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Volumn 22, Issue 5, 2015, Pages 753-761

TDP-43 in amyotrophic lateral sclerosis - is it a prion disease?

Author keywords

Amyotrophic lateral sclerosis; Prion diseases; TDP 43

Indexed keywords

PRION PROTEIN; TAR DNA BINDING PROTEIN; TETRAMER; DNA BINDING PROTEIN; PROTEIN TDP-43;

EID: 84926319151     PISSN: 13515101     EISSN: 14681331     Source Type: Journal    
DOI: 10.1111/ene.12706     Document Type: Review
Times cited : (40)

References (93)
  • 1
    • 79952486262 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Kiernan MC, Vucic S, Cheah BC, et al. Amyotrophic lateral sclerosis. Lancet 2011; 377: 942-955.
    • (2011) Lancet , vol.377 , pp. 942-955
    • Kiernan, M.C.1    Vucic, S.2    Cheah, B.C.3
  • 2
    • 84861841901 scopus 로고    scopus 로고
    • Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation?
    • Kanouchi T, Ohkubo T, Yokota T. Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation? J Neurol Neurosurg Psychiatry 2012; 83: 739-745.
    • (2012) J Neurol Neurosurg Psychiatry , vol.83 , pp. 739-745
    • Kanouchi, T.1    Ohkubo, T.2    Yokota, T.3
  • 3
    • 70349581626 scopus 로고    scopus 로고
    • ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration
    • Ravits JM, La Spada AR. ALS motor phenotype heterogeneity, focality, and spread: deconstructing motor neuron degeneration. Neurology 2009; 73: 805-811.
    • (2009) Neurology , vol.73 , pp. 805-811
    • Ravits, J.M.1    La Spada, A.R.2
  • 4
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: what do we really know?
    • Andersen PM, Al-Chalabi A. Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat Rev Neurol 2011; 7: 603-615.
    • (2011) Nat Rev Neurol , vol.7 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 5
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006; 314: 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 6
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010; 11: 301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 7
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Munch C, O'Brien J, Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci USA 2011; 108: 3548-3553.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3548-3553
    • Munch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 8
    • 84891947306 scopus 로고    scopus 로고
    • Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis
    • Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y. Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. J Biol Chem 2014; 289: 1192-1202.
    • (2014) J Biol Chem , vol.289 , pp. 1192-1202
    • Nomura, T.1    Watanabe, S.2    Kaneko, K.3    Yamanaka, K.4    Nukina, N.5    Furukawa, Y.6
  • 9
    • 0038609639 scopus 로고    scopus 로고
    • Epidemiology and genetics of frontotemporal dementia/Pick's disease
    • Bird T, Knopman D, VanSwieten J, et al. Epidemiology and genetics of frontotemporal dementia/Pick's disease. Ann Neurol 2003; 54(Suppl. 5): S29-S31.
    • (2003) Ann Neurol , vol.54 , pp. S29-S31
    • Bird, T.1    Knopman, D.2    VanSwieten, J.3
  • 10
    • 80052628820 scopus 로고    scopus 로고
    • Population based epidemiology of amyotrophic lateral sclerosis using capture-recapture methodology
    • Huisman MH, de Jong SW, van Doormaal PT, et al. Population based epidemiology of amyotrophic lateral sclerosis using capture-recapture methodology. J Neurol Neurosurg Psychiatry 2011; 82: 1165-1170.
    • (2011) J Neurol Neurosurg Psychiatry , vol.82 , pp. 1165-1170
    • Huisman, M.H.1    de Jong, S.W.2    van Doormaal, P.T.3
  • 12
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • 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
  • 13
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo JL, Lee VM. Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 2014; 20: 130-138.
    • (2014) Nat Med , vol.20 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.2
  • 14
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 16
    • 84905590992 scopus 로고    scopus 로고
    • Neurodegeneration: Alzheimer's disease under strain
    • Aguzzi A. Neurodegeneration: Alzheimer's disease under strain. Nature 2014; 512: 32-34.
