메뉴 건너뛰기




Volumn 53, Issue 7, 2016, Pages 4893-4904

The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy

Author keywords

Genetics; MAPT; Neurodegeneration; Pathogenesis; Therapy

Indexed keywords

ACETYLCHOLINE; MINOCYCLINE; NONSTEROID ANTIINFLAMMATORY AGENT; PHOSPHOPEPTIDE; TAU PROTEIN; TELMISARTAN; MAPT PROTEIN, HUMAN;

EID: 84941334167     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-015-9415-8     Document Type: Review
Times cited : (54)

References (129)
  • 1
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau—a toxic pas de deux in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3MXjvFeq, PID: 21193853
    • Ittner LM, Gotz J (2011) Amyloid-beta and tau—a toxic pas de deux in Alzheimer's disease. Nat Rev Neurosci 12(2):65–72. doi:10.1038/nrn2967
    • (2011) Nat Rev Neurosci , vol.12 , Issue.2 , pp. 65-72
    • Ittner, L.M.1    Gotz, J.2
  • 2
    • 84904678185 scopus 로고    scopus 로고
    • Apolipoprotein E in Alzheimer's disease: an update
    • COI: 1:CAS:528:DC%2BC2cXhsVKgt7fP, PID: 24821312
    • Yu JT, Tan L, Hardy J (2014) Apolipoprotein E in Alzheimer's disease: an update. Annu Rev Neurosci 37:79–100. doi:10.1146/annurev-neuro-071013-014300
    • (2014) Annu Rev Neurosci , vol.37 , pp. 79-100
    • Yu, J.T.1    Tan, L.2    Hardy, J.3
  • 3
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • COI: 1:CAS:528:DC%2BC3sXnvVGkur0%3D, PID: 23684085
    • Spillantini MG, Goedert M (2013) Tau pathology and neurodegeneration. Lancet Neurol 12(6):609–622. doi:10.1016/s1474-4422(13)70090-5
    • (2013) Lancet Neurol , vol.12 , Issue.6 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 4
    • 0031949084 scopus 로고    scopus 로고
    • Frontotemporal dementia and Parkinsonism linked to chromosome 17: a new group of tauopathies
    • COI: 1:CAS:528:DyaK1cXjslKhsrc%3D, PID: 9546295
    • Spillantini MG, Bird TD, Ghetti B (1998) Frontotemporal dementia and Parkinsonism linked to chromosome 17: a new group of tauopathies. Brain Pathol 8(2):387–402
    • (1998) Brain Pathol , vol.8 , Issue.2 , pp. 387-402
    • Spillantini, M.G.1    Bird, T.D.2    Ghetti, B.3
  • 5
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • COI: 1:CAS:528:DyaK1cXktVyqsr0%3D, PID: 9641683
    • Hutton M, Lendon CL, Rizzu P, Baker M, Froelich S, Houlden H, Pickering-Brown S, Chakraverty S et al (1998) Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393(6686):702–705. doi:10.1038/31508
    • (1998) Nature , vol.393 , Issue.6686 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3    Baker, M.4    Froelich, S.5    Houlden, H.6    Pickering-Brown, S.7    Chakraverty, S.8
  • 6
    • 84887232005 scopus 로고    scopus 로고
    • Different mutations at V363 MAPT codon are associated with atypical clinical phenotypes and show unusual structural and functional features
    • COI: 1:CAS:528:DC%2BC3sXhsVKnsL7L, PID: 24018212
    • Rossi G, Bastone A, Piccoli E, Morbin M, Mazzoleni G, Fugnanesi V, Beeg M, Del Favero E et al (2014) Different mutations at V363 MAPT codon are associated with atypical clinical phenotypes and show unusual structural and functional features. Neurobiol Aging 35(2):408–417. doi:10.1016/j.neurobiolaging.2013.08.004
    • (2014) Neurobiol Aging , vol.35 , Issue.2 , pp. 408-417
    • Rossi, G.1    Bastone, A.2    Piccoli, E.3    Morbin, M.4    Mazzoleni, G.5    Fugnanesi, V.6    Beeg, M.7    Del Favero, E.8
  • 7
    • 84904015566 scopus 로고    scopus 로고
    • Lower motor neuron disease with respiratory failure caused by a novel MAPT mutation
    • PID: 24808015
    • Di Fonzo A, Ronchi D, Gallia F, Cribiu FM, Trezzi I, Vetro A, Della Mina E, Limongelli I et al (2014) Lower motor neuron disease with respiratory failure caused by a novel MAPT mutation. Neurology 82(22):1990–1998. doi:10.1212/wnl.0000000000000476
    • (2014) Neurology , vol.82 , Issue.22 , pp. 1990-1998
    • Di Fonzo, A.1    Ronchi, D.2    Gallia, F.3    Cribiu, F.M.4    Trezzi, I.5    Vetro, A.6    Della Mina, E.7    Limongelli, I.8
  • 8
    • 84884681457 scopus 로고    scopus 로고
    • A novel MAPT mutation, G55R, in a frontotemporal dementia patient leads to altered Tau function
    • COI: 1:CAS:528:DC%2BC3sXhsFOntb%2FM, PID: 24086739
    • Iyer A, Lapointe NE, Zielke K, Berdynski M, Guzman E, Barczak A, Chodakowska-Zebrowska M, Barcikowska M et al (2013) A novel MAPT mutation, G55R, in a frontotemporal dementia patient leads to altered Tau function. PLoS One 8(9), e76409. doi:10.1371/journal.pone.0076409
    • (2013) PLoS One , vol.8 , Issue.9
    • Iyer, A.1    Lapointe, N.E.2    Zielke, K.3    Berdynski, M.4    Guzman, E.5    Barczak, A.6    Chodakowska-Zebrowska, M.7    Barcikowska, M.8
  • 9
    • 84864505483 scopus 로고    scopus 로고
    • Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases
    • COI: 1:CAS:528:DC%2BC38XhtVeiu7vO, PID: 22556362
    • Coppola G, Chinnathambi S, Lee JJ, Dombroski BA, Baker MC, Soto-Ortolaza AI, Lee SE, Klein E et al (2012) Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases. Hum Mol Genet 21(15):3500–3512. doi:10.1093/hmg/dds161
    • (2012) Hum Mol Genet , vol.21 , Issue.15 , pp. 3500-3512
    • Coppola, G.1    Chinnathambi, S.2    Lee, J.J.3    Dombroski, B.A.4    Baker, M.C.5    Soto-Ortolaza, A.I.6    Lee, S.E.7    Klein, E.8
  • 10
    • 84884150340 scopus 로고    scopus 로고
    • TDP-43 pathology in a patient carrying G2019S LRRK2 mutation and a novel p.Q124E MAPT
    • PID: 23664753, e2885-2889
    • Ling H, Kara E, Bandopadhyay R, Hardy J, Holton J, Xiromerisiou G, Lees A, Houlden H et al (2013) TDP-43 pathology in a patient carrying G2019S LRRK2 mutation and a novel p.Q124E MAPT. Neurobiol Aging 34(12):2889. doi:10.1016/j.neurobiolaging.2013.04.011, e2885-2889
    • (2013) Neurobiol Aging , vol.34 , Issue.12 , pp. 2889
    • Ling, H.1    Kara, E.2    Bandopadhyay, R.3    Hardy, J.4    Holton, J.5    Xiromerisiou, G.6    Lees, A.7    Houlden, H.8
  • 13
    • 77951185469 scopus 로고    scopus 로고
    • Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease
    • COI: 1:CAS:528:DC%2BC3cXksVKgt7s%3D, PID: 20070850
    • Edwards TL, Scott WK, Almonte C, Burt A, Powell EH, Beecham GW, Wang L, Zuchner S et al (2010) Genome-wide association study confirms SNPs in SNCA and the MAPT region as common risk factors for Parkinson disease. Ann Hum Genet 74(2):97–109. doi:10.1111/j.1469-1809.2009.00560.x
    • (2010) Ann Hum Genet , vol.74 , Issue.2 , pp. 97-109
    • Edwards, T.L.1    Scott, W.K.2    Almonte, C.3    Burt, A.4    Powell, E.H.5    Beecham, G.W.6    Wang, L.7    Zuchner, S.8
  • 14
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • COI: 1:CAS:528:DC%2BD1MXhsVWlsbrP, PID: 19915575
    • Simon-Sanchez J, Schulte C, Bras JM, Sharma M, Gibbs JR, Berg D, Paisan-Ruiz C, Lichtner P et al (2009) Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nat Genet 41(12):1308–1312. doi:10.1038/ng.487
    • (2009) Nat Genet , vol.41 , Issue.12 , pp. 1308-1312
    • Simon-Sanchez, J.1    Schulte, C.2    Bras, J.M.3    Sharma, M.4    Gibbs, J.R.5    Berg, D.6    Paisan-Ruiz, C.7    Lichtner, P.8
  • 15
    • 70549084415 scopus 로고    scopus 로고
    • Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease
