메뉴 건너뛰기




Volumn 9, Issue 4, 2011, Pages

Molecular determinants and genetic modifiers of aggregation and toxicity for the als disease protein fus/tls

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOMER; PROTEIN FUS; PROTEIN TLS; RNA BINDING PROTEIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; HYBRID PROTEIN; PROTEIN TDP-43;

EID: 79955502687     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1000614     Document Type: Article
Times cited : (366)

References (105)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D, Siddique T, Patterson D, Figlewicz D, Sapp P, et al. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362: 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.4    Sapp, P.5
  • 2
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS
    • Cleveland D. W, Rothstein J. D, (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2: 806-819.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 3
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu D. M, Kwong L. K, Truax A. C, Micsenyi M. C, et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314: 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5
  • 4
    • 34447103093 scopus 로고    scopus 로고
    • TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease
    • Kwong L. K, Neumann M, Sampathu D. M, Lee V. M, Trojanowski J. Q, (2007) TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol 114: 63-70.
    • (2007) Acta Neuropathol , vol.114 , pp. 63-70
    • Kwong, L.K.1    Neumann, M.2    Sampathu, D.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 5
    • 77950867149 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 in neurodegenerative disease
    • Chen-Plotkin A. S, Lee V. M, Trojanowski J. Q, (2010) TAR DNA-binding protein 43 in neurodegenerative disease. Nat Rev Neurol 6: 211-220.
    • (2010) Nat Rev Neurol , vol.6 , pp. 211-220
    • Chen-Plotkin, A.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 6
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis G. S, Lee V. M, Trojanowski J. Q, (2009) Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum Mol Genet 18: R156-R162.
    • (2009) Hum Mol Genet , vol.18
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 8
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis P. N, Dion P, Spiegelman D, McConkey B. J, 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
  • 9
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair I. P, Tripathi V. B, 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
  • 10
    • 41949100148 scopus 로고    scopus 로고
    • TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis
    • Van Deerlin V. M, Leverenz J. B, Bekris L. M, Bird T. D, Yuan W, et al. (2008) TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol 7: 409-416.
    • (2008) Lancet Neurol , vol.7 , pp. 409-416
    • Van Deerlin, V.M.1    Leverenz, J.B.2    Bekris, L.M.3    Bird, T.D.4    Yuan, W.5
  • 11
    • 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
  • 12
    • 70350572209 scopus 로고    scopus 로고
    • TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea
    • Kovacs G. G, Murrell J. R, Horvath S, Haraszti L, Majtenyi K, et al. (2009) TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea. Mov Disord 24: 1843-1847.
    • (2009) Mov Disord , vol.24 , pp. 1843-1847
    • Kovacs, G.G.1    Murrell, J.R.2    Horvath, S.3    Haraszti, L.4    Majtenyi, K.5
  • 13
    • 37349072946 scopus 로고    scopus 로고
    • Beer and bread to brains and beyond: can yeast cells teach us about neurodegenerative disease?
    • Gitler A. D, (2008) Beer and bread to brains and beyond: can yeast cells teach us about neurodegenerative disease? Neurosignals 16: 52-62.
    • (2008) Neurosignals , vol.16 , pp. 52-62
    • Gitler, A.D.1
  • 14
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson B. S, McCaffery J. M, Lindquist S, Gitler A. D, (2008) A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci U S A 105: 6439-6444.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 15
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson B. S, Snead D, Lee J. J, McCaffery J. M, Shorter J, et al. (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284: 20329-20339.
    • (2009) J Biol Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5
  • 16
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • Elden A. C, Kim H. J, Hart M. P, Chen-Plotkin A. S, Johnson B. S, et al. (2010) Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466: 1069-1075.
    • (2010) 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
  • 17
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T. J Jr, Bosco D. A, Leclerc A. L, Tamrazian E, Vanderburg C. R, 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
  • 18
    • 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 K. J, Nishimura A. L, 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
  • 19
    • 78650645588 scopus 로고    scopus 로고
    • FUS mutations in frontotemporal lobar degeneration with amyotrophic lateral sclerosis
    • Broustal O, Camuzat A, Guillot-Noel L, Guy N, Millecamps S, et al. (2010) FUS mutations in frontotemporal lobar degeneration with amyotrophic lateral sclerosis. J Alzheimers Dis 22: 765-769.