    • (2014) Nature , vol.512 , pp. 32-34
    • Aguzzi, A.1
  • 17
    • 84885825520 scopus 로고    scopus 로고
    • Human prion diseases: from Kuru to variant Creutzfeldt-Jakob disease
    • Sikorska B, Liberski PP. Human prion diseases: from Kuru to variant Creutzfeldt-Jakob disease. Subcell Biochem 2012; 65: 457-496.
    • (2012) Subcell Biochem , vol.65 , pp. 457-496
    • Sikorska, B.1    Liberski, P.P.2
  • 18
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi A, Rajendran L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009; 64: 783-790.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 19
    • 84879895467 scopus 로고    scopus 로고
    • Distinct alpha-synuclein strains differentially promote tau inclusions in neurons
    • Guo JL, Covell DJ, Daniels JP, et al. Distinct alpha-synuclein strains differentially promote tau inclusions in neurons. Cell 2013; 154: 103-117.
    • (2013) Cell , vol.154 , pp. 103-117
    • Guo, J.L.1    Covell, D.J.2    Daniels, J.P.3
  • 20
    • 84887031600 scopus 로고    scopus 로고
    • Seeded strain-like transmission of beta-amyloid morphotypes in APP transgenic mice
    • Heilbronner G, Eisele YS, Langer F, et al. Seeded strain-like transmission of beta-amyloid morphotypes in APP transgenic mice. EMBO Rep 2013; 14: 1017-1022.
    • (2013) EMBO Rep , vol.14 , pp. 1017-1022
    • Heilbronner, G.1    Eisele, Y.S.2    Langer, F.3
  • 21
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • Sanders DW, Kaufman SK, DeVos SL, et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 2014; 82: 1271-1288.
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, D.W.1    Kaufman, S.K.2    DeVos, S.L.3
  • 22
    • 84876137748 scopus 로고    scopus 로고
    • Evaluation of potential infectivity of Alzheimer and Parkinson disease proteins in recipients of cadaver-derived human growth hormone
    • Irwin DJ, Abrams JY, Schonberger LB, et al. Evaluation of potential infectivity of Alzheimer and Parkinson disease proteins in recipients of cadaver-derived human growth hormone. JAMA Neurol 2013; 70: 462-468.
    • (2013) JAMA Neurol , vol.70 , pp. 462-468
    • Irwin, D.J.1    Abrams, J.Y.2    Schonberger, L.B.3
  • 23
    • 0034858025 scopus 로고    scopus 로고
    • The fluorescent Congo red derivative, (trans, trans)-1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene (BSB), labels diverse beta-pleated sheet structures in postmortem human neurodegenerative disease brains
    • Schmidt ML, Schuck T, Sheridan S, et al. The fluorescent Congo red derivative, (trans, trans)-1-bromo-2, 5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene (BSB), labels diverse beta-pleated sheet structures in postmortem human neurodegenerative disease brains. Am J Pathol 2001; 159: 937-943.
    • (2001) Am J Pathol , vol.159 , pp. 937-943
    • Schmidt, M.L.1    Schuck, T.2    Sheridan, S.3
  • 24
    • 34547663747 scopus 로고    scopus 로고
    • TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions
    • Cairns NJ, Neumann M, Bigio EH, et al. TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions. Am J Pathol 2007; 171: 227-240.
    • (2007) Am J Pathol , vol.171 , pp. 227-240
    • Cairns, N.J.1    Neumann, M.2    Bigio, E.H.3
  • 25
    • 84872347515 scopus 로고    scopus 로고
    • TDP-43 skeins show properties of amyloid in a subset of ALS cases
    • Robinson JL, Geser F, Stieber A, et al. TDP-43 skeins show properties of amyloid in a subset of ALS cases. Acta Neuropathol 2013; 125: 121-131.