    • COI: 1:CAS:528:DC%2BD1MXhsVWlsb7O, PID: 19915576
    • Satake W, Nakabayashi Y, Mizuta I, Hirota Y, Ito C, Kubo M, Kawaguchi T, Tsunoda T et al (2009) Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nat Genet 41(12):1303–1307. doi:10.1038/ng.485
    • (2009) Nat Genet , vol.41 , Issue.12 , pp. 1303-1307
    • Satake, W.1    Nakabayashi, Y.2    Mizuta, I.3    Hirota, Y.4    Ito, C.5    Kubo, M.6    Kawaguchi, T.7    Tsunoda, T.8
  • 16
    • 84927747465 scopus 로고    scopus 로고
    • The role of tau in neurodegenerative diseases and its potential as a therapeutic target
    • PID: 24278740
    • Wolfe MS (2012) The role of tau in neurodegenerative diseases and its potential as a therapeutic target. Scientifica 2012:796024. doi:10.6064/2012/796024
    • (2012) Scientifica , vol.2012 , pp. 796024
    • Wolfe, M.S.1
  • 17
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization
    • COI: 1:CAS:528:DyaK3MXlvFKitw%3D%3D, PID: 2124967
    • Goedert M, Jakes R (1990) Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J 9(13):4225–4230
    • (1990) EMBO J , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 18
    • 84858664547 scopus 로고    scopus 로고
    • Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation
    • COI: 1:CAS:528:DC%2BC38Xislygu7c%3D, PID: 22366723
    • Yuzwa SA, Shan X, Macauley MS, Clark T, Skorobogatko Y, Vosseller K, Vocadlo DJ (2012) Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat Chem Biol 8(4):393–399. doi:10.1038/nchembio.797
    • (2012) Nat Chem Biol , vol.8 , Issue.4 , pp. 393-399
    • Yuzwa, S.A.1    Shan, X.2    Macauley, M.S.3    Clark, T.4    Skorobogatko, Y.5    Vosseller, K.6    Vocadlo, D.J.7
  • 19
    • 84893460762 scopus 로고    scopus 로고
    • Increasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L mice
    • PID: 24376810
    • Borghgraef P, Menuet C, Theunis C, Louis JV, Devijver H, Maurin H, Smet-Nocca C, Lippens G et al (2013) Increasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L mice. PLoS One 8(12), e84442. doi:10.1371/journal.pone.0084442
    • (2013) PLoS One , vol.8 , Issue.12
    • Borghgraef, P.1    Menuet, C.2    Theunis, C.3    Louis, J.V.4    Devijver, H.5    Maurin, H.6    Smet-Nocca, C.7    Lippens, G.8
  • 20
    • 84891619442 scopus 로고    scopus 로고
    • Increased O-GlcNAcylation reduces pathological tau without affecting its normal phosphorylation in a mouse model of tauopathy
    • COI: 1:CAS:528:DC%2BC2cXjsVWru7w%3D, PID: 24326295
    • Graham DL, Gray AJ, Joyce JA, Yu D, O'Moore J, Carlson GA, Shearman MS, Dellovade TL et al (2014) Increased O-GlcNAcylation reduces pathological tau without affecting its normal phosphorylation in a mouse model of tauopathy. Neuropharmacology 79:307–313. doi:10.1016/j.neuropharm.2013.11.025
    • (2014) Neuropharmacology , vol.79 , pp. 307-313
    • Graham, D.L.1    Gray, A.J.2    Joyce, J.A.3    Yu, D.4    O'Moore, J.5    Carlson, G.A.6    Shearman, M.S.7    Dellovade, T.L.8
  • 21
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • COI: 1:CAS:528:DC%2BC3cXht1Wisr3K, PID: 20869593
    • Min SW, Cho SH, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, Huang EJ, Shen Y et al (2010) Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67(6):953–966. doi:10.1016/j.neuron.2010.08.044
    • (2010) Neuron , vol.67 , Issue.6 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3    Schroeder, S.4    Haroutunian, V.5    Seeley, W.W.6    Huang, E.J.7    Shen, Y.8
  • 23
    • 80052846665 scopus 로고    scopus 로고
    • Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3MXhtFynsbvI, PID: 21872849
    • Reddy PH (2011) Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease. Brain Res 1415:136–148. doi:10.1016/j.brainres.2011.07.052
    • (2011) Brain Res , vol.1415 , pp. 136-148
    • Reddy, P.H.1
  • 24
    • 80052841914 scopus 로고    scopus 로고
    • A novel MAPT mutation associated with the clinical phenotype of progressive nonfluent aphasia
    • COI: 1:CAS:528:DC%2BC3MXhtFWltbnF, PID: 21558644
    • Villa C, Ghezzi L, Pietroboni AM, Fenoglio C, Cortini F, Serpente M, Cantoni C, Ridolfi E et al (2011) A novel MAPT mutation associated with the clinical phenotype of progressive nonfluent aphasia. J Alzheimers Dis 26(1):19–26. doi:10.3233/jad-2011-102124
    • (2011) J Alzheimers Dis , vol.26 , Issue.1 , pp. 19-26
    • Villa, C.1    Ghezzi, L.2    Pietroboni, A.M.3    Fenoglio, C.4    Cortini, F.5    Serpente, M.6    Cantoni, C.7    Ridolfi, E.8
  • 25
    • 35649028013 scopus 로고    scopus 로고
    • Interaction of tau protein with the dynactin complex
    • COI: 1:CAS:528:DC%2BD2sXht1emtbjM, PID: 17932487
    • Magnani E, Fan J, Gasparini L, Golding M, Williams M, Schiavo G, Goedert M, Amos LA et al (2007) Interaction of tau protein with the dynactin complex. EMBO J 26(21):4546–4554. doi:10.1038/sj.emboj.7601878
    • (2007) EMBO J , vol.26 , Issue.21 , pp. 4546-4554
    • Magnani, E.1    Fan, J.2    Gasparini, L.3    Golding, M.4    Williams, M.5    Schiavo, G.6    Goedert, M.7    Amos, L.A.8
  • 26
    • 84896702979 scopus 로고    scopus 로고
    • Neuropathological characterization of two siblings carrying the MAPT S305S mutation demonstrates features resembling argyrophilic grain disease
    • PID: 24337498
    • Ronnback A, Nennesmo I, Tuominen H, Grueninger F, Viitanen M, Graff C (2014) Neuropathological characterization of two siblings carrying the MAPT S305S mutation demonstrates features resembling argyrophilic grain disease. Acta Neuropathol 127(2):297–298. doi:10.1007/s00401-013-1229-z
    • (2014) Acta Neuropathol , vol.127 , Issue.2 , pp. 297-298
    • Ronnback, A.1    Nennesmo, I.2    Tuominen, H.3    Grueninger, F.4    Viitanen, M.5    Graff, C.6
  • 28
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • PID: 15190058
    • Alonso Adel C, Mederlyova A, Novak M, Grundke-Iqbal I, Iqbal K (2004) Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem 279(33):34873–34881. doi:10.1074/jbc.M405131200
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34873-34881
    • Alonso Adel, C.1    Mederlyova, A.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 30
    • 79955688386 scopus 로고    scopus 로고
    • Familial semantic dementia with P301L mutation in the Tau gene
    • COI: 1:CAS:528:DC%2BC3MXovF2nt7g%3D, PID: 21555888
    • Ishizuka T, Nakamura M, Ichiba M, Sano A (2011) Familial semantic dementia with P301L mutation in the Tau gene. Dement Geriatr Cogn Disord 31(5):334–340. doi:10.1159/000328412
    • (2011) Dement Geriatr Cogn Disord , vol.31 , Issue.5 , pp. 334-340
    • Ishizuka, T.1    Nakamura, M.2    Ichiba, M.3    Sano, A.4
  • 31
    • 84892682478 scopus 로고    scopus 로고
    • Juvenile frontotemporal dementia with parkinsonism associated with tau mutation G389R
    • COI: 1:CAS:528:DC%2BC3sXhs1SgtrbF, PID: 23948919
    • Chaunu MP, Deramecourt V, Buee-Scherrer V, Le Ber I, Brice A, Ehrle N, El Hachimi K, Pluot M et al (2013) Juvenile frontotemporal dementia with parkinsonism associated with tau mutation G389R. J Alzheimers Dis 37(4):769–776. doi:10.3233/jad-130413
    • (2013) J Alzheimers Dis , vol.37 , Issue.4 , pp. 769-776
