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Volumn 278, Issue 19, 2011, Pages 3550-3568

TDP-43 and FUS/TLS: Cellular functions and implications for neurodegeneration

Author keywords

ALS; autophagy; FTLD; FUS; HDAC6; RNA; RNA metabolism; splicing; TDP 43; transcription

Indexed keywords

BINDING PROTEIN; FUSED IN SARCOMA PROTEIN; HISTONE DEACETYLASE 6; MESSENGER RNA; MICRORNA; TAR DNA BINDING PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 80052968310     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08258.x     Document Type: Review
Times cited : (59)

References (159)
  • 3
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, &, Neumann M, (2010) TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol 9, 995-1007.
    • (2010) Lancet Neurol , vol.9 , pp. 995-1007
    • MacKenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 11
    • 77957317483 scopus 로고    scopus 로고
    • The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
    • Buratti E, &, Baralle FE, (2010) The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol 7, 420-429.
    • (2010) RNA Biol , vol.7 , pp. 420-429
    • Buratti, E.1    Baralle, F.E.2
  • 12
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, &, Cleveland DW, (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet 19, R46-64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 14
    • 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
    • Fujii R, Okabe S, Urushido T, Inoue K, Yoshimura A, Tachibana T, Nishikawa T, Hicks GG, &, Takumi T, (2005) The RNA binding protein TLS is translocated to dendritic spines by mGluR5 activation and regulates spine morphology. Curr Biol 15, 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
  • 15
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang IF, Wu LS, Chang HY, &, Shen CK, (2008) TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J Neurochem 105, 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
  • 18
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: The relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Baloh RH, (2011) TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. FEBS J 278, 3539-3549.
    • (2011) FEBS J , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 22
    • 74749107048 scopus 로고    scopus 로고
    • TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis
    • Wu LS, Cheng WC, Hou SC, Yan YT, Jiang ST, &, Shen CK, (2010) TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis. Genesis 48, 56-62.
    • (2010) Genesis , vol.48 , pp. 56-62
    • Wu, L.S.1    Cheng, W.C.2    Hou, S.C.3    Yan, Y.T.4    Jiang, S.T.5    Shen, C.K.6
  • 24
    • 77949878273 scopus 로고    scopus 로고
    • TDP-43 is a developmentally regulated protein essential for early embryonic development
    • Sephton CF, Good SK, Atkin S, Dewey CM, Mayer P III, Herz J, &, Yu G, (2010) TDP-43 is a developmentally regulated protein essential for early embryonic development. J Biol Chem 285, 6826-6834.
    • (2010) J Biol Chem , vol.285 , pp. 6826-6834
    • Sephton, C.F.1    Good, S.K.2    Atkin, S.3    Dewey, C.M.4    Mayer Iii, P.5    Herz, J.6    Yu, G.7
  • 33
    • 36949024480 scopus 로고    scopus 로고
    • Severe subcortical TDP-43 pathology in sporadic frontotemporal lobar degeneration with motor neuron disease
    • DOI 10.1007/s00401-007-0315-5
    • Brandmeir NJ, Geser F, Kwong LK, Zimmerman E, Qian J, Lee VM, &, Trojanowski JQ, (2008) Severe subcortical TDP-43 pathology in sporadic frontotemporal lobar degeneration with motor neuron disease. Acta Neuropathol 115, 123-131. (Pubitemid 50003187)
    • (2008) Acta Neuropathologica , vol.115 , Issue.1 , pp. 123-131
    • Brandmeir, N.J.1    Geser, F.2    Kwong, L.K.3    Zimmerman, E.4    Qian, J.5    Lee, V.M.-Y.6    Trojanowski, J.Q.7
  • 35
    • 0027227651 scopus 로고
    • Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
    • DOI 10.1038/363640a0
    • 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. (Pubitemid 23227627)
    • (1993) Nature , vol.363 , Issue.6430 , pp. 640-644
    • Crozat, A.1    Aman, P.2    Mandahl, N.3    Ron, D.4
  • 36
    • 33746776838 scopus 로고    scopus 로고
    • Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2
    • DOI 10.1016/j.cell.2006.05.049, PII S009286740600910X
    • Lee BJ, Cansizoglu AE, Suel KE, Louis TH, Zhang Z, &, Chook YM, (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126, 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
  • 37
    • 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
  • 38
    • 79954616116 scopus 로고    scopus 로고
    • Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations
    • Kino Y, Washizu C, Aquilanti E, Okuno M, Kurosawa M, Yamada M, Doi H, &, Nukina N, (2010) Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations. Nucleic Acids Res 39, 2781-2798.
