메뉴 건너뛰기




Volumn 1462, Issue , 2012, Pages 44-60

FUS-related proteinopathies: Lessons from animal models

Author keywords

Amyotrophic lateral sclerosis; Animal models; FUS; Neurodegeneration; TDP 43

Indexed keywords

FUSED IN SARCOMA PROTEIN; MESSENGER RNA; MICRORNA; PRION PROTEIN; RNA; RNA BINDING PROTEIN; RNA BINDING PROTEIN EWS; TAR DNA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR 15; UNCLASSIFIED DRUG;

EID: 84862149644     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2012.01.039     Document Type: Review
Times cited : (52)

References (155)
  • 1
    • 84155163741 scopus 로고    scopus 로고
    • A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis
    • A. Al-Saif, F. Al-Mohanna, and S. Bohlega A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis Ann. Neurol. 2011 913 919
    • (2011) Ann. Neurol. , pp. 913-919
    • Al-Saif, A.1    Al-Mohanna, F.2    Bohlega, S.3
  • 2
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • S. Alberti, R. Halfmann, O. King, A. Kapila, and S. Lindquist A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137 2009 146 158
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 3
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • M.K. Andersson, A. Stahlberg, Y. Arvidsson, A. Olofsson, H. Semb, G. Stenman, O. Nilsson, and P. Aman The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response BMC Cell Biol. 9 2008 37
    • (2008) BMC Cell Biol. , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5    Stenman, G.6    Nilsson, O.7    Aman, P.8
  • 7
    • 0033607753 scopus 로고    scopus 로고
    • Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation
    • H. Baechtold, M. Kuroda, J. Sok, D. Ron, B.S. Lopez, and A.T. Akhmedov Human 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formation J. Biol. Chem. 274 1999 34337 34342 (Pubitemid 129511776)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.48 , pp. 34337-34342
    • Baechtold, H.1    Kuroda, M.2    Sok, J.3    Ron, D.4    Lopez, B.S.5    Akhmedov, A.T.6
  • 9
    • 17444381645 scopus 로고    scopus 로고
    • Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: Exclusion from the nucleus and accumulation in dendritic granules and spine heads
    • DOI 10.1016/j.neulet.2004.12.071
    • A. Belly, F. Moreau-Gachelin, R. Sadoul, and Y. Goldberg Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads Neurosci. Lett. 379 2005 152 157 (Pubitemid 40544525)
    • (2005) Neuroscience Letters , vol.379 , Issue.3 , pp. 152-157
    • Belly, A.1    Moreau-Gachelin, F.2    Sadoul, R.3    Goldberg, Y.4
  • 13
    • 0017744030 scopus 로고
    • Identification and characterization of the packaging proteins of core 40S hnRNP particles
    • A.L. Beyer, M.E. Christensen, B.W. Walker, and W.M. LeStourgeon Identification and characterization of the packaging proteins of core 40S hnRNP particles Cell 11 1977 127 138 (Pubitemid 8126060)
    • (1977) Cell , vol.11 , Issue.1 , pp. 127-138
    • Beyer, A.L.1    Christensen, M.E.2    Walker, B.W.3    LeStourgeon, W.M.4
  • 20
  • 21
    • 0000918282 scopus 로고
    • On intracellular inclusions in familial amyotrophic lateral sclerosis
    • T.L. BUNINA On intracellular inclusions in familial amyotrophic lateral sclerosis Zh. Nevropatol. Psikhiatr. Im. S S Korsakova 62 1962 1293 1299
    • (1962) Zh. Nevropatol. Psikhiatr. Im. S S Korsakova , vol.62 , pp. 1293-1299
    • Bunina, T.L.1
  • 22
    • 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
    • E. Buratti, and F.E. Baralle 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 2001 36337 36343
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 26
    • 77956270117 scopus 로고    scopus 로고
    • Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis
    • R. Chia, M.H. Tattum, S. Jones, J. Collinge, E.M. Fisher, and G.S. Jackson Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis PLoS One 5 2010 e10627
    • (2010) PLoS One , vol.5 , pp. 10627
    • Chia, R.1    Tattum, M.H.2    Jones, S.3    Collinge, J.4    Fisher, E.M.5    Jackson, G.S.6
  • 32
    • 0034639940 scopus 로고    scopus 로고
    • A role for Caenorhabditis elegans in understanding the function and interactions of human disease genes
