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Volumn 140, Issue 1, 2017, Pages 13-26

Nuclear trafficking in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Author keywords

Amyotrophic lateral sclerosis; C9ORF72; Frontotemporal lobar degeneration; FUS; Nucleocytoplasmic transport; TDP 43

Indexed keywords

DIPEPTIDE; GUANINE NUCLEOTIDE EXCHANGE C9ORF72; TAR DNA BINDING PROTEIN; C9ORF72 PROTEIN, HUMAN; DNA BINDING PROTEIN; FUS PROTEIN, HUMAN; PROTEIN; RNA BINDING PROTEIN FUS; TDP-43 PROTEIN, HUMAN;

EID: 85015606615     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/aww197     Document Type: Review
Times cited : (47)

References (121)
  • 1
    • 84928136247 scopus 로고    scopus 로고
    • Cytoplasmic hGle1A regulates stress granules by modulation of translation
    • Aditi, Folkmann AW, Wente SR. Cytoplasmic hGle1A regulates stress granules by modulation of translation. Mol Biol Cell 2015a; 26: 1476-90.
    • (2015) Mol Biol Cell , vol.26 , pp. 1476-1490
    • Aditi Folkmann, A.W.1    Wente, S.R.2
  • 2
    • 84994807617 scopus 로고    scopus 로고
    • An amyotrophic lateral sclerosis-linked mutation in GLE1 alters the cellular pool of human Gle1 functional isoforms
    • in press
    • Aditi, Glass L, Dawson TR, Wente SR. An amyotrophic lateral sclerosis-linked mutation in GLE1 alters the cellular pool of human Gle1 functional isoforms. Adv Biol Regul 2015b, in press. http://dx.doi. org/10.1016/j.jbior.2015.11.001.
    • (2015) Adv Biol Regul
    • Aditi Glass, L.1    Dawson, T.R.2    Wente, S.R.3
  • 3
    • 33745736445 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export
    • Alcazar-Roman AR, Tran EJ, Guo S, Wente SR. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat Cell Biol 2006; 8: 711-16.
    • (2006) Nat Cell Biol , vol.8 , pp. 711-716
    • Alcazar-Roman, A.R.1    Tran, E.J.2    Guo, S.3    Wente, S.R.4
  • 4
    • 82355180826 scopus 로고    scopus 로고
    • P62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS
    • Al-Sarraj S, King A, Troakes C, Smith B, Maekawa S, Bodi I, et al. p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS. Acta Neuropathol 2011; 122: 691-702.
    • (2011) Acta Neuropathol , vol.122 , pp. 691-702
    • Al-Sarraj, S.1    King, A.2    Troakes, C.3    Smith, B.4    Maekawa, S.5    Bodi, I.6
  • 7
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala YM, Zago P, D'Ambrogio A, Xu Y-F, Petrucelli L, Buratti E, et al. Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 2008; 121: 3778-85.
    • (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    Buratti, E.6
  • 8
    • 0028937195 scopus 로고
    • Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
    • Bischoff FR, Krebber H, Smirnova E, Dong W, Ponstingl H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J 1995; 14: 705-15.
    • (1995) EMBO J , vol.14 , pp. 705-715
    • Bischoff, F.R.1    Krebber, H.2    Smirnova, E.3    Dong, W.4    Ponstingl, H.5
  • 10
  • 11
    • 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, Kwiatkowski TJ, et al. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 2010; 19: 4160-75.
    • (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    Kwiatkowski, T.J.6
  • 13
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci 2008; 13: 867-78.
    • (2008) Front Biosci , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 14
    • 84921797642 scopus 로고    scopus 로고
    • Components and regulation of nuclear transport processes
    • Cautain B, Hill R, de Pedro N, Link W. Components and regulation of nuclear transport processes. FEBS J 2015; 282: 445-62.
    • (2015) FEBS J , vol.282 , pp. 445-462
    • Cautain, B.1    Hill, R.2    De Pedro, N.3    Link, W.4
  • 16
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-bs: Recognition and inhibition
    • Chook YM, Suel KE. Nuclear import by karyopherin-bs: recognition and inhibition. Biochim Biophys Acta 2011; 1813: 1593-606.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 17
    • 84896699287 scopus 로고    scopus 로고
    • The widening spectrum of C9ORF72-related disease; Genotype/phenotype correlations and potential modifiers of clinical phenotype
    • Cooper-Knock J, Shaw PJ, Kirby J. The widening spectrum of C9ORF72-related disease; genotype/phenotype correlations and potential modifiers of clinical phenotype. Acta Neuropathol 2014; 127: 333-45.
    • (2014) Acta Neuropathol , vol.127 , pp. 333-345
    • Cooper-Knock, J.1    Shaw, P.J.2    Kirby, J.3
  • 19
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo MA, Raices M, Panowski SH, Hetzer MW. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 2009; 136: 284-95.
    • (2009) Cell , vol.136 , pp. 284-295
    • Ma, D.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 20
    • 84949844936 scopus 로고    scopus 로고
    • Phosphorylation of C-terminal tyrosine 526 in FUS impairs its nuclear import
    • Darovic S, Prpar Mihevc S, Zupunski V, Guncar G, Stalekar M, Lee Y., et al. Phosphorylation of C-terminal tyrosine 526 in FUS impairs its nuclear import. J Cell Sci 2015; 128: 4151-9. doi: 10.1242/jcs.176602.