    • (2010) 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
  • 40
    • 77957875397 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • doi
    • Gal J, Zhang J, Kwinter DM, Zhai J, Jia H, Jia J, &, Zhu H, (2010) Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol Aging, doi: S0197-4580.
    • (2010) Neurobiol Aging
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5    Jia, J.6    Zhu, H.7
  • 43
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • DOI 10.1242/jcs.02692
    • Fujii R, &, Takumi T, (2005) TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J Cell Sci 118, 5755-5765. (Pubitemid 43079269)
    • (2005) Journal of Cell Science , vol.118 , Issue.24 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 47
    • 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
    • Andersson MK, Stahlberg A, Arvidsson Y, Olofsson A, Semb H, Stenman G, Nilsson O, &, Aman P, (2008) 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, 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
  • 51
    • 0022497178 scopus 로고
    • Characteristic ribonucleolytic activity of human angiogenin
    • Shapiro R, Riordan JF, &, Vallee BL, (1986) Characteristic ribonucleolytic activity of human angiogenin. Biochemistry 25, 3527-3532. (Pubitemid 16067144)
    • (1986) Biochemistry , vol.25 , Issue.12 , pp. 3527-3532
    • Shapiro, R.1    Riordan, J.F.2    Vallee, B.L.3
  • 52
    • 69449101422 scopus 로고    scopus 로고
    • Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation
    • Suraweera A, Lim Y, Woods R, Birrell GW, Nasim T, Becherel OJ, &, Lavin MF, (2009) Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation. Hum Mol Genet 18, 3384-3396.
    • (2009) Hum Mol Genet , vol.18 , pp. 3384-3396
    • Suraweera, A.1    Lim, Y.2    Woods, R.3    Birrell, G.W.4    Nasim, T.5    Becherel, O.J.6    Lavin, M.F.7
  • 53
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou SH, Wu F, Harrich D, Garcia-Martinez LF, &, Gaynor RB, (1995) Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 69, 3584-3596.
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 55
    • 37549025044 scopus 로고    scopus 로고
    • A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: Role for TDP-43 in insulator function
    • Abhyankar MM, Urekar C, &, Reddi PP, (2007) A novel CpG-free vertebrate insulator silences the testis-specific SP-10 gene in somatic tissues: role for TDP-43 in insulator function. J Biol Chem 282, 36143-36154.
    • (2007) J Biol Chem , vol.282 , pp. 36143-36154
    • Abhyankar, M.M.1    Urekar, C.2    Reddi, P.P.3
  • 56
    • 33745277599 scopus 로고    scopus 로고
    • Cis-Requirement for the maintenance of round spermatid-specific transcription
    • DOI 10.1016/j.ydbio.2006.04.443, PII S0012160606007238
    • Acharya KK, Govind CK, Shore AN, Stoler MH, &, Reddi PP, (2006) cis-requirement for the maintenance of round spermatid-specific transcription. Dev Biol 295, 781-790. (Pubitemid 43927709)
    • (2006) Developmental Biology , vol.295 , Issue.2 , pp. 781-790
    • Acharya, K.K.1    Govind, C.K.2    Shore, A.N.3    Stoler, M.H.4    Reddi, P.P.5
  • 58
    • 34447550769 scopus 로고    scopus 로고
    • The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3′ processing and transcription termination
    • DOI 10.1101/gad.1565207
    • Kaneko S, Rozenblatt-Rosen O, Meyerson M, &, Manley JL, (2007) The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3′ processing and transcription termination. Genes Dev 21, 1779-1789. (Pubitemid 47076477)
    • (2007) Genes and Development , vol.21 , Issue.14 , pp. 1779-1789
    • Kaneko, S.1    Rozenblatt-Rosen, O.2    Meyerson, M.3    Manley, J.L.4
  • 59
    • 9644308046 scopus 로고    scopus 로고
    • Human 5′ → 3′ exonuclease Xm2 promotes transcription termination at co-transcriptional cleavage sites
    • DOI 10.1038/nature03035
    • West S, Gromak N, &, Proudfoot NJ, (2004) Human 5′ 3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432, 522-525. (Pubitemid 39576535)
    • (2004) Nature , vol.432 , Issue.7016 , pp. 522-525
    • West, S.1    Gromak, N.2    Proudfoot, N.J.3
  • 60
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • DOI 10.1101/gr.2122004
    • Lehner B, &, Sanderson CM, (2004) A protein interaction framework for human mRNA degradation. Genome Res 14, 1315-1323. (Pubitemid 39029228)