    • E. Culetto, and D.B. Sattelle A role for Caenorhabditis elegans in understanding the function and interactions of human disease genes Hum. Mol. Genet. 9 2000 869 877 (Pubitemid 30216097)
    • (2000) Human Molecular Genetics , vol.9 , Issue.6 , pp. 869-877
    • Culetto, E.1    Sattelle, D.B.2
  • 33
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: Blurring the divide between transmissibility and infectivity
    • M. Cushman, B.S. Johnson, O.D. King, A.D. Gitler, and J. Shorter Prion-like disorders: blurring the divide between transmissibility and infectivity J. Cell Sci. 123 2010 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
  • 40
    • 77955841798 scopus 로고    scopus 로고
    • Neurodegenerative disorders: Insights from the nematode Caenorhabditis elegans
    • M. Dimitriadi, and A.C. Hart Neurodegenerative disorders: insights from the nematode Caenorhabditis elegans Neurobiol. Dis. 40 2010 4 11
    • (2010) Neurobiol. Dis. , vol.40 , pp. 4-11
    • Dimitriadi, M.1    Hart, A.C.2
  • 43
    • 79151471350 scopus 로고    scopus 로고
    • TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation
    • K. Du, S. Arai, T. Kawamura, A. Matsushita, and R. Kurokawa TLS and PRMT1 synergistically coactivate transcription at the survivin promoter through TLS arginine methylation Biochem. Biophys. Res. Commun. 404 2011 991 996
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 991-996
    • Du, K.1    Arai, S.2    Kawamura, T.3    Matsushita, A.4    Kurokawa, R.5
  • 44
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • B.D. Freibaum, R.K. Chitta, A.A. High, and J.P. Taylor Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery J. Proteome Res. 9 2010 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
  • 45
    • 15744378126 scopus 로고    scopus 로고
    • The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology
    • DOI 10.1016/j.cub.2005.01.058
    • R. Fujii, S. Okabe, T. Urushido, K. Inoue, A. Yoshimura, T. Tachibana, T. Nishikawa, G.G. Hicks, and T. Takumi The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology Curr. Biol. 15 2005 587 593 (Pubitemid 40413401)
    • (2005) Current Biology , vol.15 , Issue.6 , pp. 587-593
    • Fujii, R.1    Okabe, S.2    Urushido, T.3    Inoue, K.4    Yoshimura, A.5    Tachibana, T.6    Nishikawa, T.7    Hicks, G.G.8    Takumi, T.9
  • 46
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions
    • Y. Furukawa, K. Kaneko, S. Watanabe, K. Yamanaka, and N. Nukina A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions J. Biol. Chem. 286 2011 18664 18672
    • (2011) J. Biol. Chem. , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 47
    • 79953183632 scopus 로고    scopus 로고
    • Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy
    • K. Fushimi, C. Long, N. Jayaram, X. Chen, L. Li, and J.Y. Wu Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy Protein Cell 2 2011 141 149
    • (2011) Protein Cell , vol.2 , pp. 141-149
    • Fushimi, K.1    Long, C.2    Jayaram, N.3    Chen, X.4    Li, L.5    Wu, J.Y.6
  • 48
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • J. Gal, J. Zhang, D.M. Kwinter, J. Zhai, H. Jia, J. Jia, and H. Zhu Nuclear localization sequence of FUS and induction of stress granules by ALS mutants Neurobiol. Aging 32 2011 2323 2340
    • (2011) Neurobiol. Aging , vol.32 , pp. 2323-2340
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5    Jia, J.6    Zhu, H.7
  • 49
    • 54049138797 scopus 로고    scopus 로고
    • Identification and characterization of FUS/TLS as a new target of ATM
    • M. Gardiner, R. Toth, F. Vandermoere, N.A. Morrice, and J. Rouse Identification and characterization of FUS/TLS as a new target of ATM Biochem. J. 415 2008 297 307
    • (2008) Biochem. J. , vol.415 , pp. 297-307
    • Gardiner, M.1    Toth, R.2    Vandermoere, F.3    Morrice, N.A.4    Rouse, J.5
  • 51
    • 80052802585 scopus 로고    scopus 로고
    • RNA-binding proteins with prion-like domains in ALS and FTLD-U
    • A.D. Gitler, and J. Shorter RNA-binding proteins with prion-like domains in ALS and FTLD-U Prion 5 2011 179 187
    • (2011) Prion , vol.5 , pp. 179-187
    • Gitler, A.D.1    Shorter, J.2
  • 52
    • 36549065720 scopus 로고    scopus 로고
    • Young-onset sporadic amyotrophic lateral sclerosis: A distinct nosological entity?