    • (2015) J Cell Sci , vol.128 , pp. 4151-4159
    • Darovic, S.1    Prpar Mihevc, S.2    Zupunski, V.3    Guncar, G.4    Stalekar, M.5    Lee, Y.6
  • 21
    • 84873052814 scopus 로고    scopus 로고
    • Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes
    • Davidson YS, Robinson AC, Hu Q, Mishra M, Baborie A, Jaros E, et al. Nuclear carrier and RNA-binding proteins in frontotemporal lobar degeneration associated with fused in sarcoma (FUS) pathological changes. Neuropathol Appl Neurobiol 2013; 39: 157-65.
    • (2013) Neuropathol Appl Neurobiol , vol.39 , pp. 157-165
    • Davidson, Y.S.1    Robinson, A.C.2    Hu, Q.3    Mishra, M.4    Baborie, A.5    Jaros, E.6
  • 22
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M, Rutherford NJ, et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 2011; 72: 245-56.
    • (2011) Neuron , vol.72 , pp. 245-256
    • DeJesus-Hernandez, M.1    Mackenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5    Rutherford, N.J.6
  • 23
    • 85050578276 scopus 로고    scopus 로고
    • Multiple Export Mechanisms for mRNAs
    • Delaleau M, Borden KLB. Multiple Export Mechanisms for mRNAs. Cells 2015; 4: 452-73.
    • (2015) Cells , vol.4 , pp. 452-473
    • Delaleau, M.1    Klb, B.2
  • 24
  • 25
    • 84869237956 scopus 로고    scopus 로고
    • Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS
    • Dormann D, Madl T, Valori CF, Bentmann E, Tahirovic S, Abou-Ajram C, et al. Arginine methylation next to the PY-NLS modulates transportin binding and nuclear import of FUS. EMBO J 2012; 31: 4258-75.
    • (2012) EMBO J , vol.31 , pp. 4258-4275
    • Dormann, D.1    Madl, T.2    Valori, C.F.3    Bentmann, E.4    Tahirovic, S.5    Abou-Ajram, C.6
  • 26
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import
    • Dormann D, Rodde R, Edbauer D, Bentmann E, Fischer I, Hruscha A, et al. ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import. EMBO J 2010; 29: 2841-57.
    • (2010) EMBO J , vol.29 , pp. 2841-2857
    • Dormann, D.1    Rodde, R.2    Edbauer, D.3    Bentmann, E.4    Fischer, I.5    Hruscha, A.6
  • 27
    • 84901038797 scopus 로고    scopus 로고
    • C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking
    • Farg MA, Sundaramoorthy V, Sultana JM, Yang S, Atkinson RAK, Levina V, et al. C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking. Hum Mol Genet 2014; 23: 3579-95.
    • (2014) Hum Mol Genet , vol.23 , pp. 3579-3595
    • Ma, F.1    Sundaramoorthy, V.2    Sultana, J.M.3    Yang, S.4    Rak, A.5    Levina, V.6
  • 28
    • 84900852084 scopus 로고    scopus 로고
    • Fifty years of nuclear pores and nucleocytoplasmic transport studies: Multiple tools revealing complex rules
    • Floch AG, Palancade B, Doye V. Fifty years of nuclear pores and nucleocytoplasmic transport studies: multiple tools revealing complex rules. Methods Cell Biol 2014; 122: 1-40.
    • (2014) Methods Cell Biol , vol.122 , pp. 1-40
    • Floch, A.G.1    Palancade, B.2    Doye, V.3
  • 29
    • 84940925534 scopus 로고    scopus 로고
    • GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
    • Freibaum BD, Lu Y, Lopez-Gonzalez R, Kim NC, Almeida S, Lee KH, et al. GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport. Nature 2015; 525: 129-33.
    • (2015) Nature , vol.525 , pp. 129-133
    • Freibaum, B.D.1    Lu, Y.2    Lopez-Gonzalez, R.3    Kim, N.C.4    Almeida, S.5    Lee, K.H.6
  • 30
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda M, Asano S, Nakamura T, Adachi M, Yoshida M, Yanagida M, et al. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 1997; 390: 308-11.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6
  • 31
    • 80053646130 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, Jia J, et al. Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging 2011; 32: 2323.e27-40.
    • (2011) Neurobiol Aging , vol.32 , Issue.2323 , pp. e27-40
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5    Jia, J.6
  • 32
    • 84892590289 scopus 로고    scopus 로고
    • Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeatassociated non-ATG translation in c9FTD/ALS
    • Gendron TF, Bieniek KF, Zhang Y-J, Jansen-West K, Ash PEA, Caulfield T, et al. Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeatassociated non-ATG translation in c9FTD/ALS. Acta Neuropathol 2013; 126: 829-44.
    • (2013) Acta Neuropathol , vol.126 , pp. 829-844
    • Gendron, T.F.1    Bieniek, K.F.2    Zhang, Y.-J.3    Jansen-West, K.4    Pea, A.5    Caulfield, T.6
  • 33
    • 83555166183 scopus 로고    scopus 로고
    • A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: A gene identification study
    • Gijselinck I, Van Langenhove T, van der Zee J, Sleegers K, Philtjens S, Kleinberger G, et al. A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study. Lancet Neurol 2012; 11: 54-65.
