메뉴 건너뛰기




Volumn , Issue , 2014, Pages 111-129

Alzheimer's disease and frontotemporal lobar degeneration: Mouse models

Author keywords

APP; FUS; Mouse model; Tau; TDP 43

Indexed keywords


EID: 84919729169     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4471-6380-0_8     Document Type: Chapter
Times cited : (1)

References (94)
  • 1
    • 0015515006 scopus 로고
    • Effect of copper on the preimplantation mouse embryo
    • Brinster RL, Cross PC. Effect of copper on the preimplantation mouse embryo. Nature. 1972;238(5364):398-9.
    • (1972) Nature , vol.238 , Issue.5364 , pp. 398-399
    • Brinster, R.L.1    Cross, P.C.2
  • 2
    • 34250219566 scopus 로고    scopus 로고
    • Pronuclear injection for the production of transgenic mice
    • Ittner LM, Gotz J. Pronuclear injection for the production of transgenic mice. Nat Protoc. 2007;2:1206-15.
    • (2007) Nat Protoc. , vol.2 , pp. 1206-1215
    • Ittner, L.M.1    Gotz, J.2
  • 5
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • Gotz J, Ittner LM. Animal models of Alzheimer's disease and frontotemporal dementia. Nat Rev Neurosci. 2008;9:532-44.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 6
    • 0028985574 scopus 로고
    • Alzheimertype neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein
    • Games D, Adams D, Alessandrini R, Barbour R, Berthelette P, Blackwell C, et al. Alzheimertype neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature. 1995;373(6514):523-7.
    • (1995) Nature , vol.373 , Issue.6514 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3    Barbour, R.4    Berthelette, P.5    Blackwell, C.6
  • 7
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science. 2006;313(5794):1781-4.
    • (2006) Science , vol.313 , Issue.5794 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3    Kaeser, S.4    Schaefer, C.5    Kilger, E.6
  • 9
    • 84875640007 scopus 로고    scopus 로고
    • Neuroinfl ammation and neuronal loss precede Abeta plaque deposition in the hAPP-J20 mouse model of Alzheimer's disease
    • Wright AL, Zinn R, Hohensinn B, Konen LM, Beynon SB, Tan RP, et al. Neuroinfl ammation and neuronal loss precede Abeta plaque deposition in the hAPP-J20 mouse model of Alzheimer's disease. PLoS One. 2013;8(4):e59586.
    • (2013) PLoS One. , vol.8 , Issue.4 , pp. e59586
    • Wright, A.L.1    Zinn, R.2    Hohensinn, B.3    Konen, L.M.4    Beynon, S.B.5    Tan, R.P.6
  • 10
    • 84855483701 scopus 로고    scopus 로고
    • APP physiological and pathophysiological functions: Insights from animal models
    • Guo Q, Wang Z, Li H, Wiese M, Zheng H. APP physiological and pathophysiological functions: insights from animal models. Cell Res. 2012;22(1):78-89.
    • (2012) Cell Res. , vol.22 , Issue.1 , pp. 78-89
    • Guo, Q.1    Wang, Z.2    Li, H.3    Wiese, M.4    Zheng, H.5
  • 11
    • 13944274830 scopus 로고    scopus 로고
    • Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2
    • Wang P, Yang G, Mosier DR, Chang P, Zaidi T, Gong YD, et al. Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2. J Neurosci. 2005;25:1219-25.
    • (2005) J Neurosci , vol.25 , pp. 1219-1225
    • Wang, P.1    Yang, G.2    Mosier, D.R.3    Chang, P.4    Zaidi, T.5    Gong, Y.D.6
  • 12
    • 0028988801 scopus 로고
    • Beta- Amyloid precursor protein-defi cient mice show reactive gliosis and decreased locomotor activity
    • Zheng H, Jiang M, Trumbauer ME, Sirinathsinghji DJ, Hopkins R, Smith DW, et al. beta- Amyloid precursor protein-defi cient mice show reactive gliosis and decreased locomotor activity. Cell. 1995;8:525-31.