    • DOI 10.1080/17482960701553956, PII 781175714
    • L.O. Gouveia, and C.M. de Young-onset sporadic amyotrophic lateral sclerosis: a distinct nosological entity? Amyotroph. Lateral Scler. 8 2007 323 327 (Pubitemid 350176929)
    • (2007) Amyotrophic Lateral Sclerosis , vol.8 , Issue.6 , pp. 323-327
    • Gouveia, L.O.1    De Carvalho, M.2
  • 57
    • 0032570707 scopus 로고    scopus 로고
    • The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS
    • DOI 10.1074/jbc.273.9.4838
    • M. Hallier, A. Lerga, S. Barnache, A. Tavitian, and F. Moreau-Gachelin The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS J. Biol. Chem. 273 1998 4838 4842 (Pubitemid 28108632)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 4838-4842
    • Hallier, M.1    Lerga, A.2    Barnache, S.3    Tavitian, A.4    Moreau-Gachelin, F.5
  • 58
    • 27844433569 scopus 로고    scopus 로고
    • Dynamics of human protein arginine methyltransferase 1 (PRMT1) in vivo
    • DOI 10.1074/jbc.M502458200
    • F. Herrmann, J. Lee, M.T. Bedford, and F.O. Fackelmayer Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo J. Biol. Chem. 280 2005 38005 38010 (Pubitemid 41642414)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 38005-38010
    • Herrmann, F.1    Lee, J.2    Bedford, M.T.3    Fackelmayer, F.O.4
  • 59
    • 66149108467 scopus 로고    scopus 로고
    • Human protein arginine methyltransferases in vivo - Distinct properties of eight canonical members of the PRMT family
    • F. Herrmann, P. Pably, C. Eckerich, M.T. Bedford, and F.O. Fackelmayer Human protein arginine methyltransferases in vivo - distinct properties of eight canonical members of the PRMT family J. Cell Sci. 122 2009 667 677
    • (2009) J. Cell Sci. , vol.122 , pp. 667-677
    • Herrmann, F.1    Pably, P.2    Eckerich, C.3    Bedford, M.T.4    Fackelmayer, F.O.5
  • 63
    • 79953743204 scopus 로고    scopus 로고
    • FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • C. Huang, H. Zhou, J. Tong, H. Chen, Y.J. Liu, D. Wang, X. Wei, and X.G. Xia FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration PLoS Genet. 7 2011 e1002011
    • (2011) PLoS Genet. , vol.7 , pp. 1002011
    • Huang, C.1    Zhou, H.2    Tong, J.3    Chen, H.4    Liu, Y.J.5    Wang, D.6    Wei, X.7    Xia, X.G.8
  • 66
    • 79551472601 scopus 로고    scopus 로고
    • Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS
    • D. Ito, M. Seki, Y. Tsunoda, H. Uchiyama, and N. Suzuki Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS Ann. Neurol. 2010 152 162
    • (2010) Ann. Neurol. , pp. 152-162
    • Ito, D.1    Seki, M.2    Tsunoda, Y.3    Uchiyama, H.4    Suzuki, N.5
  • 67
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • B.S. Johnson, D. Snead, J.J. Lee, J.M. McCaffery, J. Shorter, and A.D. Gitler TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity J. Biol. Chem. 284 2009 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    Gitler, A.D.6
  • 69
    • 80051551180 scopus 로고    scopus 로고
    • SOD1 and TDP-43 animal models of amyotrophic lateral sclerosis: Recent advances in understanding disease toward the development of clinical treatments
    • P.I. Joyce, P. Fratta, E.M. Fisher, and A. Acevedo-Arozena SOD1 and TDP-43 animal models of amyotrophic lateral sclerosis: recent advances in understanding disease toward the development of clinical treatments Mamm. Genome 22 2011 420 448
    • (2011) Mamm. Genome , vol.22 , pp. 420-448
    • Joyce, P.I.1    Fratta, P.2    Fisher, E.M.3    Acevedo-Arozena, A.4
  • 74
    • 2442435550 scopus 로고    scopus 로고
    • nrb associates with the 5′ splice site within large transcription/splicing complexes
    • DOI 10.1038/sj.emboj.7600187