    • (2010) J Alzheimers Dis , vol.22 , pp. 765-769
    • Broustal, O.1    Camuzat, A.2    Guillot-Noel, L.3    Guy, N.4    Millecamps, S.5
  • 20
    • 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: 955-1007.
    • (2010) Lancet Neurol , vol.9 , pp. 955-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 21
    • 78449287318 scopus 로고    scopus 로고
    • Extensive FUS-immunoreactive pathology in juvenile amyotrophic lateral sclerosis with basophilic inclusions
    • Huang E. J, Zhang J, Geser F, Trojanowski J. Q, Strober J. B, et al. (2010) Extensive FUS-immunoreactive pathology in juvenile amyotrophic lateral sclerosis with basophilic inclusions. Brain Pathol 20: 1069-1076.
    • (2010) Brain Pathol , vol.20 , pp. 1069-1076
    • Huang, E.J.1    Zhang, J.2    Geser, F.3    Trojanowski, J.Q.4    Strober, J.B.5
  • 23
    • 77953872890 scopus 로고    scopus 로고
    • FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration
    • Urwin H, Josephs K. A, Rohrer J. D, Mackenzie I. R, Neumann M, et al. (2010) FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration. Acta Neuropathol 120: 33-41.
    • (2010) Acta Neuropathol , vol.120 , pp. 33-41
    • Urwin, H.1    Josephs, K.A.2    Rohrer, J.D.3    Mackenzie, I.R.4    Neumann, M.5
  • 24
    • 73249135817 scopus 로고    scopus 로고
    • The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases
    • Doi H, Koyano S, Suzuki Y, Nukina N, Kuroiwa Y, (2010) The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases. Neurosci Res 66: 131-133.
    • (2010) Neurosci Res , vol.66 , pp. 131-133
    • Doi, H.1    Koyano, S.2    Suzuki, Y.3    Nukina, N.4    Kuroiwa, Y.5
  • 25
    • 77950788517 scopus 로고    scopus 로고
    • FUS-immunoreactive intranuclear inclusions in neurodegenerative disease
    • Woulfe J, Gray D. A, Mackenzie I. R, (2010) FUS-immunoreactive intranuclear inclusions in neurodegenerative disease. Brain Pathol 20: 589-597.
    • (2010) Brain Pathol , vol.20 , pp. 589-597
    • Woulfe, J.1    Gray, D.A.2    Mackenzie, I.R.3
  • 26
    • 0027227651 scopus 로고
    • Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
    • Crozat A, Aman P, Mandahl N, Ron D, (1993) Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature 363: 640-644.
    • (1993) Nature , vol.363 , pp. 640-644
    • Crozat, A.1    Aman, P.2    Mandahl, N.3    Ron, D.4
  • 27
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner H, Sok J, Immanuel D, Yin Y, Ron D, (1997) TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J Cell Sci 110 (Pt 15): 1741-1750.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 15 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5
  • 28
    • 23944464489 scopus 로고    scopus 로고
    • Mass spectroscopy identifies the splicing-associated proteins, PSF, hnRNP H3, hnRNP A2/B1, and TLS/FUS as interacting partners of the ZNF198 protein associated with rearrangement in myeloproliferative disease
    • Kasyapa C. S, Kunapuli P, Cowell J. K, (2005) Mass spectroscopy identifies the splicing-associated proteins, PSF, hnRNP H3, hnRNP A2/B1, and TLS/FUS as interacting partners of the ZNF198 protein associated with rearrangement in myeloproliferative disease. Exp Cell Res 309: 78-85.
    • (2005) Exp Cell Res , vol.309 , pp. 78-85
    • Kasyapa, C.S.1    Kunapuli, P.2    Cowell, J.K.3
  • 29
    • 0029812470 scopus 로고    scopus 로고
    • hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • Bertolotti A, Lutz Y, Heard D. J, Chambon P, Tora L, (1996) hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II. EMBO J 15: 5022-5031.