    • (1995) Cell , vol.8 , pp. 525-531
    • Zheng, H.1    Jiang, M.2    Trumbauer, M.E.3    Sirinathsinghji, D.J.4    Hopkins, R.5    Smith, D.W.6
  • 13
    • 0029954239 scopus 로고    scopus 로고
    • Generation of mice with a 200-kb amyloid precursor protein gene deletion by Cre recombinase-mediated site-specifi c recombination in embryonic stem cells
    • Li ZW, Stark G, Gotz J, Rulicke T, Gschwind M, Huber G, et al. Generation of mice with a 200-kb amyloid precursor protein gene deletion by Cre recombinase-mediated site-specifi c recombination in embryonic stem cells. Proc Natl Acad Sci U S A. 1996;93:6158-62.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6158-6162
    • Li, Z.W.1    Stark, G.2    Gotz, J.3    Rulicke, T.4    Gschwind, M.5    Huber, G.6
  • 14
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • Duce JA, Tsatsanis A, Cater MA, James SA, Robb E, Wikhe K, et al. Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell. 2010;142:857-67.
    • (2010) Cell , vol.142 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3    James, S.A.4    Robb, E.5    Wikhe, K.6
  • 15
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • Holcomb L, Gordon MN, McGowan E, Yu X, Benkovic S, Jantzen P, et al. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat Med. 1998;4(1):97-100.
    • (1998) Nat Med. , vol.4 , Issue.1 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3    Yu, X.4    Benkovic, S.5    Jantzen, P.6
  • 16
    • 12144288683 scopus 로고    scopus 로고
    • Hippocampal neuron loss exceeds amyloid plaque load in a transgenic mouse model of Alzheimer's disease
    • Schmitz C, Rutten BP, Pielen A, Schafer S, Wirths O, Tremp G, et al. Hippocampal neuron loss exceeds amyloid plaque load in a transgenic mouse model of Alzheimer's disease. Am J Pathol. 2004;164:1495-502.
    • (2004) Am J Pathol. , vol.164 , pp. 1495-1502
    • Schmitz, C.1    Rutten, B.P.2    Pielen, A.3    Schafer, S.4    Wirths, O.5    Tremp, G.6
  • 17
    • 33744952846 scopus 로고    scopus 로고
    • Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology
    • Wang R, Wang B, He W, Zheng H. Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology. J Biol Chem. 2006;281:15330-6.
    • (2006) J Biol Chem , vol.281 , pp. 15330-15336
    • Wang, R.1    Wang, B.2    He, W.3    Zheng, H.4
  • 18
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 defi-ciency rescues memory defi cits and cholinergic dysfunction in a mouse model of Alzheimer's disease
    • Ohno M, Sametsky EA, Younkin LH, Oakley H, Younkin SG, Citron M, et al. BACE1 defi - ciency rescues memory defi cits and cholinergic dysfunction in a mouse model of Alzheimer's disease. Neuron. 2004;41:27-33.
    • (2004) Neuron , vol.41 , pp. 27-33
    • Ohno, M.1    Sametsky, E.A.2    Younkin, L.H.3    Oakley, H.4    Younkin, S.G.5    Citron, M.6
  • 19
    • 34548847452 scopus 로고    scopus 로고
    • Partial reduction of BACE1 has dramatic effects on Alzheimer plaque and synaptic pathology in APP Transgenic Mice
    • McConlogue L, Buttini M, Anderson JP, Brigham EF, Chen KS, Freedman SB, et al. Partial reduction of BACE1 has dramatic effects on Alzheimer plaque and synaptic pathology in APP Transgenic Mice. J Biol Chem. 2007;282:26326-34.
    • (2007) J Biol Chem. , vol.282 , pp. 26326-26334
    • McConlogue, L.1    Buttini, M.2    Anderson, J.P.3    Brigham, E.F.4    Chen, K.S.5    Freedman, S.B.6
  • 20
    • 34249951869 scopus 로고    scopus 로고
    • Involvement of beta-site APP cleaving enzyme 1 (BACE1) in amyloid precursor protein-mediated enhancement of memory and activity-dependent synaptic plasticity
    • Ma H, Lesne S, Kotilinek L, Steidl-Nichols JV, Sherman M, Younkin L, et al. Involvement of beta-site APP cleaving enzyme 1 (BACE1) in amyloid precursor protein-mediated enhancement of memory and activity-dependent synaptic plasticity. Proc Natl Acad Sci U S A. 2007;104:8167-72.