    • (2012) Lancet Neurol , vol.11 , pp. 54-65
    • Gijselinck, I.1    Van Langenhove, T.2    Van Der Zee, J.3    Sleegers, K.4    Philtjens, S.5    Kleinberger, G.6
  • 34
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Gorlich D. Transport into and out of the cell nucleus. EMBO J 1998; 17: 2721-7.
    • (1998) EMBO J , vol.17 , pp. 2721-2727
    • Gorlich, D.1
  • 35
    • 68949200962 scopus 로고    scopus 로고
    • Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody
    • Hung C-J, Lee Y-J, Chen D-H, Li C. Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody. Protein J 2009; 28: 139-47.
    • (2009) Protein J , vol.28 , pp. 139-147
    • Hung, C.-J.1    Lee, Y.-J.2    Chen, D.-H.3    Li, C.4
  • 36
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • Jobert L, Argentini M, Tora L. PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp Cell Res 2009; 315: 1273-86.
    • (2009) Exp Cell Res , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 38
    • 84940426318 scopus 로고    scopus 로고
    • Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS
    • Jovicic A, Mertens J, Boeynaems S, Bogaert E, Chai N, Yamada SB, et al. Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS. Nat Neurosci 2015; 18: 1226-9.
    • (2015) Nat Neurosci , vol.18 , pp. 1226-1229
    • Jovicic, A.1    Mertens, J.2    Boeynaems, S.3    Bogaert, E.4    Chai, N.5    Yamada, S.B.6
  • 39
    • 68549083700 scopus 로고    scopus 로고
    • Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes
    • Kahms M, Lehrich P, Huve J, Sanetra N, Peters R. Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes. Traffic Cph Den 2009; 10: 1228-42.
    • (2009) Traffic Cph Den , vol.10 , pp. 1228-1242
    • Kahms, M.1    Lehrich, P.2    Huve, J.3    Sanetra, N.4    Peters, R.5
  • 40
    • 84924489696 scopus 로고    scopus 로고
    • Deleterious mutations in the essential mRNA metabolism factor, hGle1, in amyotrophic lateral sclerosis
    • Kaneb HM, Folkmann AW, Belzil VV, Jao L-E, Leblond CS, Girard SL, et al. Deleterious mutations in the essential mRNA metabolism factor, hGle1, in amyotrophic lateral sclerosis. Hum Mol Genet 2015; 24: 1363-73.
    • (2015) Hum Mol Genet , vol.24 , pp. 1363-1373
    • Kaneb, H.M.1    Folkmann, A.W.2    Belzil, V.V.3    Jao, L.-E.4    Leblond, C.S.5    Girard, S.L.6
  • 41
    • 70449393271 scopus 로고    scopus 로고
    • Nuclear contour irregularity and abnormal transporter protein distribution in anterior horn cells in amyotrophic lateral sclerosis
    • Kinoshita Y, Ito H, Hirano A, Fujita K, Wate R, Nakamura M, et al. Nuclear contour irregularity and abnormal transporter protein distribution in anterior horn cells in amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2009; 68: 1184-92.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 1184-1192
    • Kinoshita, Y.1    Ito, H.2    Hirano, A.3    Fujita, K.4    Wate, R.5    Nakamura, M.6
  • 42
    • 34648816826 scopus 로고    scopus 로고
    • Exporting RNA from the nucleus to the cytoplasm
    • Kohler A, Hurt E. Exporting RNA from the nucleus to the cytoplasm. Nat Rev Mol Cell Biol 2007; 8: 761-73
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 761-773
    • Kohler, A.1    Hurt, E.2
  • 43
    • 0342276108 scopus 로고    scopus 로고
    • Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor
    • Kutay U, Bischoff FR, Kostka S, Kraft R, Gorlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell 1997; 90: 1061-71.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Gorlich, D.5
  • 44
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, Russ C, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 2009; 323: 1205-08.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, T.J.1    Bosco, D.A.2    Leclerc, A.L.3    Tamrazian, E.4    Vanderburg, C.R.5    Russ, C.6
  • 45
    • 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 LK, Neumann M, Sampathu DM, Lee VM-Y, Trojanowski JQ. TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease. Acta Neuropathol 2007; 114: 63-70.
    • (2007) Acta Neuropathol , vol.114 , pp. 63-70
    • Kwong, L.K.1    Neumann, M.2    Sampathu, D.M.3    Vm-Y, L.4    Trojanowski, J.Q.5
  • 46
    • 80052942395 scopus 로고    scopus 로고
    • A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies
    • Lashley T, Rohrer JD, Bandopadhyay R, Fry C, Ahmed Z, Isaacs AM, et al. A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies. Brain J Neurol 2011; 134: 2548-64.
    • (2011) Brain J Neurol , vol.134 , pp. 2548-2564
    • Lashley, T.1    Rohrer, J.D.2    Bandopadhyay, R.3    Fry, C.4    Ahmed, Z.5    Isaacs, A.M.6
  • 47
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, Chook YM. Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 2006; 126: 543-58.