    • (1996) EMBO J , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 30
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, et al. (2005) The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr Biol 15: 587-593.
    • (2005) Curr Biol , vol.15 , pp. 587-593
    • Fujii, R.1    Okabe, S.2    Urushido, T.3    Inoue, K.4    Yoshimura, A.5
  • 31
    • 58149250327 scopus 로고    scopus 로고
    • TLS-GFP cannot rescue mRNP formation near spines and spine phenotype in TLS-KO
    • Fujii R, Grossenbacher-Zinchuk O, Jamari I, Wang Y, Zinchuk V, et al. (2009) TLS-GFP cannot rescue mRNP formation near spines and spine phenotype in TLS-KO. Neuroreport 20: 57-61.
    • (2009) Neuroreport , vol.20 , pp. 57-61
    • Fujii, R.1    Grossenbacher-Zinchuk, O.2    Jamari, I.3    Wang, Y.4    Zinchuk, V.5
  • 32
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S, (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 33
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: blurring the divide between transmissibility and infectivity
    • Cushman M, Johnson B. S, King O. D, Gitler A. D, Shorter J, (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123: 1191-1201.
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 34
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S, (2005) Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 6: 435-450.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 35
    • 77956155794 scopus 로고    scopus 로고
    • Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
    • Fuentealba R. A, Udan M, Bell S, Wegorzewska I, Shao J, et al. (2010) Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J Biol Chem 285: 26304-26314.
    • (2010) J Biol Chem , vol.285 , pp. 26304-26314
    • Fuentealba, R.A.1    Udan, M.2    Bell, S.3    Wegorzewska, I.4    Shao, J.5
  • 36
    • 78651394950 scopus 로고    scopus 로고
    • Implications of the prion-related Q/N domains in TDP-43 and FUS
    • Udan M, Baloh R. H, (2011) Implications of the prion-related Q/N domains in TDP-43 and FUS. Prion 5.
    • (2011) Prion , vol.5
    • Udan, M.1    Baloh, R.H.2
  • 37
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland D. W, (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19: R46-R64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 38
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: the FUS about TDP-43
    • Lagier-Tourenne C, Cleveland D. W, (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
  • 39
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • Cooper A. A, Gitler A. D, Cashikar A, Haynes C. M, Hill K. J, et al. (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313: 324-328.
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3    Haynes, C.M.4    Hill, K.J.5
  • 40
    • 61349147706 scopus 로고    scopus 로고
    • Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity
    • Gitler A. D, Chesi A, Geddie M. L, Strathearn K. E, Hamamichi S, et al. (2009) Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41: 308-315.
    • (2009) Nat Genet , vol.41 , pp. 308-315
    • Gitler, A.D.1    Chesi, A.2    Geddie, M.L.3    Strathearn, K.E.4    Hamamichi, S.5
  • 41
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, et al. (1997) Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90: 549-558.
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5
  • 43
    • 71449084004 scopus 로고    scopus 로고
    • The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
    • Tam S, Spiess C, Auyeung W, Joachimiak L, Chen B, et al. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat Struct Mol Biol 16: 1279-1285.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1279-1285
    • Tam, S.1    Spiess, C.2    Auyeung, W.3    Joachimiak, L.4    Chen, B.5
  • 44
    • 18144406846 scopus 로고    scopus 로고
    • A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease
    • Giorgini F, Guidetti P, Nguyen Q, Bennett S. C, Muchowski P. J, (2005) A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet 37: 526-531.
    • (2005) Nat Genet , vol.37 , pp. 526-531
    • Giorgini, F.1    Guidetti, P.2    Nguyen, Q.3    Bennett, S.C.4    Muchowski, P.J.5
  • 45
    • 0345189365 scopus 로고    scopus 로고
    • Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein
    • Willingham S, Outeiro T. F, DeVit M. J, Lindquist S. L, Muchowski P. J, (2003) Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 302: 1769-1772.
    • (2003) Science , vol.302 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 46
  • 47
    • 70449528427 scopus 로고    scopus 로고
    • TARDBP 3′-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy
    • Gitcho M. A, Bigio E. H, Mishra M, Johnson N, Weintraub S, et al. (2009) TARDBP 3′-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy. Acta Neuropathol 118: 633-645.