    • S. Kameoka, P. Duque, and M.M. Konarska p54(nrb) associates with the 5′ splice site within large transcription/splicing complexes EMBO J. 23 2004 1782 1791 (Pubitemid 38649641)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 75
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule
    • DOI 10.1016/j.neuron.2004.07.022, PII S0896627304004635
    • Y. Kanai, N. Dohmae, and N. Hirokawa Kinesin transports RNA: isolation and characterization of an RNA-transporting granule Neuron 43 2004 513 525 (Pubitemid 39094678)
    • (2004) Neuron , vol.43 , Issue.4 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 76
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • M. Kiledjian, and G. Dreyfuss Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box EMBO J. 11 1992 2655 2664
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 77
    • 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
    • S.H. Kim, N.P. Shanware, M.J. Bowler, and R.S. Tibbetts 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 2010 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
  • 78
    • 79954616116 scopus 로고    scopus 로고
    • Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations
    • Y. Kino, C. Washizu, E. Aquilanti, M. Okuno, M. Kurosawa, M. Yamada, H. Doi, and N. Nukina Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations Nucleic Acids Res. 39 2011 2781 2798
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2781-2798
    • Kino, Y.1    Washizu, C.2    Aquilanti, E.3    Okuno, M.4    Kurosawa, M.5    Yamada, M.6    Doi, H.7    Nukina, N.8
  • 79
    • 83755172992 scopus 로고    scopus 로고
    • Modeling ALS and FTLD proteinopathies in yeast: An efficient approach for studying protein aggregation and toxicity
    • D. Kryndushkin, and F. Shewmaker Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity Prion 5 2011 250 257
    • (2011) Prion , vol.5 , pp. 250-257
    • Kryndushkin, D.1    Shewmaker, F.2
  • 80
    • 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
    • D. Kryndushkin, R.B. Wickner, and F. Shewmaker FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis Protein Cell 2 2011 223 236
    • (2011) Protein Cell , vol.2 , pp. 223-236
    • Kryndushkin, D.1    Wickner, R.B.2    Shewmaker, F.3
  • 83
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • C. Lagier-Tourenne, M. Polymenidou, and D.W. Cleveland TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration Hum. Mol. Genet. 19 2010 R46 R64
    • (2010) Hum. Mol. Genet. , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 86
    • 33746776838 scopus 로고    scopus 로고
    • Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2
    • DOI 10.1016/j.cell.2006.05.049, PII S009286740600910X
    • B.J. Lee, A.E. Cansizoglu, K.E. Suel, T.H. Louis, Z. Zhang, and Y.M. Chook Rules for nuclear localization sequence recognition by karyopherin beta 2 Cell 126 2006 543 558 (Pubitemid 44163605)
    • (2006) Cell , vol.126 , Issue.3 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 88
    • 79959354904 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein
    • R.P. Leemann-Zakaryan, S. Pahlich, D. Grossenbacher, and H. Gehring Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein Sarcoma 2011 2011 218483
    • (2011) Sarcoma , vol.2011 , pp. 218483
    • Leemann-Zakaryan, R.P.1    Pahlich, S.2    Grossenbacher, D.3    Gehring, H.4
  • 89
    • 79961148135 scopus 로고    scopus 로고
    • Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
    • H.Y. Li, P.A. Yeh, H.C. Chiu, C.Y. Tang, and B.P. Tu Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation PLoS One 6 2011 e23075
    • (2011) PLoS One , vol.6 , pp. 23075