    • Chaunu, M.P.1    Deramecourt, V.2    Buee-Scherrer, V.3    Le Ber, I.4    Brice, A.5    Ehrle, N.6    El Hachimi, K.7    Pluot, M.8
  • 33
    • 79953301545 scopus 로고    scopus 로고
    • Novel L284R MAPT mutation in a family with an autosomal dominant progressive supranuclear palsy syndrome
    • COI: 1:CAS:528:DC%2BC3MXjvFKqtLY%3D, PID: 20838030
    • Rohrer JD, Paviour D, Vandrovcova J, Hodges J, de Silva R, Rossor MN (2011) Novel L284R MAPT mutation in a family with an autosomal dominant progressive supranuclear palsy syndrome. Neurodegener Dis 8(3):149–152. doi:10.1159/000319454
    • (2011) Neurodegener Dis , vol.8 , Issue.3 , pp. 149-152
    • Rohrer, J.D.1    Paviour, D.2    Vandrovcova, J.3    Hodges, J.4    de Silva, R.5    Rossor, M.N.6
  • 34
    • 47749146164 scopus 로고    scopus 로고
    • MAPT S305I mutation: implications for argyrophilic grain disease
    • COI: 1:CAS:528:DC%2BD1cXosVOjtb8%3D, PID: 18066559
    • Kovacs GG, Pittman A, Revesz T, Luk C, Lees A, Kiss E, Tariska P, Laszlo L et al (2008) MAPT S305I mutation: implications for argyrophilic grain disease. Acta Neuropathol 116(1):103–118. doi:10.1007/s00401-007-0322-6
    • (2008) Acta Neuropathol , vol.116 , Issue.1 , pp. 103-118
    • Kovacs, G.G.1    Pittman, A.2    Revesz, T.3    Luk, C.4    Lees, A.5    Kiss, E.6    Tariska, P.7    Laszlo, L.8
  • 36
    • 84892465251 scopus 로고    scopus 로고
    • Altered CpG methylation in sporadic Alzheimer's disease is associated with APP and MAPT dysregulation
    • COI: 1:CAS:528:DC%2BC2cXlvFensA%3D%3D, PID: 24101602
    • Iwata A, Nagata K, Hatsuta H, Takuma H, Bundo M, Iwamoto K, Tamaoka A, Murayama S et al (2014) Altered CpG methylation in sporadic Alzheimer's disease is associated with APP and MAPT dysregulation. Hum Mol Genet 23(3):648–656. doi:10.1093/hmg/ddt451
    • (2014) Hum Mol Genet , vol.23 , Issue.3 , pp. 648-656
    • Iwata, A.1    Nagata, K.2    Hatsuta, H.3    Takuma, H.4    Bundo, M.5    Iwamoto, K.6    Tamaoka, A.7    Murayama, S.8
  • 37
    • 84911391652 scopus 로고    scopus 로고
    • DNA methylation of the MAPT gene in Parkinson's disease cohorts and modulation by vitamin E in vitro
    • COI: 1:CAS:528:DC%2BC2cXhvVKmsLfE, PID: 24375821
    • Coupland KG, Mellick GD, Silburn PA, Mather K, Armstrong NJ, Sachdev PS, Brodaty H, Huang Y et al (2014) DNA methylation of the MAPT gene in Parkinson's disease cohorts and modulation by vitamin E in vitro. Mov Disord 29(13):1606–1614. doi:10.1002/mds.25784
    • (2014) Mov Disord , vol.29 , Issue.13 , pp. 1606-1614
    • Coupland, K.G.1    Mellick, G.D.2    Silburn, P.A.3    Mather, K.4    Armstrong, N.J.5    Sachdev, P.S.6    Brodaty, H.7    Huang, Y.8
  • 38
    • 84859503786 scopus 로고    scopus 로고
    • MicroRNAs in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC38Xltlagurs%3D, PID: 22285895
    • Delay C, Mandemakers W, Hebert SS (2012) MicroRNAs in Alzheimer's disease. Neurobiol Dis 46(2):285–290. doi:10.1016/j.nbd.2012.01.003
    • (2012) Neurobiol Dis , vol.46 , Issue.2 , pp. 285-290
    • Delay, C.1    Mandemakers, W.2    Hebert, S.S.3
  • 39
    • 84897398392 scopus 로고    scopus 로고
    • An epigenetic signature in peripheral blood associated with the haplotype on 17q21.31, a risk factor for neurodegenerative tauopathy
    • PID: 24603599
    • Li Y, Chen JA, Sears RL, Gao F, Klein ED, Karydas A, Geschwind MD, Rosen HJ et al (2014) An epigenetic signature in peripheral blood associated with the haplotype on 17q21.31, a risk factor for neurodegenerative tauopathy. PLoS Genet 10(3), e1004211. doi:10.1371/journal.pgen.1004211
    • (2014) PLoS Genet , vol.10 , Issue.3
    • Li, Y.1    Chen, J.A.2    Sears, R.L.3    Gao, F.4    Klein, E.D.5    Karydas, A.6    Geschwind, M.D.7    Rosen, H.J.8
  • 40
    • 84871609151 scopus 로고    scopus 로고
    • MicroRNAs and neurodegeneration: role and impact
    • COI: 1:CAS:528:DC%2BC3sXhsVGmtg%3D%3D, PID: 23026030
    • Abe M, Bonini NM (2013) MicroRNAs and neurodegeneration: role and impact. Trends Cell Biol 23(1):30–36. doi:10.1016/j.tcb.2012.08.013
    • (2013) Trends Cell Biol , vol.23 , Issue.1 , pp. 30-36
    • Abe, M.1    Bonini, N.M.2
  • 41
    • 84939893709 scopus 로고    scopus 로고
    • Causes and Consequences of MicroRNA Dysregulation in Neurodegenerative Diseases. Molecular neurobiology
    • Tan L, Yu JT, Tan L (2014) Causes and Consequences of MicroRNA Dysregulation in Neurodegenerative Diseases. Molecular neurobiology. doi:10.1007/s12035-014-8803-9.
    • (2014) doi:10.1007/s12035-014-8803-9
    • Tan, L.1    Yu, J.T.2    Tan, L.3
  • 42
    • 84922195168 scopus 로고    scopus 로고
    • Dysregulation of microRNA-219 promotes neurodegeneration through post-transcriptional regulation of tau
    • PID: 25574843
    • Santa-Maria I, Alaniz ME, Renwick N, Cela C, Fulga TA, Van Vactor D, Tuschl T, Clark LN et al (2015) Dysregulation of microRNA-219 promotes neurodegeneration through post-transcriptional regulation of tau. J Clin Invest 125(2):681–686. doi:10.1172/JCI78421
    • (2015) J Clin Invest , vol.125 , Issue.2 , pp. 681-686
    • Santa-Maria, I.1    Alaniz, M.E.2    Renwick, N.3    Cela, C.4    Fulga, T.A.5    Van Vactor, D.6    Tuschl, T.7    Clark, L.N.8
  • 43
    • 67349142329 scopus 로고    scopus 로고
    • Mechanisms of tau-induced neurodegeneration
    • COI: 1:CAS:528:DC%2BD1MXmt1ahu7k%3D, PID: 19184068
    • Iqbal K, Liu F, Gong CX, Alonso Adel C, Grundke-Iqbal I (2009) Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 118(1):53–69. doi:10.1007/s00401-009-0486-3
    • (2009) Acta Neuropathol , vol.118 , Issue.1 , pp. 53-69
    • Iqbal, K.1    Liu, F.2    Gong, C.X.3    Alonso Adel, C.4    Grundke-Iqbal, I.5
  • 45
    • 84936994657 scopus 로고    scopus 로고
    • Axonal transport defects in Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC2cXht1Sjs77M, PID: 25052480
    • Wang ZX, Tan L, Yu JT (2015) Axonal transport defects in Alzheimer's disease. Mol Neurobiol 51(3):1309–1321. doi:10.1007/s12035-014-8810-x
    • (2015) Mol Neurobiol , vol.51 , Issue.3 , pp. 1309-1321
    • Wang, Z.X.1    Tan, L.2    Yu, J.T.3
  • 46
    • 84947713425 scopus 로고    scopus 로고
    • Early maturation and distinct tau pathology in induced pluripotent stem cell-derived neurons from patients with MAPT mutations. Brain: a journal of neurology
    • Iovino M, Agathou S, Gonzalez-Rueda A, Del Castillo Velasco-Herrera M, Borroni B, Alberici A, Lynch T, O'Dowd S, et al. (2015) Early maturation and distinct tau pathology in induced pluripotent stem cell-derived neurons from patients with MAPT mutations. Brain: a journal of neurology. doi: 10.1093/brain/awv222
    • (2015) doi: 10.1093/brain/awv222
    • Iovino, M.1    Agathou, S.2    Gonzalez-Rueda, A.3
  • 47
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • COI: 1:CAS:528:DC%2BC3sXis1aht78%3D, PID: 23412472
    • Pooler AM, Phillips EC, Lau DH, Noble W, Hanger DP (2013) Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep 14(4):389–394. doi:10.1038/embor.2013.15
    • (2013) EMBO Rep , vol.14 , Issue.4 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.3    Noble, W.4    Hanger, D.P.5
  • 48
    • 79958110883 scopus 로고    scopus 로고
    • Alzheimer's pathogenesis: is there neuron-to-neuron propagation?