    • (2009) Acta Neuropathol , vol.118 , pp. 633-645
    • Gitcho, M.A.1    Bigio, E.H.2    Mishra, M.3    Johnson, N.4    Weintraub, S.5
  • 48
  • 50
    • 77954643023 scopus 로고    scopus 로고
    • Sustained expression of TDP-43 and FUS in motor neurons in rodent's lifetime
    • Huang C, Xia P. Y, Zhou H, (2010) Sustained expression of TDP-43 and FUS in motor neurons in rodent's lifetime. Int J Biol Sci 6: 396-406.
    • (2010) Int J Biol Sci , vol.6 , pp. 396-406
    • Huang, C.1    Xia, P.Y.2    Zhou, H.3
  • 51
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco D. A, Lemay N, Ko H. K, Zhou H, Burke C, et al. (2010) Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 19: 4160-4175.
    • (2010) 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
  • 52
    • 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. (2010) ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import. EMBO J 29: 2841-2857.
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5
  • 53
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Neurobiol Aging, E-pub ahead of print. doi:10.1016/j.neurobiolaging.2010.06.010
    • Gal J, Zhang J, Kwinter D. M, Zhai J, Jia H, et al. (2010) Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging E-pub ahead of print. doi:10.1016/j.neurobiolaging.2010.06.010.
    • (2010)
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5
  • 54
    • 79954616116 scopus 로고    scopus 로고
    • Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations
    • E-pub ahead of print. doi: 10.1093/nar/gkq1162
    • Kino Y, Washizu C, Aquilanti E, Okuno M, Kurosawa M, et al. (2010) Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations. Nucleic Acids Res E-pub ahead of print. doi: 10.1093/nar/gkq1162.
    • (2010) Nucleic Acids Res
    • Kino, Y.1    Washizu, C.2    Aquilanti, E.3    Okuno, M.4    Kurosawa, M.5
  • 55
    • 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, (2010) Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann Neurol 69: 152-162.
    • (2010) Ann Neurol , vol.69 , pp. 152-162
    • Ito, D.1    Seki, M.2    Tsunoda, Y.3    Uchiyama, H.4    Suzuki, N.5
  • 56
    • 79955495201 scopus 로고    scopus 로고
    • A yeast model of FUS/TLS-dependent cytotoxicity
    • 10.1371/journal.pbio.1001052
    • Ju S, Tardiff D. F, Han H, Divya K, Zhong Q, et al. (2011) A yeast model of FUS/TLS-dependent cytotoxicity. PLoS Biology doi:10.1371/journal.pbio.1001052.
    • (2011) PLoS Biology
    • Ju, S.1    Tardiff, D.F.2    Han, H.3    Divya, K.4    Zhong, Q.5
  • 57
    • 0022516246 scopus 로고
    • Synthetic peptides as nuclear localization signals
    • Schoolnik G, Kornberg RD
    • Goldfarb D. S, Gariepy J, Schoolnik G, Kornberg RD (1986) Synthetic peptides as nuclear localization signals. Nature 322: 641-644.
    • (1986) Nature , vol.322 , pp. 641-644
    • Goldfarb, D.S.1    Gariepy, J.2
  • 58
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan J. R, Muhlrad D, Parker R, (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 183: 441-455.
    • (2008) J Cell Biol , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 59
    • 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
  • 60
    • 34247229733 scopus 로고    scopus 로고
    • Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules
    • Nonhoff U, Ralser M, Welzel F, Piccini I, Balzereit D, et al. (2007) Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules. Mol Biol Cell 18: 1385-1396.
    • (2007) Mol Biol Cell , vol.18 , pp. 1385-1396
    • Nonhoff, U.1    Ralser, M.2    Welzel, F.3    Piccini, I.4    Balzereit, D.5
  • 61
    • 26444552945 scopus 로고    scopus 로고
    • Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways
    • Ralser M, Nonhoff U, Albrecht M, Lengauer T, Wanker E. E, et al. (2005) Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways. Hum Mol Genet 14: 2893-2909.