    • (2006) Cell , vol.126 , 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
  • 48
    • 85048315629 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein, tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein
    • Leemann-Zakaryan RP, Pahlich S, Grossenbacher D, Gehring H. Tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein, tyrosine phosphorylation in the C-terminal nuclear localization and retention signal (C-NLS) of the EWS protein. Sarcoma 2011; 2011: e218483.
    • (2011) Sarcoma , vol.2011 , pp. e218483
    • Leemann-Zakaryan, R.P.1    Pahlich, S.2    Grossenbacher, D.3    Gehring, H.4
  • 49
    • 84874246696 scopus 로고    scopus 로고
    • The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs
    • Levine TP, Daniels RD, Gatta AT, Wong LH, Hayes MJ. The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs. Bioinformatics 2013; 29: 499-503.
    • (2013) Bioinformatics , vol.29 , pp. 499-503
    • Levine, T.P.1    Daniels, R.D.2    Gatta, A.T.3    Wong, L.H.4    Hayes, M.J.5
  • 50
    • 84944884978 scopus 로고    scopus 로고
    • Formation and maturation of phase-separated liquid droplets by RNA-binding proteins
    • Lin Y, Protter DSW, Rosen MK, Parker R. Formation and maturation of phase-separated liquid droplets by RNA-binding proteins. Mol Cell 2015; 60: 208-19.
    • (2015) Mol Cell , vol.60 , pp. 208-219
    • Lin, Y.1    Dsw, P.2    Rosen, M.K.3    Parker, R.4
  • 51
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis
    • Ling S-C, Polymenidou M, Cleveland DW. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 2013; 79: 416-38.
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.-C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 52
    • 79959615773 scopus 로고    scopus 로고
    • Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: Two distinct patterns correlating with disease severity and mutation
    • Mackenzie IRA, Ansorge O, Strong M, Bilbao J, Zinman L, Ang L-C, et al. Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation. Acta Neuropathol 2011; 122: 87-98.
    • (2011) Acta Neuropathol , vol.122 , pp. 87-98
    • Ira, M.1    Ansorge, O.2    Strong, M.3    Bilbao, J.4    Zinman, L.5    Ang, L.-C.6
  • 53
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R, Delphin C, Guan T, Gerace L, Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997; 88: 97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 54
    • 84879515784 scopus 로고    scopus 로고
    • Identification of novel stress granule components that are involved in nuclear transport
    • Mahboubi H, Seganathy E, Kong D, Stochaj U. Identification of novel stress granule components that are involved in nuclear transport. PloS One 2013; 8: e68356.
    • (2013) PloS One , vol.8 , pp. e68356
    • Mahboubi, H.1    Seganathy, E.2    Kong, D.3    Stochaj, U.4
  • 55
    • 79960928189 scopus 로고    scopus 로고
    • Molecular basis for specificity of nuclear import and prediction of nuclear localization
    • Marfori M, Mynott A, Ellis JJ, Mehdi AM, Saunders NFW, Curmi PM, et al. Molecular basis for specificity of nuclear import and prediction of nuclear localization. Biochim Biophys Acta 2011; 1813: 1562-77.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1562-1577
    • Marfori, M.1    Mynott, A.2    Ellis, J.J.3    Mehdi, A.M.4    Nfw, S.5    Curmi, P.M.6
  • 56
    • 84864547364 scopus 로고    scopus 로고
    • Domains involved in TAF15 subcellular localisation: Dependence on cell type and ongoing transcription
    • Marko M, Vlassis A, Guialis A, Leichter M. Domains involved in TAF15 subcellular localisation: dependence on cell type and ongoing transcription. Gene 2012; 506: 331-8.
    • (2012) Gene , vol.506 , pp. 331-338
    • Marko, M.1    Vlassis, A.2    Guialis, A.3    Leichter, M.4
  • 57
    • 84892585908 scopus 로고    scopus 로고
    • C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci
    • Mizielinska S, Lashley T, Norona FE, Clayton EL, Ridler CE, Fratta P, et al. C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci. Acta Neuropathol 2013; 126: 845-57.
    • (2013) Acta Neuropathol , vol.126 , pp. 845-857
    • Mizielinska, S.1    Lashley, T.2    Norona, F.E.3    Clayton, E.L.4    Ridler, C.E.5    Fratta, P.6
  • 58
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
    • Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, et al. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 2015; 163: 123-33.
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1    Temirov, J.2    Lee, J.3    Coughlin, M.4    Kanagaraj, A.P.5    Kim, H.J.6
  • 59
    • 84892585689 scopus 로고    scopus 로고
    • Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins
    • Mori K, Arzberger T, Grasser FA, Gijselinck I, May S, Rentzsch K, et al. Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins. Acta Neuropathol 2013a; 126: 881-93.
    • (2013) Acta Neuropathol , vol.126 , pp. 881-893
    • Mori, K.1    Arzberger, T.2    Grasser, F.A.3    Gijselinck, I.4    May, S.5    Rentzsch, K.6
  • 60
    • 84874962380 scopus 로고    scopus 로고
    • The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS
    • Mori K, Weng S-M, Arzberger T, May S, Rentzsch K, Kremmer E, et al. The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. Science 2013b; 339: 1335-8.