    • (2007) Proc Natl Acad Sci U S A. , vol.104 , pp. 8167-8172
    • Ma, H.1    Lesne, S.2    Kotilinek, L.3    Steidl-Nichols, J.V.4    Sherman, M.5    Younkin, L.6
  • 21
    • 7244234177 scopus 로고    scopus 로고
    • Beta-site amyloid precursor protein cleaving enzyme 1 increases amyloid deposition in brain parenchyma but reduces cerebrovascular amyloid angiopathy in aging BACE x APP[V717I] doubletransgenic mice
    • Willem M, Dewachter I, Smyth N, Van Dooren T, Borghgraef P, Haass C, et al. beta-site amyloid precursor protein cleaving enzyme 1 increases amyloid deposition in brain parenchyma but reduces cerebrovascular amyloid angiopathy in aging BACE x APP[V717I] doubletransgenic mice. Am J Pathol. 2004;165:1621-31.
    • (2004) Am J Pathol. , vol.165 , pp. 1621-1631
    • Willem, M.1    Dewachter, I.2    Smyth, N.3    Van Dooren, T.4    Borghgraef, P.5    Haass, C.6
  • 22
    • 20444504698 scopus 로고    scopus 로고
    • The genetic epidemiology of neurodegenerative disease
    • Bertram L, Tanzi RE. The genetic epidemiology of neurodegenerative disease. J Clin Invest. 2005;115:1449-57.
    • (2005) J Clin Invest. , vol.115 , pp. 1449-1457
    • Bertram, L.1    Tanzi, R.E.2
  • 23
    • 0031278270 scopus 로고    scopus 로고
    • Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition
    • Bales KR, Verina T, Dodel RC, Du Y, Altstiel L, Bender M, et al. Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition. Nat Genet. 1997;17:263-4.
    • (1997) Nat Genet. , vol.17 , pp. 263-264
    • Bales, K.R.1    Verina, T.2    Dodel, R.C.3    Du, Y.4    Altstiel, L.5    Bender, M.6
  • 25
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofi - brillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL, Chisholm L, Corral A, Jones G, et al. Enhanced neurofi - brillary degeneration in transgenic mice expressing mutant tau and APP. Science. 2001; 293(5534):1487-91.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3    Chisholm, L.4    Corral, A.5    Jones, G.6
  • 26
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofi brillary tangles in P301l tau transgenic mice induced by Abeta 42 fi brils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofi brillary tangles in P301l tau transgenic mice induced by Abeta 42 fi brils. Science. 2001;293(5534):1491-5.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 27
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced defi cits in an Alzheimer's disease mouse model
    • Roberson ED, Scearce-Levie K, Palop JJ, Yan F, Cheng IH, Wu T, et al. Reducing endogenous tau ameliorates amyloid beta-induced defi cits in an Alzheimer's disease mouse model. Science. 2007;316(5825):750-4.
    • (2007) Science , vol.316 , Issue.5825 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 28
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • Ittner LM, Ke YD, Delerue F, Bi M, Gladbach A, van Eersel J, et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell. 2010;142:387-97.
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    Van Eersel, J.6
  • 29
    • 78751644048 scopus 로고    scopus 로고
    • Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease
    • Ittner LM, Gotz J. Amyloid-beta and tau-a toxic pas de deux in Alzheimer's disease. Nat Rev Neurosci. 2011;12:67-72.
    • (2011) Nat Rev Neurosci. , vol.12 , pp. 67-72
    • Ittner, L.M.1    Gotz, J.2
  • 30
    • 84866361333 scopus 로고    scopus 로고
    • Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D- Aspartate receptor-dependent tau phosphorylation
    • Mondragon-Rodriguez S, Trillaud-Doppia E, Dudilot A, Bourgeois C, Lauzon M, Leclerc N, et al. Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D- Aspartate receptor-dependent tau phosphorylation. J Biol Chem. 2012;287(38): 32040-53.
    • (2012) J Biol Chem. , vol.287 , Issue.38 , pp. 32040-32053
    • Mondragon-Rodriguez, S.1    Trillaud-Doppia, E.2    Dudilot, A.3    Bourgeois, C.4    Lauzon, M.5    Leclerc, N.6
  • 31
    • 84882940367 scopus 로고    scopus 로고
    • Synaptic protein alpha1- Takusan mitigates amyloid-beta-induced synaptic loss via interaction with tau and postsynaptic density-95 at postsynaptic sites
    • Nakanishi N, Ryan SD, Zhang X, Khan A, Holland T, Cho EG, et al. Synaptic protein alpha1- Takusan mitigates amyloid-beta-induced synaptic loss via interaction with tau and postsynaptic density-95 at postsynaptic sites. J Neurosci. 2013;33:14170-83.