    • (2005) Hum Mol Genet , vol.14 , pp. 2893-2909
    • Ralser, M.1    Nonhoff, U.2    Albrecht, M.3    Lengauer, T.4    Wanker, E.E.5
  • 62
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum B. D, Chitta R. K, High A. A, Taylor J. P, (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J Proteome Res 9: 1104-1120.
    • (2010) J Proteome Res , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 63
    • 77956047670 scopus 로고    scopus 로고
    • Analyzing P-bodies and stress granules in Saccharomyces cerevisiae
    • Buchan J. R, Nissan T, Parker R, (2010) Analyzing P-bodies and stress granules in Saccharomyces cerevisiae. Methods Enzymol 470: 619-640.
    • (2010) Methods Enzymol , vol.470 , pp. 619-640
    • Buchan, J.R.1    Nissan, T.2    Parker, R.3
  • 64
  • 65
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies
    • Igaz L. M, Kwong L. K, Chen-Plotkin A, Winton M. J, Unger T. L, et al. (2009) Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J Biol Chem 284: 8516-8524.
    • (2009) J Biol Chem , vol.284 , pp. 8516-8524
    • Igaz, L.M.1    Kwong, L.K.2    Chen-Plotkin, A.3    Winton, M.J.4    Unger, T.L.5
  • 66
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala Y. M, Zago P, D'Ambrogio A, Xu Y. F, 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
  • 67
    • 67650718130 scopus 로고    scopus 로고
    • NLStradamus: a simple Hidden Markov Model for nuclear localization signal prediction
    • Nguyen Ba A. N, Pogoutse A, Provart N, Moses A. M, (2009) NLStradamus: a simple Hidden Markov Model for nuclear localization signal prediction. BMC Bioinformatics 10: 202.
    • (2009) BMC Bioinformatics , vol.10 , pp. 202
    • Nguyen Ba, A.N.1    Pogoutse, A.2    Provart, N.3    Moses, A.M.4
  • 68
    • 77951784437 scopus 로고    scopus 로고
    • De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis
    • Dejesus-Hernandez M, Kocerha J, Finch N, Crook R, Baker M, et al. (2010) De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis. Hum Mutat 31: E1377-E1389.
    • (2010) Hum Mutat , vol.31
    • Dejesus-Hernandez, M.1    Kocerha, J.2    Finch, N.3    Crook, R.4    Baker, M.5
  • 69
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle F. E, (2001) Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 276: 36337-36343.
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 70
    • 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 S. H, Shanware N. P, Bowler M. J, Tibbetts R. S, (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
  • 71
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D. B, Johnson K. S, (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67: 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 73
    • 37349039461 scopus 로고    scopus 로고
    • TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis
    • Kwong L. K, Uryu K, Trojanowski J. Q, Lee V. M, (2008) TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis. Neurosignals 16: 41-51.
    • (2008) Neurosignals , vol.16 , pp. 41-51
    • Kwong, L.K.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 74
    • 23644449548 scopus 로고    scopus 로고
    • Influence of the N-terminal domain on the aggregation properties of the prion protein
    • Frankenfield K. N, Powers E. T, Kelly J. W, (2005) Influence of the N-terminal domain on the aggregation properties of the prion protein. Protein Sci 14: 2154-2166.
    • (2005) Protein Sci , vol.14 , pp. 2154-2166
    • Frankenfield, K.N.1    Powers, E.T.2    Kelly, J.W.3
  • 75
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman A. R, White J. T, Powers E. T, Kelly J. W, (2004) Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43: 7365-7381.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 76
    • 0022456807 scopus 로고
    • The measurement of cooperative protein self-assembly by turbidity and other techniques
    • Andreu J. M, Timasheff S. N, (1986) The measurement of cooperative protein self-assembly by turbidity and other techniques. Methods Enzymol 130: 47-59.
    • (1986) Methods Enzymol , vol.130 , pp. 47-59
    • Andreu, J.M.1    Timasheff, S.N.2
  • 77
    • 77955897545 scopus 로고    scopus 로고
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
    • Baumer D, Hilton D, Paine S. M, Turner M. R, Lowe J, et al. (2010) Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75: 611-618.
