메뉴 건너뛰기




Volumn 12, Issue 1, 2017, Pages

Glial contributions to neurodegeneration in tauopathies

Author keywords

Alzheimer's disease; Astrocyte; Gliosis; Microglia; Neurodegeneration; Neuroinflammation; Tau; Tauopathy

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; COMPLEMENT; GLUCOCORTICOID; INTERLEUKIN 10; INTERLEUKIN 13; INTERLEUKIN 1BETA; INTERLEUKIN 34; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 8; NONSTEROID ANTIINFLAMMATORY AGENT; TAU PROTEIN; TUMOR NECROSIS FACTOR;

EID: 85021683314     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/s13024-017-0192-x     Document Type: Review
Times cited : (293)

References (186)
  • 1
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • 1:CAS:528:DC%2BC3sXnvVGkur0%3D 23684085
    • Spillantini MG, Goedert M. Tau pathology and neurodegeneration. Lancet Neurol. 2013;12:609-22.
    • (2013) Lancet Neurol , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 2
  • 3
    • 84929938315 scopus 로고    scopus 로고
    • Three dimensions of the amyloid hypothesis: Time, space and "wingmen.
    • 1:CAS:528:DC%2BC2MXhtFeit7bM 26007213 4445458
    • Musiek ES, Holtzman DM. Three dimensions of the amyloid hypothesis: time, space and "wingmen.". Nat Neurosci. 2015;18:800-6.
    • (2015) Nat Neurosci , vol.18 , pp. 800-806
    • Musiek, E.S.1    Holtzman, D.M.2
  • 4
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurodegenerative disease - A double-edged sword
    • 1:CAS:528:DC%2BD38Xmt12isrs%3D 12165466
    • Wyss-Coray T, Mucke L. Inflammation in neurodegenerative disease - a double-edged sword. Neuron. 2002;35:419-32.
    • (2002) Neuron , vol.35 , pp. 419-432
    • Wyss-Coray, T.1    Mucke, L.2
  • 5
    • 84983071295 scopus 로고    scopus 로고
    • How neuroinflammation contributes to neurodegeneration
    • 1:CAS:528:DC%2BC28XhtlCju73I 27540165
    • Ransohoff RM. How neuroinflammation contributes to neurodegeneration. Science. 2016;353:777-83.
    • (2016) Science , vol.353 , pp. 777-783
    • Ransohoff, R.M.1
  • 6
    • 77957028140 scopus 로고    scopus 로고
    • Microglial activation and chronic neurodegeneration
    • 1:CAS:528:DC%2BC3cXht1SqsLnO 20880500 2951017
    • Lull ME, Block ML. Microglial activation and chronic neurodegeneration. Neurotherapeutics. 2010;7:354-65.
    • (2010) Neurotherapeutics , vol.7 , pp. 354-365
    • Lull, M.E.1    Block, M.L.2
  • 7
    • 84945474523 scopus 로고    scopus 로고
    • Depletion of microglia and inhibition of exosome synthesis halt tau propagation
    • 1:CAS:528:DC%2BC2MXhs1Wls7bJ 26436904 4694577
    • Asai H, Ikezu S, Tsunoda S, Medalla M, Luebke J, Haydar T, et al. Depletion of microglia and inhibition of exosome synthesis halt tau propagation. Nat Neurosci. 2015;18:1584-93.
    • (2015) Nat Neurosci , vol.18 , pp. 1584-1593
    • Asai, H.1    Ikezu, S.2    Tsunoda, S.3    Medalla, M.4    Luebke, J.5    Haydar, T.6
  • 8
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • 1:CAS:528:DyaK38XjvFSmsQ%3D%3D 2484340
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron. 1989;3:519-26.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 9
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • 1:STN:280:DyaL2s7lvVKnsg%3D%3D 3103857
    • Neve RL, Harris P, Kosik KS, Kurnit DM, Donlon TA. Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res. 1986;387:271-80.
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 10
    • 80155166000 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms
    • 1:CAS:528:DC%2BC3MXht1aisbnM
    • Combs B, Voss K, Gamblin TC. Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms. Biochemistry Mosc. 2011;50:9446-56.
    • (2011) Biochemistry Mosc , vol.50 , pp. 9446-9456
    • Combs, B.1    Voss, K.2    Gamblin, T.C.3
  • 11
    • 77956542660 scopus 로고    scopus 로고
    • Three repeat isoforms of tau inhibit assembly of four repeat tau filaments
    • e10810 20520830 2876030
    • Adams SJ, DeTure MA, McBride M, Dickson DW, Petrucelli L. Three repeat isoforms of tau inhibit assembly of four repeat tau filaments. PLoS One. 2010;5:e10810.
    • (2010) PLoS One , vol.5
    • Adams, S.J.1    DeTure, M.A.2    McBride, M.3    Dickson, D.W.4    Petrucelli, L.5
  • 12
    • 84975519193 scopus 로고    scopus 로고
    • Increased 4R-tau induces pathological changes in a human-tau mouse model
    • 1:CAS:528:DC%2BC28XotlemsrY%3D 27210553 5040069
    • Schoch KM, DeVos SL, Miller RL, Chun SJ, Norrbom M, Wozniak DF, et al. Increased 4R-tau induces pathological changes in a human-tau mouse model. Neuron. 2016;90:941-7.
    • (2016) Neuron , vol.90 , pp. 941-947
    • Schoch, K.M.1    DeVos, S.L.2    Miller, R.L.3    Chun, S.J.4    Norrbom, M.5    Wozniak, D.F.6
  • 13
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen M, Barghorn S, Li L, Marx A, Biernat J, Mandelkow EM, et al. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. J Biol Chem. 2001;276:48165-74.
    • (2001) J Biol Chem , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6
  • 14
    • 79955670132 scopus 로고    scopus 로고
    • The many faces of tau
    • 1:CAS:528:DC%2BC3MXlvVeku7g%3D 21555069 3319390
    • Morris M, Maeda S, Vossel K, Mucke L. The many faces of tau. Neuron. 2011;70:410-26.
    • (2011) Neuron , vol.70 , pp. 410-426
    • Morris, M.1    Maeda, S.2    Vossel, K.3    Mucke, L.4
  • 16
    • 85021644294 scopus 로고    scopus 로고
    • Tau Regulates the Attachment/Detachment but Not the Speed of Motors in Microtubule-Dependent Transport of Single Vesicles and Organelles [Internet] [cited 2017 Feb 22]
    • Tau Regulates the Attachment/Detachment but Not the Speed of Motors in Microtubule-Dependent Transport of Single Vesicles and Organelles [Internet]. PubMed J. [cited 2017 Feb 22]. Available from: https://ncbi.nlm.nih.gov/labs/articles/10381391/.
    • PubMed J
  • 18
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • 1:CAS:528:DC%2BC3cXht1Wisr3K 20869593 3035103
    • Min S-W, Cho S-H, Zhou Y, Schroeder S, Haroutunian V, Seeley WW, et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron. 2010;67:953-66.
    • (2010) Neuron , vol.67 , pp. 953-966
    • Min, S.-W.1    Cho, S.-H.2    Zhou, Y.3    Schroeder, S.4    Haroutunian, V.5    Seeley, W.W.6
  • 19
    • 84857620173 scopus 로고    scopus 로고
    • Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
    • Irwin DJ, Cohen TJ, Grossman M, Arnold SE, Xie SX, Lee VM-Y, et al. Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies. Brain J Neurol. 2012;135:807-18.
    • (2012) Brain J Neurol , vol.135 , pp. 807-818
    • Irwin, D.J.1    Cohen, T.J.2    Grossman, M.3    Arnold, S.E.4    Xie, S.X.5    Lee, V.M.-Y.6
  • 20
    • 79953087890 scopus 로고    scopus 로고
    • The acetylation of tau inhibits its function and promotes pathological tau aggregation
    • 21427723 3120096
    • Cohen TJ, Guo JL, Hurtado DE, Kwong LK, Mills IP, Trojanowski JQ, et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat Commun. 2011;2:252.
    • (2011) Nat Commun , vol.2 , pp. 252
    • Cohen, T.J.1    Guo, J.L.2    Hurtado, D.E.3    Kwong, L.K.4    Mills, I.P.5    Trojanowski, J.Q.6
  • 21
    • 85006137585 scopus 로고    scopus 로고
    • Tau protein hyperphosphorylation and aggregation in Alzheimer's disease and other Tauopathies, and possible Neuroprotective strategies
    • Šimić G, Babić Leko M, Wray S, Harrington C, Delalle I, Jovanov-Milošević N, et al. Tau protein hyperphosphorylation and aggregation in Alzheimer's disease and other Tauopathies, and possible Neuroprotective strategies. Biomol Ther. 2016;6:6.
    • (2016) Biomol Ther , vol.6 , pp. 6
    • Šimić, G.1    Babić Leko, M.2    Wray, S.3    Harrington, C.4    Delalle, I.5    Jovanov-Milošević, N.6
  • 22
    • 0042090541 scopus 로고    scopus 로고
    • Phosphorylation pattern of tau associated with distinct changes of the growth cone cytoskeleton
    • 12827970
    • Simić G, Diana A, Hof PR. Phosphorylation pattern of tau associated with distinct changes of the growth cone cytoskeleton. Prog Mol Subcell Biol. 2003;32:33-48.
    • (2003) Prog Mol Subcell Biol , vol.32 , pp. 33-48
    • Simić, G.1    Diana, A.2    Hof, P.R.3
  • 23
    • 84857035370 scopus 로고    scopus 로고
    • Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: A mass spectrometry approach
    • 1:CAS:528:DC%2BC38Xkt1eqsA%3D%3D 22033876
    • Thomas SN, Funk KE, Wan Y, Liao Z, Davies P, Kuret J, et al. Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach. Acta Neuropathol Berl. 2012;123:105-17.
    • (2012) Acta Neuropathol Berl , vol.123 , pp. 105-117
    • Thomas, S.N.1    Funk, K.E.2    Wan, Y.3    Liao, Z.4    Davies, P.5    Kuret, J.6
  • 24
    • 84904602584 scopus 로고    scopus 로고
    • Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity
    • 1:CAS:528:DC%2BC2cXht1Wqt7rO 24869773 4292886
    • Funk KE, Thomas SN, Schafer KN, Cooper GL, Liao Z, Clark DJ, et al. Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity. Biochem J. 2014;462:77-88.
    • (2014) Biochem J , vol.462 , pp. 77-88
    • Funk, K.E.1    Thomas, S.N.2    Schafer, K.N.3    Cooper, G.L.4    Liao, Z.5    Clark, D.J.6
  • 25
    • 0042926482 scopus 로고    scopus 로고
    • Nitration of tau protein is linked to neurodegeneration in tauopathies
    • 1:CAS:528:DC%2BD3sXnsVCisr4%3D 12937143 1868254
    • Horiguchi T, Uryu K, Giasson BI, Ischiropoulos H, LightFoot R, Bellmann C, et al. Nitration of tau protein is linked to neurodegeneration in tauopathies. Am J Pathol. 2003;163:1021-31.
    • (2003) Am J Pathol , vol.163 , pp. 1021-1031
    • Horiguchi, T.1    Uryu, K.2    Giasson, B.I.3    Ischiropoulos, H.4    LightFoot, R.5    Bellmann, C.6
  • 26
    • 33750940057 scopus 로고    scopus 로고
    • Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies
    • 1:CAS:528:DC%2BD28XhtFygu7nK 17050703
    • Reynolds MR, Reyes JF, Fu Y, Bigio EH, Guillozet-Bongaarts AL, Berry RW, et al. Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies. J Neurosci. 2006;26:10636-45.