    • (2013) Acta Neuropathol , vol.125 , pp. 121-131
    • Robinson, J.L.1    Geser, F.2    Stieber, A.3
  • 26
    • 77950377360 scopus 로고    scopus 로고
    • Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis
    • Chen AK, Lin RY, Hsieh EZ, et al. Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis. J Am Chem Soc 2010; 132: 1186-1187.
    • (2010) J Am Chem Soc , vol.132 , pp. 1186-1187
    • Chen, A.K.1    Lin, R.Y.2    Hsieh, E.Z.3
  • 27
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L, Teng PK, Riek R, Eisenberg D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc Natl Acad Sci USA 2010; 107: 3487-3492.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 28
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007; 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 29
    • 84923238777 scopus 로고    scopus 로고
    • Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients
    • Fang YS, Tsai KJ, Chang YJ, et al. Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients. Nat Commun 2014; 5: 4824.
    • (2014) Nat Commun , vol.5 , pp. 4824
    • Fang, Y.S.1    Tsai, K.J.2    Chang, Y.J.3
  • 30
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • Hong M, Zhukareva V, Vogelsberg-Ragaglia V, et al. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science 1998; 282: 1914-1917.
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1    Zhukareva, V.2    Vogelsberg-Ragaglia, V.3
  • 31
    • 84873352895 scopus 로고    scopus 로고
    • The spectrum of disease in chronic traumatic encephalopathy
    • McKee AC, Stern RA, Nowinski CJ, et al. The spectrum of disease in chronic traumatic encephalopathy. Brain 2013; 136: 43-64.
    • (2013) Brain , vol.136 , pp. 43-64
    • McKee, A.C.1    Stern, R.A.2    Nowinski, C.J.3
  • 32
    • 84899054266 scopus 로고    scopus 로고
    • Can lesions to the motor cortex induce amyotrophic lateral sclerosis?
    • Rosenbohm A, Kassubek J, Weydt P, et al. Can lesions to the motor cortex induce amyotrophic lateral sclerosis? J Neurol 2014; 261: 283-290.
    • (2014) J Neurol , vol.261 , pp. 283-290
    • Rosenbohm, A.1    Kassubek, J.2    Weydt, P.3
  • 33
    • 15044342282 scopus 로고    scopus 로고
    • Severely increased risk of amyotrophic lateral sclerosis among Italian professional football players
    • Chio A, Benzi G, Dossena M, Mutani R, Mora G. Severely increased risk of amyotrophic lateral sclerosis among Italian professional football players. Brain 2005; 128: 472-476.
    • (2005) Brain , vol.128 , pp. 472-476
    • Chio, A.1    Benzi, G.2    Dossena, M.3    Mutani, R.4    Mora, G.5
  • 34
    • 80053652133 scopus 로고    scopus 로고
    • Intermolecular transmission of superoxide dismutase 1 misfolding in living cells
    • Grad LI, Guest WC, Yanai A, et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells. Proc Natl Acad Sci USA 2011; 108: 16398-16403.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16398-16403
    • Grad, L.I.1    Guest, W.C.2    Yanai, A.3
  • 35
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn LI, Houseweart MK, Kato S, et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 1998; 281: 1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1    Houseweart, M.K.2    Kato, S.3
  • 36
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng HX, Shi Y, Furukawa Y, et al. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc Natl Acad Sci USA 2006; 103: 7142-7147.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7142-7147
    • Deng, H.X.1    Shi, Y.2    Furukawa, Y.3
  • 37
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo JL, Lee VM. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem 2011; 286: 15317-15331.
    • (2011) J Biol Chem , vol.286 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 38
    • 0027363383 scopus 로고
    • Evidence for the experimental transmission of cerebral beta-amyloidosis to primates
    • Baker HF, Ridley RM, Duchen LW, Crow TJ, Bruton CJ. Evidence for the experimental transmission of cerebral beta-amyloidosis to primates. Int J Exp Pathol 1993; 74: 441-454.