    • (2010) Neurology , vol.75 , pp. 611-618
    • Baumer, D.1    Hilton, D.2    Paine, S.M.3    Turner, M.R.4    Lowe, J.5
  • 78
    • 77953194507 scopus 로고    scopus 로고
    • TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97
    • Ritson G. P, Custer S. K, Freibaum B. D, Guinto J. B, Geffel D, et al. (2010) TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97. J Neurosci 30: 7729-7739.
    • (2010) 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
  • 79
    • 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 M. L, Dion P. A, 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
  • 80
    • 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 S. J, Skibinski G, Korb E, Rao E. J, Wu J. Y, et al. (2010) 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.
    • (2010) 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
  • 81
    • 61349114190 scopus 로고    scopus 로고
    • Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity
    • Yeger-Lotem E, Riva L, Su L. J, Gitler A. D, Cashikar A. G, et al. (2009) Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity. Nat Genet 41: 316-323.
    • (2009) Nat Genet , vol.41 , pp. 316-323
    • Yeger-Lotem, E.1    Riva, L.2    Su, L.J.3    Gitler, A.D.4    Cashikar, A.G.5
  • 82
    • 34147092780 scopus 로고    scopus 로고
    • Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae
    • Hu Y, Rolfs A, Bhullar B, Murthy T. V, Zhu C, et al. (2007) Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Genome Res 17: 536-543.
    • (2007) Genome Res , vol.17 , pp. 536-543
    • Hu, Y.1    Rolfs, A.2    Bhullar, B.3    Murthy, T.V.4    Zhu, C.5
  • 83
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan J. R, Parker R, (2009) Eukaryotic stress granules: the ins and outs of translation. Mol Cell 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 84
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever G, Chu A. M, Ni L, Connelly C, Riles L, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418: 387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1    Chu, A.M.2    Ni, L.3    Connelly, C.4    Riles, L.5
  • 86
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • Tong A. H, Lesage G, Bader G. D, Ding H, Xu H, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303: 808-813.
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.1    Lesage, G.2    Bader, G.D.3    Ding, H.4    Xu, H.5
  • 87
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong A. H, Evangelista M, Parsons A. B, Xu H, Bader G. D, et al. (2001) Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294: 2364-2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5
  • 88
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
    • 10.1371/journal.pone.0001763
    • Sadlish H, Rampelt H, Shorter J, Wegrzyn R. D, Andreasson C, et al. (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 3: e1763 doi:10.1371/journal.pone.0001763.
    • (2008) PLoS One , vol.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andreasson, C.5
  • 89
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, et al. (2004) Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell 15: 5383-5398.
    • (2004) Mol Biol Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1    Kedersha, N.2    Ayodele, M.3    Shen, L.4    Stoecklin, G.5
  • 90
    • 65549100291 scopus 로고    scopus 로고
    • Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases
    • Furukawa Y, Kaneko K, Matsumoto G, Kurosawa M, Nukina N, (2009) Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases. J Neurosci 29: 5153-5162.
    • (2009) J Neurosci , vol.29 , pp. 5153-5162
    • Furukawa, Y.1    Kaneko, K.2    Matsumoto, G.3    Kurosawa, M.4    Nukina, N.5
  • 91
    • 44449177217 scopus 로고    scopus 로고
    • RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells
    • Doi H, Okamura K, Bauer P. O, Furukawa Y, Shimizu H, et al. (2008) RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. J Biol Chem 283: 6489-6500.
    • (2008) J Biol Chem , vol.283 , pp. 6489-6500
    • Doi, H.1    Okamura, K.2    Bauer, P.O.3    Furukawa, Y.4    Shimizu, H.5
  • 92
    • 77952932485 scopus 로고    scopus 로고
    • FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis
    • Deng H. X, Zhai H, Bigio E. H, Yan J, Fecto F, et al. (2010) FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis. Ann Neurol 67: 739-748.
    • (2010) Ann Neurol , vol.67 , pp. 739-748
    • Deng, H.X.1    Zhai, H.2    Bigio, E.H.3    Yan, J.4    Fecto, F.5
  • 93
    • 77954653461 scopus 로고    scopus 로고
    • Neurotoxic effects of TDP-43 overexpression in C. elegans
    • Ash P. E, Zhang Y. J, Roberts C. M, Saldi T, Hutter H, et al. (2010) Neurotoxic effects of TDP-43 overexpression in C. elegans. Hum Mol Genet 19: 3206-3218.