    • (2013) J Neurosci. , vol.33 , pp. 14170-14183
    • Nakanishi, N.1    Ryan, S.D.2    Zhang, X.3    Khan, A.4    Holland, T.5    Cho, E.G.6
  • 33
    • 0028965635 scopus 로고
    • Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform
    • Gotz J, Probst A, Spillantini MG, Schafer T, Jakes R, Burki K, et al. Somatodendritic localization and hyperphosphorylation of tau protein in transgenic mice expressing the longest human brain tau isoform. Embo J. 1995;14:1304-13.
    • (1995) Embo J. , vol.14 , pp. 1304-1313
    • Gotz, J.1    Probst, A.2    Spillantini, M.G.3    Schafer, T.4    Jakes, R.5    Burki, K.6
  • 34
    • 0034426011 scopus 로고    scopus 로고
    • Neurofi brillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J, McGowan E, Rockwood J, Melrose H, Nacharaju P, Van Slegtenhorst M, et al. Neurofi brillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat Genet. 2000;25:402-5.
    • (2000) Nat Genet. , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3    Melrose, H.4    Nacharaju, P.5    Van Slegtenhorst, M.6
  • 35
    • 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
    • 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
  • 36
    • 0036850725 scopus 로고    scopus 로고
    • Abundant tau fi laments and nonapoptotic neurodegeneration in transgenic mice expressing human P301S tau protein
    • Allen B, Ingram E, Takao M, Smith MJ, Jakes R, Virdee K, et al. Abundant tau fi laments 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
  • 37
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama Y, Higuchi M, Zhang B, Huang SM, 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
  • 38
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K, Lewis J, Spires T, Paulson J, Kotilinek L, Ingelsson M, et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science. 2005; 309:476-81.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1    Lewis, J.2    Spires, T.3    Paulson, J.4    Kotilinek, L.5    Ingelsson, M.6
  • 39
    • 38549129613 scopus 로고    scopus 로고
    • The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy
    • Mocanu MM, Nissen A, Eckermann K, Khlistunova I, Biernat J, Drexler D, et al. The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J Neurosci. 2008;28:737-48.
    • (2008) J Neurosci. , vol.28 , pp. 737-748
    • Mocanu, M.M.1    Nissen, A.2    Eckermann, K.3    Khlistunova, I.4    Biernat, J.5    Drexler, D.6
  • 40
    • 17044411592 scopus 로고    scopus 로고
    • Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration
    • Forman MS, Lal D, Zhang B, Dabir DV, Swanson E, Lee VM, et al. Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration. J Neurosci. 2005;6(25):3539-50.
    • (2005) J Neurosci , vol.6 , Issue.25 , pp. 3539-3550
    • Forman, M.S.1    Lal, D.2    Zhang, B.3    Dabir, D.V.4    Swanson, E.5    Lee, V.M.6
  • 41
    • 26844433190 scopus 로고    scopus 로고
    • Axonal degeneration induced by targeted expression of mutant human tau in oligodendrocytes of transgenic mice that model glial tauopathies
    • Higuchi M, Zhang B, Forman MS, Yoshiyama Y, Trojanowski JQ, Lee VM. Axonal degeneration induced by targeted expression of mutant human tau in oligodendrocytes of transgenic mice that model glial tauopathies. J Neurosci. 2005;25:9434-43.
    • (2005) J Neurosci. , vol.25 , pp. 9434-9443
    • Higuchi, M.1    Zhang, B.2    Forman, M.S.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 42
    • 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;64:783-90.
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 46
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni AA, Boutajangout A, Quartermain D, Sigurdsson EM. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J Neurosci. 2007;27(34):9115-29.
    • (2007) J Neurosci. , vol.27 , Issue.34 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 47
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofi brillary histopathology in aged P301L tau transgenic mice
    • Epub 2011 Dec 8
    • Bi M, Ittner A, Ke YD, Gotz J, Ittner LM. Tau-targeted immunization impedes progression of neurofi brillary histopathology in aged P301L tau transgenic mice. PLoS One. 2011;6(12):e26860. doi:10.1371/journal.pone.0026860 . Epub 2011 Dec 8.
    • (2011) PLoS One. , vol.6 , Issue.12 , pp. e26860
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 48
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofi brillary tangles in mice
    • Boimel M, Grigoriadis N, Lourbopoulos A, Haber E, Abramsky O, Rosenmann H. Effi cacy and safety of immunization with phosphorylated tau against neurofi brillary tangles in mice. Exp Neurol. 2010;224:472-85.