    • (2006) J Neurosci , vol.26 , pp. 10636-10645
    • Reynolds, M.R.1    Reyes, J.F.2    Fu, Y.3    Bigio, E.H.4    Guillozet-Bongaarts, A.L.5    Berry, R.W.6
  • 27
    • 10544236116 scopus 로고    scopus 로고
    • The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine
    • 1:CAS:528:DyaK28XntFKntLs%3D 8910513
    • Arnold CS, Johnson GV, Cole RN, Dong DL, Lee M, Hart GW. The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. J Biol Chem. 1996;271:28741-4.
    • (1996) J Biol Chem , vol.271 , pp. 28741-28744
    • Arnold, C.S.1    Johnson, G.V.2    Cole, R.N.3    Dong, D.L.4    Lee, M.5    Hart, G.W.6
  • 28
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • 1:CAS:528:DC%2BD2cXmtFWmtLs%3D 15249677 490015
    • Liu F, Iqbal K, Grundke-Iqbal I, Hart GW, Gong C-X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci U S A. 2004;101:10804-9.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.-X.5
  • 29
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • 16630055
    • Li X, Lu F, Wang J-Z, Gong C-X. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur J Neurosci. 2006;23:2078-86.
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.-Z.3    Gong, C.-X.4
  • 30
    • 0033600242 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
    • 1:CAS:528:DyaK1MXksVSgt7w%3D 10391244
    • Lu PJ, Wulf G, Zhou XZ, Davies P, Lu KP. The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature. 1999;399:784-8.
    • (1999) Nature , vol.399 , pp. 784-788
    • Lu, P.J.1    Wulf, G.2    Zhou, X.Z.3    Davies, P.4    Lu, K.P.5
  • 31
    • 84859185373 scopus 로고    scopus 로고
    • Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease
    • 1:CAS:528:DC%2BC38XltVaku7w%3D 22464332 3601591
    • Nakamura K, Greenwood A, Binder L, Bigio EH, Denial S, Nicholson L, et al. Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease. Cell. 2012;149:232-44.
    • (2012) Cell , vol.149 , pp. 232-244
    • Nakamura, K.1    Greenwood, A.2    Binder, L.3    Bigio, E.H.4    Denial, S.5    Nicholson, L.6
  • 32
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein
    • 1:CAS:528:DC%2BD28Xjt1Knt7c%3D 16464864
    • Dorval V, Fraser PE. Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein. J Biol Chem. 2006;281:9919-24.
    • (2006) J Biol Chem , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 33
    • 34249733176 scopus 로고
    • SUMO on the road to neurodegeneration
    • Dorval V, Fraser PE. SUMO on the road to neurodegeneration. Biochim Biophys Acta. 1773;2007:694-706.
    • (1773) Biochim Biophys Acta , vol.2007 , pp. 694-706
    • Dorval, V.1    Fraser, P.E.2
  • 34
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • 1:CAS:528:DyaL1cXkslWnur8%3D 3132715 280459
    • Wischik CM, Novak M, Thøgersen HC, Edwards PC, Runswick MJ, Jakes R, et al. Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc Natl Acad Sci U S A. 1988;85:4506-10.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thøgersen, H.C.3    Edwards, P.C.4    Runswick, M.J.5    Jakes, R.6
  • 35
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • 1:CAS:528:DC%2BD3sXmvVeisrc%3D 12888622 187753
    • Gamblin TC, Chen F, Zambrano A, Abraha A, Lagalwar S, Guillozet AL, et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci U S A. 2003;100:10032-7.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3    Abraha, A.4    Lagalwar, S.5    Guillozet, A.L.6
  • 36
    • 33747401659 scopus 로고    scopus 로고
    • Tau phosphorylation and proteolysis: Insights and perspectives
    • 1:CAS:528:DC%2BD28XotFKktrY%3D 16914862
    • Johnson GVW. Tau phosphorylation and proteolysis: insights and perspectives. J. Alzheimers Dis. 2006;9:243-50.
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 243-250
    • Johnson, G.V.W.1
  • 37
    • 84990966921 scopus 로고    scopus 로고
    • Caspase-2 cleavage of tau reversibly impairs memory
    • 1:CAS:528:DC%2BC28Xhs1ektrfI 27723722
    • Zhao X, Kotilinek LA, Smith B, Hlynialuk C, Zahs K, Ramsden M, et al. Caspase-2 cleavage of tau reversibly impairs memory. Nat Med. 2016;22:1268-76.
    • (2016) Nat Med , vol.22 , pp. 1268-1276
    • Zhao, X.1    Kotilinek, L.A.2    Smith, B.3    Hlynialuk, C.4    Zahs, K.5    Ramsden, M.6
  • 38
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • 1:CAS:528:DyaL2sXitFWqtrc%3D 3029875
    • Mori H, Kondo J, Ihara Y. Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science. 1987;235:1641-4.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 39
    • 33744950091 scopus 로고    scopus 로고
    • Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation
    • 1:CAS:528:DC%2BD28XjsFSqurc%3D 16443603
    • Cripps D, Thomas SN, Jeng Y, Yang F, Davies P, Yang AJ. Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. J Biol Chem. 2006;281:10825-38.
    • (2006) J Biol Chem , vol.281 , pp. 10825-10838
    • Cripps, D.1    Thomas, S.N.2    Jeng, Y.3    Yang, F.4    Davies, P.5    Yang, A.J.6
  • 40
    • 84954291382 scopus 로고    scopus 로고
    • Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling
    • 1:CAS:528:DC%2BC2MXitVKrurfN 26692334
    • Myeku N, Clelland CL, Emrani S, Kukushkin NV, Yu WH, Goldberg AL, et al. Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling. Nat Med. 2016;22:46-53.
    • (2016) Nat Med , vol.22 , pp. 46-53
    • Myeku, N.1    Clelland, C.L.2    Emrani, S.3    Kukushkin, N.V.4    Yu, W.H.5    Goldberg, A.L.6
  • 41
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol
    • 1:STN:280:DyaK387gtFOiug%3D%3D
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. Berl. 1991;82:239-59.
    • (1991) Berl , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 42
    • 80054904670 scopus 로고    scopus 로고
    • Stages of the pathologic process in Alzheimer disease: Age categories from 1 to 100 years
    • 1:CAS:528:DC%2BC3MXhtlChs7bJ 22002422
    • Braak H, Thal DR, Ghebremedhin E, Del Tredici K. Stages of the pathologic process in Alzheimer disease: age categories from 1 to 100 years. J Neuropathol Exp Neurol. 2011;70:960-9.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 960-969
    • Braak, H.1    Thal, D.R.2    Ghebremedhin, E.3    Del Tredici, K.4
  • 44
  • 46
    • 84962081972 scopus 로고    scopus 로고
    • A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
    • 1:CAS:528:DC%2BC28XksVKksbk%3D 26988744
    • Walsh DM, Selkoe DJ. A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration. Nat Rev Neurosci. 2016;17:251-60.
    • (2016) Nat Rev Neurosci , vol.17 , pp. 251-260
    • Walsh, D.M.1    Selkoe, D.J.2
  • 47
    • 84926513913 scopus 로고    scopus 로고
    • Spreading of pathology in neurodegenerative diseases: A focus on human studies
    • 1:CAS:528:DC%2BC2MXosF2gsA%3D%3D 25588378 4312418
    • Brettschneider J, Del Tredici K, Lee VM-Y, Trojanowski JQ. Spreading of pathology in neurodegenerative diseases: a focus on human studies. Nat Rev Neurosci. 2015;16:109-20.
    • (2015) Nat Rev Neurosci , vol.16 , pp. 109-120
    • Brettschneider, J.1    Del Tredici, K.2    Lee, V.M.-Y.3    Trojanowski, J.Q.4
  • 48
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • 1:CAS:528:DC%2BC2cXitVenu7s%3D 24504409 4011661
    • Guo JL, Lee VMY. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med. 2014;20:130-8.
    • (2014) Nat Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.Y.2
  • 49
    • 84863808563 scopus 로고    scopus 로고
    • Prion-like spread of protein aggregates in neurodegeneration
    • 1:CAS:528:DC%2BC38Xmsl2itLw%3D 22566400 3348110
    • Polymenidou M, Cleveland DW. Prion-like spread of protein aggregates in neurodegeneration. J Exp Med. 2012;209:889-93.
    • (2012) J Exp Med , vol.209 , pp. 889-893
    • Polymenidou, M.1    Cleveland, D.W.2
  • 50
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • 1:CAS:528:DC%2BC3sXhtlyrtLzP 24005412 3963807
    • Jucker M, Walker LC. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature. 2013;501:45-51.
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 51
    • 77954176744 scopus 로고    scopus 로고
    • Secretion of human tau fragments resembling CSF-tau in Alzheimer's disease is modulated by the presence of the exon 2 insert
    • 1:CAS:528:DC%2BC3cXosVygs78%3D 20553717
    • Kim W, Lee S, Hall GF. Secretion of human tau fragments resembling CSF-tau in Alzheimer's disease is modulated by the presence of the exon 2 insert. FEBS Lett. 2010;584:3085-8.
    • (2010) FEBS Lett , vol.584 , pp. 3085-3088
    • Kim, W.1    Lee, S.2    Hall, G.F.3
  • 52
    • 77049123465 scopus 로고    scopus 로고
    • Interneuronal transfer of human tau between lamprey central neurons in situ
    • 1:CAS:528:DC%2BC3cXht1SltLo%3D 20110609
    • Kim W, Lee S, Jung C, Ahmed A, Lee G, Hall GF. Interneuronal transfer of human tau between lamprey central neurons in situ. J. Alzheimers Dis. 2010;19:647-64.
    • (2010) J. Alzheimers Dis. , vol.19 , pp. 647-664
    • Kim, W.1    Lee, S.2    Jung, C.3    Ahmed, A.4    Lee, G.5    Hall, G.F.6
  • 53
    • 84871141635 scopus 로고    scopus 로고
    • Extracellular tau levels are influenced by variability in tau that is associated with tauopathies
    • 1:CAS:528:DC%2BC38XhvVeksbrN 23105105 3522274
    • Karch CM, Jeng AT, Goate AM. Extracellular tau levels are influenced by variability in tau that is associated with tauopathies. J Biol Chem. 2012;287:42751-62.
    • (2012) J Biol Chem , vol.287 , pp. 42751-42762
    • Karch, C.M.1    Jeng, A.T.2    Goate, A.M.3
  • 54
    • 84876459364 scopus 로고    scopus 로고
    • Physiological release of endogenous tau is stimulated by neuronal activity
    • 1:CAS:528:DC%2BC3sXis1aht78%3D 23412472 3615658
    • Pooler AM, Phillips EC, Lau DHW, Noble W, Hanger DP. Physiological release of endogenous tau is stimulated by neuronal activity. EMBO Rep. 2013;14:389-94.
    • (2013) EMBO Rep , vol.14 , pp. 389-394
    • Pooler, A.M.1    Phillips, E.C.2    Lau, D.H.W.3    Noble, W.4    Hanger, D.P.5
  • 55
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • 1:CAS:528:DC%2BC38XhvVSjt7w%3D 22057275
    • Saman S, Kim W, Raya M, Visnick Y, Miro S, Saman S, et al. Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem. 2012;287:3842-9.
