메뉴 건너뛰기




Volumn 7, Issue 8, 2011, Pages

Fus and tardbp but not sod1 interact in genetic models of amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE MORPHOLINO OLIGONUCLEOTIDE; ANTISENSE OLIGONUCLEOTIDE; COPPER ZINC SUPEROXIDE DISMUTASE; FUSED IN SARCOMA PROTEIN; MESSENGER RNA; RNA BINDING PROTEIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; PROTEIN TDP-43; SUPEROXIDE DISMUTASE;

EID: 80052374038     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002214     Document Type: Article
Times cited : (159)

References (73)
  • 1
    • 0029433185 scopus 로고
    • Epidemiology of ALS
    • Nelson LM, (1995) Epidemiology of ALS. Clin Neurosci 3: 327-331.
    • (1995) Clin Neurosci , vol.3 , pp. 327-331
    • Nelson, L.M.1
  • 2
    • 33749056809 scopus 로고    scopus 로고
    • ALS: a disease of motor neurons and their nonneuronal neighbors
    • Boillee S, Van de Velde C, Cleveland DW, (2006) ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 52: 39-59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    van de Velde, C.2    Cleveland, D.W.3
  • 4
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli P, Brown RH, (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 7: 710-723.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 5
    • 0027164824 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364: 362.
    • (1993) Nature , vol.364 , pp. 362
    • Rosen, D.R.1
  • 6
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?
    • Kabashi E, Valdmanis PN, Dion P, Rouleau GA, (2007) Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Ann Neurol 62: 553-559.
    • (2007) Ann Neurol , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 7
    • 4043075622 scopus 로고    scopus 로고
    • Lessons from models of SOD1-linked familial ALS
    • Bendotti C, Carri MT, (2004) Lessons from models of SOD1-linked familial ALS. Trends Mol Med 10: 393-400.
    • (2004) Trends Mol Med , vol.10 , pp. 393-400
    • Bendotti, C.1    Carri, M.T.2
  • 8
    • 34548740744 scopus 로고    scopus 로고
    • Overexpression of mutant superoxide dismutase 1 causes a motor axonopathy in the zebrafish
    • Lemmens R, Van Hoecke A, Hersmus N, Geelen V, D'Hollander I, et al. (2007) Overexpression of mutant superoxide dismutase 1 causes a motor axonopathy in the zebrafish. Hum Mol Genet 16: 2359-2365.
    • (2007) Hum Mol Genet , vol.16 , pp. 2359-2365
    • Lemmens, R.1    Van Hoecke, A.2    Hersmus, N.3    Geelen, V.4    D'Hollander, I.5
  • 9
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40: 572-574.
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Spiegelman, D.4    McConkey, B.J.5
  • 10
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5
  • 11
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: the FUS about TDP-43
    • Lagier-Tourenne C, Cleveland DW, (2009) Rethinking ALS: the FUS about TDP-43. Cell 136: 1001-1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 13
    • 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, et al. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323: 1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3    De Vos, K.J.4    Nishimura, A.L.5
  • 14
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323: 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5
  • 15
  • 16
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, Neumann M, TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 9: 995-1007.
    • Lancet Neurol , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 19
    • 70350045802 scopus 로고    scopus 로고
    • Mutations in FUS cause FALS and SALS in French and French Canadian populations
    • Belzil VV, Valdmanis PN, Dion PA, Daoud H, Kabashi E, et al. (2009) Mutations in FUS cause FALS and SALS in French and French Canadian populations. Neurology 73: 1176-1179.
    • (2009) Neurology , vol.73 , pp. 1176-1179
    • Belzil, V.V.1    Valdmanis, P.N.2    Dion, P.A.3    Daoud, H.4    Kabashi, E.5
  • 20
    • 67349155310 scopus 로고    scopus 로고
    • Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation
    • Chio A, Restagno G, Brunetti M, Ossola I, Calvo A, et al. (2009) Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation. Neurobiol Aging 30: 1272-1275.
    • (2009) Neurobiol Aging , vol.30 , pp. 1272-1275
    • Chio, A.1    Restagno, G.2    Brunetti, M.3    Ossola, I.4    Calvo, A.5
  • 21
    • 70350156915 scopus 로고    scopus 로고
    • Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort
    • Ticozzi N, Silani V, LeClerc AL, Keagle P, Gellera C, et al. (2009) Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort. Neurology 73: 1180-1185.