    • (2004) Genome Research , vol.14 , Issue.7 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 62
    • 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
    • Uranishi H, Tetsuka T, Yamashita M, Asamitsu K, Shimizu M, Itoh M, &, Okamoto T, (2001) Involvement of the pro-oncoprotein TLS (translocated in liposarcoma) in nuclear factor-kappa B p65-mediated transcription as a coactivator. J Biol Chem 276, 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
  • 63
    • 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
    • Hallier M, Lerga A, Barnache S, Tavitian A, &, Moreau-Gachelin F, (1998) The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS. J Biol Chem 273, 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
  • 64
    • 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
    • Powers CA, Mathur M, Raaka BM, Ron D, &, Samuels HH, (1998) TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors. Mol Endocrinol 12, 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
  • 65
    • 54049138797 scopus 로고    scopus 로고
    • Identification and characterization of FUS/TLS as a new target of ATM
    • Gardiner M, Toth R, Vandermoere F, Morrice NA, &, Rouse J, (2008) Identification and characterization of FUS/TLS as a new target of ATM. Biochem J 415, 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
  • 66
    • 46649093597 scopus 로고    scopus 로고
    • Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription
    • DOI 10.1038/nature06992, PII NATURE06992
    • Wang X, Arai S, Song X, Reichart D, Du K, Pascual G, Tempst P, Rosenfeld MG, Glass CK, &, Kurokawa R, (2008) Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription. Nature 454, 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
  • 67
    • 77149134314 scopus 로고    scopus 로고
    • Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity
    • Oh SM, Liu Z, Okada M, Jang SW, Liu X, Chan CB, Luo H, &, Ye K, (2010) Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity. Oncogene 29, 1017-1030.
    • (2010) Oncogene , vol.29 , pp. 1017-1030
    • Oh, S.M.1    Liu, Z.2    Okada, M.3    Jang, S.W.4    Liu, X.5    Chan, C.B.6    Luo, H.7    Ye, K.8
  • 68
    • 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 DJ, 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. (Pubitemid 26315812)
    • (1996) EMBO Journal , vol.15 , Issue.18 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 69
    • 0034053964 scopus 로고    scopus 로고
    • TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins
    • DOI 10.1128/MCB.20.10.3345-3354.2000
    • Yang L, Embree LJ, &, Hickstein DD, (2000) TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Mol Cell Biol 20, 3345-3354. (Pubitemid 30243880)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.10 , pp. 3345-3354
    • Yang, L.1    Embree, L.J.2    Hickstein, D.D.3
  • 70
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan JR, (2008) CFTR function and prospects for therapy. Annu Rev Biochem 77, 701-726.
    • (2008) Annu Rev Biochem , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 71
    • 0029616734 scopus 로고
    • Cystic fibrosis: Genotypic and phenotypic variations
    • Zielenski J, &, Tsui LC, (1995) Cystic fibrosis: genotypic and phenotypic variations. Annu Rev Genet 29, 777-807. (Pubitemid 26005359)
    • (1995) Annual Review of Genetics , vol.29 , pp. 777-807
    • Zielenski, J.1    Tsui, L.-C.2
  • 73
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • DOI 10.1093/emboj/20.7.1774
    • Buratti E, Dork T, Zuccato E, Pagani F, Romano M, &, Baralle FE, (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J 20, 1774-1784. (Pubitemid 32299413)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 74
    • 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 FE, (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
  • 76
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • DOI 10.1093/nar/gki897
    • Mercado PA, Ayala YM, Romano M, Buratti E, &, Baralle FE, (2005) Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res 33, 6000-6010. (Pubitemid 41742619)
    • (2005) Nucleic Acids Research , vol.33 , Issue.18 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 78
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose JK, Wang IF, Hung L, Tarn WY, &, Shen CK, (2008) TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J Biol Chem 283, 28852-28859.