    • (1993) Int J Exp Pathol , vol.74 , pp. 441-454
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 39
    • 0028376473 scopus 로고
    • Induction of beta (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy
    • Baker HF, Ridley RM, Duchen LW, Crow TJ, Bruton CJ. Induction of beta (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy. Mol Neurobiol 1994; 8: 25-39.
    • (1994) Mol Neurobiol , vol.8 , pp. 25-39
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 40
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of beta-amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice
    • Kane MD, Lipinski WJ, Callahan MJ, et al. Evidence for seeding of beta-amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice. J Neurosci 2000; 20: 3606-3611.
    • (2000) J Neurosci , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3
  • 41
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 2006; 313: 1781-1784.
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3
  • 42
    • 84857145664 scopus 로고    scopus 로고
    • Exogenous seeding of cerebral beta-amyloid deposition in betaAPP-transgenic rats
    • Rosen RF, Fritz JJ, Dooyema J, et al. Exogenous seeding of cerebral beta-amyloid deposition in betaAPP-transgenic rats. J Neurochem 2012; 120: 660-666.
    • (2012) J Neurochem , vol.120 , pp. 660-666
    • Rosen, R.F.1    Fritz, J.J.2    Dooyema, J.3
  • 43
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera F, Bolmont T, Crowther RA, et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat Cell Biol 2009; 11: 909-913.
    • (2009) Nat Cell Biol , vol.11 , pp. 909-913
    • Clavaguera, F.1    Bolmont, T.2    Crowther, R.A.3
  • 44
    • 84878723720 scopus 로고    scopus 로고
    • Brain homogenates from human tauopathies induce tau inclusions in mouse brain
    • Clavaguera F, Akatsu H, Fraser G, et al. Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc Natl Acad Sci USA 2013; 110: 9535-9540.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 9535-9540
    • Clavaguera, F.1    Akatsu, H.2    Fraser, G.3
  • 45
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida Y, Kurosawa M, Nukina N, Ito K, Oda T, Tanaka M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci USA 2009; 106: 9679-9684.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 46
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-bind ing protein-43 inclusions
    • Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N. A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-bind ing protein-43 inclusions. J Biol Chem 2011; 286: 18664-18672.
    • (2011) J Biol Chem , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 47
    • 84885484356 scopus 로고    scopus 로고
    • Prion-like properties of pathological TDP-43 aggregates from diseased brains
    • Nonaka T, Masuda-Suzukake M, Arai T, et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep 2013; 4: 124-134.
    • (2013) Cell Rep , vol.4 , pp. 124-134
    • Nonaka, T.1    Masuda-Suzukake, M.2    Arai, T.3
  • 48
    • 62449262536 scopus 로고    scopus 로고
    • Cerebrospinal fluid {beta}-amyloid 42 and tau proteins as biomarkers of Alzheimer-type pathologic changes in the brain
    • Tapiola T, Alafuzoff I, Herukka SK, et al. Cerebrospinal fluid {beta}-amyloid 42 and tau proteins as biomarkers of Alzheimer-type pathologic changes in the brain. Arch Neurol 2009; 66: 382-389.
    • (2009) Arch Neurol , vol.66 , pp. 382-389
    • Tapiola, T.1    Alafuzoff, I.2    Herukka, S.K.3
  • 49
    • 84871077687 scopus 로고    scopus 로고
    • Total CSF alpha-synuclein is lower in de novo Parkinson patients than in healthy subjects
    • Mollenhauer B, Trautmann E, Taylor P, et al. Total CSF alpha-synuclein is lower in de novo Parkinson patients than in healthy subjects. Neurosci Lett 2013; 532: 44-48.
    • (2013) Neurosci Lett , vol.532 , pp. 44-48
    • Mollenhauer, B.1    Trautmann, E.2    Taylor, P.3
  • 50
    • 80052940324 scopus 로고    scopus 로고
    • In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice
    • Yamada K, Cirrito JR, Stewart FR, 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: 13110-13117.