    • (2012) J Biol Chem , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6
  • 56
    • 84872714502 scopus 로고    scopus 로고
    • Small Misfolded tau species are internalized via bulk Endocytosis and Anterogradely and Retrogradely transported in neurons
    • 1:CAS:528:DC%2BC3sXhtFagu7Y%3D 23188818
    • Wu JW, Herman M, Liu L, Simoes S, Acker CM, Figueroa H, et al. Small Misfolded tau species are internalized via bulk Endocytosis and Anterogradely and Retrogradely transported in neurons. J Biol Chem. 2013;288:1856-70.
    • (2013) J Biol Chem , vol.288 , pp. 1856-1870
    • Wu, J.W.1    Herman, M.2    Liu, L.3    Simoes, S.4    Acker, C.M.5    Figueroa, H.6
  • 57
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • 1:CAS:528:DC%2BD1MXltlemsro%3D 19282288 2676015
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem. 2009;284:12845-52.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 58
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice
    • 1:CAS:528:DC%2BC3MXht1OgurfJ 21917794 4299126
    • Yamada K, Cirrito JR, Stewart FR, Jiang H, Finn MB, Holmes BB, et al. In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice. J Neurosci. 2011;31:13110-7.
    • (2011) J Neurosci , vol.31 , pp. 13110-13117
    • Yamada, K.1    Cirrito, J.R.2    Stewart, F.R.3    Jiang, H.4    Finn, M.B.5    Holmes, B.B.6
  • 59
    • 84896830709 scopus 로고    scopus 로고
    • Neuronal activity regulates extracellular tau in vivo
    • 1:CAS:528:DC%2BC2cXktlOmsbY%3D 24534188 3949564
    • Yamada K, Holth JK, Liao F, Stewart FR, Mahan TE, Jiang H, et al. Neuronal activity regulates extracellular tau in vivo. J Exp Med. 2014;211:387-93.
    • (2014) J Exp Med , vol.211 , pp. 387-393
    • Yamada, K.1    Holth, J.K.2    Liao, F.3    Stewart, F.R.4    Mahan, T.E.5    Jiang, H.6
  • 61
    • 84860142897 scopus 로고    scopus 로고
    • Tau elevations in the brain extracellular space correlate with reduced amyloid-β levels and predict adverse clinical outcomes after severe traumatic brain injury
    • 22116192
    • Magnoni S, Esparza TJ, Conte V, Carbonara M, Carrabba G, Holtzman DM, et al. Tau elevations in the brain extracellular space correlate with reduced amyloid-β levels and predict adverse clinical outcomes after severe traumatic brain injury. Brain. 2012;135:1268-80.
    • (2012) Brain , vol.135 , pp. 1268-1280
    • Magnoni, S.1    Esparza, T.J.2    Conte, V.3    Carbonara, M.4    Carrabba, G.5    Holtzman, D.M.6
  • 62
    • 79551542416 scopus 로고    scopus 로고
    • Selective transfer of exosomes from oligodendrocytes to microglia by macropinocytosis
    • 1:CAS:528:DC%2BC3MXisFyjsro%3D 21242314
    • Fitzner D, Schnaars M, van Rossum D, Krishnamoorthy G, Dibaj P, Bakhti M, et al. Selective transfer of exosomes from oligodendrocytes to microglia by macropinocytosis. J Cell Sci. 2011;124:447-58.
    • (2011) J Cell Sci , vol.124 , pp. 447-458
    • Fitzner, D.1    Schnaars, M.2    Van Rossum, D.3    Krishnamoorthy, G.4    Dibaj, P.5    Bakhti, M.6
  • 63
    • 84882306577 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
    • 1:CAS:528:DC%2BC3sXhtlCrtbfL 23898162 3746848
    • Holmes BB, DeVos SL, Kfoury N, Li M, Jacks R, Yanamandra K, et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci U S A. 2013;110:E3138-47.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E3138-E3147
    • Holmes, B.B.1    DeVos, S.L.2    Kfoury, N.3    Li, M.4    Jacks, R.5    Yanamandra, K.6
  • 64
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles
    • 1:CAS:528:DC%2BC3MXltVSqu70%3D 21372138 3083182
    • Guo JL, Lee VM-Y. Seeding of normal tau by pathological tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem. 2011;286:15317-31.
    • (2011) J Biol Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.-Y.2
  • 65
    • 84891905725 scopus 로고    scopus 로고
    • Extracellular Monomeric tau protein is sufficient to initiate the spread of tau protein pathology
    • 1:CAS:528:DC%2BC2cXns1Wnsg%3D%3D 24235150
    • Michel CH. Kumar S, Pinotsi D, Tunnacliffe a, St. George-Hyslop P, Mandelkow E, et al. extracellular Monomeric tau protein is sufficient to initiate the spread of tau protein pathology. J Biol Chem. 2014;289:956-67.
    • (2014) J Biol Chem , vol.289 , pp. 956-967
    • Michel, C.H.1    Kumar, S.2    Pinotsi, D.3    Tunnacliffe, A.4    St George-Hyslop, P.5    Mandelkow, E.6
  • 67
    • 84944088611 scopus 로고    scopus 로고
    • Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain
    • [Internet] [cited 2017 Feb 23]
    • Takeda S, Wegmann S, Cho H, DeVos SL, Commins C, Roe AD, et al. Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer's disease brain. Nat. Commun. [Internet]. 2015 [cited 2017 Feb 23];6. Available from: https://www.ncbi.nlm.nih.gov/pubmed/26458742.
    • (2015) Nat. Commun , vol.6
    • Takeda, S.1    Wegmann, S.2    Cho, H.3    DeVos, S.L.4    Commins, C.5    Roe, A.D.6
  • 68
    • 84985947118 scopus 로고    scopus 로고
    • Seed-competent high-molecular-weight tau species accumulates in the cerebrospinal fluid of Alzheimer's disease mouse model and human patients
    • 1:CAS:528:DC%2BC28XhsVOit77F 27351289
    • Takeda S, Commins C, DeVos SL, Nobuhara CK, Wegmann S, Roe AD, et al. Seed-competent high-molecular-weight tau species accumulates in the cerebrospinal fluid of Alzheimer's disease mouse model and human patients. Ann Neurol. 2016;80:355-67.
    • (2016) Ann Neurol , vol.80 , pp. 355-367
    • Takeda, S.1    Commins, C.2    DeVos, S.L.3    Nobuhara, C.K.4    Wegmann, S.5    Roe, A.D.6
  • 69
  • 70
    • 84878723720 scopus 로고    scopus 로고
    • Brain homogenates from human tauopathies induce tau inclusions in mouse brain
    • 1:CAS:528:DC%2BC3sXhtFGrtrbO 23690619 3677441
    • Clavaguera F, Akatsu H, Fraser G, Crowther RA, Frank S, Hench J, et al. Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc Natl Acad Sci U S A. 2013;110:9535-40.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9535-9540
    • Clavaguera, F.1    Akatsu, H.2    Fraser, G.3    Crowther, R.A.4    Frank, S.5    Hench, J.6
  • 71
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of Neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like Tauopathy
    • 1:CAS:528:DC%2BC3sXhsVems70%3D 23325240 3575082
    • Iba M, Guo JL, McBride JD, Zhang B, Trojanowski JQ, Lee VM-Y. Synthetic tau fibrils mediate transmission of Neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like Tauopathy. J Neurosci. 2013;33:1024-37.
    • (2013) J Neurosci , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.-Y.6
  • 73
    • 84999766500 scopus 로고    scopus 로고
    • Unique pathological tau conformers from Alzheimer's brains transmit tau pathology in nontransgenic mice
    • 1:CAS:528:DC%2BC2sXitlWitbo%3D 27810929 5110027
    • Guo JL, Narasimhan S, Changolkar L, He Z, Stieber A, Zhang B, et al. Unique pathological tau conformers from Alzheimer's brains transmit tau pathology in nontransgenic mice. J Exp Med. 2016;213:2635-54.
    • (2016) J Exp Med , vol.213 , pp. 2635-2654
    • Guo, J.L.1    Narasimhan, S.2    Changolkar, L.3    He, Z.4    Stieber, A.5    Zhang, B.6
  • 74
    • 84979283576 scopus 로고    scopus 로고
    • Glial tau pathology in Tauopathies: Functional consequences
    • 26884683
    • Kahlson MA, Colodner KJ. Glial tau pathology in Tauopathies: functional consequences. J Exp Neurosci. 2015;9:43-50.
    • (2015) J Exp Neurosci , vol.9 , pp. 43-50
    • Kahlson, M.A.1    Colodner, K.J.2
  • 75
    • 0032886469 scopus 로고    scopus 로고
    • Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease
    • 1:STN:280:DyaK1MvksFSqtg%3D%3D
    • Komori T. Tau-positive glial inclusions in progressive supranuclear palsy, corticobasal degeneration and Pick's disease. Brain Pathol Zurich Switz. 1999;9:663-79.
    • (1999) Brain Pathol Zurich Switz , vol.9 , pp. 663-679
    • Komori, T.1
  • 76
    • 33749007666 scopus 로고    scopus 로고
    • Ultrastructural characteristics of tau filaments in tauopathies: Immuno-electron microscopic demonstration of tau filaments in tauopathies
    • Arima K. Ultrastructural characteristics of tau filaments in tauopathies: immuno-electron microscopic demonstration of tau filaments in tauopathies. Neuropathol Off J Jpn Soc Neuropathol. 2006;26:475-83.
    • (2006) Neuropathol off J Jpn Soc Neuropathol , vol.26 , pp. 475-483
    • Arima, K.1
  • 77
    • 0028889282 scopus 로고
    • Thorn-shaped astrocytes: Possibly secondarily induced tau-positive glial fibrillary tangles. Acta Neuropathol
    • 1:STN:280:DyaK287ptFOlsg%3D%3D
    • Ikeda K, Akiyama H, Kondo H, Haga C, Tanno E, Tokuda T, et al. Thorn-shaped astrocytes: possibly secondarily induced tau-positive glial fibrillary tangles. Acta Neuropathol. Berl. 1995;90:620-5.
    • (1995) Berl. , vol.90 , pp. 620-625
    • Ikeda, K.1    Akiyama, H.2    Kondo, H.3    Haga, C.4    Tanno, E.5    Tokuda, T.6
  • 78
    • 0036943019 scopus 로고    scopus 로고
    • Tau accumulation in astrocytes in progressive supranuclear palsy is a degenerative rather than a reactive process
    • 1:CAS:528:DC%2BD38XmsFGrtrY%3D 12200627
    • Togo T, Dickson DW. Tau accumulation in astrocytes in progressive supranuclear palsy is a degenerative rather than a reactive process. Acta Neuropathol. Berl. 2002;104:398-402.
    • (2002) Acta Neuropathol. Berl. , vol.104 , pp. 398-402
    • Togo, T.1    Dickson, D.W.2
  • 79
    • 84891831616 scopus 로고    scopus 로고
    • Glial and neuronal tau pathology in tauopathies: Characterization of disease-specific phenotypes and tau pathology progression
    • 1:CAS:528:DC%2BC3sXhvF2ku7nN 24335532
    • Ferrer I, López-González I, Carmona M, Arregui L, Dalfó E, Torrejón-Escribano B, et al. Glial and neuronal tau pathology in tauopathies: characterization of disease-specific phenotypes and tau pathology progression. J Neuropathol Exp Neurol. 2014;73:81-97.