    • COI: 1:CAS:528:DC%2BC3MXlsVKqtLs%3D, PID: 21516512
    • Braak H, Del Tredici K (2011) Alzheimer's pathogenesis: is there neuron-to-neuron propagation? Acta Neuropathol 121(5):589–595. doi:10.1007/s00401-011-0825-z
    • (2011) Acta Neuropathol , vol.121 , Issue.5 , pp. 589-595
    • Braak, H.1    Del Tredici, K.2
  • 49
    • 84876250854 scopus 로고    scopus 로고
    • "Prion-like" templated misfolding in tauopathies
    • COI: 1:CAS:528:DC%2BC3sXptVajurk%3D, PID: 23587140
    • Clavaguera F, Lavenir I, Falcon B, Frank S, Goedert M, Tolnay M (2013) "Prion-like" templated misfolding in tauopathies. Brain Pathol 23(3):342–349. doi:10.1111/bpa.12044
    • (2013) Brain Pathol , vol.23 , Issue.3 , pp. 342-349
    • Clavaguera, F.1    Lavenir, I.2    Falcon, B.3    Frank, S.4    Goedert, M.5    Tolnay, M.6
  • 50
    • 84918565681 scopus 로고    scopus 로고
    • Prion-like mechanisms in the pathogenesis of tauopathies and synucleinopathies
    • PID: 25218483
    • Goedert M, Falcon B, Clavaguera F, Tolnay M (2014) Prion-like mechanisms in the pathogenesis of tauopathies and synucleinopathies. Curr Neurol Neurosci Rep 14(11):495. doi:10.1007/s11910-014-0495-z
    • (2014) Curr Neurol Neurosci Rep , vol.14 , Issue.11 , pp. 495
    • Goedert, M.1    Falcon, B.2    Clavaguera, F.3    Tolnay, M.4
  • 51
    • 84879232559 scopus 로고    scopus 로고
    • Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission
    • PID: 23773063
    • Mohamed NV, Herrou T, Plouffe V, Piperno N, Leclerc N (2013) Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission. Eur J Neurosci 37(12):1939–1948. doi:10.1111/ejn.12229
    • (2013) Eur J Neurosci , vol.37 , Issue.12 , pp. 1939-1948
    • Mohamed, N.V.1    Herrou, T.2    Plouffe, V.3    Piperno, N.4    Leclerc, N.5
  • 53
    • 41149111293 scopus 로고    scopus 로고
    • Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells
    • COI: 1:CAS:528:DC%2BD1cXktlGgsrk%3D, PID: 18272392
    • Gomez-Ramos A, Diaz-Hernandez M, Rubio A, Miras-Portugal MT, Avila J (2008) Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells. Mol Cell Neurosci 37(4):673–681. doi:10.1016/j.mcn.2007.12.010
    • (2008) Mol Cell Neurosci , vol.37 , Issue.4 , pp. 673-681
    • Gomez-Ramos, A.1    Diaz-Hernandez, M.2    Rubio, A.3    Miras-Portugal, M.T.4    Avila, J.5
  • 54
    • 77953499350 scopus 로고    scopus 로고
    • The revitalized tau hypothesis on Alzheimer's disease
    • COI: 1:CAS:528:DC%2BC3cXntVemt7o%3D, PID: 20682182
    • Maccioni RB, Farias G, Morales I, Navarrete L (2010) The revitalized tau hypothesis on Alzheimer's disease. Arch Med Res 41(3):226–231. doi:10.1016/j.arcmed.2010.03.007
    • (2010) Arch Med Res , vol.41 , Issue.3 , pp. 226-231
    • Maccioni, R.B.1    Farias, G.2    Morales, I.3    Navarrete, L.4
  • 55
    • 84907279965 scopus 로고    scopus 로고
    • Microglia in Alzheimer's disease
    • PID: 25197646
    • Li Y, Tan MS, Jiang T, Tan L (2014) Microglia in Alzheimer's disease. BioMed Res Int 2014:437483. doi:10.1155/2014/437483
    • (2014) BioMed Res Int , vol.2014 , pp. 437483
    • Li, Y.1    Tan, M.S.2    Jiang, T.3    Tan, L.4
  • 56
    • 80053289984 scopus 로고    scopus 로고
    • Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain
    • COI: 1:CAS:528:DC%2BC3MXhsVSqtbnI, PID: 21854751
    • Kopeikina KJ, Carlson GA, Pitstick R, Ludvigson AE, Peters A, Luebke JI, Koffie RM, Frosch MP et al (2011) Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain. Am J Pathol 179(4):2071–2082. doi:10.1016/j.ajpath.2011.07.004
    • (2011) Am J Pathol , vol.179 , Issue.4 , pp. 2071-2082
    • Kopeikina, K.J.1    Carlson, G.A.2    Pitstick, R.3    Ludvigson, A.E.4    Peters, A.5    Luebke, J.I.6    Koffie, R.M.7    Frosch, M.P.8
  • 57
    • 84861130196 scopus 로고    scopus 로고
    • Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage
    • COI: 1:CAS:528:DC%2BC38XmvVyns7g%3D, PID: 22367970
    • Manczak M, Reddy PH (2012) Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage. Hum Mol Genet 21(11):2538–2547. doi:10.1093/hmg/dds072
    • (2012) Hum Mol Genet , vol.21 , Issue.11 , pp. 2538-2547
    • Manczak, M.1    Reddy, P.H.2
  • 58
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • COI: 1:CAS:528:DC%2BC38Xht1KjtbnI, PID: 22920254
    • DuBoff B, Gotz J, Feany MB (2012) Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron 75(4):618–632. doi:10.1016/j.neuron.2012.06.026
    • (2012) Neuron , vol.75 , Issue.4 , pp. 618-632
    • DuBoff, B.1    Gotz, J.2    Feany, M.B.3
  • 59
    • 84855761078 scopus 로고    scopus 로고
    • Truncated tau and Abeta cooperatively impair mitochondria in primary neurons
    • Quintanilla RA, Dolan PJ, Jin YN, Johnson GV (2012) Truncated tau and Abeta cooperatively impair mitochondria in primary neurons. Neurobiology of aging 33 (3):619 e625-635. doi:10.1016/j.neurobiolaging.2011.02.007
    • (2012) Neurobiology of aging 33 (3) , vol.619 , pp. e625-e635
    • Quintanilla, R.A.1    Dolan, P.J.2    Jin, Y.N.3    Johnson, G.V.4
  • 63
    • 84961152790 scopus 로고    scopus 로고
    • The Essential Role of Soluble Abeta Oligomers in Alzheimer's Disease, Molecular neurobiology
    • Wang ZX, Tan L, Liu J, Yu JT (2015) The Essential Role of Soluble Abeta Oligomers in Alzheimer's Disease. Molecular neurobiology. doi:10.1007/s12035-015-9143-0
    • (2015) Yu JT
    • Wang, Z.X.1    Tan, L.2    Liu, J.3
  • 64
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • COI: 1:CAS:528:DC%2BC3cXpvFKrtr4%3D, PID: 20655099
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, van Eersel J, Wolfing H, Chieng BC et al (2010) Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell 142(3):387–397. doi:10.1016/j.cell.2010.06.036
    • (2010) Cell , vol.142 , Issue.3 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    van Eersel, J.6    Wolfing, H.7    Chieng, B.C.8
  • 65
    • 1842731881 scopus 로고    scopus 로고
    • Src kinases: a hub for NMDA receptor regulation
    • COI: 1:CAS:528:DC%2BD2cXit12nu7k%3D, PID: 15034556
    • Salter MW, Kalia LV (2004) Src kinases: a hub for NMDA receptor regulation. Nat Rev Neurosci 5(4):317–328. doi:10.1038/nrn1368
    • (2004) Nat Rev Neurosci , vol.5 , Issue.4 , pp. 317-328
    • Salter, M.W.1    Kalia, L.V.2
  • 66
    • 27444437758 scopus 로고    scopus 로고
    • Disease-related modifications in tau affect the interaction between Fyn and Tau
    • COI: 1:CAS:528:DC%2BD2MXhtFWmtbrK, PID: 16115884
    • Bhaskar K, Yen SH, Lee G (2005) Disease-related modifications in tau affect the interaction between Fyn and Tau. J Biol Chem 280(42):35119–35125. doi:10.1074/jbc.M505895200
    • (2005) J Biol Chem , vol.280 , Issue.42 , pp. 35119-35125
    • Bhaskar, K.1    Yen, S.H.2    Lee, G.3
  • 67
    • 84908210642 scopus 로고    scopus 로고
    • Phosphorylated tau potentiates Abeta-induced mitochondrial damage in mature neurons
    • COI: 1:CAS:528:DC%2BC2cXhsVSqsbnP, PID: 25134729
    • Quintanilla RA, von Bernhardi R, Godoy JA, Inestrosa NC, Johnson GV (2014) Phosphorylated tau potentiates Abeta-induced mitochondrial damage in mature neurons. Neurobiol Dis 71:260–269. doi:10.1016/j.nbd.2014.08.016
    • (2014) Neurobiol Dis , vol.71 , pp. 260-269
    • Quintanilla, R.A.1    von Bernhardi, R.2    Godoy, J.A.3    Inestrosa, N.C.4    Johnson, G.V.5
  • 68
    • 84920989472 scopus 로고    scopus 로고