    • (2011) J Neurosci , vol.31 , pp. 13110-13117
    • Yamada, K.1    Cirrito, J.R.2    Stewart, F.R.3
  • 51
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular propagation of Tau aggregation by fibrillar species
    • Kfoury N, Holmes BB, Jiang H, Holtzman DM, Diamond MI. Trans-cellular propagation of Tau aggregation by fibrillar species. J Biol Chem 2012; 287: 19440-19451.
    • (2012) J Biol Chem , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 52
    • 77952648551 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival
    • Emmanouilidou E, Melachroinou K, Roumeliotis T, et al. Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. J Neurosci 2010; 30: 6838-6851.
    • (2010) J Neurosci , vol.30 , pp. 6838-6851
    • Emmanouilidou, E.1    Melachroinou, K.2    Roumeliotis, T.3
  • 53
    • 84865307818 scopus 로고    scopus 로고
    • Exosomal cell-to-cell transmission of alpha synuclein oligomers
    • Danzer KM, Kranich LR, Ruf WP, et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener 2012; 7: 42.
    • (2012) Mol Neurodegener , vol.7 , pp. 42
    • Danzer, K.M.1    Kranich, L.R.2    Ruf, W.P.3
  • 54
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman S, Kim W, Raya M, 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: 3842-3849.
    • (2012) J Biol Chem , vol.287 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3
  • 55
    • 84895796816 scopus 로고    scopus 로고
    • Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms
    • Grad LI, Yerbury JJ, Turner BJ, et al. Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Proc Natl Acad Sci USA 2014; 111: 3620-3625.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 3620-3625
    • Grad, L.I.1    Yerbury, J.J.2    Turner, B.J.3
  • 56
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284: 12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 57
    • 80053613574 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death
    • Volpicelli-Daley LA, Luk KC, Patel TP, et al. Exogenous alpha-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron 2011; 72: 57-71.
    • (2011) Neuron , vol.72 , pp. 57-71
    • Volpicelli-Daley, L.A.1    Luk, K.C.2    Patel, T.P.3
  • 58
    • 84882306577 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
    • Holmes BB, DeVos SL, Kfoury N, et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds. Proc Natl Acad Sci USA 2013; 110: E3138-E3147.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E3138-E3147
    • Holmes, B.B.1    DeVos, S.L.2    Kfoury, N.3
  • 59
    • 84872714502 scopus 로고    scopus 로고
    • Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons
    • Wu JW, Herman M, Liu L, et al. Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J Biol Chem 2013; 288: 1856-1870.
    • (2013) J Biol Chem , vol.288 , pp. 1856-1870
    • Wu, J.W.1    Herman, M.2    Liu, L.3
  • 61
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 2009; 11: 219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 62
    • 61849178720 scopus 로고    scopus 로고
    • Prions hijack tunnelling nanotubes for intercellular spread
    • Gousset K, Schiff E, Langevin C, et al. Prions hijack tunnelling nanotubes for intercellular spread. Nat Cell Biol 2009; 11: 328-336.
    • (2009) Nat Cell Biol , vol.11 , pp. 328-336
    • Gousset, K.1    Schiff, E.2    Langevin, C.3
  • 63
    • 84865063851 scopus 로고    scopus 로고
    • The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth
    • Fallini C, Bassell GJ, Rossoll W. The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth. Hum Mol Genet 2012; 21: 3703-3718.
    • (2012) Hum Mol Genet , vol.21 , pp. 3703-3718
    • Fallini, C.1    Bassell, G.J.2    Rossoll, W.3
  • 64
    • 84868148328 scopus 로고    scopus 로고
    • Neuron-to-neuron transmission of alpha-synuclein fibrils through axonal transport
    • Freundt EC, Maynard N, Clancy EK, et al. Neuron-to-neuron transmission of alpha-synuclein fibrils through axonal transport. Ann Neurol 2012; 72: 517-524.