    • (2013) Science , vol.339 , pp. 1335-1338
    • Mori, K.1    Weng, S.-M.2    Arzberger, T.3    May, S.4    Rentzsch, K.5    Kremmer, E.6
  • 61
    • 84960129723 scopus 로고    scopus 로고
    • ALS/FTD Mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function
    • Murakami T, Qamar S, Lin JQ, Schierle GSK, Rees E, Miyashita A, et al. ALS/FTD Mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function. Neuron 2015; 88: 678-90.
    • (2015) Neuron , vol.88 , pp. 678-690
    • Murakami, T.1    Qamar, S.2    Lin, J.Q.3    Gsk, S.4    Rees, E.5    Miyashita, A.6
  • 62
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny S, Dreyfuss G. Transport of proteins and RNAs in and out of the nucleus. Cell 1999; 99: 677-90.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 64
    • 80052959701 scopus 로고    scopus 로고
    • FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
    • Neumann M, Bentmann E, Dormann D, Jawaid A, DeJesus-Hernandez M, Ansorge O, et al. FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain J Neurol 2011; 134: 2595-609.
    • (2011) Brain J Neurol , vol.134 , pp. 2595-2609
    • Neumann, M.1    Bentmann, E.2    Dormann, D.3    Jawaid, A.4    DeJesus-Hernandez, M.5    Ansorge, O.6
  • 67
    • 70449521091 scopus 로고    scopus 로고
    • Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease
    • Neumann M, Roeber S, Kretzschmar HA, Rademakers R, Baker M, Mackenzie IRA. Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease. Acta Neuropathol 2009b; 118: 605-16.
    • (2009) Acta Neuropathol , vol.118 , pp. 605-616
    • Neumann, M.1    Roeber, S.2    Kretzschmar, H.A.3    Rademakers, R.4    Baker, M.5    Ira, M.6
  • 68
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006; 314: 130-33.
    • (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    Chou, T.T.6
  • 69
    • 84871019907 scopus 로고    scopus 로고
    • Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations
    • Neumann M, Valori CF, Ansorge O, Kretzschmar HA, Munoz DG, Kusaka H, et al. Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol 2012; 124: 705-16.
    • (2012) Acta Neuropathol , vol.124 , pp. 705-716
    • Neumann, M.1    Valori, C.F.2    Ansorge, O.3    Kretzschmar, H.A.4    Munoz, D.G.5    Kusaka, H.6
  • 70
    • 77953019135 scopus 로고    scopus 로고
    • Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
    • Nishimura AL, Zupunski V, Troakes C, Kathe C, Fratta P, Howell M, et al. Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration. Brain J Neurol 2010; 133: 1763-71.
    • (2010) Brain J Neurol , vol.133 , pp. 1763-1771
    • Nishimura, A.L.1    Zupunski, V.2    Troakes, C.3    Kathe, C.4    Fratta, P.5    Howell, M.6
  • 71
    • 84867290759 scopus 로고    scopus 로고
    • FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS
    • Niu C, Zhang J, Gao F, Yang L, Jia M, Zhu H, et al. FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS. PloS One 2012; 7: e47056.
    • (2012) PloS One , vol.7 , pp. e47056
    • Niu, C.1    Zhang, J.2    Gao, F.3    Yang, L.4    Jia, M.5    Zhu, H.6
  • 73
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B, Bachelerie F, Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 1997; 278: 141-4.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 74
    • 84940403835 scopus 로고    scopus 로고
    • A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation
    • Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, et al. A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation. Cell 2015; 162: 1066-77.
    • (2015) Cell , vol.162 , pp. 1066-1077
    • Patel, A.1    Lee, H.O.2    Jawerth, L.3    Maharana, S.4    Jahnel, M.5    Hein, M.Y.6
  • 75
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton LF, Paschal BM. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 2005; 6: 187-98.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 76
    • 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, Liang TY, et al. Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat Neurosci 2011; 14: 459-68.
    • (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    Liang, T.Y.6
  • 78
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • Rappsilber J, Friesen WJ, Paushkin S, Dreyfuss G, Mann M. Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode. Anal Chem 2003; 75: 3107-14.
    • (2003) Anal Chem , vol.75 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 80
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton AE, Majounie E, Waite A, Simo n-Sanchez J, Rollinson S, Gibbs JR, et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 2011; 72: 257-68.
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1    Majounie, E.2    Waite, A.3    Simon-Sanchez, J.4    Rollinson, S.5    Gibbs, J.R.6
  • 81
    • 84866126892 scopus 로고    scopus 로고
    • Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain
    • Rogelj B, Easton LE, Bogu GK, Stanton LW, Rot G, Curk T, et al. Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain. Sci Rep 2012; 2: 603.
    • (2012) Sci Rep , vol.2 , pp. 603
    • Rogelj, B.1    Easton, L.E.2    Bogu, G.K.3    Stanton, L.W.4    Rot, G.5    Curk, T.6
  • 82
    • 84929486078 scopus 로고    scopus 로고
    • Nuclear accumulation of mRNAs underlies G4C2-repeatinduced translational repression in a cellular model of C9orf72 ALS
    • Rossi S, Serrano A, Gerbino V, Giorgi A, Di Francesco L, Nencini M, et al. Nuclear accumulation of mRNAs underlies G4C2-repeatinduced translational repression in a cellular model of C9orf72 ALS. J Cell Sci 2015; 128: 1787-99.