    • Abeta(1–42) induces abnormal alternative splicing of tau exons 2/3 in NGF-induced PC12 cells
    • PID: 25590729
    • Lagunes T, Herrera-Rivero M, Hernandez-Aguilar ME, Aranda-Abreu GE (2014) Abeta(1–42) induces abnormal alternative splicing of tau exons 2/3 in NGF-induced PC12 cells. An Acad Bras Cienc 86(4):1927–1934. doi:10.1590/0001-3765201420130333
    • (2014) An Acad Bras Cienc , vol.86 , Issue.4 , pp. 1927-1934
    • Lagunes, T.1    Herrera-Rivero, M.2    Hernandez-Aguilar, M.E.3    Aranda-Abreu, G.E.4
  • 71
    • 84879958098 scopus 로고    scopus 로고
    • Antisense oligonucleotides: treating neurodegeneration at the level of RNA
    • COI: 1:CAS:528:DC%2BC3sXhtVyqsr%2FK, PID: 23686823
    • DeVos SL, Miller TM (2013) Antisense oligonucleotides: treating neurodegeneration at the level of RNA. Neurotherapeutics 10(3):486–497. doi:10.1007/s13311-013-0194-5
    • (2013) Neurotherapeutics , vol.10 , Issue.3 , pp. 486-497
    • DeVos, S.L.1    Miller, T.M.2
  • 72
    • 84905270419 scopus 로고    scopus 로고
    • Antisense-mediated exon skipping decreases Tau protein expression: a potential therapy for Tauopathies
    • COI: 1:CAS:528:DC%2BC2cXhsFagurrF, PID: 25072694
    • Sud R, Geller ET, Schellenberg GD (2014) Antisense-mediated exon skipping decreases Tau protein expression: a potential therapy for Tauopathies. Molecular Therapy Nucleic Acids 3, e180. doi:10.1038/mtna.2014.30
    • (2014) Molecular Therapy Nucleic Acids , vol.3
    • Sud, R.1    Geller, E.T.2    Schellenberg, G.D.3
  • 73
    • 84910031803 scopus 로고    scopus 로고
    • Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BC2MXkt12qs7o%3D, PID: 25292434
    • Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP (2015) Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases. Annu Rev Pharmacol Toxicol 55:353–371. doi:10.1146/annurev-pharmtox-010814-124332
    • (2015) Annu Rev Pharmacol Toxicol , vol.55 , pp. 353-371
    • Pratt, W.B.1    Gestwicki, J.E.2    Osawa, Y.3    Lieberman, A.P.4
  • 74
    • 67849111948 scopus 로고    scopus 로고
    • Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein
    • COI: 1:CAS:528:DC%2BD1MXmvVOiurk%3D, PID: 19363271
    • Tortosa E, Santa-Maria I, Moreno F, Lim F, Perez M, Avila J (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J Alzheimers Dis 17(2):319–325. doi:10.3233/JAD-2009-1049
    • (2009) J Alzheimers Dis , vol.17 , Issue.2 , pp. 319-325
    • Tortosa, E.1    Santa-Maria, I.2    Moreno, F.3    Lim, F.4    Perez, M.5    Avila, J.6
  • 75
    • 84862281225 scopus 로고    scopus 로고
    • Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
    • COI: 1:CAS:528:DC%2BC38Xht1art73N, PID: 22361619
    • Congdon EE, Wu JW, Myeku N, Figueroa YH, Herman M, Marinec PS, Gestwicki JE, Dickey CA et al (2012) Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo. Autophagy 8(4):609–622. doi:10.4161/auto.19048
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 609-622
    • Congdon, E.E.1    Wu, J.W.2    Myeku, N.3    Figueroa, Y.H.4    Herman, M.5    Marinec, P.S.6    Gestwicki, J.E.7    Dickey, C.A.8
  • 76
    • 84858153335 scopus 로고    scopus 로고
    • Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: implications of autophagy promotion
    • COI: 1:CAS:528:DC%2BC38Xjs1OntL4%3D, PID: 22249108
    • Shimada K, Motoi Y, Ishiguro K, Kambe T, Matsumoto SE, Itaya M, Kunichika M, Mori H et al (2012) Long-term oral lithium treatment attenuates motor disturbance in tauopathy model mice: implications of autophagy promotion. Neurobiol Dis 46(1):101–108. doi:10.1016/j.nbd.2011.12.050
    • (2012) Neurobiol Dis , vol.46 , Issue.1 , pp. 101-108
    • Shimada, K.1    Motoi, Y.2    Ishiguro, K.3    Kambe, T.4    Matsumoto, S.E.5    Itaya, M.6    Kunichika, M.7    Mori, H.8
  • 77
    • 33845530335 scopus 로고    scopus 로고
    • 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
    • COI: 1:CAS:528:DC%2BD2sXjsFGkug%3D%3D, PID: 17059563
    • Engel T, Goni-Oliver P, Lucas JJ, Avila J, Hernandez F (2006) 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 99(6):1445–1455. doi:10.1111/j.1471-4159.2006.04139.x
    • (2006) J Neurochem , vol.99 , Issue.6 , pp. 1445-1455
    • Engel, T.1    Goni-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernandez, F.5
  • 78
    • 67649206084 scopus 로고    scopus 로고
    • Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study
    • COI: 1:CAS:528:DC%2BD1MXhsFentbbL, PID: 19573486
    • Hampel H, Ewers M, Burger K, Annas P, Mortberg A, Bogstedt A, Frolich L, Schroder J et al (2009) Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. J Clin Psychiatry 70(6):922–931
    • (2009) J Clin Psychiatry , vol.70 , Issue.6 , pp. 922-931
    • Hampel, H.1    Ewers, M.2    Burger, K.3    Annas, P.4    Mortberg, A.5    Bogstedt, A.6    Frolich, L.7    Schroder, J.8
  • 79
    • 68149150844 scopus 로고    scopus 로고
    • A novel GSK-3beta inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo
    • COI: 1:CAS:528:DC%2BD1MXpsFylsrY%3D, PID: 19523516
    • Sereno L, Coma M, Rodriguez M, Sanchez-Ferrer P, Sanchez MB, Gich I, Agullo JM, Perez M et al (2009) A novel GSK-3beta inhibitor reduces Alzheimer's pathology and rescues neuronal loss in vivo. Neurobiol Dis 35(3):359–367. doi:10.1016/j.nbd.2009.05.025
    • (2009) Neurobiol Dis , vol.35 , Issue.3 , pp. 359-367
    • Sereno, L.1    Coma, M.2    Rodriguez, M.3    Sanchez-Ferrer, P.4    Sanchez, M.B.5    Gich, I.6    Agullo, J.M.7    Perez, M.8
  • 81
    • 84898056918 scopus 로고    scopus 로고
    • A phase 2 trial of the GSK-3 inhibitor tideglusib in progressive supranuclear palsy
    • COI: 1:CAS:528:DC%2BC2cXlvFSmtL8%3D, PID: 24532007
    • Tolosa E, Litvan I, Hoglinger GU, Burn D, Lees A, Andres MV, Gomez-Carrillo B, Leon T et al (2014) A phase 2 trial of the GSK-3 inhibitor tideglusib in progressive supranuclear palsy. Mov Disord 29(4):470–478. doi:10.1002/mds.25824
    • (2014) Mov Disord , vol.29 , Issue.4 , pp. 470-478
    • Tolosa, E.1    Litvan, I.2    Hoglinger, G.U.3    Burn, D.4    Lees, A.5    Andres, M.V.6    Gomez-Carrillo, B.7    Leon, T.8
  • 82
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • COI: 1:CAS:528:DC%2BD3cXjsVGq, PID: 10604467
    • Patrick GN, Zukerberg L, Nikolic M, de la Monte S, Dikkes P, Tsai LH (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402(6762):615–622. doi:10.1038/45159
    • (1999) Nature , vol.402 , Issue.6762 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    de la Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 83
    • 77958608578 scopus 로고    scopus 로고
    • Silencing of CDK5 reduces neurofibrillary tangles in transgenic alzheimer's mice
    • COI: 1:CAS:528:DC%2BC3cXhtlyqtLrE, PID: 20962218
    • Piedrahita D, Hernandez I, Lopez-Tobon A, Fedorov D, Obara B, Manjunath BS, Boudreau RL, Davidson B et al (2010) Silencing of CDK5 reduces neurofibrillary tangles in transgenic alzheimer's mice. J Neurosci 30(42):13966–13976. doi:10.1523/JNEUROSCI.3637-10.2010
    • (2010) J Neurosci , vol.30 , Issue.42 , pp. 13966-13976
    • Piedrahita, D.1    Hernandez, I.2    Lopez-Tobon, A.3    Fedorov, D.4    Obara, B.5    Manjunath, B.S.6    Boudreau, R.L.7    Davidson, B.8
  • 84
    • 84883192412 scopus 로고    scopus 로고
    • Troglitazone, a thiazolidinedione, decreases tau phosphorylation through the inhibition of cyclin-dependent kinase 5 activity in SH-SY5Y neuroblastoma cells and primary neurons