    • (2012) Ann Neurol , vol.72 , pp. 517-524
    • Freundt, E.C.1    Maynard, N.2    Clancy, E.K.3
  • 65
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • Iba M, Guo JL, McBride JD, Zhang B, Trojanowski JQ, Lee VM. Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J Neurosci 2013; 33: 1024-1037.
    • (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.6
  • 66
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice
    • Luk KC, Kehm VM, Zhang B, O'Brien P, Trojanowski JQ, Lee VM. Intracerebral inoculation of pathological alpha-synuclein initiates a rapidly progressive neurodegenerative alpha-synucleinopathy in mice. J Exp Med 2012; 209: 975-986.
    • (2012) J Exp Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 67
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological staging of Alzheimer-related changes. Acta Neuropathol 1991; 82: 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 68
    • 47949099336 scopus 로고    scopus 로고
    • Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
    • Mori F, Tanji K, Zhang HX, et al. Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol 2008; 116: 193-203.
    • (2008) Acta Neuropathol , vol.116 , pp. 193-203
    • Mori, F.1    Tanji, K.2    Zhang, H.X.3
  • 69
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak H, Alafuzoff I, Arzberger T, Kretzschmar H, Del Tredici K. Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol 2006; 112: 389-404.
    • (2006) Acta Neuropathol , vol.112 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 70
    • 0032868750 scopus 로고    scopus 로고
    • Neuronal cytoskeletal changes are an early consequence of repetitive head injury
    • Geddes JF, Vowles GH, Nicoll JA, Revesz T. Neuronal cytoskeletal changes are an early consequence of repetitive head injury. Acta Neuropathol 1999; 98: 171-178.
    • (1999) Acta Neuropathol , vol.98 , pp. 171-178
    • Geddes, J.F.1    Vowles, G.H.2    Nicoll, J.A.3    Revesz, T.4
  • 71
    • 84883292041 scopus 로고    scopus 로고
    • Stages of pTDP-43 pathology in amyotrophic lateral sclerosis
    • Brettschneider J, Del Tredici K, Toledo JB, et al. Stages of pTDP-43 pathology in amyotrophic lateral sclerosis. Ann Neurol 2013; 74: 20-38.
    • (2013) Ann Neurol , vol.74 , pp. 20-38
    • Brettschneider, J.1    Del Tredici, K.2    Toledo, J.B.3
  • 72
    • 84901475346 scopus 로고    scopus 로고
    • Diffusion tensor imaging analysis of sequential spreading of disease in amyotrophic lateral sclerosis confirms patterns of TDP-43 pathology
    • Kassubek J, Muller HP, Del Tredici K, et al. Diffusion tensor imaging analysis of sequential spreading of disease in amyotrophic lateral sclerosis confirms patterns of TDP-43 pathology. Brain 2014; 137: 1733-1740.
    • (2014) Brain , vol.137 , pp. 1733-1740
    • Kassubek, J.1    Muller, H.P.2    Del Tredici, K.3
  • 73
    • 35248823549 scopus 로고    scopus 로고
    • Cognitive impairment in amyotrophic lateral sclerosis
    • Phukan J, Pender NP, Hardiman O. Cognitive impairment in amyotrophic lateral sclerosis. Lancet Neurol 2007; 6: 994-1003.
    • (2007) Lancet Neurol , vol.6 , pp. 994-1003
    • Phukan, J.1    Pender, N.P.2    Hardiman, O.3
  • 74
    • 34249949338 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
    • Amador-Ortiz C, Lin WL, Ahmed Z, et al. TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease. Ann Neurol 2007; 61: 435-445.
    • (2007) Ann Neurol , vol.61 , pp. 435-445
    • Amador-Ortiz, C.1    Lin, W.L.2    Ahmed, Z.3
  • 75
    • 59249097160 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies
    • Arai T, Mackenzie IR, Hasegawa M, et al. Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies. Acta Neuropathol 2009; 117: 125-136.