    • (2010) Exp Neurol. , vol.224 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5    Rosenmann, H.6
  • 49
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti- Tau antibodies in two transgenic models: Reduction of Tau pathology and delay of disease progression
    • Chai X, Wu S, Murray TK, Kinley R, Cella CV, Sims H, et al. Passive immunization with anti- Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. J Biol Chem. 2011;286:34457-67.
    • (2011) J Biol Chem. , vol.286 , pp. 34457-34467
    • Chai, X.1    Wu, S.2    Murray, T.K.3    Kinley, R.4    Cella, C.V.5    Sims, H.6
  • 50
    • 77956385203 scopus 로고    scopus 로고
    • Sodium selenate mitigates tau pathology, neurodegeneration, and functional defi cits in Alzheimer's disease models
    • van Eersel J, Ke YD, Liu X, Delerue F, Kril JJ, Gotz J, et al. Sodium selenate mitigates tau pathology, neurodegeneration, and functional defi cits in Alzheimer's disease models. Proc Natl Acad Sci U S A. 2010;107:13888-93.
    • (2010) Proc Natl Acad Sci U S A. , vol.107 , pp. 13888-13893
    • Van Eerse, J.1    Ke, Y.D.2    Liu, X.3    Delerue, F.4    Kril, J.J.5    Gotz, J.6
  • 51
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science. 2006;314(5796):130-3.
    • (2006) Science , vol.314 , Issue.5796 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 52
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci. 2008;13:867-78.
    • (2008) Front Biosci. , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 54
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I, Bell S, Cairns NJ, Miller TM, Baloh RH. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci U S A. 2009;106:18809-14.
    • (2009) Proc Natl Acad Sci U S A. , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 55
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils H, Kleinberger G, Janssens J, Pereson S, Joris G, Cuijt I, et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci U S A. 2010;107:3858-63.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3858-3863
    • Wils, H.1    Kleinberger, G.2    Janssens, J.3    Pereson, S.4    Joris, G.5    Cuijt, I.6
  • 56
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor defi cits, and early mortality in transgenic mice
    • Xu YF, Gendron TF, Zhang YJ, Lin WL, D'Alton S, Sheng H, et al. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor defi cits, and early mortality in transgenic mice. J Neurosci. 2010;30:10851-9.
    • (2010) J Neurosci. , vol.30 , pp. 10851-10859
    • Xu, Y.F.1    Gendron, T.F.2    Zhang, Y.J.3    Lin, W.L.4    D'alton, S.5    Sheng, H.6
  • 57
    • 79551523377 scopus 로고    scopus 로고
    • Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
    • Igaz LM, Kwong LK, Lee EB, Chen-Plotkin A, Swanson E, Unger T, et al. Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice. J Clin Invest. 2011;121:726-38.
    • (2011) J Clin Invest , vol.121 , pp. 726-738
    • Igaz, L.M.1    Kwong, L.K.2    Lee, E.B.3    Chen-Plotkin, A.4    Swanson, E.5    Unger, T.6
  • 59
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup V, Phaneuf D, Bareil C, Robertson J, Rouleau GA, Kriz J, et al. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain. 2011;134:2610-26.
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1    Phaneuf, D.2    Bareil, C.3    Robertson, J.4    Rouleau, G.A.5    Kriz, J.6
  • 60
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, Lee VM. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem. 2008;283:13302-9.
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 62
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
    • Baker M, Mackenzie IR, Pickering-Brown SM, Gass J, Rademakers R, Lindholm C, et al. Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature. 2006;442:916-9.
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1    Mackenzie, I.R.2    Pickering-Brown, S.M.3    Gass, J.4    Rademakers, R.5    Lindholm, C.6
  • 63
    • 33746910649 scopus 로고    scopus 로고
    • Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
    • Cruts M, Gijselinck I, van der Zee J, Engelborghs S, Wils H, Pirici D, et al. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature. 2006;442(7105):920-4.
    • (2006) Nature , vol.442 , Issue.7105 , pp. 920-924
    • Cruts, M.1    Gijselinck, I.2    Van Der Zee, J.3    Engelborghs, S.4    Wils, H.5    Pirici, D.6
  • 64
    • 38349173569 scopus 로고    scopus 로고
    • Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitinimmunoreactive inclusions reduce progranulin production and secretion
    • Shankaran SS, Capell A, Hruscha AT, Fellerer K, Neumann M, Schmid B, et al. Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitinimmunoreactive inclusions reduce progranulin production and secretion. J Biol Chem. 2008;283:1744-53.