    • (2014) J Neuropathol Exp Neurol , vol.73 , pp. 81-97
    • Ferrer, I.1    López-González, I.2    Carmona, M.3    Arregui, L.4    Dalfó, E.5    Torrejón-Escribano, B.6
  • 80
    • 0029055025 scopus 로고
    • Investigation of tau-2 positive microglia-like cells in the subcortical nuclei of human neurodegenerative disorders
    • 1:CAS:528:DyaK2MXms1yqs7Y%3D 7566636
    • Odawara T, Iseki E, Kosaka K, Akiyama H, Ikeda K, Yamamoto T. Investigation of tau-2 positive microglia-like cells in the subcortical nuclei of human neurodegenerative disorders. Neurosci Lett. 1995;192:145-8.
    • (1995) Neurosci Lett , vol.192 , pp. 145-148
    • Odawara, T.1    Iseki, E.2    Kosaka, K.3    Akiyama, H.4    Ikeda, K.5    Yamamoto, T.6
  • 81
    • 0035011587 scopus 로고    scopus 로고
    • Tau-66: Evidence for a novel tau conformation in Alzheimer's disease
    • 1:CAS:528:DC%2BD3MXkt12qtb8%3D 11389188
    • Ghoshal N, García-Sierra F, Fu Y, Beckett LA, Mufson EJ, Kuret J, et al. Tau-66: evidence for a novel tau conformation in Alzheimer's disease. J Neurochem. 2001;77:1372-85.
    • (2001) J Neurochem , vol.77 , pp. 1372-1385
    • Ghoshal, N.1    García-Sierra, F.2    Fu, Y.3    Beckett, L.A.4    Mufson, E.J.5    Kuret, J.6
  • 84
    • 84966393366 scopus 로고    scopus 로고
    • TREM2 function in Alzheimer's disease and Neurodegeneration
    • 1:CAS:528:DC%2BC28XitFeqtLY%3D 26854967
    • Ulrich JD, Holtzman DM. TREM2 function in Alzheimer's disease and Neurodegeneration. ACS Chem Neurosci. 2016;7:420-7.
    • (2016) ACS Chem Neurosci , vol.7 , pp. 420-427
    • Ulrich, J.D.1    Holtzman, D.M.2
  • 86
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein e type 4 allele and the risk of Alzheimer's disease in late onset families
    • 1:CAS:528:DyaK3sXmtVWjur8%3D 8346443
    • Corder EH, Saunders AM, Strittmatter WJ, Schmechel DE, Gaskell PC, Small GW, et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science. 1993;261:921-3.
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3    Schmechel, D.E.4    Gaskell, P.C.5    Small, G.W.6
  • 87
    • 79959772357 scopus 로고    scopus 로고
    • Human apoE isoforms differentially regulate brain amyloid-β peptide clearance
    • 1:CAS:528:DC%2BC3MXhtFOisL7J 21715678 3192364
    • Castellano JM, Kim J, Stewart FR, Jiang H, DeMattos RB, Patterson BW, et al. Human apoE isoforms differentially regulate brain amyloid-β peptide clearance. Sci Transl Med. 2011;3:89ra57.
    • (2011) Sci Transl Med , vol.3 , pp. 89ra57
    • Castellano, J.M.1    Kim, J.2    Stewart, F.R.3    Jiang, H.4    DeMattos, R.B.5    Patterson, B.W.6
  • 88
    • 0029043032 scopus 로고
    • Apolipoprotein e polymorphism influences not only cerebral senile plaque load but also Alzheimer-type neurofibrillary tangle formation
    • 1:CAS:528:DyaK2MXlvVahtrk%3D 7644022
    • Ohm TG, Kirca M, Bohl J, Scharnagl H, Gross W, März W. Apolipoprotein E polymorphism influences not only cerebral senile plaque load but also Alzheimer-type neurofibrillary tangle formation. Neuroscience. 1995;66:583-7.
    • (1995) Neuroscience , vol.66 , pp. 583-587
    • Ohm, T.G.1    Kirca, M.2    Bohl, J.3    Scharnagl, H.4    Gross, W.5    März, W.6
  • 89
    • 84880424719 scopus 로고    scopus 로고
    • Apolipoprotein e ϵ4 frequency is increased among Chinese patients with Frontotemporal dementia and Alzheimer's disease
    • 1:CAS:528:DC%2BC3sXhsFelsLrL 23887281 4068025
    • Ji Y, Liu M, Huo YR, Liu S, Shi Z, Liu S, et al. Apolipoprotein E ϵ4 frequency is increased among Chinese patients with Frontotemporal dementia and Alzheimer's disease. Dement Geriatr Cogn Disord. 2013;36:163-70.
    • (2013) Dement Geriatr Cogn Disord , vol.36 , pp. 163-170
    • Ji, Y.1    Liu, M.2    Huo, Y.R.3    Liu, S.4    Shi, Z.5    Liu, S.6
  • 90
    • 0035072923 scopus 로고    scopus 로고
    • Clinic-based cases with frontotemporal dementia show increased cerebrospinal fluid tau and high apolipoprotein e epsilon4 frequency, but no tau gene mutations
    • 1:STN:280:DC%2BD3M7mtFOgug%3D%3D 11259129
    • Fabre SF, Forsell C, Viitanen M, Sjögren M, Wallin A, Blennow K, et al. Clinic-based cases with frontotemporal dementia show increased cerebrospinal fluid tau and high apolipoprotein E epsilon4 frequency, but no tau gene mutations. Exp Neurol. 2001;168:413-8.
    • (2001) Exp Neurol , vol.168 , pp. 413-418
    • Fabre, S.F.1    Forsell, C.2    Viitanen, M.3    Sjögren, M.4    Wallin, A.5    Blennow, K.6
  • 91
    • 60549114681 scopus 로고    scopus 로고
    • Apolipoprotein e ϵ4 is associated with disease-specific effects on brain atrophy in Alzheimer's disease and frontotemporal dementia
    • 1:CAS:528:DC%2BD1MXitVKksr4%3D 19164761 2644156
    • Agosta F, Vossel KA, Miller BL, Migliaccio R, Bonasera SJ, Filippi M, et al. Apolipoprotein E ϵ4 is associated with disease-specific effects on brain atrophy in Alzheimer's disease and frontotemporal dementia. Proc Natl Acad Sci U S A. 2009;106:2018-22.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2018-2022
    • Agosta, F.1    Vossel, K.A.2    Miller, B.L.3    Migliaccio, R.4    Bonasera, S.J.5    Filippi, M.6
  • 92
    • 84957604608 scopus 로고    scopus 로고
    • Genetic and Transcriptomic Profiles of Inflammation in Neurodegenerative Diseases: Alzheimer, Parkinson, Creutzfeldt-Jakob and Tauopathies
    • [cited 2017 Feb 27]
    • López González I, Garcia-Esparcia P, Llorens F, Ferrer I. Genetic and Transcriptomic Profiles of Inflammation in Neurodegenerative Diseases: Alzheimer, Parkinson, Creutzfeldt-Jakob and Tauopathies. Int J Mol Sci. [Internet]. 2016 [cited 2017 Feb 27];17. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4783939/.
    • (2016) Int J Mol Sci. [Internet] , vol.17
    • López González, I.1    Garcia-Esparcia, P.2    Llorens, F.3    Ferrer, I.4
  • 93
    • 84943174081 scopus 로고    scopus 로고
    • Genetics ignite focus on microglial inflammation in Alzheimer's disease
    • 26438529 4595327
    • Malik M, Parikh I, Vasquez JB, Smith C, Tai L, Bu G, et al. Genetics ignite focus on microglial inflammation in Alzheimer's disease. Mol Neurodegener. 2015;10:52.
    • (2015) Mol Neurodegener , vol.10 , pp. 52
    • Malik, M.1    Parikh, I.2    Vasquez, J.B.3    Smith, C.4    Tai, L.5    Bu, G.6
  • 94
    • 84878433339 scopus 로고    scopus 로고
    • Alzheimer's disease risk gene CD33 inhibits microglial uptake of amyloid beta
    • 1:CAS:528:DC%2BC3sXmvVWiu70%3D 23623698 3706457
    • Griciuc A, Serrano-Pozo A, Parrado AR, Lesinski AN, Asselin CN, Mullin K, et al. Alzheimer's disease risk gene CD33 inhibits microglial uptake of amyloid beta. Neuron. 2013;78:631-43.
    • (2013) Neuron , vol.78 , pp. 631-643
    • Griciuc, A.1    Serrano-Pozo, A.2    Parrado, A.R.3    Lesinski, A.N.4    Asselin, C.N.5    Mullin, K.6
  • 95
    • 0036678856 scopus 로고    scopus 로고
    • Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease
    • 1:CAS:528:DC%2BD38Xmt1ChtLc%3D 12145324 125060
    • DeMattos RB, O'dell MA, Parsadanian M, Taylor JW, Harmony JAK, Bales KR, et al. Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A. 2002;99:10843-8.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10843-10848
    • DeMattos, R.B.1    O'Dell, M.A.2    Parsadanian, M.3    Taylor, J.W.4    Harmony, J.A.K.5    Bales, K.R.6
  • 96
    • 84952979499 scopus 로고    scopus 로고
    • The first NINDS/NIBIB consensus meeting to define neuropathological criteria for the diagnosis of chronic traumatic encephalopathy
    • 1:CAS:528:DC%2BC2MXitVenu7%2FN 26667418
    • McKee AC, Cairns NJ, Dickson DW, Folkerth RD, Keene CD, Litvan I, et al. The first NINDS/NIBIB consensus meeting to define neuropathological criteria for the diagnosis of chronic traumatic encephalopathy. Acta Neuropathol Berl. 2016;131:75-86.
    • (2016) Acta Neuropathol Berl , vol.131 , pp. 75-86
    • McKee, A.C.1    Cairns, N.J.2    Dickson, D.W.3    Folkerth, R.D.4    Keene, C.D.5    Litvan, I.6
  • 98
    • 84920949798 scopus 로고    scopus 로고
    • Neuroinflammatory responses to traumatic brain injury: Etiology, clinical consequences, and therapeutic opportunities
    • 1:CAS:528:DC%2BC28XhsVWgur3E 25657582 4295534
    • Lozano D, Gonzales-Portillo GS, Acosta S, de la Pena I, Tajiri N, Kaneko Y, et al. Neuroinflammatory responses to traumatic brain injury: etiology, clinical consequences, and therapeutic opportunities. Neuropsychiatr Dis Treat. 2015;11:97-106.
    • (2015) Neuropsychiatr Dis Treat , vol.11 , pp. 97-106
    • Lozano, D.1    Gonzales-Portillo, G.S.2    Acosta, S.3    De La Pena, I.4    Tajiri, N.5    Kaneko, Y.6
  • 99
    • 85013813587 scopus 로고    scopus 로고
    • Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy
    • [Internet] [cited 2017 Feb 27]
    • Cherry JD, Tripodis Y, Alvarez VE, Huber B, Kiernan PT, Daneshvar DH, et al. Microglial neuroinflammation contributes to tau accumulation in chronic traumatic encephalopathy. Acta Neuropathol. Commun. [Internet]. 2016 [cited 2017 Feb 27];4. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5084333/.