    • (2015) J Cell Sci , vol.128 , pp. 1787-1799
    • Rossi, S.1    Serrano, A.2    Gerbino, V.3    Giorgi, A.4    Di Francesco, L.5    Nencini, M.6
  • 83
    • 84876437828 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo
    • Scaramuzzino C, Monaghan J, Milioto C, Lanson NA, Maltare A, Aggarwal T, et al. Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo. PloS One 2013; 8: e61576.
    • (2013) PloS One , vol.8 , pp. e61576
    • Scaramuzzino, C.1    Monaghan, J.2    Milioto, C.3    Lanson, N.A.4    Maltare, A.5    Aggarwal, T.6
  • 84
    • 84988974586 scopus 로고    scopus 로고
    • Prevalence of brain and spinal cord inclusions, including dipeptide repeat proteins, in patients with the C9ORF72 hexanucleotide repeat expansion: A systematic neuropathological review
    • 2015 in press
    • Schipper LJ, Raaphorst J, Aronica E, Baas F, de Haan R, de Visser M, et al. Prevalence of brain and spinal cord inclusions, including dipeptide repeat proteins, in patients with the C9ORF72 hexanucleotide repeat expansion: a systematic neuropathological review. Neuropathol Appl Neurobiol 2015, in press. doi: 10.1111/nan.12284.
    • Neuropathol Appl Neurobiol
    • Schipper, L.J.1    Raaphorst, J.2    Aronica, E.3    Baas, F.4    De Haan, R.5    De Visser, M.6
  • 86
    • 79959605078 scopus 로고    scopus 로고
    • The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene
    • Snowden JS, Hu Q, Rollinson S, Halliwell N, Robinson A, Davidson YS, et al. The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene. Acta Neuropathol 2011; 122: 99-110.
    • (2011) Acta Neuropathol , vol.122 , pp. 99-110
    • Snowden, J.S.1    Hu, Q.2    Rollinson, S.3    Halliwell, N.4    Robinson, A.5    Davidson, Y.S.6
  • 87
    • 84934920273 scopus 로고    scopus 로고
    • Nuclear localization signals for four distinct karyopherin-b nuclear import systems
    • Soniat M, Chook YM. Nuclear localization signals for four distinct karyopherin-b nuclear import systems. Biochem J 2015; 468: 353-62.
    • (2015) Biochem J , vol.468 , pp. 353-362
    • Soniat, M.1    Chook, Y.M.2
  • 88
    • 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, Rogelj B, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008; 319: 1668-72.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5    Rogelj, B.6
  • 89
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade K, Ford CS, Guthrie C, Weis K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 1997; 90: 1041-50.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 90
    • 84925307620 scopus 로고    scopus 로고
    • Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport
    • S talekar M, Yin X, Rebolj K, Darovic S, Troakes C, Mayr M, et al. Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport. Neuroscience 2015; 293: 157-70
    • (2015) Neuroscience , vol.293 , pp. 157-170
    • Talekar M, S.1    Yin, X.2    Rebolj, K.3    Darovic, S.4    Troakes, C.5    Mayr, M.6
  • 91
    • 84961231197 scopus 로고    scopus 로고
    • Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS
    • Sua rez-Calvet M, Neumann M, Arzberger T, Abou-Ajram C, Funk E, Hartmann H, et al. Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS. Acta Neuropathol 2016; 131: 587-604
    • (2016) Acta Neuropathol , vol.131 , pp. 587-604
    • Suarez-Calvet, M.1    Neumann, M.2    Arzberger, T.3    Abou-Ajram, C.4    Funk, E.5    Hartmann, H.6
  • 92
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: Hierarchical regulation of nucleocytoplasmic transport
    • Terry LJ, Shows EB, Wente SR. Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 2007; 318: 1412-16.
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 93
    • 79953180492 scopus 로고    scopus 로고
    • Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
    • Tollervey JR, Curk T, Rogelj B, Briese M, Cereda M, Kayikci M, et al. Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat Neurosci 2011; 14: 452-8.
    • (2011) Nat Neurosci , vol.14 , pp. 452-458
    • Tollervey, J.R.1    Curk, T.2    Rogelj, B.3    Briese, M.4    Cereda, M.5    Kayikci, M.6
  • 94
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell ML, Yu Z, Tibshirani M, Boulanger M-C, Durham HD, Richard S. Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum Mol Genet 2012; 21: 136-49.
    • (2012) Hum Mol Genet , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.-C.4    Durham, H.D.5    Richard, S.6
  • 95
    • 84880177442 scopus 로고    scopus 로고
    • Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions
    • Troakes C, Hortoba gyi T, Vance C, Al-Sarraj S, Rogelj B, Shaw CE. Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from frontotemporal lobar degeneration with FUS inclusions. Neuropathol Appl Neurobiol 2013; 39: 553-61.