    • (2009) Neurology , vol.73 , pp. 1180-1185
    • Ticozzi, N.1    Silani, V.2    LeClerc, A.L.3    Keagle, P.4    Gellera, C.5
  • 23
    • 77956357112 scopus 로고    scopus 로고
    • Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia
    • Yan J, Deng HX, Siddique N, Fecto F, Chen W, et al. (2010) Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia. Neurology 75: 807-814.
    • (2010) Neurology , vol.75 , pp. 807-814
    • Yan, J.1    Deng, H.X.2    Siddique, N.3    Fecto, F.4    Chen, W.5
  • 24
    • 77955396350 scopus 로고    scopus 로고
    • SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype-phenotype correlations
    • Millecamps S, Salachas F, Cazeneuve C, Gordon P, Bricka B, et al. (2010) SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype-phenotype correlations. J Med Genet 47: 554-560.
    • (2010) J Med Genet , vol.47 , pp. 554-560
    • Millecamps, S.1    Salachas, F.2    Cazeneuve, C.3    Gordon, P.4    Bricka, B.5
  • 26
    • 77952107930 scopus 로고    scopus 로고
    • Multiple system degeneration with basophilic inclusions in Japanese ALS patients with FUS mutation
    • Tateishi T, Hokonohara T, Yamasaki R, Miura S, Kikuchi H, et al. (2010) Multiple system degeneration with basophilic inclusions in Japanese ALS patients with FUS mutation. Acta Neuropathol 119: 355-364.
    • (2010) Acta Neuropathol , vol.119 , pp. 355-364
    • Tateishi, T.1    Hokonohara, T.2    Yamasaki, R.3    Miura, S.4    Kikuchi, H.5
  • 27
    • 77951712967 scopus 로고    scopus 로고
    • FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion
    • Suzuki N, Aoki M, Warita H, Kato M, Mizuno H, et al. (2010) FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion. J Hum Genet 55: 252-254.
    • (2010) J Hum Genet , vol.55 , pp. 252-254
    • Suzuki, N.1    Aoki, M.2    Warita, H.3    Kato, M.4    Mizuno, H.5
  • 28
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, Neumann M, (2010) TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 9: 995-1007.
    • (2010) Lancet Neurol , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 29
    • 65649112431 scopus 로고    scopus 로고
    • TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration
    • Benajiba L, Le Ber I, Camuzat A, Lacoste M, Thomas-Anterion C, et al. (2009) TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration. Ann Neurol 65: 470-473.
    • (2009) Ann Neurol , vol.65 , pp. 470-473
    • Benajiba, L.1    Le Ber, I.2    Camuzat, A.3    Lacoste, M.4    Thomas-Anterion, C.5
  • 30
    • 70350721803 scopus 로고    scopus 로고
    • Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease
    • Borroni B, Bonvicini C, Alberici A, Buratti E, Agosti C, et al. (2009) Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease. Hum Mutat 30: E974-983.
    • (2009) Hum Mutat , vol.30
    • Borroni, B.1    Bonvicini, C.2    Alberici, A.3    Buratti, E.4    Agosti, C.5
  • 31
    • 77954049858 scopus 로고    scopus 로고
    • Molecular pathways of frontotemporal lobar degeneration
    • Sleegers K, Cruts M, Van Broeckhoven C, (2010) Molecular pathways of frontotemporal lobar degeneration. Annu Rev Neurosci 33: 71-88.
    • (2010) Annu Rev Neurosci , vol.33 , pp. 71-88
    • Sleegers, K.1    Cruts, M.2    Van Broeckhoven, C.3
  • 33
    • 77952932485 scopus 로고    scopus 로고
    • FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis
    • Deng HX, Zhai H, Bigio EH, Yan J, Fecto F, et al. FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis. Ann Neurol 67: 739-748.
    • Ann Neurol , vol.67 , pp. 739-748
    • Deng, H.X.1    Zhai, H.2    Bigio, E.H.3    Yan, J.4    Fecto, F.5
  • 34
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie IR, Bigio EH, Ince PG, Geser F, Neumann M, et al. (2007) Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 61: 427-434.