    • (2016) Acta Neuropathol. Commun. , vol.4
    • Cherry, J.D.1    Tripodis, Y.2    Alvarez, V.E.3    Huber, B.4    Kiernan, P.T.5    Daneshvar, D.H.6
  • 100
    • 81855199724 scopus 로고    scopus 로고
    • The role of environmental exposures in neurodegeneration and neurodegenerative diseases
    • 1:CAS:528:DC%2BC3MXhsFSkt77O
    • Cannon JR, Greenamyre JT. The role of environmental exposures in neurodegeneration and neurodegenerative diseases. Toxicol Sci Off J Soc Toxicol. 2011;124:225-50.
    • (2011) Toxicol Sci off J Soc Toxicol , vol.124 , pp. 225-250
    • Cannon, J.R.1    Greenamyre, J.T.2
  • 101
    • 85010284850 scopus 로고    scopus 로고
    • Neuronal cell death and degeneration through increased Nitroxidative stress and tau Phosphorylation in HIV-1 transgenic rats
    • e0169945 28107387 5249108
    • Cho Y-E, Lee M-H, Song B-J. Neuronal cell death and degeneration through increased Nitroxidative stress and tau Phosphorylation in HIV-1 transgenic rats. PLoS One. 2017;12:e0169945.
    • (2017) PLoS One , vol.12
    • Cho, Y.-E.1    Lee, M.-H.2    Song, B.-J.3
  • 102
    • 0034938031 scopus 로고    scopus 로고
    • Experimenting on the past: The enigma of von Economo's encephalitis lethargica
    • 1:STN:280:DC%2BD3MzptVGlsQ%3D%3D 11444794
    • Reid AH, McCall S, Henry JM, Taubenberger JK. Experimenting on the past: the enigma of von Economo's encephalitis lethargica. J Neuropathol Exp Neurol. 2001;60:663-70.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 663-670
    • Reid, A.H.1    McCall, S.2    Henry, J.M.3    Taubenberger, J.K.4
  • 103
    • 33947727192 scopus 로고    scopus 로고
    • Interleukins, inflammation, and mechanisms of Alzheimer's disease
    • 1:CAS:528:DC%2BD1cXjslWrtrk%3D 17027528
    • Weisman D, Hakimian E, Ho GJ. Interleukins, inflammation, and mechanisms of Alzheimer's disease. Vitam Horm. 2006;74:505-30.
    • (2006) Vitam Horm , vol.74 , pp. 505-530
    • Weisman, D.1    Hakimian, E.2    Ho, G.J.3
  • 105
    • 85015484234 scopus 로고    scopus 로고
    • Role of pro-inflammatory cytokines released from microglia in Alzheimer's disease
    • [Internet] [cited 2017 Mar 6]
    • Wang W-Y, Tan M-S, Yu J-T, Tan L. Role of pro-inflammatory cytokines released from microglia in Alzheimer's disease. Ann Transl Med. [Internet]. 2015 [cited 2017 Mar 6];3. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486922/.
    • (2015) Ann Transl Med , vol.3
    • Wang, W.-Y.1    Tan, M.-S.2    Yu, J.-T.3    Tan, L.4
  • 108
    • 0036098247 scopus 로고    scopus 로고
    • Cerebrovascular transforming growth factor-β contributes to inflammation in the Alzheimer's disease brain
    • 1:CAS:528:DC%2BD38XksVKrtL8%3D 12000710 1850858
    • Grammas P, Ovase R. Cerebrovascular transforming growth factor-β contributes to inflammation in the Alzheimer's disease brain. Am J Pathol. 2002;160:1583-7.
    • (2002) Am J Pathol , vol.160 , pp. 1583-1587
    • Grammas, P.1    Ovase, R.2
  • 109
    • 84873087532 scopus 로고    scopus 로고
    • NLRP3 is activated in Alzheimer's disease and contributes to pathology in APP/PS1 mice
    • 1:CAS:528:DC%2BC38XhvV2ntLfM 23254930
    • Heneka MT, Kummer MP, Stutz A, Delekate A, Schwartz S, Saecker A, et al. NLRP3 is activated in Alzheimer's disease and contributes to pathology in APP/PS1 mice. Nature. 2013;493:674-8.
    • (2013) Nature , vol.493 , pp. 674-678
    • Heneka, M.T.1    Kummer, M.P.2    Stutz, A.3    Delekate, A.4    Schwartz, S.5    Saecker, A.6
  • 110
    • 84936129121 scopus 로고    scopus 로고
    • Microglial cell dysregulation in brain aging and neurodegeneration. Front
    • [Internet] [cited 2017 Mar 6]
    • von Bernhardi R, Eugenín-von Bernhardi L, Eugenín J. Microglial cell dysregulation in brain aging and neurodegeneration. Front. Aging Neurosci. [Internet]. 2015 [cited 2017 Mar 6];7. Available from: https://www.ncbi.nlm.nih.gov/pubmed/26257642.
    • (2015) Aging Neurosci , vol.7
    • Von Bernhardi, R.1    Eugenín-Von Bernhardi, L.2    Eugenín, J.3
  • 111
    • 79953004994 scopus 로고    scopus 로고
    • In vivo positron emission tomographic imaging of glial responses to amyloid-beta and tau pathologies in mouse models of Alzheimer's disease and related disorders
    • 1:CAS:528:DC%2BC3MXktVKrtbk%3D 21430171 3251921
    • Maeda J, Zhang M-R, Okauchi T, Ji B, Ono M, Hattori S, et al. In vivo positron emission tomographic imaging of glial responses to amyloid-beta and tau pathologies in mouse models of Alzheimer's disease and related disorders. J Neurosci. 2011;31:4720-30.
    • (2011) J Neurosci , vol.31 , pp. 4720-4730
    • Maeda, J.1    Zhang, M.-R.2    Okauchi, T.3    Ji, B.4    Ono, M.5    Hattori, S.6
  • 112
  • 113
    • 84931271049 scopus 로고    scopus 로고
    • Mapping neuroinflammation in frontotemporal dementia with molecular PET imaging
    • [Internet] [cited 2017 Feb 27]
    • Zhang J. Mapping neuroinflammation in frontotemporal dementia with molecular PET imaging. J Neuroinflammation [Internet]. 2015 [cited 2017 Feb 27];12. Available from: https://www.ncbi.nlm.nih.gov/pubmed/26022249.
    • (2015) J Neuroinflammation , vol.12
    • Zhang, J.1
  • 114
    • 84872399695 scopus 로고    scopus 로고
    • 18F-fluorodeoxyglucose labeling: A review of the preclinical and clinical applications in cell-based diagnosis and therapy
    • 23206605
    • 18F-fluorodeoxyglucose labeling: a review of the preclinical and clinical applications in cell-based diagnosis and therapy. Clin Imaging. 2013;37:28-36.
    • (2013) Clin Imaging , vol.37 , pp. 28-36
    • Wu, C.1    Ma, G.2    Li, J.3    Zheng, K.4    Dang, Y.5    Shi, X.6
  • 115
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • 1:CAS:528:DC%2BD2sXitVektbk%3D 17270732
    • Yoshiyama Y, Higuchi M, Zhang B, Huang S-M, Iwata N, Saido TC, et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron. 2007;53:337-51.
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3    Huang, S.-M.4    Iwata, N.5    Saido, T.C.6
  • 116
    • 84930966153 scopus 로고    scopus 로고
    • Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody
    • 26057852 4460904
    • Luo W, Liu W, Hu X, Hanna M, Caravaca A, Paul SM. Microglial internalization and degradation of pathological tau is enhanced by an anti-tau monoclonal antibody. Sci Rep. 2015;5:11161.
    • (2015) Sci Rep , vol.5 , pp. 11161
    • Luo, W.1    Liu, W.2    Hu, X.3    Hanna, M.4    Caravaca, A.5    Paul, S.M.6
  • 117
    • 84931577633 scopus 로고    scopus 로고
    • Identification of preclinical Alzheimer's disease by a profile of pathogenic proteins in neurally derived blood exosomes: A case-control study. Alzheimers dement
    • Fiandaca MS, Kapogiannis D, Mapstone M, Boxer A, Eitan E, Schwartz JB, et al. Identification of preclinical Alzheimer's disease by a profile of pathogenic proteins in neurally derived blood exosomes: a case-control study. Alzheimers dement. J Alzheimers Assoc. 2015;11:600-607.e1.
    • (2015) J Alzheimers Assoc , vol.11 , pp. 600e1
    • Fiandaca, M.S.1    Kapogiannis, D.2    Mapstone, M.3    Boxer, A.4    Eitan, E.5    Schwartz, J.B.6
  • 119
    • 83755183781 scopus 로고    scopus 로고
    • Blocking IL-1 signaling rescues cognition, attenuates tau pathology, and restores neuronal β-catenin pathway function in an Alzheimer's disease model
    • Kitazawa M, Cheng D, Tsukamoto MR, Koike MA, Wes PD, Vasilevko V, et al. Blocking IL-1 signaling rescues cognition, attenuates tau pathology, and restores neuronal β-catenin pathway function in an Alzheimer's disease model. J Immunol. 2011:187, 6539-6149.
    • (2011) J Immunol , vol.187 , pp. 6149-6539
    • Kitazawa, M.1    Cheng, D.2    Tsukamoto, M.R.3    Ma, K.4    Wes, P.D.5    Vasilevko, V.6
  • 120
    • 44149085664 scopus 로고    scopus 로고
    • S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells
    • 1:CAS:528:DC%2BD1cXotlCrtLs%3D 18494933 3538024
    • Esposito G, Scuderi C, Lu J, Savani C, De Filippis D, Iuvone T, et al. S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells. J Cell Mol Med. 2008;12:914-27.
    • (2008) J Cell Mol Med , vol.12 , pp. 914-927
    • Esposito, G.1    Scuderi, C.2    Lu, J.3    Savani, C.4    De Filippis, D.5    Iuvone, T.6
  • 123
  • 124
    • 19944432508 scopus 로고    scopus 로고
    • Accumulation of filamentous tau in the cerebral cortex of human tau R406W transgenic mice
    • 1:CAS:528:DC%2BD2MXitVGmsrc%3D 15681835 1602315
    • Ikeda M, Shoji M, Kawarai T, Kawarabayashi T, Matsubara E, Murakami T, et al. Accumulation of filamentous tau in the cerebral cortex of human tau R406W transgenic mice. Am J Pathol. 2005;166:521-31.
    • (2005) Am J Pathol , vol.166 , pp. 521-531
    • Ikeda, M.1    Shoji, M.2    Kawarai, T.3    Kawarabayashi, T.4    Matsubara, E.5    Murakami, T.6
  • 125
    • 34548145867 scopus 로고    scopus 로고
    • The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model
    • 1:CAS:528:DC%2BD2sXhtVSnsLbJ 17715352
    • Dawson HN, Cantillana V, Chen L, Vitek MP. The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model. J Neurosci. 2007;27:9155-68.
    • (2007) J Neurosci , vol.27 , pp. 9155-9168
    • Dawson, H.N.1    Cantillana, V.2    Chen, L.3    Vitek, M.P.4
  • 126
    • 17044411592 scopus 로고    scopus 로고
    • Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration
    • 1:CAS:528:DC%2BD2MXjtlSju7Y%3D 15814784
    • Forman MS, Lal D, Zhang B, Dabir DV, Swanson E, Lee VM-Y, et al. Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration. J Neurosci. 2005;25:3539-50.