    • (2013) Neuropathol Appl Neurobiol , vol.39 , pp. 553-561
    • Troakes, C.1    Hortobagyi, T.2    Vance, C.3    Al-Sarraj, S.4    Rogelj, B.5    Shaw, C.E.6
  • 96
    • 84866600630 scopus 로고    scopus 로고
    • An MND/ALS phenotype associated with C9orf72 repeat expansion: Abundant p62-positive, TDP-43-negative inclusions in cerebral cortex, hippocampus and cerebellum but without associated cognitive decline
    • Troakes C, Maekawa S, Wijesekera L, Rogelj B, Siklo s L, Bell C, et al. An MND/ALS phenotype associated with C9orf72 repeat expansion: abundant p62-positive, TDP-43-negative inclusions in cerebral cortex, hippocampus and cerebellum but without associated cognitive decline. Neuropathology 2012; 32: 505-14.
    • (2012) Neuropathology , vol.32 , pp. 505-514
    • Troakes, C.1    Maekawa, S.2    Wijesekera, L.3    Rogelj, B.4    Siklo, S.L.5    Bell, C.6
  • 98
    • 84900439244 scopus 로고    scopus 로고
    • Transportin-1 and Transportin-2: Protein nuclear import and beyond
    • Twyffels L, Gueydan C, Kruys V. Transportin-1 and Transportin-2: protein nuclear import and beyond. FEBS Lett 2014; 588: 1857-68.
    • (2014) FEBS Lett , vol.588 , pp. 1857-1868
    • Twyffels, L.1    Gueydan, C.2    Kruys, V.3
  • 99
    • 84890331414 scopus 로고    scopus 로고
    • Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones
    • Udan-Johns M, Bengoechea R, Bell S, Shao J, Diamond MI, True HL, et al. Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones. Hum Mol Genet 2014; 23: 157-70.
    • (2014) Hum Mol Genet , vol.23 , pp. 157-170
    • Udan-Johns, M.1    Bengoechea, R.2    Bell, S.3    Shao, J.4    Diamond, M.I.5    True, H.L.6
  • 100
    • 77953872890 scopus 로고    scopus 로고
    • FUS pathology defines the majority of tau-and TDP-43-negative frontotemporal lobar degeneration
    • Urwin H, Josephs KA, Rohrer JD, Mackenzie IR, Neumann M, Authier A, et al. FUS pathology defines the majority of tau-and TDP-43-negative frontotemporal lobar degeneration. Acta Neuropathol 2010; 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    Authier, A.6
  • 101
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortoba gyi T, De Vos KJ, Nishimura AL, Sreedharan J, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009; 323: 1208-11.
    • (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    Sreedharan, J.6
  • 102
    • 84878565260 scopus 로고    scopus 로고
    • ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules
    • Vance C, Scotter EL, Nishimura AL, Troakes C, Mitchell JC, Kathe C, et al. ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules. Hum Mol Genet 2013; 22: 2676-88.
    • (2013) Hum Mol Genet , vol.22 , pp. 2676-2688
    • Vance, C.1    Scotter, E.L.2    Nishimura, A.L.3    Troakes, C.4    Mitchell, J.C.5    Kathe, C.6
  • 103
    • 84903819307 scopus 로고    scopus 로고
    • Unconventional features of C9ORF72 expanded repeat in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Vatovec S, Kovanda A, Rogelj B. Unconventional features of C9ORF72 expanded repeat in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Neurobiol Aging 2014; 35: 2421.e1-e12.
    • (2014) Neurobiol Aging , vol.35 , Issue.2421 , pp. e1-e12
    • Vatovec, S.1    Kovanda, A.2    Rogelj, B.3
  • 105
    • 85056706559 scopus 로고    scopus 로고
    • Reduced C9orf72 protein levels in frontal cortex of amyotrophic lateral sclerosis and frontotemporal degeneration brain with the C9ORF72 hexanucleotide repeat expansion
    • Waite AJ, Baumer D, East S, Neal J, Morris HR, Ansorge O, et al. Reduced C9orf72 protein levels in frontal cortex of amyotrophic lateral sclerosis and frontotemporal degeneration brain with the C9ORF72 hexanucleotide repeat expansion. Neurobiol Aging 2014; 35: 1779.e5-e13.
    • (2014) Neurobiol Aging , vol.35 , Issue.1779 , pp. e5-e13
    • Waite, A.J.1    Bamer, D.2    East, S.3    Neal, J.4    Morris, H.R.5    Ansorge, O.6
  • 106
    • 84945450480 scopus 로고    scopus 로고
    • Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43
    • Walker AK, Spiller KJ, Ge G, Zheng A, Xu Y, Zhou M, et al. Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43. Acta Neuropathol 2015; 130: 643-60.
    • (2015) Acta Neuropathol , vol.130 , pp. 643-660
    • Walker, A.K.1    Spiller, K.J.2    Ge, G.3    Zheng, A.4    Xu, Y.5    Zhou, M.6
  • 107
    • 84861608931 scopus 로고    scopus 로고
    • Mutations in the RNA exosome component gene EXOSC3 cause pontocerebellar hypoplasia and spinal motor neuron degeneration
    • Wan J, Yourshaw M, Mamsa H, Rudnik-Schoneborn S, Menezes MP, Hong JE, et al. Mutations in the RNA exosome component gene EXOSC3 cause pontocerebellar hypoplasia and spinal motor neuron degeneration. Nat Genet 2012; 44: 704-08.