    • COI: 1:CAS:528:DC%2BC3sXhtlSqu77E, PID: 23581463
    • Cho DH, Lee EJ, Kwon KJ, Shin CY, Song KH, Park JH, Jo I, Han SH (2013) Troglitazone, a thiazolidinedione, decreases tau phosphorylation through the inhibition of cyclin-dependent kinase 5 activity in SH-SY5Y neuroblastoma cells and primary neurons. J Neurochem 126(5):685–695. doi:10.1111/jnc.12264
    • (2013) J Neurochem , vol.126 , Issue.5 , pp. 685-695
    • Cho, D.H.1    Lee, E.J.2    Kwon, K.J.3    Shin, C.Y.4    Song, K.H.5    Park, J.H.6    Jo, I.7    Han, S.H.8
  • 85
    • 84875271571 scopus 로고    scopus 로고
    • 5-Lipoxygenase pharmacological blockade decreases tau phosphorylation in vivo: involvement of the cyclin-dependent kinase-5
    • COI: 1:CAS:528:DC%2BC3sXhsVyjsro%3D, PID: 23332172
    • Chu J, Pratico D (2013) 5-Lipoxygenase pharmacological blockade decreases tau phosphorylation in vivo: involvement of the cyclin-dependent kinase-5. Neurobiol Aging 34(6):1549–1554. doi:10.1016/j.neurobiolaging.2012.12.009
    • (2013) Neurobiol Aging , vol.34 , Issue.6 , pp. 1549-1554
    • Chu, J.1    Pratico, D.2
  • 86
    • 84871744906 scopus 로고    scopus 로고
    • Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo
    • COI: 1:CAS:528:DC%2BC3sXnsFyhtQ%3D%3D, PID: 23283346
    • Sundaram JR, Poore CP, Sulaimee NH, Pareek T, Asad AB, Rajkumar R, Cheong WF, Wenk MR et al (2013) Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo. J Neurosci 33(1):334–343. doi:10.1523/JNEUROSCI.3593-12.2013
    • (2013) J Neurosci , vol.33 , Issue.1 , pp. 334-343
    • Sundaram, J.R.1    Poore, C.P.2    Sulaimee, N.H.3    Pareek, T.4    Asad, A.B.5    Rajkumar, R.6    Cheong, W.F.7    Wenk, M.R.8
  • 87
    • 84903975926 scopus 로고    scopus 로고
    • Specific calpain inhibition by calpastatin prevents tauopathy and neurodegeneration and restores normal lifespan in tau P301L mice
    • PID: 25009256
    • Rao MV, McBrayer MK, Campbell J, Kumar A, Hashim A, Sershen H, Stavrides PH, Ohno M et al (2014) Specific calpain inhibition by calpastatin prevents tauopathy and neurodegeneration and restores normal lifespan in tau P301L mice. J Neurosci 34(28):9222–9234. doi:10.1523/jneurosci.1132-14.2014
    • (2014) J Neurosci , vol.34 , Issue.28 , pp. 9222-9234
    • Rao, M.V.1    McBrayer, M.K.2    Campbell, J.3    Kumar, A.4    Hashim, A.5    Sershen, H.6    Stavrides, P.H.7    Ohno, M.8
  • 88
    • 0034331296 scopus 로고    scopus 로고
    • Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo
    • COI: 1:CAS:528:DC%2BD3cXovFaiurw%3D, PID: 11060018
    • Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR (2000) Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J 19(21):5672–5681. doi:10.1093/emboj/19.21.5672
    • (2000) EMBO J , vol.19 , Issue.21 , pp. 5672-5681
    • Wu, J.1    Tolstykh, T.2    Lee, J.3    Boyd, K.4    Stock, J.B.5    Broach, J.R.6
  • 89
    • 84925487085 scopus 로고    scopus 로고
    • Folic acid inhibits tau phosphorylation through regulation of PP2A methylation in SH-SY5Y cells
    • COI: 1:CAS:528:DC%2BC2cXhslOjsb7P, PID: 25651436
    • Li W, Jiang M, Xiao Y, Zhang X, Cui S, Huang G (2015) Folic acid inhibits tau phosphorylation through regulation of PP2A methylation in SH-SY5Y cells. J Nutr Health Aging 19(2):123–129. doi:10.1007/s12603-014-0514-4
    • (2015) J Nutr Health Aging , vol.19 , Issue.2 , pp. 123-129
    • Li, W.1    Jiang, M.2    Xiao, Y.3    Zhang, X.4    Cui, S.5    Huang, G.6
  • 91
    • 33745370049 scopus 로고    scopus 로고
    • Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine
    • COI: 1:CAS:528:DC%2BD28Xms1agsr0%3D, PID: 16806196
    • Chohan MO, Khatoon S, Iqbal IG, Iqbal K (2006) Involvement of I2PP2A in the abnormal hyperphosphorylation of tau and its reversal by Memantine. FEBS Lett 580(16):3973–3979. doi:10.1016/j.febslet.2006.06.021
    • (2006) FEBS Lett , vol.580 , Issue.16 , pp. 3973-3979
    • Chohan, M.O.1    Khatoon, S.2    Iqbal, I.G.3    Iqbal, K.4
  • 92
    • 76149120867 scopus 로고    scopus 로고
    • Memantine improves cognition and reduces Alzheimer's-like neuropathology in transgenic mice
    • COI: 1:CAS:528:DC%2BC3cXitFCmsbo%3D, PID: 20042680
    • Martinez-Coria H, Green KN, Billings LM, Kitazawa M, Albrecht M, Rammes G, Parsons CG, Gupta S et al (2010) Memantine improves cognition and reduces Alzheimer's-like neuropathology in transgenic mice. Am J Pathol 176(2):870–880. doi:10.2353/ajpath.2010.090452
    • (2010) Am J Pathol , vol.176 , Issue.2 , pp. 870-880
    • Martinez-Coria, H.1    Green, K.N.2    Billings, L.M.3    Kitazawa, M.4    Albrecht, M.5    Rammes, G.6    Parsons, C.G.7    Gupta, S.8
  • 94
    • 77956385203 scopus 로고    scopus 로고
    • Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models
    • PID: 20643941
    • van Eersel J, Ke YD, Liu X, Delerue F, Kril JJ, Gotz J, Ittner LM (2010) Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models. Proc Natl Acad Sci U S A 107(31):13888–13893. doi:10.1073/pnas.1009038107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.31 , pp. 13888-13893
    • van Eersel, J.1    Ke, Y.D.2    Liu, X.3    Delerue, F.4    Kril, J.J.5    Gotz, J.6    Ittner, L.M.7
  • 95
    • 84878870806 scopus 로고    scopus 로고
    • Nmnat2 attenuates Tau phosphorylation through activation of PP2A
    • COI: 1:CAS:528:DC%2BC3sXptFelu7o%3D, PID: 23579329
    • Cheng XS, Zhao KP, Jiang X, Du LL, Li XH, Ma ZW, Yao J, Luo Y et al (2013) Nmnat2 attenuates Tau phosphorylation through activation of PP2A. J Alzheimers Dis 36(1):185–195. doi:10.3233/JAD-122173
    • (2013) J Alzheimers Dis , vol.36 , Issue.1 , pp. 185-195
    • Cheng, X.S.1    Zhao, K.P.2    Jiang, X.3    Du, L.L.4    Li, X.H.5    Ma, Z.W.6    Yao, J.7    Luo, Y.8
  • 97
    • 14844303721 scopus 로고    scopus 로고
    • Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins
    • COI: 1:CAS:528:DC%2BD2MXhs1yisL8%3D, PID: 15611092
    • Taniguchi S, Suzuki N, Masuda M, Hisanaga S, Iwatsubo T, Goedert M, Hasegawa M (2005) Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J Biol Chem 280(9):7614–7623. doi:10.1074/jbc.M408714200
    • (2005) J Biol Chem , vol.280 , Issue.9 , pp. 7614-7623
    • Taniguchi, S.1    Suzuki, N.2    Masuda, M.3    Hisanaga, S.4    Iwatsubo, T.5    Goedert, M.6    Hasegawa, M.7
  • 98
    • 79953707326 scopus 로고    scopus 로고
    • Oleuropein and derivatives from olives as Tau aggregation inhibitors
    • COI: 1:CAS:528:DC%2BC3MXksFGmtLw%3D, PID: 21333710
    • Daccache A, Lion C, Sibille N, Gerard M, Slomianny C, Lippens G, Cotelle P (2011) Oleuropein and derivatives from olives as Tau aggregation inhibitors. Neurochem Int 58(6):700–707. doi:10.1016/j.neuint.2011.02.010
    • (2011) Neurochem Int , vol.58 , Issue.6 , pp. 700-707
    • Daccache, A.1    Lion, C.2    Sibille, N.3    Gerard, M.4    Slomianny, C.5    Lippens, G.6    Cotelle, P.7
  • 99
    • 0029742937 scopus 로고    scopus 로고
    • Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines
    • COI: 1:CAS:528:DyaK28XmtVOqsLg%3D, PID: 8855335
    • Wischik CM, Edwards PC, Lai RY, Roth M, Harrington CR (1996) Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines. Proc Natl Acad Sci U S A 93(20):11213–11218
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.20 , pp. 11213-11218
    • Wischik, C.M.1    Edwards, P.C.2    Lai, R.Y.3    Roth, M.4    Harrington, C.R.5
  • 100