    • (2008) J Biol Chem , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 79
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum BD, Chitta RK, High AA, &, Taylor JP, (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
  • 82
    • 3042581034 scopus 로고    scopus 로고
    • Multiple functional domains of the oncoproteins Spi-1/PU.1 and TLS are involved in their opposite splicing effects in erythroleukemic cells
    • DOI 10.1038/sj.onc.1207578
    • Delva L, Gallais I, Guillouf C, Denis N, Orvain C, &, Moreau-Gachelin F, (2004) Multiple functional domains of the oncoproteins Spi-1/PU.1 and TLS are involved in their opposite splicing effects in erythroleukemic cells. Oncogene 23, 4389-4399. (Pubitemid 38850418)
    • (2004) Oncogene , vol.23 , Issue.25 , pp. 4389-4399
    • Delva, L.1    Gallais, I.2    Guillouf, C.3    Denis, N.4    Orvain, C.5    Moreau-Gachelin, F.6
  • 83
    • 0028077730 scopus 로고
    • Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors
    • Caceres JF, Stamm S, Helfman DM, &, Krainer AR, (1994) Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265, 1706-1709. (Pubitemid 24314901)
    • (1994) Science , vol.265 , Issue.5179 , pp. 1706-1709
    • Caceres, J.F.1    Stamm, S.2    Helfman, D.M.3    Krainer, A.R.4
  • 84
    • 0035328667 scopus 로고    scopus 로고
    • Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein
    • Chansky HA, Hu M, Hickstein DD, &, Yang L, (2001) Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein. Cancer Res 61, 3586-3590. (Pubitemid 32694966)
    • (2001) Cancer Research , vol.61 , Issue.9 , pp. 3586-3590
    • Chansky, H.A.1    Hu, M.2    Hickstein, D.D.3    Yang, L.4
  • 85
    • 0036319256 scopus 로고    scopus 로고
    • RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells
    • DOI 10.1016/S0736-0266(02)00006-2, PII S0736026602000062
    • Rapp TB, Yang L, Conrad EU III, Mandahl N, &, Chansky HA, (2002) RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells. J Orthop Res 20, 723-729. (Pubitemid 34822991)
    • (2002) Journal of Orthopaedic Research , vol.20 , Issue.4 , pp. 723-729
    • Rapp, T.B.1    Yang, L.2    Conrad III, E.U.3    Mandahl, N.4    Chansky, H.A.5
  • 86
    • 26844516084 scopus 로고    scopus 로고
    • β-Catenin interacts with the FUS proto-oncogene product and regulates pre-mRNA splicing
    • DOI 10.1053/j.gastro.2005.07.025, PII S0016508505013892
    • Sato S, Idogawa M, Honda K, Fujii G, Kawashima H, Takekuma K, Hoshika A, Hirohashi S, &, Yamada T, (2005) Beta-catenin interacts with the FUS proto-oncogene product and regulates pre-mRNA splicing. Gastroenterology 129, 1225-1236. (Pubitemid 41446862)
    • (2005) Gastroenterology , vol.129 , Issue.4 , pp. 1225-1236
    • Sato, S.1    Idogawa, M.2    Honda, K.3    Fujii, G.4    Kawashima, H.5    Takekuma, K.6    Hoshika, A.7    Hirohashi, S.8    Yamada, T.9
  • 87
    • 51449107580 scopus 로고    scopus 로고
    • P68 RNA helicase (DDX5) alters activity of cis- and trans-acting factors of the alternative splicing of H-Ras
    • Camats M, Guil S, Kokolo M, &, Bach-Elias M, (2008) P68 RNA helicase (DDX5) alters activity of cis- and trans-acting factors of the alternative splicing of H-Ras. PLoS ONE 3, e2926.
    • (2008) PLoS ONE , vol.3
    • Camats, M.1    Guil, S.2    Kokolo, M.3    Bach-Elias, M.4
  • 89
    • 30444437477 scopus 로고    scopus 로고
    • Subnuclear organelles: New insights into form and function
    • DOI 10.1016/j.tcb.2005.11.005, PII S0962892405003004
    • Handwerger KE, &, Gall JG, (2006) Subnuclear organelles: new insights into form and function. Trends Cell Biol 16, 19-26. (Pubitemid 43077091)
    • (2006) Trends in Cell Biology , vol.16 , Issue.1 , pp. 19-26
    • Handwerger, K.E.1    Gall, J.G.2
  • 90
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • DOI 10.1038/nrm1172
    • Lamond AI, &, Spector DL, (2003) Nuclear speckles: a model for nuclear organelles. Nat Rev Mol Cell Biol 4, 605-612. (Pubitemid 36934962)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.8 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 91
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • DOI 10.1038/nrm2277, PII NRM2277
    • Bernardi R, &, Pandolfi PP, (2007) Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol 8, 1006-1016. (Pubitemid 350174636)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 92
    • 67650747230 scopus 로고    scopus 로고
    • TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons
    • Casafont I, Bengoechea R, Tapia O, Berciano MT, &, Lafarga M, (2009) TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons. J Struct Biol 167, 235-241.