    • (2008) J Biol Chem , vol.283 , pp. 1744-1753
    • Shankaran, S.S.1    Capell, A.2    Hruscha, A.T.3    Fellerer, K.4    Neumann, M.5    Schmid, B.6
  • 65
    • 75949130374 scopus 로고    scopus 로고
    • Pathogenic cysteine mutations affect progranulin function and production of mature granulins
    • Wang J, Van Damme P, Cruchaga C, Gitcho MA, Vidal JM, Seijo-Martinez M, et al. Pathogenic cysteine mutations affect progranulin function and production of mature granulins. J Neurochem. 2010;112:1305-15.
    • (2010) J Neurochem. , vol.112 , pp. 1305-1315
    • Wang, J.1    Van Damme, P.2    Cruchaga, C.3    Gitcho, M.A.4    Vidal, J.M.5    Seijo-Martinez, M.6
  • 66
    • 35448929818 scopus 로고    scopus 로고
    • Alteration of behavioural phenotype in mice by targeted disruption of the progranulin gene
    • Kayasuga Y, Chiba S, Suzuki M, Kikusui T, Matsuwaki T, Yamanouchi K, et al. Alteration of behavioural phenotype in mice by targeted disruption of the progranulin gene. Behav Brain Res. 2007;185:110-8.
    • (2007) Behav Brain Res. , vol.185 , pp. 110-118
    • Kayasuga, Y.1    Chiba, S.2    Suzuki, M.3    Kikusui, T.4    Matsuwaki, T.5    Yamanouchi, K.6
  • 67
    • 76149118401 scopus 로고    scopus 로고
    • Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-defi cient mice
    • Yin F, Banerjee R, Thomas B, Zhou P, Qian L, Jia T, et al. Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-defi cient mice. J Exp Med. 2010; 207:117-28.
    • (2010) J Exp Med. , vol.207 , pp. 117-128
    • Yin, F.1    Banerjee, R.2    Thomas, B.3    Zhou, P.4    Qian, L.5    Jia, T.6
  • 69
    • 84868623124 scopus 로고    scopus 로고
    • Progranulin defi ciency promotes neuroinfl ammation and neuron loss following toxin-induced injury
    • Martens LH, Zhang J, Barmada SJ, Zhou P, Kamiya S, Sun B, et al. Progranulin defi ciency promotes neuroinfl ammation and neuron loss following toxin-induced injury. J Clin Invest. 2012;122:3955-9.
    • (2012) J Clin Invest , vol.122 , pp. 3955-3959
    • Martens, L.H.1    Zhang, J.2    Barmada, S.J.3    Zhou, P.4    Kamiya, S.5    Sun, B.6
  • 70
    • 84864744790 scopus 로고    scopus 로고
    • Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice
    • PubMed PMID: 22733568
    • Wils H, Kleinberger G, Pereson S, Janssens J, Capell A, Van Dam D, et al. Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice. J Pathol. 2012;228(1):67-76. PubMed PMID: 22733568.
    • (2012) J Pathol. , vol.228 , Issue.1 , pp. 67-76
    • Wils, H.1    Kleinberger, G.2    Pereson, S.3    Janssens, J.4    Capell, A.5    Van Dam, D.6
  • 71
    • 77954578417 scopus 로고    scopus 로고
    • Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging
    • PubMed PMID: 20522652. Pubmed Central PMCID: 2893674
    • Ahmed Z, Sheng H, Xu YF, Lin WL, Innes AE, Gass J, et al. Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging. Am J Pathol. 2010;177(1):311-24. PubMed PMID: 20522652. Pubmed Central PMCID: 2893674.
    • (2010) Am J Pathol. , vol.177 , Issue.1 , pp. 311-324
    • Ahmed, Z.1    Sheng, H.2    Xu, Y.F.3    Lin, W.L.4    Innes, A.E.5    Gass, J.6
  • 72
    • 81955160693 scopus 로고    scopus 로고
    • Core features of frontotemporal dementia recapitulated in progranulin knockout mice
    • Ghoshal N, Dearborn JT, Wozniak DF, Cairns NJ. Core features of frontotemporal dementia recapitulated in progranulin knockout mice. Neurobiol Dis. 2012;45(1):395-408.