    • Li, H.Y.1    Yeh, P.A.2    Chiu, H.C.3    Tang, C.Y.4    Tu, B.P.5
  • 91
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Q. Liu, and G. Dreyfuss In vivo and in vitro arginine methylation of RNA-binding proteins Mol. Cell. Biol. 15 1995 2800 2808
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 94
    • 77950858460 scopus 로고    scopus 로고
    • The sigma-1 receptor is enriched in postsynaptic sites of C-terminals in mouse motoneurons. An anatomical and behavioral study
    • T.A. Mavlyutov, M.L. Epstein, K.A. Andersen, L. Ziskind-Conhaim, and A.E. Ruoho The sigma-1 receptor is enriched in postsynaptic sites of C-terminals in mouse motoneurons. An anatomical and behavioral study Neuroscience 167 2010 247 255
    • (2010) Neuroscience , vol.167 , pp. 247-255
    • Mavlyutov, T.A.1    Epstein, M.L.2    Andersen, K.A.3    Ziskind-Conhaim, L.4    Ruoho, A.E.5
  • 96
    • 58049221032 scopus 로고    scopus 로고
    • Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: Implications for TDP-43 in the physiological response to neuronal injury
    • K. Moisse, K. Volkening, C. Leystra-Lantz, I. Welch, T. Hill, and M.J. Strong Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury Brain Res. 1249 2009 202 211
    • (2009) Brain Res. , vol.1249 , pp. 202-211
    • Moisse, K.1    Volkening, K.2    Leystra-Lantz, C.3    Welch, I.4    Hill, T.5    Strong, M.J.6
  • 101
    • 77953032534 scopus 로고    scopus 로고
    • Emerging paradigms of regulated microRNA processing
    • M.A. Newman, and S.M. Hammond Emerging paradigms of regulated microRNA processing Genes Dev. 24 2010 1086 1092
    • (2010) Genes Dev. , vol.24 , pp. 1086-1092
    • Newman, M.A.1    Hammond, S.M.2
  • 104
    • 35948958216 scopus 로고    scopus 로고
    • Erratum: HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration (Autophagy)
    • U.B. Pandey, Y. Batlevi, E.H. Baehrecke, and J.P. Taylor HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration Autophagy 3 2007 643 645 (Pubitemid 350064219)
    • (2007) Autophagy , vol.3 , Issue.6 , pp. 643-645
    • Pandey, U.B.1    Batlevi, Y.2    Baehrecke, E.H.3    Taylor, J.P.4
  • 105
    • 79955749505 scopus 로고    scopus 로고
    • Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery
    • U.B. Pandey, and C.D. Nichols Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery Pharmacol. Rev. 63 2011 411 436
    • (2011) Pharmacol. Rev. , vol.63 , pp. 411-436
    • Pandey, U.B.1    Nichols, C.D.2
  • 107
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in ALS
    • M. Polymenidou, and D.W. Cleveland The seeds of neurodegeneration: prion-like spreading in ALS Cell 147 2011 498 508
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 109
    • 0031915988 scopus 로고    scopus 로고
    • TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors
    • DOI 10.1210/me.12.1.4
    • C.A. Powers, M. Mathur, B.M. Raaka, D. Ron, and H.H. Samuels TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors Mol. Endocrinol. 12 1998 4 18 (Pubitemid 28124775)
    • (1998) Molecular Endocrinology , vol.12 , Issue.1 , pp. 4-18
    • Powers, C.A.1    Mathur, M.2    Raaka, B.M.3    Ron, D.4    Samuels, H.H.5
  • 110
    • 0027948152 scopus 로고
    • TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain
    • D.D. Prasad, M. Ouchida, L. Lee, V.N. Rao, and E.S. Reddy TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain Oncogene 9 1994 3717 3729 (Pubitemid 24359413)
    • (1994) Oncogene , vol.9 , Issue.12 , pp. 3717-3729
    • Prasad, D.D.K.1    Ouchida, M.2    Lee, L.3    Rao, V.N.4    Reddy, E.S.P.5
  • 113
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • DOI 10.1021/ac026283q