    • 77954954324 scopus 로고    scopus 로고
    • Methylene blue fails to inhibit Tau and polyglutamine protein dependent toxicity in zebrafish
    • PID: 20381619
    • van Bebber F, Paquet D, Hruscha A, Schmid B, Haass C (2010) Methylene blue fails to inhibit Tau and polyglutamine protein dependent toxicity in zebrafish. Neurobiol Dis 39(3):265–271. doi:10.1016/j.nbd.2010.03.023
    • (2010) Neurobiol Dis , vol.39 , Issue.3 , pp. 265-271
    • van Bebber, F.1    Paquet, D.2    Hruscha, A.3    Schmid, B.4    Haass, C.5
  • 101
    • 84893473873 scopus 로고    scopus 로고
    • Methylene blue does not reverse existing neurofibrillary tangle pathology in the rTg4510 mouse model of tauopathy
    • COI: 1:CAS:528:DC%2BC2cXislOhtbk%3D, PID: 24462887
    • Spires-Jones TL, Friedman T, Pitstick R, Polydoro M, Roe A, Carlson GA, Hyman BT (2014) Methylene blue does not reverse existing neurofibrillary tangle pathology in the rTg4510 mouse model of tauopathy. Neurosci Lett 562:63–68. doi:10.1016/j.neulet.2014.01.013
    • (2014) Neurosci Lett , vol.562 , pp. 63-68
    • Spires-Jones, T.L.1    Friedman, T.2    Pitstick, R.3    Polydoro, M.4    Roe, A.5    Carlson, G.A.6    Hyman, B.T.7
  • 102
    • 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
    • COI: 1:STN:280:DC%2BD1M3it1WgtQ%3D%3D, PID: 19300883
    • Wischik C, Staff R (2009) 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 13(4):367–369
    • (2009) J Nutr Health Aging , vol.13 , Issue.4 , pp. 367-369
    • Wischik, C.1    Staff, R.2
  • 103
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice
    • COI: 1:CAS:528:DC%2BC3MXhs1Oqur7K, PID: 22174735
    • Bi M, Ittner A, Ke YD, Gotz J, Ittner LM (2011) Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice. PLoS One 6(12), e26860. doi:10.1371/journal.pone.0026860
    • (2011) PLoS One , vol.6 , Issue.12
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 104
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression
    • COI: 1:CAS:528:DC%2BC3MXht1ajtbrJ, PID: 21841002
    • Chai X, Wu S, Murray TK, Kinley R, Cella CV, Sims H, Buckner N, Hanmer J et al (2011) Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. J Biol Chem 286(39):34457–34467. doi:10.1074/jbc.M111.229633
    • (2011) J Biol Chem , vol.286 , Issue.39 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3    Kinley, R.4    Cella, C.V.5    Sims, H.6    Buckner, N.7    Hanmer, J.8
  • 106
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • COI: 1:CAS:528:DC%2BD2sXhtVSnsLbN, PID: 17715348
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM (2007) Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci 27(34):9115–9129. doi:10.1523/JNEUROSCI.2361-07.2007
    • (2007) J Neurosci , vol.27 , Issue.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 107
    • 79960563632 scopus 로고    scopus 로고
    • Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain
    • COI: 1:CAS:528:DC%2BC3MXhtVSit7bM, PID: 21644996
    • Boutajangout A, Ingadottir J, Davies P, Sigurdsson EM (2011) Passive immunization targeting pathological phospho-tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain. J Neurochem 118(4):658–667. doi:10.1111/j.1471-4159.2011.07337.x
    • (2011) J Neurochem , vol.118 , Issue.4 , pp. 658-667
    • Boutajangout, A.1    Ingadottir, J.2    Davies, P.3    Sigurdsson, E.M.4
  • 108
    • 78650065372 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model
    • COI: 1:CAS:528:DC%2BC3cXhsF2nurjI, PID: 21147995
    • Boutajangout A, Quartermain D, Sigurdsson EM (2010) Immunotherapy targeting pathological tau prevents cognitive decline in a new tangle mouse model. J Neurosci 30(49):16559–16566. doi:10.1523/JNEUROSCI.4363-10.2010
    • (2010) J Neurosci , vol.30 , Issue.49 , pp. 16559-16566
    • Boutajangout, A.1    Quartermain, D.2    Sigurdsson, E.M.3
  • 109
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • COI: 1:CAS:528:DC%2BC3cXovFCgt7s%3D, PID: 20546729
    • Boimel M, Grigoriadis N, Lourbopoulos A, Haber E, Abramsky O, Rosenmann H (2010) Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp Neurol 224(2):472–485. doi:10.1016/j.expneurol.2010.05.010
    • (2010) Exp Neurol , vol.224 , Issue.2 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5    Rosenmann, H.6
  • 110
    • 84887837879 scopus 로고    scopus 로고
    • Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathology
    • COI: 1:CAS:528:DC%2BC3sXhslyrt7fF, PID: 24089520
    • Gu J, Congdon EE, Sigurdsson EM (2013) Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathology. J Biol Chem 288(46):33081–33095. doi:10.1074/jbc.M113.494922
    • (2013) J Biol Chem , vol.288 , Issue.46 , pp. 33081-33095
    • Gu, J.1    Congdon, E.E.2    Sigurdsson, E.M.3
  • 111
    • 84865607168 scopus 로고    scopus 로고
    • Mechanistic studies of antibody-mediated clearance of Tau Aggregates using an ex vivo brain slice model
    • COI: 1:CAS:528:DC%2BC38XjvFWktw%3D%3D
    • Krishnamurthy PK, Deng Y, Sigurdsson EM (2011) Mechanistic studies of antibody-mediated clearance of Tau Aggregates using an ex vivo brain slice model. Frontiers Psychiatry 2:59. doi:10.3389/fpsyt.2011.00059
    • (2011) Frontiers Psychiatry , vol.2 , pp. 59
    • Krishnamurthy, P.K.1    Deng, Y.2    Sigurdsson, E.M.3
  • 112
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • COI: 1:CAS:528:DC%2BD2sXitVektbk%3D, PID: 17270732
    • Yoshiyama Y, Higuchi M, Zhang B, Huang SM, Iwata N, Saido TC, Maeda J, Suhara T et al (2007) Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 53(3):337–351. doi:10.1016/j.neuron.2007.01.010
    • (2007) Neuron , vol.53 , Issue.3 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3    Huang, S.M.4    Iwata, N.5    Saido, T.C.6    Maeda, J.7    Suhara, T.8
  • 113
    • 13144279282 scopus 로고    scopus 로고
    • Role for neuronally derived fractalkine in mediating interactions between neurons and CX3CR1-expressing microglia
    • COI: 1:CAS:528:DyaK1cXlvFWgt7c%3D, PID: 9724801
    • Harrison JK, Jiang Y, Chen S, Xia Y, Maciejewski D, McNamara RK, Streit WJ, Salafranca MN et al (1998) Role for neuronally derived fractalkine in mediating interactions between neurons and CX3CR1-expressing microglia. Proc Natl Acad Sci U S A 95(18):10896–10901
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.18 , pp. 10896-10901
    • Harrison, J.K.1    Jiang, Y.2    Chen, S.3    Xia, Y.4    Maciejewski, D.5    McNamara, R.K.6    Streit, W.J.7    Salafranca, M.N.8
  • 114
    • 84875247375 scopus 로고    scopus 로고
    • Fractalkine overexpression suppresses tau pathology in a mouse model of tauopathy
    • COI: 1:CAS:528:DC%2BC3sXhsV2jtLg%3D, PID: 23332170
    • Nash KR, Lee DC, Hunt JB Jr, Morganti JM, Selenica ML, Moran P, Reid P, Brownlow M et al (2013) Fractalkine overexpression suppresses tau pathology in a mouse model of tauopathy. Neurobiol Aging 34(6):1540–1548. doi:10.1016/j.neurobiolaging.2012.12.011
    • (2013) Neurobiol Aging , vol.34 , Issue.6 , pp. 1540-1548
    • Nash, K.R.1    Lee, D.C.2    Hunt, J.B.3    Morganti, J.M.4    Selenica, M.L.5    Moran, P.6    Reid, P.7    Brownlow, M.8
  • 115
    • 78650653951 scopus 로고    scopus 로고
    • Anti-inflammatory action of donepezil ameliorates tau pathology, synaptic loss, and neurodegeneration in a tauopathy mouse model
    • COI: 1:CAS:528:DC%2BC3cXhtlWmtb%2FM, PID: 20847440