    • (2012) Neurobiol Dis. , vol.45 , Issue.1 , pp. 395-408
    • Ghoshal, N.1    Dearborn, J.T.2    Wozniak, D.F.3    Cairns, N.J.4
  • 73
    • 78149296002 scopus 로고    scopus 로고
    • Behavioral defi cits and progressive neuropathology in progranulin-defi cient mice: A mouse model of frontotemporal dementia
    • Yin F, Dumont M, Banerjee R, Ma Y, Li H, Lin MT, et al. Behavioral defi cits and progressive neuropathology in progranulin-defi cient mice: A mouse model of frontotemporal dementia. FASEB J. 2010;24:4639-47.
    • (2010) FASEB J. , vol.24 , pp. 4639-4647
    • Yin, F.1    Dumont, M.2    Banerjee, R.3    Ma, Y.4    Li, H.5    Lin, M.T.6
  • 74
    • 84877099960 scopus 로고    scopus 로고
    • Dissociation of frontotemporal dementia-related defi cits and neuroinfl ammation in progranulin haploinsufficient mice
    • Filiano AJ, Martens LH, Young AH, Warmus BA, Zhou P, Diaz-Ramirez G, et al. Dissociation of frontotemporal dementia-related defi cits and neuroinfl ammation in progranulin haploinsufficient mice. J Neurosci. 2013;33:5352-61.
    • (2013) J Neurosci. , vol.33 , pp. 5352-5361
    • Filiano, A.J.1    Martens, L.H.2    Young, A.H.3    Warmus, B.A.4    Zhou, P.5    Diaz-Ramirez, G.6
  • 75
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet. 2004;36:377-81.
    • (2004) Nat Genet. , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6
  • 76
    • 40449133507 scopus 로고    scopus 로고
    • Clinical studies in familial VCP myopathy associated with Paget disease of bone and frontotemporal dementia
    • Kimonis VE, Mehta SG, Fulchiero EC, Thomasova D, Pasquali M, Boycott K, et al. Clinical studies in familial VCP myopathy associated with Paget disease of bone and frontotemporal dementia. Am J Med Genet A. 2008;146A:745-57.
    • (2008) Am J Med, Genet A. , vol.146 A , pp. 745-757
    • Kimonis, V.E.1    Mehta, S.G.2    Fulchiero, E.C.3    Thomasova, D.4    Pasquali, M.5    Boycott, K.6
  • 78
  • 79
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
    • Tang WK, Li D, Li CC, Esser L, Dai R, Guo L, et al. A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J. 2010;29:2217-29.
    • (2010) EMBO J. , vol.29 , pp. 2217-2229
    • Tang, W.K.1    Li, D.2    Li, C.C.3    Esser, L.4    Dai, R.5    Guo, L.6
  • 80
    • 84880579253 scopus 로고    scopus 로고
    • Neuronal-specifi c overexpression of a mutant valosin-containing protein associated with IBMPFD promotes aberrant ubiquitin and TDP-43 accumulation and cognitive dysfunction in transgenic mice
    • Rodriguez-Ortiz CJ, Hoshino H, Cheng D, Liu-Yescevitz L, Blurton-Jones M, Wolozin B, et al. Neuronal-specifi c overexpression of a mutant valosin-containing protein associated with IBMPFD promotes aberrant ubiquitin and TDP-43 accumulation and cognitive dysfunction in transgenic mice. Am J Pathol. 2013;183:504-15.
    • (2013) Am J Pathol. , vol.183 , pp. 504-515
    • Rodriguez-Ortiz, C.J.1    Hoshino, H.2    Cheng, D.3    Liu-Yescevitz, L.4    Blurton-Jones, M.5    Wolozin, B.6
  • 81
    • 34447093377 scopus 로고    scopus 로고
    • Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
    • Weihl CC, Miller SE, Hanson PI, Pestronk A. Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice. Hum Mol Genet. 2007;16:919-28.
    • (2007) Hum Mol, Genet , vol.16 , pp. 919-928
    • Weihl, C.C.1    Miller, S.E.2    Hanson, P.I.3    Pestronk, A.4
  • 82
    • 77952486387 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone
    • Custer SK, Neumann M, Lu H, Wright AC, Taylor JP. Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum Mol Genet. 2010;19:1741-55.