    • J. Rappsilber, W.J. Friesen, S. Paushkin, G. Dreyfuss, and M. Mann Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode Anal. Chem. 75 2003 3107 3114 (Pubitemid 36830440)
    • (2003) Analytical Chemistry , vol.75 , Issue.13 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 114
    • 34248226362 scopus 로고    scopus 로고
    • Implications of ALS focality: Rostral-caudal distribution of lower motor neuron loss postmortem
    • DOI 10.1212/01.wnl.0000261045.57095.56, PII 0000611420070508000006
    • J. Ravits, P. Laurie, Y. Fan, and D.H. Moore Implications of ALS focality: rostral-caudal distribution of lower motor neuron loss postmortem Neurology 68 2007 1576 1582 (Pubitemid 46717981)
    • (2007) Neurology , vol.68 , Issue.19 , pp. 1576-1582
    • Ravits, J.1    Laurie, P.2    Fan, Y.3    Moore, D.H.4
  • 115
    • 34248202138 scopus 로고    scopus 로고
    • Focality of upper and lower motor neuron degeneration at the clinical onset of ALS
    • DOI 10.1212/01.wnl.0000260965.20021.47, PII 0000611420070508000005
    • J. Ravits, P. Paul, and C. Jorg Focality of upper and lower motor neuron degeneration at the clinical onset of ALS Neurology 68 2007 1571 1575 (Pubitemid 46717980)
    • (2007) Neurology , vol.68 , Issue.19 , pp. 1571-1575
    • Ravits, J.1    Paul, P.2    Jorg, C.3
  • 120
    • 77950457762 scopus 로고    scopus 로고
    • Transgenic zebrafish models of neurodegenerative diseases
    • J.J. Sager, Q. Bai, and E.A. Burton Transgenic zebrafish models of neurodegenerative diseases Brain Struct. Funct. 214 2010 285 302
    • (2010) Brain Struct. Funct. , vol.214 , pp. 285-302
    • Sager, J.J.1    Bai, Q.2    Burton, E.A.3
  • 122
    • 36048958883 scopus 로고    scopus 로고
    • Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins
    • DOI 10.1016/j.yexcr.2007.07.020, PII S0014482707003278
    • A. Shiohama, T. Sasaki, S. Noda, S. Minoshima, and N. Shimizu Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins Exp. Cell Res. 313 2007 4196 4207 (Pubitemid 350087044)
    • (2007) Experimental Cell Research , vol.313 , Issue.20 , pp. 4196-4207
    • Shiohama, A.1    Sasaki, T.2    Noda, S.3    Minoshima, S.4    Shimizu, N.5
  • 125
    • 0028968330 scopus 로고
    • Cabeza, a Drosophila gene encoding a novel RNA binding protein, shares homology with EWS and TLS, two genes involved in human sarcoma formation
    • D.T. Stolow, and S.R. Haynes Cabeza, a Drosophila gene encoding a novel RNA binding protein, shares homology with EWS and TLS, two genes involved in human sarcoma formation Nucleic Acids Res. 23 1995 835 843
    • (1995) Nucleic Acids Res. , vol.23 , pp. 835-843
    • Stolow, D.T.1    Haynes, S.R.2
  • 126
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Z. Sun, Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter, and A.D. Gitler Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS PLoS Biol. 9 2011 e1000614
    • (2011) PLoS Biol. , vol.9 , pp. 1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 128
    • 84855515796 scopus 로고    scopus 로고
    • Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor kappaB-mediated pathogenic pathways
    • V. Swarup, D. Phaneuf, N. Dupre, S. Petri, M. Strong, J. Kriz, and J.P. Julien Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor kappaB-mediated pathogenic pathways J. Exp. Med. 208 2011 2429 2447
    • (2011) J. Exp. Med. , vol.208 , pp. 2429-2447
    • Swarup, V.1    Phaneuf, D.2    Dupre, N.3    Petri, S.4    Strong, M.5    Kriz, J.6    Julien, J.P.7
  • 129
    • 79951733684 scopus 로고    scopus 로고
    • FUS/TLS gene mutations are the second most frequent cause of familial ALS in the Spanish population