    • (2005) J Neurosci , vol.25 , pp. 3539-3550
    • Forman, M.S.1    Lal, D.2    Zhang, B.3    Dabir, D.V.4    Swanson, E.5    Lee, V.M.-Y.6
  • 127
    • 78649723354 scopus 로고    scopus 로고
    • Glial fibrillary tangles and JAK/STAT-mediated glial and neuronal cell death in a drosophila model of glial tauopathy
    • 1:CAS:528:DC%2BC3cXhs1SlurvN 21123557 3073608
    • Colodner KJ, Feany MB. Glial fibrillary tangles and JAK/STAT-mediated glial and neuronal cell death in a drosophila model of glial tauopathy. J Neurosci. 2010;30:16102-13.
    • (2010) J Neurosci , vol.30 , pp. 16102-16113
    • Colodner, K.J.1    Feany, M.B.2
  • 128
    • 0032805573 scopus 로고    scopus 로고
    • Immunohistochemical localization of interleukin-1beta, interleukin-1 receptor antagonist and interleukin-1beta converting enzyme/caspase-1 in the rat brain after peripheral administration of kainic acid
    • 1:CAS:528:DyaK1MXltlKmtrw%3D 10473257
    • Eriksson C, Van Dam AM, Lucassen PJ, Bol JG, Winblad B, Schultzberg M. Immunohistochemical localization of interleukin-1beta, interleukin-1 receptor antagonist and interleukin-1beta converting enzyme/caspase-1 in the rat brain after peripheral administration of kainic acid. Neuroscience. 1999;93:915-30.
    • (1999) Neuroscience , vol.93 , pp. 915-930
    • Eriksson, C.1    Van Dam, A.M.2    Lucassen, P.J.3    Bol, J.G.4    Winblad, B.5    Schultzberg, M.6
  • 129
    • 42649084052 scopus 로고    scopus 로고
    • The role of interleukin-1 in neuroinflammation and Alzheimer disease: An evolving perspective
    • 18302763 2335091
    • Shaftel SS, Griffin WST, O'Banion MK. The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective. J Neuroinflammation. 2008;5:7.
    • (2008) J Neuroinflammation , vol.5 , pp. 7
    • Shaftel, S.S.1    Griffin, W.S.T.2    O'Banion, M.K.3
  • 130
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • 1:CAS:528:DC%2BD1cXoslCmu74%3D 18604209 3101478
    • Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 2008;9:857-65.
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3    Stewart, C.R.4    Monks, B.G.5    Reinheckel, T.6
  • 131
    • 84874882726 scopus 로고    scopus 로고
    • Sustained interleukin-1β overexpression exacerbates tau pathology despite reduced amyloid burden in an Alzheimer's mouse model
    • 1:CAS:528:DC%2BC3sXhtlOjs7nM 23486975 3637949
    • Ghosh S, Wu MD, Shaftel SS, Kyrkanides S, LaFerla FM, Olschowka JA, et al. Sustained interleukin-1β overexpression exacerbates tau pathology despite reduced amyloid burden in an Alzheimer's mouse model. J Neurosci. 2013;33:5053-64.
    • (2013) J Neurosci , vol.33 , pp. 5053-5064
    • Ghosh, S.1    Wu, M.D.2    Shaftel, S.S.3    Kyrkanides, S.4    LaFerla, F.M.5    Olschowka, J.A.6
  • 132
    • 0037336701 scopus 로고    scopus 로고
    • Interleukin-1 mediates pathological effects of microglia on tau Phosphorylation and on Synaptophysin synthesis in cortical neurons through a p38-MAPK pathway
    • 1:CAS:528:DC%2BD3sXjtFylt7c%3D 12629164 3833596
    • Li Y, Liu L, Barger SW, Griffin WST. Interleukin-1 mediates pathological effects of microglia on tau Phosphorylation and on Synaptophysin synthesis in cortical neurons through a p38-MAPK pathway. J Neurosci. 2003;23:1605-11.
    • (2003) J Neurosci , vol.23 , pp. 1605-1611
    • Li, Y.1    Liu, L.2    Barger, S.W.3    Griffin, W.S.T.4
  • 134
    • 25644456097 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclin-dependent kinase 5-mediated pathway in a transgenic model of Alzheimer's disease
    • 1:CAS:528:DC%2BD2MXhtVOqs7rP 16192374
    • Kitazawa M, Oddo S, Yamasaki TR, Green KN, LaFerla FM. Lipopolysaccharide-induced inflammation exacerbates tau pathology by a cyclin-dependent kinase 5-mediated pathway in a transgenic model of Alzheimer's disease. J Neurosci. 2005;25:8843-53.
    • (2005) J Neurosci , vol.25 , pp. 8843-8853
    • Kitazawa, M.1    Oddo, S.2    Yamasaki, T.R.3    Green, K.N.4    LaFerla, F.M.5
  • 135
    • 84920937355 scopus 로고    scopus 로고
    • SIRT1 deficiency in microglia contributes to cognitive decline in aging and neurodegeneration via epigenetic regulation of IL-1β
    • 25589773 4293425
    • Cho S-H, Chen JA, Sayed F, Ward ME, Gao F, Nguyen TA, et al. SIRT1 deficiency in microglia contributes to cognitive decline in aging and neurodegeneration via epigenetic regulation of IL-1β. J Neurosci. 2015;35:807-18.
    • (2015) J Neurosci , vol.35 , pp. 807-818
    • Cho, S.-H.1    Chen, J.A.2    Sayed, F.3    Ward, M.E.4    Gao, F.5    Nguyen, T.A.6
  • 137
    • 84938709394 scopus 로고    scopus 로고
    • Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain
    • 25833819 4542622
    • Maphis N, Xu G, Kokiko-Cochran ON, Jiang S, Cardona A, Ransohoff RM, et al. Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain. Brain. 2015;138:1738-55.
    • (2015) Brain , vol.138 , pp. 1738-1755
    • Maphis, N.1    Xu, G.2    Kokiko-Cochran, O.N.3    Jiang, S.4    Cardona, A.5    Ransohoff, R.M.6
  • 139
    • 33747379123 scopus 로고    scopus 로고
    • Up-regulation of BDNF in astrocytes by TNF-alpha: A case for the neuroprotective role of cytokine
    • 18040799 2131740
    • Saha RN, Liu X, Pahan K. Up-regulation of BDNF in astrocytes by TNF-alpha: a case for the neuroprotective role of cytokine. J NeuroImmune Pharmacol. 2006;1:212-22.
    • (2006) J NeuroImmune Pharmacol , vol.1 , pp. 212-222
    • Saha, R.N.1    Liu, X.2    Pahan, K.3
  • 141
    • 68949205705 scopus 로고    scopus 로고
    • Tumour necrosis factor modulation for treatment of Alzheimer's disease: Rationale and current evidence
    • 1:CAS:528:DC%2BD1MXht1KiurjI 19689163
    • Tobinick E. Tumour necrosis factor modulation for treatment of Alzheimer's disease: rationale and current evidence. CNS Drugs. 2009;23:713-25.
    • (2009) CNS Drugs , vol.23 , pp. 713-725
    • Tobinick, E.1
  • 142
    • 77953136143 scopus 로고    scopus 로고
    • TNF receptor 2 pathway: Drug target for autoimmune diseases
    • 1:CAS:528:DC%2BC3cXmtlamtr0%3D 20489699
    • Faustman D, Davis M. TNF receptor 2 pathway: drug target for autoimmune diseases. Nat Rev Drug Discov. 2010;9:482-93.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 482-493
    • Faustman, D.1    Davis, M.2
  • 143
    • 80052811773 scopus 로고    scopus 로고
    • JNK plays a key role in tau hyperphosphorylation in Alzheimer's disease models
    • 1:CAS:528:DC%2BC3MXhtFeks7fF 21628793
    • Ploia C, Antoniou X, Sclip A, Grande V, Cardinetti D, Colombo A, et al. JNK plays a key role in tau hyperphosphorylation in Alzheimer's disease models. J Alzheimers Dis. 2011;26:315-29.
    • (2011) J Alzheimers Dis , vol.26 , pp. 315-329
    • Ploia, C.1    Antoniou, X.2    Sclip, A.3    Grande, V.4    Cardinetti, D.5    Colombo, A.6
  • 144
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • 1:STN:280:DyaK2s3lsFeitA%3D%3D 9100663
    • Dickson DW. The pathogenesis of senile plaques. J Neuropathol Exp Neurol. 1997;56:321-39.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 145
    • 0032868874 scopus 로고    scopus 로고
    • Intracerebral production of tumor necrosis factor-alpha, a local neuroprotective agent, in Alzheimer disease and vascular dementia
    • 1:CAS:528:DyaK1MXmsFCmurY%3D 10471976
    • Tarkowski E, Blennow K, Wallin A, Tarkowski A. Intracerebral production of tumor necrosis factor-alpha, a local neuroprotective agent, in Alzheimer disease and vascular dementia. J Clin Immunol. 1999;19:223-30.
    • (1999) J Clin Immunol , vol.19 , pp. 223-230
    • Tarkowski, E.1    Blennow, K.2    Wallin, A.3    Tarkowski, A.4
  • 146
    • 0141740742 scopus 로고    scopus 로고
    • Intrathecal inflammation precedes development of Alzheimer's disease
    • 1:STN:280:DC%2BD3svks1elsA%3D%3D 12933918 1738668
    • Tarkowski E, Andreasen N, Tarkowski A, Blennow K. Intrathecal inflammation precedes development of Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2003;74:1200-5.
    • (2003) J Neurol Neurosurg Psychiatry , vol.74 , pp. 1200-1205
    • Tarkowski, E.1    Andreasen, N.2    Tarkowski, A.3    Blennow, K.4
  • 147
    • 1242274383 scopus 로고    scopus 로고
    • Tumor necrosis factor death receptor signaling cascade is required for amyloid-beta protein-induced neuron death
    • 1:CAS:528:DC%2BD2cXhvVCnsrs%3D 14973251
    • Li R, Yang L, Lindholm K, Konishi Y, Yue X, Hampel H, et al. Tumor necrosis factor death receptor signaling cascade is required for amyloid-beta protein-induced neuron death. J Neurosci. 2004;24:1760-71.
    • (2004) J Neurosci , vol.24 , pp. 1760-1771
    • Li, R.1    Yang, L.2    Lindholm, K.3    Konishi, Y.4    Yue, X.5    Hampel, H.6
  • 148
    • 57149101898 scopus 로고    scopus 로고
    • Chronic neuron-specific tumor necrosis factor-alpha expression enhances the local inflammatory environment ultimately leading to neuronal death in 3xTg-AD mice
    • 1:CAS:528:DC%2BD1MXkt1Cqsw%3D%3D 18974297 2626388
    • Janelsins MC, Mastrangelo MA, Park KM, Sudol KL, Narrow WC, Oddo S, et al. Chronic neuron-specific tumor necrosis factor-alpha expression enhances the local inflammatory environment ultimately leading to neuronal death in 3xTg-AD mice. Am J Pathol. 2008;173:1768-82.
    • (2008) Am J Pathol , vol.173 , pp. 1768-1782
    • Janelsins, M.C.1    Mastrangelo, M.A.2    Park, K.M.3    Sudol, K.L.4    Narrow, W.C.5    Oddo, S.6
  • 149
    • 80053268668 scopus 로고    scopus 로고
    • Ablation of TNF-RI/RII expression in Alzheimer's disease mice leads to an unexpected enhancement of pathology: Implications for chronic pan-TNF-α suppressive therapeutic strategies in the brain
    • 1:CAS:528:DC%2BC3MXhsVSqtbnP 21835156 3181376
    • Montgomery SL, Mastrangelo MA, Habib D, Narrow WC, Knowlden SA, Wright TW, et al. Ablation of TNF-RI/RII expression in Alzheimer's disease mice leads to an unexpected enhancement of pathology: implications for chronic pan-TNF-α suppressive therapeutic strategies in the brain. Am J Pathol. 2011;179:2053-70.