    • (2007) Ann Neurol , vol.61 , pp. 427-434
    • Mackenzie, I.R.1    Bigio, E.H.2    Ince, P.G.3    Geser, F.4    Neumann, M.5
  • 36
    • 77958604956 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA
    • Kim SH, Shanware NP, Bowler MJ, Tibbetts RS, (2010) Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J Biol Chem 285: 34097-34105.
    • (2010) J Biol Chem , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.P.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 37
    • 79958720175 scopus 로고    scopus 로고
    • A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43
    • Lanson NA Jr, Maltare A, King H, Smith R, Kim JH, et al. (2011) A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43. Hum Mol Genet.
    • (2011) Hum Mol Genet
    • Lanson Jr., N.A.1    Maltare, A.2    King, H.3    Smith, R.4    Kim, J.H.5
  • 38
    • 75649135319 scopus 로고    scopus 로고
    • Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6
    • Fiesel FC, Voigt A, Weber SS, Van den Haute C, Waldenmaier A, et al. (2010) Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6. EMBO J 29: 209-221.
    • (2010) EMBO J , vol.29 , pp. 209-221
    • Fiesel, F.C.1    Voigt, A.2    Weber, S.S.3    Van den Haute, C.4    Waldenmaier, A.5
  • 39
    • 79953185674 scopus 로고    scopus 로고
    • Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
    • Polymenidou M, Lagier-Tourenne C, Hutt KR, Huelga SC, Moran J, et al. (2011) Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat Neurosci 14: 459-468.
    • (2011) Nat Neurosci , vol.14 , pp. 459-468
    • Polymenidou, M.1    Lagier-Tourenne, C.2    Hutt, K.R.3    Huelga, S.C.4    Moran, J.5
  • 40
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, et al. (2008) Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 121: 3778-3785.
    • (2008) J Cell Sci , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1    Zago, P.2    D'Ambrogio, A.3    Xu, Y.F.4    Petrucelli, L.5
  • 41
    • 77957317483 scopus 로고    scopus 로고
    • The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
    • Buratti E, Baralle FE, (2010) The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol 7: 420-429.
    • (2010) RNA Biol , vol.7 , pp. 420-429
    • Buratti, E.1    Baralle, F.E.2
  • 42
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J, Lee SB, Lee S, Kim Y, Song S, et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441: 1157-1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5
  • 43
    • 33745586290 scopus 로고    scopus 로고
    • Neurodegenerative disease: pink, parkin and the brain
    • Pallanck L, Greenamyre JT, (2006) Neurodegenerative disease: pink, parkin and the brain. Nature 441: 1058.
    • (2006) Nature , vol.441 , pp. 1058
    • Pallanck, L.1    Greenamyre, J.T.2
  • 44
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, et al. (2004) Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304: 1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5
  • 45
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5
  • 46
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • Elden AC, Kim HJ, Hart MP, Chen-Plotkin AS, Johnson BS, et al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466: 1069-1075.
    • Nature , vol.466 , pp. 1069-1075
    • Elden, A.C.1    Kim, H.J.2    Hart, M.P.3    Chen-Plotkin, A.S.4    Johnson, B.S.5
  • 47
    • 33845991876 scopus 로고    scopus 로고
    • Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic paraplegia
    • Valdmanis PN, Meijer IA, Reynolds A, Lei A, MacLeod P, et al. (2007) Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic paraplegia. Am J Hum Genet 80: 152-161.
    • (2007) Am J Hum Genet , vol.80 , pp. 152-161
    • Valdmanis, P.N.1    Meijer, I.A.2    Reynolds, A.3    Lei, A.4    MacLeod, P.5
  • 48
    • 78149429744 scopus 로고    scopus 로고
    • Progranulin is neurotrophic in vivo and protects against a mutant TDP-43 induced axonopathy
    • doi: 10.1371/journal.pone.0013368
    • Laird AS, Van Hoecke A, De Muynck L, Timmers M, Van den Bosch L, et al. Progranulin is neurotrophic in vivo and protects against a mutant TDP-43 induced axonopathy. PLoS ONE 5: e13368 doi:10.1371/journal.pone.0013368.