    • E. Syriani, M. Morales, and J. Gamez FUS/TLS gene mutations are the second most frequent cause of familial ALS in the Spanish population Amyotroph. Lateral Scler. 12 2011 118 123
    • (2011) Amyotroph. Lateral Scler. , vol.12 , pp. 118-123
    • Syriani, E.1    Morales, M.2    Gamez, J.3
  • 130
    • 73549089900 scopus 로고    scopus 로고
    • TLS inhibits RNA polymerase III transcription
    • A.Y. Tan, and J.L. Manley TLS inhibits RNA polymerase III transcription Mol. Cell. Biol. 30 2010 186 196
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 186-196
    • Tan, A.Y.1    Manley, J.L.2
  • 135
    • 79954633016 scopus 로고    scopus 로고
    • Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: Mechanistic relationship and differential sensitivity to intervention
    • M.L. Tradewell, L.A. Cooper, S. Minotti, and H.D. Durham Calcium dysregulation, mitochondrial pathology and protein aggregation in a culture model of amyotrophic lateral sclerosis: mechanistic relationship and differential sensitivity to intervention Neurobiol. Dis. 42 2011 265 275
    • (2011) Neurobiol. Dis. , vol.42 , pp. 265-275
    • Tradewell, M.L.1    Cooper, L.A.2    Minotti, S.3    Durham, H.D.4
  • 136
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • M.L. Tradewell, Z. Yu, M. Tibshirani, M.C. Boulanger, H.D. Durham, and S. Richard Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations Hum. Mol. Genet. 2011 136 149
    • (2011) Hum. Mol. Genet. , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.C.4    Durham, H.D.5    Richard, S.6
  • 138
    • 0035918291 scopus 로고    scopus 로고
    • Involvement of the pro-oncoprotein TLS (translocated in liposarcoma) in nuclear factor-kappa B p65-mediated transcription as a coactivator
    • H. Uranishi, T. Tetsuka, M. Yamashita, K. Asamitsu, M. Shimizu, M. Itoh, and T. Okamoto Involvement of the pro-oncoprotein TLS (translocated in liposarcoma) in nuclear factor-kappa B p65-mediated transcription as a coactivator J. Biol. Chem. 276 2001 13395 13401
    • (2001) J. Biol. Chem. , vol.276 , pp. 13395-13401
    • Uranishi, H.1    Tetsuka, T.2    Yamashita, M.3    Asamitsu, K.4    Shimizu, M.5    Itoh, M.6    Okamoto, T.7
  • 139
    • 41149083411 scopus 로고
    • Pick's dementia associated with atypical amyotrophic lateral sclerosis. (Anatomoclinical study)
    • P.C. Van Reeth, O. Perier, C. Coers, and B.L. Van Pick's dementia associated with atypical amyotrophic lateral sclerosis. (Anatomoclinical study) Acta Neurol. Belg. 61 1961 309 325
    • (1961) Acta Neurol. Belg. , vol.61 , pp. 309-325
    • Van Reeth, P.C.1    Perier, O.2    Coers, C.3    Van, B.L.4
  • 142
    • 77956384199 scopus 로고    scopus 로고
    • Novel missense and truncating mutations in FUS/TLS in familial ALS
    • S. Waibel, M. Neumann, M. Rabe, T. Meyer, and A.C. Ludolph Novel missense and truncating mutations in FUS/TLS in familial ALS Neurology 75 2010 815 817
    • (2010) Neurology , vol.75 , pp. 815-817
    • Waibel, S.1    Neumann, M.2    Rabe, M.3    Meyer, T.4    Ludolph, A.C.5
  • 143
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • I.F. Wang, L.S. Wu, H.Y. Chang, and C.K. Shen TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor J. Neurochem. 105 2008 797 806
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 144
    • 80053424095 scopus 로고    scopus 로고
    • The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span
    • J.W. Wang, J.R. Brent, A. Tomlinson, N.A. Shneider, and B.D. McCabe The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span J. Clin. Invest. 121 2011 4118 4126
    • (2011) J. Clin. Invest. , vol.121 , pp. 4118-4126
    • Wang, J.W.1    Brent, J.R.2    Tomlinson, A.3    Shneider, N.A.4    McCabe, B.D.5