    • (2010) Hum Mol, Genet , vol.19 , pp. 1741-1755
    • Custer, S.K.1    Neumann, M.2    Lu, H.3    Wright, A.C.4    Taylor, J.P.5
  • 83
    • 78049244477 scopus 로고    scopus 로고
    • VCP associated inclusion body myopathy and Paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease
    • Badadani M, Nalbandian A, Watts GD, Vesa J, Kitazawa M, Su H, et al. VCP associated inclusion body myopathy and Paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease. PLoS One. 2010;5(10):e13183.
    • (2010) PLoS One. , vol.5 , Issue.10 , pp. e13183
    • Badadani, M.1    Nalbandian, A.2    Watts, G.D.3    Vesa, J.4    Kitazawa, M.5    Su, H.6
  • 84
    • 84873029243 scopus 로고    scopus 로고
    • A progressive translational mouse model of human valosin-containing protein disease: The VCP(R155H/+) mouse
    • Nalbandian A, Llewellyn KJ, Badadani M, Yin HZ, Nguyen C, Katheria V, et al. A progressive translational mouse model of human valosin-containing protein disease: The VCP(R155H/+) mouse. Muscle Nerve. 2013;47(2):260-70.
    • (2013) Muscle Nerve , vol.47 , Issue.2 , pp. 260-270
    • Nalbandian, A.1    Llewellyn, K.J.2    Badadani, M.3    Yin, H.Z.4    Nguyen, C.5    Katheria, V.6
  • 85
    • 84865752018 scopus 로고    scopus 로고
    • Slow development of ALS-like spinal cord pathology in mutant valosin-containing protein gene knock-in mice
    • Yin HZ, Nalbandian A, Hsu CI, Li S, Llewellyn KJ, Mozaffar T, et al. Slow development of ALS-like spinal cord pathology in mutant valosin-containing protein gene knock-in mice. Cell Death Dis. 2012;3:e374.
    • (2012) Cell Death Dis. , vol.3 , pp. e374
    • Yin, H.Z.1    Nalbandian, A.2    Hsu, C.I.3    Li, S.4    Llewellyn, K.J.5    Mozaffar, T.6
  • 87
    • 84857568926 scopus 로고    scopus 로고
    • Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice
    • Ghazi-Noori S, Froud KE, Mizielinska S, Powell C, Smidak M, Fernandez de Marco M, et al. Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice. Brain. 2012;135(Pt 3):819-32.
    • (2012) Brain , vol.135 , pp. 819-832
    • Ghazi-Noori, S.1    Froud, K.E.2    Mizielinska, S.3    Powell, C.4    Smidak, M.5    Fernandez, D.M.M.6
  • 89
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski Jr. TJ, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, Russ C, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science. 2009;323(5918):1205-8.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1205-1208
    • Kwiatkowski, T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5    Russ, C.6
  • 90
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, Sreedharan J, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science. 2009;323(5918):1208-11.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5    Sreedharan, J.6
  • 91
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import
    • Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, Hruscha A, et al. ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J. 2010;29:2841-57.
    • (2010) EMBO J. , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5    Hruscha, A.6
  • 92
    • 84875427900 scopus 로고    scopus 로고
    • Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- And dose-dependent fashion
    • Mitchell JC, McGoldrick P, Vance C, Hortobagyi T, Sreedharan J, Rogelj B, et al. Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- And dose-dependent fashion. Acta Neuropathol. 2013;125:273-88.
    • (2013) Acta Neuropathol , vol.125 , pp. 273-288
    • Mitchell, J.C.1    McGoldrick, P.2    Vance, C.3    Hortobagyi, T.4    Sreedharan, J.5    Rogelj, B.6
  • 93
    • 79953743204 scopus 로고    scopus 로고
    • FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Huang C, Zhou H, Tong J, Chen H, Liu YJ, Wang D, et al. FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. PLoS Genet. 2011;7:e1002011.
    • (2011) PLoS Genet , vol.7 , pp. e1002011
    • Huang, C.1    Zhou, H.2    Tong, J.3    Chen, H.4    Liu, Y.J.5    Wang, D.6
  • 94
    • 80052959701 scopus 로고    scopus 로고
    • FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
    • Neumann M, Bentmann E, Dormann D, Jawaid A, DeJesus-Hernandez M, Ansorge O, et al. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain. 2011;134(Pt 9):2595-609.
    • (2011) Brain , vol.134 , pp. 2595-2609
    • Neumann, M.1    Bentmann, E.2    Dormann, D.3    Jawaid, A.4    Dejesus-Hernandez, M.5    Ansorge, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.