    • (2010) Hum Mol Genet , vol.19 , pp. 3206-3218
    • Ash, P.E.1    Zhang, Y.J.2    Roberts, C.M.3    Saldi, T.4    Hutter, H.5
  • 94
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y, Eisenberg D, (2002) 3D domain swapping: as domains continue to swap. Protein Sci 11: 1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 95
    • 33744497267 scopus 로고    scopus 로고
    • Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I
    • Guo Z, Eisenberg D, (2006) Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proc Natl Acad Sci U S A 103: 8042-8047.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8042-8047
    • Guo, Z.1    Eisenberg, D.2
  • 97
    • 77955784599 scopus 로고    scopus 로고
    • ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
    • Ling S. C, Albuquerque C. P, Han J. S, Lagier-Tourenne C, Tokunaga S, et al. (2010) ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc Natl Acad Sci U S A 107: 13318-13323.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13318-13323
    • Ling, S.C.1    Albuquerque, C.P.2    Han, J.S.3    Lagier-Tourenne, C.4    Tokunaga, S.5
  • 98
    • 66049158810 scopus 로고    scopus 로고
    • Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs
    • Balagopal V, Parker R, (2009) Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs. Curr Opin Cell Biol 21: 403-408.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 403-408
    • Balagopal, V.1    Parker, R.2
  • 99
    • 0032032013 scopus 로고    scopus 로고
    • Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis
    • Lin C. L, Bristol L. A, Jin L, Dykes-Hoberg M, Crawford T, et al. (1998) Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron 20: 589-602.
    • (1998) Neuron , vol.20 , pp. 589-602
    • Lin, C.L.1    Bristol, L.A.2    Jin, L.3    Dykes-Hoberg, M.4    Crawford, T.5
  • 100
    • 35349022993 scopus 로고    scopus 로고
    • A suite of Gateway((R)) cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae
    • Alberti S, Gitler A. D, Lindquist S, (2007) A suite of Gateway((R)) cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast 24: 913-919.
    • (2007) Yeast , vol.24 , pp. 913-919
    • Alberti, S.1    Gitler, A.D.2    Lindquist, S.3
  • 101
    • 79955489230 scopus 로고    scopus 로고
    • Methods in ezymology: guide to yeast genetics and molecular and cell biology
    • Guthrie C, Fink G. R, (2002) Methods in ezymology: guide to yeast genetics and molecular and cell biology. Academic Press 169.
    • (2002) Academic Press , vol.169
    • Guthrie, C.1    Fink, G.R.2
  • 102
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A, (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168.
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 103
    • 33644807842 scopus 로고    scopus 로고
    • Synthetic genetic array analysis in Saccharomyces cerevisiae
    • Tong A. H, Boone C, (2006) Synthetic genetic array analysis in Saccharomyces cerevisiae. Methods Mol Biol 313: 171-192.
    • (2006) Methods Mol Biol , vol.313 , pp. 171-192
    • Tong, A.H.1    Boone, C.2
  • 104
    • 33747367151 scopus 로고    scopus 로고
    • A strategy for extracting and analyzing large-scale quantitative epistatic interaction data
    • Collins S. R, Schuldiner M, Krogan N. J, Weissman J. S, (2006) A strategy for extracting and analyzing large-scale quantitative epistatic interaction data. Genome Biol 7: R63.
    • (2006) Genome Biol , vol.7
    • Collins, S.R.1    Schuldiner, M.2    Krogan, N.J.3    Weissman, J.S.4
  • 105
    • 23844471326 scopus 로고    scopus 로고
    • HnRNP L represses exon splicing via a regulated exonic splicing silencer
    • Rothrock C. R, House A. E, Lynch K. W, (2005) HnRNP L represses exon splicing via a regulated exonic splicing silencer. EMBO J 24: 2792-2802.
    • (2005) EMBO J , vol.24 , pp. 2792-2802
    • Rothrock, C.R.1    House, A.E.2    Lynch, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.