    • (2009) Acta Neuropathol , vol.117 , pp. 125-136
    • Arai, T.1    Mackenzie, I.R.2    Hasegawa, M.3
  • 76
    • 77953870289 scopus 로고    scopus 로고
    • TDP-43 pathology in primary progressive aphasia and frontotemporal dementia with pathologic Alzheimer disease
    • Bigio EH, Mishra M, Hatanpaa KJ, et al. TDP-43 pathology in primary progressive aphasia and frontotemporal dementia with pathologic Alzheimer disease. Acta Neuropathol 2010; 120: 43-54.
    • (2010) Acta Neuropathol , vol.120 , pp. 43-54
    • Bigio, E.H.1    Mishra, M.2    Hatanpaa, K.J.3
  • 77
    • 82355181107 scopus 로고    scopus 로고
    • TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onsheimer's disease and Down's syndrome: association with age, hippocampal sclerosis and clinical phenotype
    • Davidson YS, Raby S, Foulds PG, et al. TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onset Alzheimer's disease and Down's syndrome: association with age, hippocampal sclerosis and clinical phenotype. Acta Neuropathol 2011; 122: 703-713.
    • (2011) Acta Neuropathol , vol.122 , pp. 703-713
    • Davidson, Y.S.1    Raby, S.2    Foulds, P.G.3
  • 78
    • 47949084000 scopus 로고    scopus 로고
    • Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease
    • Hu WT, Josephs KA, Knopman DS, et al. Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease. Acta Neuropathol 2008; 116: 215-220.
    • (2008) Acta Neuropathol , vol.116 , pp. 215-220
    • Hu, W.T.1    Josephs, K.A.2    Knopman, D.S.3
  • 79
    • 43249094487 scopus 로고    scopus 로고
    • Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype
    • Josephs KA, Whitwell JL, Knopman DS, et al. Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype. Neurology 2008; 70: 1850-1857.
    • (2008) Neurology , vol.70 , pp. 1850-1857
    • Josephs, K.A.1    Whitwell, J.L.2    Knopman, D.S.3
  • 80
    • 84896713213 scopus 로고    scopus 로고
    • Staging TDP-43 pathology in Alzheimer's disease
    • Josephs KA, Murray ME, Whitwell JL, et al. Staging TDP-43 pathology in Alzheimer's disease. Acta Neuropathol 2014; 127: 441-450.
    • (2014) Acta Neuropathol , vol.127 , pp. 441-450
    • Josephs, K.A.1    Murray, M.E.2    Whitwell, J.L.3
  • 81
    • 84906314307 scopus 로고    scopus 로고
    • Sequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD)
    • Brettschneider J, Del Tredici K, Irwin DJ, et al. Sequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD). Acta Neuropathol 2014; 127: 423-439.
    • (2014) Acta Neuropathol , vol.127 , pp. 423-439
    • Brettschneider, J.1    Del Tredici, K.2    Irwin, D.J.3
  • 82
    • 79959599081 scopus 로고    scopus 로고
    • A harmonized classification system for FTLD-TDP pathology
    • Mackenzie IR, Neumann M, Baborie A, et al. A harmonized classification system for FTLD-TDP pathology. Acta Neuropathol 2011; 122: 111-113.
    • (2011) Acta Neuropathol , vol.122 , pp. 111-113
    • Mackenzie, I.R.1    Neumann, M.2    Baborie, A.3
  • 83
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Igaz LM, Kwong LK, Xu Y, et al. Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am J Pathol 2008; 173: 182-194.