    • (2011) Am J Pathol , vol.179 , pp. 2053-2070
    • Montgomery, S.L.1    Mastrangelo, M.A.2    Habib, D.3    Narrow, W.C.4    Knowlden, S.A.5    Wright, T.W.6
  • 150
    • 68849123079 scopus 로고    scopus 로고
    • Accumulation of tau induced in neurites by microglial proinflammatory mediators
    • 1:CAS:528:DC%2BD1MXpvFOltrc%3D 19289607
    • Gorlovoy P, Larionov S, Pham TTH, Neumann H. Accumulation of tau induced in neurites by microglial proinflammatory mediators. FASEB J. 2009;23:2502-13.
    • (2009) FASEB J , vol.23 , pp. 2502-2513
    • Gorlovoy, P.1    Larionov, S.2    Pham, T.T.H.3    Neumann, H.4
  • 151
    • 0034234414 scopus 로고    scopus 로고
    • Comparative evaluation of cytokine profiles and reactive gliosis supports a critical role for interleukin-6 in neuron-glia signaling during regeneration
    • 1:CAS:528:DC%2BD3cXksF2iu74%3D 10861795
    • Streit WJ, Hurley SD, McGraw TS, Semple-Rowland SL. Comparative evaluation of cytokine profiles and reactive gliosis supports a critical role for interleukin-6 in neuron-glia signaling during regeneration. J Neurosci Res. 2000;61:10-20.
    • (2000) J Neurosci Res , vol.61 , pp. 10-20
    • Streit, W.J.1    Hurley, S.D.2    McGraw, T.S.3    Semple-Rowland, S.L.4
  • 152
    • 0028012270 scopus 로고
    • Reactive astrogliosis in the neonatal mouse brain and its modulation by cytokines
    • 1:CAS:528:DyaK2cXhvV2gtbo%3D 8301364
    • Balasingam V, Tejada-Berges T, Wright E, Bouckova R, Yong VW. Reactive astrogliosis in the neonatal mouse brain and its modulation by cytokines. J Neurosci. 1994;14:846-56.
    • (1994) J Neurosci , vol.14 , pp. 846-856
    • Balasingam, V.1    Tejada-Berges, T.2    Wright, E.3    Bouckova, R.4    Yong, V.W.5
  • 153
    • 0038017110 scopus 로고    scopus 로고
    • Brain activation of monocyte-lineage cells: Involvement of interleukin-6
    • 12759566
    • Shafer LL, McNulty JA, Young MRI. Brain activation of monocyte-lineage cells: involvement of interleukin-6. Neuroimmunomodulation. 2002;10:295-304.
    • (2002) Neuroimmunomodulation , vol.10 , pp. 295-304
    • Shafer, L.L.1    McNulty, J.A.2    Young, M.R.I.3
  • 155
    • 0033876817 scopus 로고    scopus 로고
    • Cytokine gene expression as a function of the clinical progression of Alzheimer disease dementia
    • 1:STN:280:DC%2BD3cvisVWktw%3D%3D 10927795
    • Luterman JD, Haroutunian V, Yemul S, Ho L, Purohit D, Aisen PS, et al. Cytokine gene expression as a function of the clinical progression of Alzheimer disease dementia. Arch Neurol. 2000;57:1153-60.
    • (2000) Arch Neurol , vol.57 , pp. 1153-1160
    • Luterman, J.D.1    Haroutunian, V.2    Yemul, S.3    Ho, L.4    Purohit, D.5    Aisen, P.S.6
  • 156
    • 0037072285 scopus 로고    scopus 로고
    • Interleukin-6 and risk of cognitive decline: Mac Arthur studies of successful aging
    • 1:CAS:528:DC%2BD38XmvVarurk%3D 12177370
    • Weaver JD, Huang M-H, Albert M, Harris T, Rowe JW, Seeman TE. Interleukin-6 and risk of cognitive decline: Mac Arthur studies of successful aging. Neurology. 2002;59:371-8.
    • (2002) Neurology , vol.59 , pp. 371-378
    • Weaver, J.D.1    Huang, M.-H.2    Albert, M.3    Harris, T.4    Rowe, J.W.5    Seeman, T.E.6
  • 157
    • 76149092520 scopus 로고    scopus 로고
    • Massive gliosis induced by interleukin-6 suppresses Abeta deposition in vivo: Evidence against inflammation as a driving force for amyloid deposition
    • 1:CAS:528:DC%2BC3cXhs1Ggsr4%3D 19825975 3083918
    • Chakrabarty P, Jansen-West K, Beccard A, Ceballos-Diaz C, Levites Y, Verbeeck C, et al. Massive gliosis induced by interleukin-6 suppresses Abeta deposition in vivo: evidence against inflammation as a driving force for amyloid deposition. FASEB J. 2010;24:548-59.
    • (2010) FASEB J , vol.24 , pp. 548-559
    • Chakrabarty, P.1    Jansen-West, K.2    Beccard, A.3    Ceballos-Diaz, C.4    Levites, Y.5    Verbeeck, C.6
  • 158
    • 1642420308 scopus 로고    scopus 로고
    • Interleukin-6 induces Alzheimer-type phosphorylation of tau protein by deregulating the cdk5/p35 pathway
    • 1:CAS:528:DC%2BD2cXis1Wgs7w%3D 15051507
    • Quintanilla RA, Orellana DI, González-Billault C, Maccioni RB. Interleukin-6 induces Alzheimer-type phosphorylation of tau protein by deregulating the cdk5/p35 pathway. Exp Cell Res. 2004;295:245-57.
    • (2004) Exp Cell Res , vol.295 , pp. 245-257
    • Quintanilla, R.A.1    Orellana, D.I.2    González-Billault, C.3    Maccioni, R.B.4
  • 159
    • 33645942122 scopus 로고    scopus 로고
    • Role of the JAKs/STATs pathway in the intracellular calcium changes induced by interleukin-6 in hippocampal neurons
    • 1:CAS:528:DC%2BD28XhtFKiurnF 16371324
    • Orellana DI, Quintanilla RA, Gonzalez-Billault C, Maccioni RB. Role of the JAKs/STATs pathway in the intracellular calcium changes induced by interleukin-6 in hippocampal neurons. Neurotox Res. 2005;8:295-304.
    • (2005) Neurotox Res , vol.8 , pp. 295-304
    • Orellana, D.I.1    Quintanilla, R.A.2    Gonzalez-Billault, C.3    Maccioni, R.B.4
  • 160
    • 79960447858 scopus 로고    scopus 로고
    • Complement in the brain
    • 1:CAS:528:DC%2BC3MXpt1ahur8%3D 21546088 3142281
    • Veerhuis R, Nielsen HM, Tenner AJ. Complement in the brain. Mol Immunol. 2011;48:1592-603.
    • (2011) Mol Immunol , vol.48 , pp. 1592-1603
    • Veerhuis, R.1    Nielsen, H.M.2    Tenner, A.J.3
  • 161
    • 0029053689 scopus 로고
    • Complement expression in human brain. Biosynthesis of terminal pathway components and regulators in human glial cells and cell lines
    • 1:CAS:528:DyaK2MXltF2nsr0%3D
    • Gasque P, Fontaine M, Morgan BP. Complement expression in human brain. Biosynthesis of terminal pathway components and regulators in human glial cells and cell lines. J Immunol Baltim Md. 1995;154:4726-33.
    • (1995) J Immunol Baltim Md , vol.154 , pp. 4726-4733
    • Gasque, P.1    Fontaine, M.2    Morgan, B.P.3
  • 162
    • 0029932195 scopus 로고    scopus 로고
    • Localization and cell association of C1q in Alzheimer's disease brain
    • 1:STN:280:DyaK287ntlajtQ%3D%3D 8593893
    • Afagh A, Cummings BJ, Cribbs DH, Cotman CW, Tenner AJ. Localization and cell association of C1q in Alzheimer's disease brain. Exp Neurol. 1996;138:22-32.
    • (1996) Exp Neurol , vol.138 , pp. 22-32
    • Afagh, A.1    Cummings, B.J.2    Cribbs, D.H.3    Cotman, C.W.4    Tenner, A.J.5
  • 163
    • 36849076770 scopus 로고    scopus 로고
    • The classical complement cascade mediates CNS synapse elimination
    • 1:CAS:528:DC%2BD1cXksFGnsw%3D%3D 18083105
    • Stevens B, Allen NJ, Vazquez LE, Howell GR, Christopherson KS, Nouri N, et al. The classical complement cascade mediates CNS synapse elimination. Cell. 2007;131:1164-78.
    • (2007) Cell , vol.131 , pp. 1164-1178
    • Stevens, B.1    Allen, N.J.2    Vazquez, L.E.3    Howell, G.R.4    Christopherson, K.S.5    Nouri, N.6
  • 164
    • 84861427387 scopus 로고    scopus 로고
    • Microglia sculpt postnatal neural circuits in an activity and complement-dependent manner
    • 1:CAS:528:DC%2BC38Xns1WnsL0%3D 22632727 3528177
    • Schafer DP, Lehrman EK, Kautzman AG, Koyama R, Mardinly AR, Yamasaki R, et al. Microglia sculpt postnatal neural circuits in an activity and complement-dependent manner. Neuron. 2012;74:691-705.
    • (2012) Neuron , vol.74 , pp. 691-705
    • Schafer, D.P.1    Lehrman, E.K.2    Kautzman, A.G.3    Koyama, R.4    Mardinly, A.R.5    Yamasaki, R.6
  • 165
    • 84962418507 scopus 로고    scopus 로고
    • Complement and microglia mediate early synapse loss in Alzheimer mouse models
    • 1:CAS:528:DC%2BC28XntVeqt74%3D 27033548 5094372
    • Hong S, Beja-Glasser VF, Nfonoyim BM, Frouin A, Li S, Ramakrishnan S, et al. Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science. 2016;352:712-6.
    • (2016) Science , vol.352 , pp. 712-716
    • Hong, S.1    Beja-Glasser, V.F.2    Nfonoyim, B.M.3    Frouin, A.4    Li, S.5    Ramakrishnan, S.6
  • 166
    • 84986000940 scopus 로고    scopus 로고
    • Novel allele-dependent role for APOE in controlling the rate of synapse pruning by astrocytes
    • 1:CAS:528:DC%2BC28Xhtl2ktbnF 27559087 5018780
    • Chung W-S, Verghese PB, Chakraborty C, Joung J, Hyman BT, Ulrich JD, et al. Novel allele-dependent role for APOE in controlling the rate of synapse pruning by astrocytes. Proc Natl Acad Sci U S A. 2016;113:10186-91.
    • (2016) Proc Natl Acad Sci U S A , vol.113 , pp. 10186-10191
    • Chung, W.-S.1    Verghese, P.B.2    Chakraborty, C.3    Joung, J.4    Hyman, B.T.5    Ulrich, J.D.6
  • 167
    • 80053281065 scopus 로고    scopus 로고
    • Interleukin-34 selectively enhances the neuroprotective effects of microglia to attenuate oligomeric amyloid-β neurotoxicity
    • 1:CAS:528:DC%2BC3MXhsVSqtbnM 21872563 3181379
    • Mizuno T, Doi Y, Mizoguchi H, Jin S, Noda M, Sonobe Y, et al. Interleukin-34 selectively enhances the neuroprotective effects of microglia to attenuate oligomeric amyloid-β neurotoxicity. Am J Pathol. 2011;179:2016-27.