    • PLoS ONE , vol.5
    • Laird, A.S.1    Van Hoecke, A.2    De Muynck, L.3    Timmers, M.4    Van den Bosch, L.5
  • 49
    • 49649085351 scopus 로고    scopus 로고
    • Als2 mRNA splicing variants detected in KO mice rescue severe motor dysfunction phenotype in Als2 knock-down zebrafish
    • Gros-Louis F, Kriz J, Kabashi E, McDearmid J, Millecamps S, et al. (2008) Als2 mRNA splicing variants detected in KO mice rescue severe motor dysfunction phenotype in Als2 knock-down zebrafish. Hum Mol Genet 17: 2691-2702.
    • (2008) Hum Mol Genet , vol.17 , pp. 2691-2702
    • Gros-Louis, F.1    Kriz, J.2    Kabashi, E.3    McDearmid, J.4    Millecamps, S.5
  • 50
    • 77950360176 scopus 로고    scopus 로고
    • Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
    • Kabashi E, Lin L, Tradewell ML, Dion PA, Bercier V, et al. (2010) Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo. Hum Mol Genet 19: 671-683.
    • (2010) Hum Mol Genet , vol.19 , pp. 671-683
    • Kabashi, E.1    Lin, L.2    Tradewell, M.L.3    Dion, P.A.4    Bercier, V.5
  • 51
    • 58749097964 scopus 로고    scopus 로고
    • Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration
    • Simpson CL, Lemmens R, Miskiewicz K, Broom WJ, Hansen VK, et al. (2009) Variants of the elongator protein 3 (ELP3) gene are associated with motor neuron degeneration. Hum Mol Genet 18: 472-481.
    • (2009) Hum Mol Genet , vol.18 , pp. 472-481
    • Simpson, C.L.1    Lemmens, R.2    Miskiewicz, K.3    Broom, W.J.4    Hansen, V.K.5
  • 52
    • 77956496676 scopus 로고    scopus 로고
    • A genetic model of amyotrophic lateral sclerosis in zebrafish displays phenotypic hallmarks of motoneuron disease
    • Ramesh T, Lyon AN, Pineda RH, Wang C, Janssen PM, et al. A genetic model of amyotrophic lateral sclerosis in zebrafish displays phenotypic hallmarks of motoneuron disease. Dis Model Mech 3: 652-662.
    • Dis Model Mech , vol.3 , pp. 652-662
    • Ramesh, T.1    Lyon, A.N.2    Pineda, R.H.3    Wang, C.4    Janssen, P.M.5
  • 53
  • 54
    • 79551472601 scopus 로고    scopus 로고
    • Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS
    • Ito D, Seki M, Tsunoda Y, Uchiyama H, Suzuki N, (2011) Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann Neurol 69: 152-162.
    • (2011) Ann Neurol , vol.69 , pp. 152-162
    • Ito, D.1    Seki, M.2    Tsunoda, Y.3    Uchiyama, H.4    Suzuki, N.5
  • 55
    • 77957875397 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, et al. (2010) Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging.
    • (2010) Neurobiol Aging
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5
  • 56
    • 77449136874 scopus 로고    scopus 로고
    • The TET family of proteins: functions and roles in disease
    • Tan AY, Manley JL, (2009) The TET family of proteins: functions and roles in disease. J Mol Cell Biol 1: 82-92.
    • (2009) J Mol Cell Biol , vol.1 , pp. 82-92
    • Tan, A.Y.1    Manley, J.L.2
  • 58
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume AG, Elliott JL, Hoffman EK, Kowall NW, Ferrante RJ, et al. (1996) Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet 13: 43-47.
    • (1996) Nat Genet , vol.13 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Hoffman, E.K.3    Kowall, N.W.4    Ferrante, R.J.5
  • 59
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 19: 4160-4175.
    • Hum Mol Genet , vol.19 , pp. 4160-4175
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5
  • 60
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada SJ, Skibinski G, Korb E, Rao EJ, Wu JY, et al. Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J Neurosci 30: 639-649.
    • J Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5
  • 61
    • 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, et al. ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 29: 2841-2857.
    • EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5
  • 62
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue
    • doi: 10.1371/journal.pone.0013250
    • Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderwyde T, Citro A, et al. Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS ONE 5: e3250 doi:10.1371/journal.pone.0013250.
