.1    Ojala, J.2    Kaarniranta, K.3
  • 85
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • DOI 10.1523/JNEUROSCI.2361-07.2007
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci 2007;27:9115-29 (Pubitemid 47312068)
    • (2007) Journal of Neuroscience , vol.27 , Issue.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 86
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A, et al. Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp Neurol 2010;224:472-85
    • (2010) Exp Neurol , vol.224 , pp. 472-85
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3
  • 88
    • 33645736326 scopus 로고    scopus 로고
    • Peripheral neuropathy induced by microtubule-stabilizing agents
    • DOI 10.1200/JCO.2005.04.0543
    • Lee JJ, Swain SM. Peripheral neuropathy induced by microtubule- stabilizing agents. J Clin Oncol 2006;24:1633-42 (Pubitemid 46638788)
    • (2006) Journal of Clinical Oncology , vol.24 , Issue.10 , pp. 1633-1642
    • Lee, J.J.1    Swain, S.M.2
  • 90
    • 64649097649 scopus 로고    scopus 로고
    • NAP protects memory, increases soluble tau and reduces tau hyperphosphorylation in a tauopathy model
    • Shiryaev N, Jouroukhin Y, Giladi E, et al. NAP protects memory, increases soluble tau and reduces tau hyperphosphorylation in a tauopathy model. Neurobiol Dis 2009;34:381-8
    • (2009) Neurobiol Dis , vol.34 , pp. 381-8
    • Shiryaev, N.1    Jouroukhin, Y.2    Giladi, E.3
  • 92
    • 34247876141 scopus 로고    scopus 로고
    • Therapies for Alzheimers disease
    • Melnikova I. Therapies for Alzheimers disease. Nat Rev Drug Discov 2007;6:341-2
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 341-2
    • Melnikova, I.1
  • 93
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden KR, Zhang B, Carroll J, et al. Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci 2010;30:13861-6
    • (2010) J Neurosci , vol.30 , pp. 13861-6
    • Brunden, K.R.1    Zhang, B.2    Carroll, J.3
  • 94
    • 0035900725 scopus 로고    scopus 로고
    • Correction of alternative splicing of tau in frontotemporal dementia and parkinsonism linked to chromosome 17
    • Kalbfuss B, Mabon SA, Misteli T. Correction of alternative splicing of tau in frontotemporal dementia and parkinsonism linked to chromosome 17. J Biol Chem 2001;276:42986-93
    • (2001) J Biol Chem , vol.276 , pp. 42986-93
    • Kalbfuss, B.1    Mabon, S.A.2    Misteli, T.3
  • 97
    • 77949962484 scopus 로고    scopus 로고
    • Intravenous immunoglobulins as a treatment for Alzheimers disease: Rationale and current evidence
    • Dodel R, Neff F, Noelker C, et al. Intravenous immunoglobulins as a treatment for Alzheimers disease: rationale and current evidence. Drugs 2010;70:513-28
    • (2010) Drugs , vol.70 , pp. 513-28
    • Dodel, R.1    Neff, F.2    Noelker, C.3
  • 98
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Aβ and tau, but not soluble Aβ alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • DOI 10.1074/jbc.M608485200
    • Oddo S, Vasilevko V, Caccamo A, et al. Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J Biol Chem 2006;281:39413-23 (Pubitemid 46041901)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 99
    • 77952548786 scopus 로고    scopus 로고
    • Tau-directed drug discovery for Alzheimers disease and related tauopathies: A focus on tau assembly inhibitors
    • Brunden KR, Ballatore C, Crowe A, et al. Tau-directed drug discovery for Alzheimers disease and related tauopathies: a focus on tau assembly inhibitors. Exp Neurol 2010;223:304-10
    • (2010) Exp Neurol , vol.223 , pp. 304-10
    • Brunden, K.R.1    Ballatore, C.2    Crowe, A.3
  • 100