  • 145
    • 46649093597 scopus 로고    scopus 로고
    • Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription
    • DOI 10.1038/nature06992, PII NATURE06992
    • X. Wang, S. Arai, X. Song, D. Reichart, K. Du, G. Pascual, P. Tempst, M.G. Rosenfeld, C.K. Glass, and R. Kurokawa Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription Nature 454 2008 126 130 (Pubitemid 351934270)
    • (2008) Nature , vol.454 , Issue.7200 , pp. 126-130
    • Wang, X.1    Arai, S.2    Song, X.3    Reichart, D.4    Du, K.5    Pascual, G.6    Tempst, P.7    Rosenfeld, M.G.8    Glass, C.K.9    Kurokawa, R.10
  • 146
    • 0022417387 scopus 로고
    • The core proteins of 35S hnRNP complexes. Characterization of nine different species
    • H.E. Wilk, H. Werr, D. Friedrich, H.H. Kiltz, and K.P. Schafer The core proteins of 35S hnRNP complexes. Characterization of nine different species Eur. J. Biochem. 146 1985 71 81
    • (1985) Eur. J. Biochem. , vol.146 , pp. 71-81
    • Wilk, H.E.1    Werr, H.2    Friedrich, D.3    Kiltz, H.H.4    Schafer, K.P.5
  • 147
    • 0030855063 scopus 로고    scopus 로고
    • Identification of a human protein that recognizes the 3' splice site during the second step of pre-mRNA splicing
    • DOI 10.1093/emboj/16.14.4421
    • S. Wu, and M.R. Green Identification of a human protein that recognizes the 3′ splice site during the second step of pre-mRNA splicing EMBO J. 16 1997 4421 4432 (Pubitemid 27298195)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4421-4432
    • Wu, S.1    Green, M.R.2
  • 150
    • 0032561190 scopus 로고    scopus 로고
    • Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing
    • DOI 10.1074/jbc.273.43.27761
    • L. Yang, L.J. Embree, S. Tsai, and D.D. Hickstein Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing J. Biol. Chem. 273 1998 27761 27764 (Pubitemid 28496059)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 27761-27764
    • Yang, L.1    Embree, L.J.2    Tsai, S.3    Hickstein, D.D.4
  • 152
    • 33748786259 scopus 로고    scopus 로고
    • Identification and Characterization of the Nuclear Localization/Retention Signal in the EWS Proto-oncoprotein
    • DOI 10.1016/j.jmb.2006.08.018, PII S002228360601031X
    • R.P. Zakaryan, and H. Gehring Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein J. Mol. Biol. 363 2006 27 38 (Pubitemid 44414847)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.1 , pp. 27-38
    • Zakaryan, R.P.1    Gehring, H.2
  • 153
    • 0027970712 scopus 로고
    • A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP
    • H. Zinszner, R. Albalat, and D. Ron A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP Genes Dev. 8 1994 2513 2526 (Pubitemid 24347243)
    • (1994) Genes and Development , vol.8 , Issue.21 , pp. 2513-2526
    • Zinszner, H.1    Albalat, R.2    Ron, D.3
  • 154
    • 0031035765 scopus 로고    scopus 로고
    • A topogenic role for the oncogenic N-terminus of TLS: Nucleolar localization when transcription is inhibited
    • H. Zinszner, D. Immanuel, Y. Yin, F.X. Liang, and D. Ron A topogenic role for the oncogenic N-terminus of TLS: nucleolar localization when transcription is inhibited Oncogene 14 1997 451 461 (Pubitemid 27087108)
    • (1997) Oncogene , vol.14 , Issue.4 , pp. 451-461
    • Zinszner, H.1    Immanuel, D.2    Yin, Y.3    Liang, F.-X.4    Ron, D.5
  • 155
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • H. Zinszner, J. Sok, D. Immanuel, Y. Yin, and D. Ron TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling J. Cell Sci. 110 Pt 15 1997 1741 1750 (Pubitemid 27352853)
    • (1997) Journal of Cell Science , vol.110 , Issue.15 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.