    • PLoS ONE , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderwyde, T.4    Citro, A.5
  • 63
    • 70350135049 scopus 로고    scopus 로고
    • TDP-43 is recruited to stress granules in conditions of oxidative insult
    • Colombrita C, Zennaro E, Fallini C, Weber M, Sommacal A, et al. (2009) TDP-43 is recruited to stress granules in conditions of oxidative insult. J Neurochem 111: 1051-1061.
    • (2009) J Neurochem , vol.111 , pp. 1051-1061
    • Colombrita, C.1    Zennaro, E.2    Fallini, C.3    Weber, M.4    Sommacal, A.5
  • 64
    • 79959869692 scopus 로고    scopus 로고
    • FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis
    • Kryndushkin D, Wickner RB, Shewmaker F, FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis. Protein Cell 2: 223-236.
    • Protein Cell , vol.2 , pp. 223-236
    • Kryndushkin, D.1    Wickner, R.B.2    Shewmaker, F.3
  • 65
    • 79953183632 scopus 로고    scopus 로고
    • Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy
    • Fushimi K, Long C, Jayaram N, Chen X, Li L, et al. Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy. Protein Cell 2: 141-149.
    • Protein Cell , vol.2 , pp. 141-149
    • Fushimi, K.1    Long, C.2    Jayaram, N.3    Chen, X.4    Li, L.5
  • 66
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW, (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19: R46-64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 67
    • 34848921202 scopus 로고    scopus 로고
    • Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
    • Zhang YJ, Xu YF, Dickey CA, Buratti E, Baralle F, et al. (2007) Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J Neurosci 27: 10530-10534.
    • (2007) J Neurosci , vol.27 , pp. 10530-10534
    • Zhang, Y.J.1    Xu, Y.F.2    Dickey, C.A.3    Buratti, E.4    Baralle, F.5
  • 68
    • 56049083010 scopus 로고    scopus 로고
    • Common variation in the miR-659 binding-site of GRN is a major risk factor for TDP43-positive frontotemporal dementia
    • Rademakers R, Eriksen JL, Baker M, Robinson T, Ahmed Z, et al. (2008) Common variation in the miR-659 binding-site of GRN is a major risk factor for TDP43-positive frontotemporal dementia. Hum Mol Genet 17: 3631-3642.
    • (2008) Hum Mol Genet , vol.17 , pp. 3631-3642
    • Rademakers, R.1    Eriksen, J.L.2    Baker, M.3    Robinson, T.4    Ahmed, Z.5
  • 69
    • 78651299905 scopus 로고    scopus 로고
    • Increased caspase activation and decreased TDP-43 solubility in progranulin knockout cortical cultures
    • Kleinberger G, Wils H, Ponsaerts P, Joris G, Timmermans JP, et al. (2010) Increased caspase activation and decreased TDP-43 solubility in progranulin knockout cortical cultures. J Neurochem 115: 735-747.
    • (2010) J Neurochem , vol.115 , pp. 735-747
    • Kleinberger, G.1    Wils, H.2    Ponsaerts, P.3    Joris, G.4    Timmermans, J.P.5
  • 70
    • 77953194507 scopus 로고    scopus 로고
    • TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97
    • Ritson GP, Custer SK, Freibaum BD, Guinto JB, Geffel D, et al. TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97. J Neurosci 30: 7729-7739.
    • J Neurosci , vol.30 , pp. 7729-7739
    • Ritson, G.P.1    Custer, S.K.2    Freibaum, B.D.3    Guinto, J.B.4    Geffel, D.5
  • 71
    • 66449134941 scopus 로고    scopus 로고
    • VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death
    • Gitcho MA, Strider J, Carter D, Taylor-Reinwald L, Forman MS, et al. (2009) VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem 284: 12384-12398.
    • (2009) J Biol Chem , vol.284 , pp. 12384-12398
    • Gitcho, M.A.1    Strider, J.2    Carter, D.3    Taylor-Reinwald, L.4    Forman, M.S.5
  • 73
    • 0034841786 scopus 로고    scopus 로고
    • Double in situ hybridization techniques in zebrafish
    • Jowett T, (2001) Double in situ hybridization techniques in zebrafish. Methods 23: 345-358.
    • (2001) Methods , vol.23 , pp. 345-358
    • Jowett, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.