    • 77956226071 scopus 로고    scopus 로고
    • Biomarker discovery for Alzheimers disease, frontotemporal lobar degeneration, and Parkinsons disease
    • Hu WT, Chen-Plotkin A, Arnold SE, et al. Biomarker discovery for Alzheimers disease, frontotemporal lobar degeneration, and Parkinsons disease. Acta Neuropathol 2010;120:385-99
    • (2010) Acta Neuropathol , vol.120 , pp. 385-99
    • Hu, W.T.1    Chen-Plotkin, A.2    Arnold, S.E.3
  • 101
    • 77954239263 scopus 로고    scopus 로고
    • Biomarkers for Alzheimers disease: Academic, industry and regulatory perspectives
    • Hampel H, Frank R, Broich K, et al. Biomarkers for Alzheimers disease: academic, industry and regulatory perspectives. Nat Rev Drug Discov 2010;9:560-74
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 560-74
    • Hampel, H.1    Frank, R.2    Broich, K.3
  • 102
    • 77951671969 scopus 로고    scopus 로고
    • Cerebrospinal fluid biomarkers of Alzheimers disease
    • Fagan AM, Holtzman DM. Cerebrospinal fluid biomarkers of Alzheimers disease. Biomark Med 2010;4:51-63
    • (2010) Biomark Med , vol.4 , pp. 51-63
    • Fagan, A.M.1    Holtzman, D.M.2
  • 105
    • 77953614566 scopus 로고    scopus 로고
    • In vivo detection of neuropathologic changes in presymptomatic MAPT mutation carriers: A PET and MRI study
    • Miyoshi M, Shinotoh H, Wszolek ZK, et al. In vivo detection of neuropathologic changes in presymptomatic MAPT mutation carriers: a PET and MRI study. Parkinsonism Relat Disord 2010;16:404-8
    • (2010) Parkinsonism Relat Disord , vol.16 , pp. 404-8
    • Miyoshi, M.1    Shinotoh, H.2    Wszolek, Z.K.3
  • 106
    • 77049090834 scopus 로고    scopus 로고
    • Selective interaction of lansoprazole and astemizole with tau polymers: Potential new clinical use in diagnosis of Alzheimers disease
    • Rojo LE, Alzate-Morales J, Saavedra IN, et al. Selective interaction of lansoprazole and astemizole with tau polymers: potential new clinical use in diagnosis of Alzheimers disease. J Alzheimers Dis 2010;19:573-89
    • (2010) J Alzheimers Dis , vol.19 , pp. 573-89
    • Rojo, L.E.1    Alzate-Morales, J.2    Saavedra, I.N.3
  • 107
    • 79960481290 scopus 로고    scopus 로고
    • [Last accessed 4 April 2011]
    • Available from: http://www.alz.org/research/diagnostic-criteria/ preclinical-recommendations.pdf [Last accessed 4 April 2011]
  • 108
    • 77955704022 scopus 로고    scopus 로고
    • Integrating ADNI results into Alzheimers disease drug development programs
    • Cummings JL. Integrating ADNI results into Alzheimers disease drug development programs. Neurobiol Aging 2010;31:1481-92
    • (2010) Neurobiol Aging , vol.31 , pp. 1481-92
    • Cummings, J.L.1
  • 109
    • 55249112456 scopus 로고    scopus 로고
    • Invited article: The Alzheimer disease-frontotemporal lobar degeneration spectrum
    • van der Zee J, Sleegers K, Van Brockhoven C. Invited article: the Alzheimer disease-frontotemporal lobar degeneration spectrum. Neurology 2008;71:1191-7
    • (2008) Neurology , vol.71 , pp. 1191-7
    • Van Der Zee, J.1    Sleegers, K.2    Van Brockhoven, C.3
  • 110
    • 77951803088 scopus 로고    scopus 로고
    • Early Alzheimers trials: New developments
    • Vellas B, Aisen PS. Early Alzheimers trials: new developments. J Nutr Health Aging 2010;14:293
    • (2010) J Nutr Health Aging , vol.14 , pp. 293
    • Vellas, B.1    Aisen, P.S.2
  • 112
    • 79960510716 scopus 로고    scopus 로고
    • [Last accessed 26 February 2011]
    • Available from: http://www.researchals. org/page/4746/6097/[Last accessed 26 February 2011]


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