    • (2008) Am J Pathol , vol.173 , pp. 182-194
    • Igaz, L.M.1    Kwong, L.K.2    Xu, Y.3
  • 84
    • 0038748401 scopus 로고    scopus 로고
    • Idiopathic Parkinson's disease: possible routes by which vulnerable neuronal types may be subject to neuroinvasion by an unknown pathogen
    • Braak H, Rub U, Gai WP, Del Tredici K. Idiopathic Parkinson's disease: possible routes by which vulnerable neuronal types may be subject to neuroinvasion by an unknown pathogen. J Neural Transm 2003; 110: 517-536.
    • (2003) J Neural Transm , vol.110 , pp. 517-536
    • Braak, H.1    Rub, U.2    Gai, W.P.3    Del Tredici, K.4
  • 85
    • 0034031598 scopus 로고    scopus 로고
    • Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis
    • Shaw PJ, Eggett CJ. Molecular factors underlying selective vulnerability of motor neurons to neurodegeneration in amyotrophic lateral sclerosis. J Neurol 2000; 247(Suppl. 1): I17-I27.
    • (2000) J Neurol , vol.247 , pp. I17-I27
    • Shaw, P.J.1    Eggett, C.J.2
  • 87
    • 84906314307 scopus 로고    scopus 로고
    • TDP-43 pathology and neuronal loss in amyotrophic lateral sclerosis spinal cord
    • Brettschneider J, Arai K, Del Tredici K, et al. TDP-43 pathology and neuronal loss in amyotrophic lateral sclerosis spinal cord. Acta Neuropathol 2014; 128: 423-437.
    • (2014) Acta Neuropathol , vol.128 , pp. 423-437
    • Brettschneider, J.1    Arai, K.2    Del Tredici, K.3
  • 88
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • Johnson SM, Connelly S, Fearns C, Powers ET, Kelly JW. The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. J Mol Biol 2012; 421: 185-203.
    • (2012) J Mol Biol , vol.421 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 89
    • 84866679781 scopus 로고    scopus 로고
    • Antibody-aided clearance of extracellular alpha-synuclein prevents cell-to-cell aggregate transmission
    • Bae EJ, Lee HJ, Rockenstein E, et al. Antibody-aided clearance of extracellular alpha-synuclein prevents cell-to-cell aggregate transmission. J Neurosci 2012; 32: 13454-13469.
    • (2012) J Neurosci , vol.32 , pp. 13454-13469
    • Bae, E.J.1    Lee, H.J.2    Rockenstein, E.3
  • 90
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • Desplats P, Lee HJ, Bae EJ, et al. Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci USA 2009; 106: 13010-13015.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3
  • 91
    • 84870061595 scopus 로고    scopus 로고
    • Cellular mechanisms of protein aggregate propagation
    • Holmes BB, Diamond MI. Cellular mechanisms of protein aggregate propagation. Curr Opin Neurol 2012; 25: 721-726.
    • (2012) Curr Opin Neurol , vol.25 , pp. 721-726
    • Holmes, B.B.1    Diamond, M.I.2
  • 92
    • 84903441419 scopus 로고    scopus 로고
    • Alpha-synuclein immunotherapy blocks uptake and templated propagation of misfolded alpha-synuclein and neurodegeneration
    • Tran HT, Chung CH, Iba M, et al. Alpha-synuclein immunotherapy blocks uptake and templated propagation of misfolded alpha-synuclein and neurodegeneration. Cell Rep 2014; 7: 2054-2065.
    • (2014) Cell Rep , vol.7 , pp. 2054-2065
    • Tran, H.T.1    Chung, C.H.2    Iba, M.3
  • 93
    • 0023112582 scopus 로고
    • Protein transfer at the blood cerebrospinal fluid barrier and the quantitation of the humoral immune response within the central nervous system
    • Reiber H, Felgenhauer K. Protein transfer at the blood cerebrospinal fluid barrier and the quantitation of the humoral immune response within the central nervous system. Clin Chim Acta 1987; 163: 319-328.
    • (1987) Clin Chim Acta , vol.163 , pp. 319-328
    • Reiber, H.1    Felgenhauer, K.2


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