    • (2012) Nat Genet , vol.44 , pp. 704-708
    • Wan, J.1    Yourshaw, M.2    Mamsa, H.3    Rudnik-Schoneborn, S.4    Menezes, M.P.5    Hong, J.E.6
  • 108
    • 84907212776 scopus 로고    scopus 로고
    • Early retinal neurodegeneration and impaired Ran-mediated nuclear import of TDP-43 in progranulin-deficient FTLD
    • Ward ME, Taubes A, Chen R, Miller BL, Sephton CF, Gelfand JM, et al. Early retinal neurodegeneration and impaired Ran-mediated nuclear import of TDP-43 in progranulin-deficient FTLD. J Exp Med 2014; 211: 1937-45.
    • (2014) J Exp Med , vol.211 , pp. 1937-1945
    • Ward, M.E.1    Taubes, A.2    Chen, R.3    Miller, B.L.4    Sephton, C.F.5    Gelfand, J.M.6
  • 109
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich CS, Erzberger JP, Flick JS, Berger JM, Thorner J, Weis K. Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat Cell Biol 2006; 8: 668-76.
    • (2006) Nat Cell Biol , vol.8 , pp. 668-676
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, J.5    Weis, K.6
  • 110
    • 84934437553 scopus 로고    scopus 로고
    • Control of mammalian gene expression by selective mRNA export
    • Wickramasinghe VO, Laskey RA. Control of mammalian gene expression by selective mRNA export. Nat Rev Mol Cell Biol 2015; 16: 431-42.
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 431-442
    • Wickramasinghe, V.O.1    Laskey, R.A.2
  • 111
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, Lee VM-Y. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 2008; 283: 13302-09.
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Vm-Y, L.6
  • 112
    • 84955098544 scopus 로고    scopus 로고
    • Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA
    • Woerner AC, Frottin F, Hornburg D, Feng LR, Meissner F, Patra M, et al. Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. Science 2016; 351: 173-6.
    • (2016) Science , vol.351 , pp. 173-176
    • Woerner, A.C.1    Frottin, F.2    Hornburg, D.3    Feng, L.R.4    Meissner, F.5    Patra, M.6
  • 113
    • 84942369240 scopus 로고    scopus 로고
    • Isoform specific antibodies reveal distinct subcellular localizations of C9orf72 in amyotrophic lateral sclerosis
    • Xiao S, MacNair L, McGoldrick P, McKeever PM, McLean JR, Zhang M, et al. Isoform specific antibodies reveal distinct subcellular localizations of C9orf72 in amyotrophic lateral sclerosis. Ann Neurol 2015; 78: 568-83.
    • (2015) Ann Neurol , vol.78 , pp. 568-583
    • Xiao, S.1    MacNair, L.2    McGoldrick, P.3    McKeever, P.M.4    McLean, J.R.5    Zhang, M.6
  • 114
    • 84869005887 scopus 로고    scopus 로고
    • The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS
    • Yamaguchi A, Kitajo K. The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS. PloS One 2012; 7: e49267.
    • (2012) PloS One , vol.7 , pp. e49267
    • Yamaguchi, A.1    Kitajo, K.2
  • 116
    • 33748786259 scopus 로고    scopus 로고
    • Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein
    • Zakaryan RP, Gehring H. Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein. J Mol Biol 2006; 363: 27-38.
    • (2006) J Mol Biol , vol.363 , pp. 27-38
    • Zakaryan, R.P.1    Gehring, H.2
  • 117
    • 84874266850 scopus 로고    scopus 로고
    • Discovery of novel DENN Proteins: Implications for the evolution of eukaryotic intracellular membrane structures and human disease
    • Zhang D, Iyer LM, He F, Aravind L. Discovery of novel DENN Proteins: implications for the evolution of eukaryotic intracellular membrane structures and human disease. Front Genet 2012; 3: 283.
    • (2012) Front Genet , vol.3 , pp. 283
    • Zhang, D.1    Iyer, L.M.2    He, F.3    Aravind, L.4
  • 119
    • 84961391578 scopus 로고    scopus 로고
    • C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins
    • Zhang Y-J, Gendron TF, Grima JC, Sasaguri H, Jansen-West K, Xu Y-F, et al. C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins. Nat Neurosci 2016; 19: 668-77.
    • (2016) Nat Neurosci , vol.19 , pp. 668-677
    • Zhang, Y.-J.1    Gendron, T.F.2    Grima, J.C.3    Sasaguri, H.4    Jansen-West, K.5    Xu, Y.-F.6
  • 120
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou Z, Luo MJ, Straesser K, Katahira J, Hurt E, Reed R. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 2000; 407: 401-5.
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1    Luo, M.J.2    Straesser, K.3    Katahira, J.4    Hurt, E.5    Reed, R.6
  • 121
    • 84890837640 scopus 로고    scopus 로고
    • RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia
    • Zu T, Liu Y, Banez-Coronel M, Reid T, Pletnikova O, Lewis J, et al. RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia. Proc Natl Acad Sci USA 2013; 110: E4968-77.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E4968-E4977
    • Zu, T.1    Liu, Y.2    Banez-Coronel, M.3    Reid, T.4    Pletnikova, O.5    Lewis, J.6


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