    • Yoshiyama Y, Kojima A, Ishikawa C, Arai K (2010) Anti-inflammatory action of donepezil ameliorates tau pathology, synaptic loss, and neurodegeneration in a tauopathy mouse model. J Alzheimers Dis 22(1):295–306. doi:10.3233/JAD-2010-100681
    • (2010) J Alzheimers Dis , vol.22 , Issue.1 , pp. 295-306
    • Yoshiyama, Y.1    Kojima, A.2    Ishikawa, C.3    Arai, K.4
  • 116
    • 84882761023 scopus 로고    scopus 로고
    • Minocycline alleviates beta-amyloid protein and tau pathology via restraining neuroinflammation induced by diabetic metabolic disorder
    • COI: 1:CAS:528:DC%2BC3sXhtlyhsrzE, PID: 23983461
    • Cai Z, Yan Y, Wang Y (2013) Minocycline alleviates beta-amyloid protein and tau pathology via restraining neuroinflammation induced by diabetic metabolic disorder. Clin Interv Aging 8:1089–1095. doi:10.2147/CIA.S46536
    • (2013) Clin Interv Aging , vol.8 , pp. 1089-1095
    • Cai, Z.1    Yan, Y.2    Wang, Y.3
  • 117
    • 84923254431 scopus 로고    scopus 로고
    • Telmisartan reduces progressive accumulation of cellular amyloid beta and phosphorylated tau with inflammatory responses in aged spontaneously hypertensive stroke resistant rat
    • PID: 25241340
    • Kurata T, Lukic V, Kozuki M, Wada D, Miyazaki K, Morimoto N, Ohta Y, Deguchi K et al (2014) Telmisartan reduces progressive accumulation of cellular amyloid beta and phosphorylated tau with inflammatory responses in aged spontaneously hypertensive stroke resistant rat. J Stroke Cerebrovasc Dis 23(10):2580–2590. doi:10.1016/j.jstrokecerebrovasdis.2014.05.023
    • (2014) J Stroke Cerebrovasc Dis , vol.23 , Issue.10 , pp. 2580-2590
    • Kurata, T.1    Lukic, V.2    Kozuki, M.3    Wada, D.4    Miyazaki, K.5    Morimoto, N.6    Ohta, Y.7    Deguchi, K.8
  • 118
    • 77958065504 scopus 로고    scopus 로고
    • Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • COI: 1:CAS:528:DC%2BC3cXhtlegsLbP, PID: 20943926
    • Brunden KR, Zhang B, Carroll J, Yao Y, Potuzak JS, Hogan AM, Iba M, James MJ et al (2010) Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J Neurosci 30(41):13861–13866. doi:10.1523/JNEUROSCI.3059-10.2010
    • (2010) J Neurosci , vol.30 , Issue.41 , pp. 13861-13866
    • Brunden, K.R.1    Zhang, B.2    Carroll, J.3    Yao, Y.4    Potuzak, J.S.5    Hogan, A.M.6    Iba, M.7    James, M.J.8
  • 119
    • 84863230105 scopus 로고    scopus 로고
    • The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice
    • COI: 1:CAS:528:DC%2BC38XktlOlsbg%3D, PID: 22423084
    • Zhang B, Carroll J, Trojanowski JQ, Yao Y, Iba M, Potuzak JS, Hogan AM, Xie SX et al (2012) The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice. J Neurosci 32(11):3601–3611. doi:10.1523/JNEUROSCI.4922-11.2012
    • (2012) J Neurosci , vol.32 , Issue.11 , pp. 3601-3611
    • Zhang, B.1    Carroll, J.2    Trojanowski, J.Q.3    Yao, Y.4    Iba, M.5    Potuzak, J.S.6    Hogan, A.M.7    Xie, S.X.8
  • 120
    • 84861313192 scopus 로고    scopus 로고
    • Hyperdynamic microtubules, cognitive deficits, and pathology are improved in tau transgenic mice with low doses of the microtubule-stabilizing agent BMS-241027
    • COI: 1:CAS:528:DC%2BC38XnvFKksb8%3D, PID: 22623658
    • Barten DM, Fanara P, Andorfer C, Hoque N, Wong PY, Husted KH, Cadelina GW, Decarr LB et al (2012) Hyperdynamic microtubules, cognitive deficits, and pathology are improved in tau transgenic mice with low doses of the microtubule-stabilizing agent BMS-241027. J Neurosci 32(21):7137–7145. doi:10.1523/JNEUROSCI.0188-12.2012
    • (2012) J Neurosci , vol.32 , Issue.21 , pp. 7137-7145
    • Barten, D.M.1    Fanara, P.2    Andorfer, C.3    Hoque, N.4    Wong, P.Y.5    Husted, K.H.6    Cadelina, G.W.7    Decarr, L.B.8
  • 121
    • 79958128165 scopus 로고    scopus 로고
    • NAP (davunetide) provides functional and structural neuroprotection
    • COI: 1:CAS:528:DC%2BC3MXmvFGgtrY%3D, PID: 21524250
    • Gozes I (2011) NAP (davunetide) provides functional and structural neuroprotection. Curr Pharm Des 17(10):1040–1044
    • (2011) Curr Pharm Des , vol.17 , Issue.10 , pp. 1040-1044
    • Gozes, I.1
  • 122
    • 64649097649 scopus 로고    scopus 로고
    • NAP protects memory, increases soluble tau and reduces tau hyperphosphorylation in a tauopathy model
    • COI: 1:CAS:528:DC%2BD1MXkslKrs7o%3D, PID: 19264130
    • Shiryaev N, Jouroukhin Y, Giladi E, Polyzoidou E, Grigoriadis NC, Rosenmann H, Gozes I (2009) NAP protects memory, increases soluble tau and reduces tau hyperphosphorylation in a tauopathy model. Neurobiol Dis 34(2):381–388. doi:10.1016/j.nbd.2009.02.011
    • (2009) Neurobiol Dis , vol.34 , Issue.2 , pp. 381-388
    • Shiryaev, N.1    Jouroukhin, Y.2    Giladi, E.3    Polyzoidou, E.4    Grigoriadis, N.C.5    Rosenmann, H.6    Gozes, I.7
  • 123
    • 84902545124 scopus 로고    scopus 로고
    • Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial
    • COI: 1:CAS:528:DC%2BC2cXptVaksbs%3D, PID: 24873720
    • Boxer AL, Lang AE, Grossman M, Knopman DS, Miller BL, Schneider LS, Doody RS, Lees A et al (2014) Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial. Lancet Neurol 13(7):676–685. doi:10.1016/S1474-4422(14)70088-2
    • (2014) Lancet Neurol , vol.13 , Issue.7 , pp. 676-685
    • Boxer, A.L.1    Lang, A.E.2    Grossman, M.3    Knopman, D.S.4    Miller, B.L.5    Schneider, L.S.6    Doody, R.S.7    Lees, A.8
  • 124
    • 57449118452 scopus 로고    scopus 로고
    • Alternative splicing of exon 10 in the tau gene as a target for treatment of tauopathies
    • PID: 19090983
    • Zhou J, Yu Q, Zou T (2008) Alternative splicing of exon 10 in the tau gene as a target for treatment of tauopathies. BMC Neurosci 9(Suppl 2):S10. doi:10.1186/1471-2202-9-S2-S10
    • (2008) BMC Neurosci , vol.9 , pp. 10
    • Zhou, J.1    Yu, Q.2    Zou, T.3
  • 125
    • 84868092702 scopus 로고    scopus 로고
    • Targeting a pre-mRNA structure with bipartite antisense molecules modulates tau alternative splicing
    • COI: 1:CAS:528:DC%2BC38XhsFygurnF, PID: 22844088
    • Peacey E, Rodriguez L, Liu Y, Wolfe MS (2012) Targeting a pre-mRNA structure with bipartite antisense molecules modulates tau alternative splicing. Nucleic Acids Res 40(19):9836–9849. doi:10.1093/nar/gks710
    • (2012) Nucleic Acids Res , vol.40 , Issue.19 , pp. 9836-9849
    • Peacey, E.1    Rodriguez, L.2    Liu, Y.3    Wolfe, M.S.4
  • 126
    • 84893832278 scopus 로고    scopus 로고
    • Fyn kinase inhibition as a novel therapy for Alzheimer's disease
    • PID: 24495408
    • Nygaard HB, van Dyck CH, Strittmatter SM (2014) Fyn kinase inhibition as a novel therapy for Alzheimer's disease. Alzheimers Res Ther 6(1):8. doi:10.1186/alzrt238
    • (2014) Alzheimers Res Ther , vol.6 , Issue.1 , pp. 8
    • Nygaard, H.B.1    van Dyck, C.H.2    Strittmatter, S.M.3
  • 128
    • 77955395834 scopus 로고    scopus 로고
    • Cell-mediated neuroprotection in a mouse model of human tauopathy
    • COI: 1:CAS:528:DC%2BC3cXhtVahsr7N, PID: 20668182
    • Hampton DW, Webber DJ, Bilican B, Goedert M, Spillantini MG, Chandran S (2010) Cell-mediated neuroprotection in a mouse model of human tauopathy. J Neurosci 30(30):9973–9983. doi:10.1523/JNEUROSCI.0834-10.2010
    • (2010) J Neurosci , vol.30 , Issue.30 , pp. 9973-9983
    • Hampton, D.W.1    Webber, D.J.2    Bilican, B.3    Goedert, M.4    Spillantini, M.G.5    Chandran, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.