    • (2011) Am J Pathol , vol.179 , pp. 2016-2027
    • Mizuno, T.1    Doi, Y.2    Mizoguchi, H.3    Jin, S.4    Noda, M.5    Sonobe, Y.6
  • 168
    • 56349125650 scopus 로고    scopus 로고
    • Interleukin-18 increases expression of kinases involved in tau phosphorylation in SH-SY5Y neuroblastoma cells
    • 1:CAS:528:DC%2BD1cXhsVWrsbzN 18947885
    • Ojala JO, Sutinen EM, Salminen A, Pirttilä T. Interleukin-18 increases expression of kinases involved in tau phosphorylation in SH-SY5Y neuroblastoma cells. J Neuroimmunol. 2008;205:86-93.
    • (2008) J Neuroimmunol , vol.205 , pp. 86-93
    • Ojala, J.O.1    Sutinen, E.M.2    Salminen, A.3    Pirttilä, T.4
  • 170
    • 0036850725 scopus 로고    scopus 로고
    • Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein
    • 1:CAS:528:DC%2BD3sXmsVemsLc%3D 12417659
    • Allen B, Ingram E, Takao M, Smith MJ, Jakes R, Virdee K, et al. Abundant tau filaments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein. J Neurosci. 2002;22:9340-51.
    • (2002) J Neurosci , vol.22 , pp. 9340-9351
    • Allen, B.1    Ingram, E.2    Takao, M.3    Smith, M.J.4    Jakes, R.5    Virdee, K.6
  • 171
    • 84949187245 scopus 로고    scopus 로고
    • Tau deposition drives neuropathological, inflammatory and behavioral abnormalities independently of neuronal loss in a novel mouse model
    • 1:CAS:528:DC%2BC2MXitVykt7rF 26276810 4599677
    • Cook C, Kang SS, Carlomagno Y, Lin W-L, Yue M, Kurti A, et al. Tau deposition drives neuropathological, inflammatory and behavioral abnormalities independently of neuronal loss in a novel mouse model. Hum Mol Genet. 2015;24:6198-212.
    • (2015) Hum Mol Genet , vol.24 , pp. 6198-6212
    • Cook, C.1    Kang, S.S.2    Carlomagno, Y.3    Lin, W.-L.4    Yue, M.5    Kurti, A.6
  • 172
    • 84894189382 scopus 로고    scopus 로고
    • Accelerated neurodegeneration and neuroinflammation in transgenic mice expressing P301L tau mutant and tau-tubulin kinase 1
    • 1:CAS:528:DC%2BC2cXis1Gjtrc%3D 24418258 3936332
    • Asai H, Ikezu S, Woodbury ME, Yonemoto GMS, Cui L, Ikezu T. Accelerated neurodegeneration and neuroinflammation in transgenic mice expressing P301L tau mutant and tau-tubulin kinase 1. Am J Pathol. 2014;184:808-18.
    • (2014) Am J Pathol , vol.184 , pp. 808-818
    • Asai, H.1    Ikezu, S.2    Woodbury, M.E.3    Yonemoto, G.M.S.4    Cui, L.5    Ikezu, T.6
  • 173
    • 44449098256 scopus 로고    scopus 로고
    • Microglial activation in brain lesions with tau deposits: Comparison of human tauopathies and tau transgenic mice TgTauP301L
    • 1:CAS:528:DC%2BD1cXmsFKls7w%3D 18457819
    • Sasaki A, Kawarabayashi T, Murakami T, Matsubara E, Ikeda M, Hagiwara H, et al. Microglial activation in brain lesions with tau deposits: comparison of human tauopathies and tau transgenic mice TgTauP301L. Brain Res. 2008;1214:159-68.
    • (2008) Brain Res , vol.1214 , pp. 159-168
    • Sasaki, A.1    Kawarabayashi, T.2    Murakami, T.3    Matsubara, E.4    Ikeda, M.5    Hagiwara, H.6
  • 174
    • 84990059646 scopus 로고    scopus 로고
    • Age-dependent neuroinflammation and cognitive decline in a novel Ala152Thr-tau transgenic mouse model of PSP and AD
    • 26916334 4766625
    • Sydow A, Hochgräfe K, Könen S, Cadinu D, Matenia D, Petrova O, et al. Age-dependent neuroinflammation and cognitive decline in a novel Ala152Thr-tau transgenic mouse model of PSP and AD. Acta Neuropathol Commun. 2016;4:17.
    • (2016) Acta Neuropathol Commun , vol.4 , pp. 17
    • Sydow, A.1    Hochgräfe, K.2    Könen, S.3    Cadinu, D.4    Matenia, D.5    Petrova, O.6
  • 175
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • 1:CAS:528:DC%2BC2cXoslClsrY%3D 24857020 4171396
    • Sanders DW, Kaufman SK, DeVos SL, Sharma AM, Mirbaha H, Li A, et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron. 2014;82:1271-88.
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, D.W.1    Kaufman, S.K.2    DeVos, S.L.3    Sharma, A.M.4    Mirbaha, H.5    Li, A.6
  • 176
    • 84951567833 scopus 로고    scopus 로고
    • Tau in physiology and pathology
    • 26631930
    • Wang Y, Mandelkow E. Tau in physiology and pathology. Nat Rev Neurosci. 2016;17:5-21.
    • (2016) Nat Rev Neurosci , vol.17 , pp. 5-21
    • Wang, Y.1    Mandelkow, E.2
  • 177
    • 84868514765 scopus 로고    scopus 로고
    • Microtubule stabilizing agents as potential treatment for Alzheimer's disease and related neurodegenerative tauopathies
    • 1:CAS:528:DC%2BC38XhsVagtLfE 23020671 3493881
    • Ballatore C, Brunden KR, Huryn DM, Trojanowski JQ, Lee VM-Y, Smith AB. Microtubule stabilizing agents as potential treatment for Alzheimer's disease and related neurodegenerative tauopathies. J Med Chem. 2012;55:8979-96.
    • (2012) J Med Chem , vol.55 , pp. 8979-8996
    • Ballatore, C.1    Brunden, K.R.2    Huryn, D.M.3    Trojanowski, J.Q.4    Lee, V.M.-Y.5    Smith, A.B.6
  • 178
    • 84946742931 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of tau aggregation by targeting Monomeric tau as a potential therapeutic approach for Tauopathies
    • 1:CAS:528:DC%2BC2MXhslGitbrE 26510979 4976804
    • Pickhardt M, Neumann T, Schwizer D, Callaway K, Vendruscolo M, Schenk D, et al. Identification of small molecule inhibitors of tau aggregation by targeting Monomeric tau as a potential therapeutic approach for Tauopathies. Curr Alzheimer Res. 2015;12:814-28.
    • (2015) Curr Alzheimer Res , vol.12 , pp. 814-828
    • Pickhardt, M.1    Neumann, T.2    Schwizer, D.3    Callaway, K.4    Vendruscolo, M.5    Schenk, D.6
  • 179
    • 84958059727 scopus 로고    scopus 로고
    • Tau immunotherapy
    • 1:CAS:528:DC%2BC28XisFSgtb0%3D 26551002
    • Sigurdsson EM. Tau immunotherapy. Neurodegener Dis. 2016;16:34-8.
    • (2016) Neurodegener Dis , vol.16 , pp. 34-38
    • Sigurdsson, E.M.1
  • 180
    • 78650210590 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • 1:CAS:528:DC%2BC3MXhsFKms7s%3D 21158978 3074967
    • Morgan D. Immunotherapy for Alzheimer's disease. J Intern Med. 2011;269:54-63.
    • (2011) J Intern Med , vol.269 , pp. 54-63
    • Morgan, D.1
  • 181
    • 84940707250 scopus 로고    scopus 로고
    • Distinct therapeutic mechanisms of tau antibodies: Promoting Microglial clearance versus blocking neuronal uptake
    • 1:CAS:528:DC%2BC2MXhsVSlur3L 26126828 4571888
    • Funk KE, Mirbaha H, Jiang H, Holtzman DM, Diamond MI. Distinct therapeutic mechanisms of tau antibodies: promoting Microglial clearance versus blocking neuronal uptake. J Biol Chem. 2015;290:21652-62.
    • (2015) J Biol Chem , vol.290 , pp. 21652-21662
    • Funk, K.E.1    Mirbaha, H.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 182
    • 84905898497 scopus 로고    scopus 로고
    • New roles for Fc receptors in neurodegeneration-The impact on Immunotherapy for Alzheimer's Disease
    • [Internet] [cited 2017 Mar 6]
    • Fuller JP, Stavenhagen JB, Teeling JL. New roles for Fc receptors in neurodegeneration-the impact on Immunotherapy for Alzheimer's Disease. Front Neurosci. [Internet]. 2014 [cited 2017 Mar 6];8. Available from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4139653/.
    • (2014) Front Neurosci , vol.8
    • Fuller, J.P.1    Stavenhagen, J.B.2    Teeling, J.L.3
  • 183
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • 1:CAS:528:DC%2BC3sXhsFems73N 24075978 3924573
    • Yanamandra K, Kfoury N, Jiang H, Mahan TE, Ma S, Maloney SE, et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron. 2013;80:402-14.
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1    Kfoury, N.2    Jiang, H.3    Mahan, T.E.4    Ma, S.5    Maloney, S.E.6
  • 184
    • 84979752510 scopus 로고    scopus 로고
    • Antibody-mediated targeting of tau in vivo does not require Effector function and Microglial engagement
    • 1:CAS:528:DC%2BC28Xht1KlsbvF 27475227
    • Lee S-H, Le Pichon CE, Adolfsson O, Gafner V, Pihlgren M, Lin H, et al. Antibody-mediated targeting of tau in vivo does not require Effector function and Microglial engagement. Cell Rep. 2016;16:1690-700.
    • (2016) Cell Rep , vol.16 , pp. 1690-1700
    • Lee, S.-H.1    Le Pichon, C.E.2    Adolfsson, O.3    Gafner, V.4    Pihlgren, M.5    Lin, H.6
  • 185
    • 84951816455 scopus 로고    scopus 로고
    • Current thinking on the mechanistic basis of Alzheimer's and implications for drug development
    • 1:STN:280:DC%2BC287gsFaqsw%3D%3D 26250900
    • Ising C, Stanley M, Holtzman DM. Current thinking on the mechanistic basis of Alzheimer's and implications for drug development. Clin Pharmacol Ther. 2015;98:469-71.
    • (2015) Clin Pharmacol Ther , vol.98 , pp. 469-471
    • Ising, C.1    Stanley, M.2    Holtzman, D.M.3
  • 186
    • 37249008654 scopus 로고    scopus 로고
    • Anti-inflammatory and immune therapy for Alzheimer's disease: Current status and future directions
    • 1:CAS:528:DC%2BD1cXnsVKruw%3D%3D 19305740 2644496
    • Walker D, Lue L-F. Anti-inflammatory and immune therapy for Alzheimer's disease: current status and future directions. Curr Neuropharmacol. 2007;5:232-43.
    • (2007) Curr Neuropharmacol , vol.5 , pp. 232-243
    • Walker, D.1    Lue, L.-F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.