    • (2009) J Struct Biol , vol.167 , pp. 235-241
    • Casafont, I.1    Bengoechea, R.2    Tapia, O.3    Berciano, M.T.4    Lafarga, M.5
  • 93
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan X, Chiang PM, Price DL, &, Wong PC, (2010) Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc Natl Acad Sci USA 107, 16325-16330.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 94
    • 0031035765 scopus 로고    scopus 로고
    • A topogenic role for the oncogenic N-terminus of TLS: Nucleolar localization when transcription is inhibited
    • Zinszner H, Immanuel D, Yin Y, Liang FX, &, Ron D, (1997) A topogenic role for the oncogenic N-terminus of TLS: nucleolar localization when transcription is inhibited. Oncogene 14, 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
  • 95
    • 73549089900 scopus 로고    scopus 로고
    • TLS inhibits RNA polymerase III transcription
    • Tan AY, &, Manley JL, (2010) TLS inhibits RNA polymerase III transcription. Mol Cell Biol 30, 186-196.
    • (2010) Mol Cell Biol , vol.30 , pp. 186-196
    • Tan, A.Y.1    Manley, J.L.2
  • 96
    • 0036970772 scopus 로고    scopus 로고
    • Nuclear structure and intranuclear retention of premature RNAs
    • DOI 10.1016/S1047-8477(02)00530-0, PII S1047847702005300
    • Gadal O, &, Nehrbass U, (2002) Nuclear structure and intranuclear retention of premature RNAs. J Struct Biol 140, 140-146. (Pubitemid 36139855)
    • (2002) Journal of Structural Biology , vol.140 , Issue.1-3 , pp. 140-146
    • Gadal, O.1    Nehrbass, U.2
  • 97
    • 34848918150 scopus 로고    scopus 로고
    • Global Analysis of mRNA Localization Reveals a Prominent Role in Organizing Cellular Architecture and Function
    • DOI 10.1016/j.cell.2007.08.003, PII S0092867407010227
    • Lecuyer E, Yoshida H, Parthasarathy N, Alm C, Babak T, Cerovina T, Hughes TR, Tomancak P, &, Krause HM, (2007) Global analysis of mRNA localization reveals a prominent role in organizing cellular architecture and function. Cell 131, 174-187. (Pubitemid 47498530)
    • (2007) Cell , vol.131 , Issue.1 , pp. 174-187
    • Lecuyer, E.1    Yoshida, H.2    Parthasarathy, N.3    Alm, C.4    Babak, T.5    Cerovina, T.6    Hughes, T.R.7    Tomancak, P.8    Krause, H.M.9
  • 98
    • 60149086205 scopus 로고    scopus 로고
    • MRNA localization: Gene expression in the spatial dimension
    • Martin KC, &, Ephrussi A, (2009) mRNA localization: gene expression in the spatial dimension. Cell 136, 719-730.
    • (2009) Cell , vol.136 , pp. 719-730
    • Martin, K.C.1    Ephrussi, A.2
  • 99
    • 56749096054 scopus 로고    scopus 로고
    • Translational control of localized mRNAs: Restricting protein synthesis in space and time
    • Besse F, &, Ephrussi A, (2008) Translational control of localized mRNAs: restricting protein synthesis in space and time. Nat Rev Mol Cell Biol 9, 971-980.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 971-980
    • Besse, F.1    Ephrussi, A.2
  • 100
    • 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
    • Kanai Y, Dohmae N, &, Hirokawa N, (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43, 513-525. (Pubitemid 39094678)
    • (2004) Neuron , vol.43 , Issue.4 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 101
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • DOI 10.1038/76615
    • Husi H, Ward MA, Choudhary JS, Blackstock WP, &, Grant SG, (2000) Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat Neurosci 3, 661-669. (Pubitemid 30437200)
    • (2000) Nature Neuroscience , vol.3 , Issue.7 , pp. 661-669
    • Husi, H.1    Ward, M.A.2    Choudhary, J.S.3    Blackstock, W.P.4    Grant, S.G.N.5
  • 102
    • 38849117246 scopus 로고    scopus 로고
    • RNA-protein interactions and control of mRNA stability in neurons
    • DOI 10.1002/jnr.21473
    • Bolognani F, &, Perrone-Bizzozero NI, (2008) RNA-protein interactions and control of mRNA stability in neurons. J Neurosci Res 86, 481-489. (Pubitemid 351204460)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.3 , pp. 481-489
    • Bolognani, F.1    Perrone-Bizzozero, N.I.2
  • 103
    • 0024456475 scopus 로고
    • The role of mRNA and protein stability in gene expression
    • Hargrove JL, &, Schmidt FH, (1989) The role of mRNA and protein stability in gene expression. FASEB J 3, 2360-2370. (Pubitemid 19263711)
    • (1989) FASEB Journal , vol.3 , Issue.12 , pp. 2360-2370
    • Hargrove, J.L.1    Schmidt, F.H.2
  • 105
    • 80052962642 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Sending a complex message about messenger RNA in Amyotrophic Lateral Sclerosis?
    • Strong MJ, &, Volkening K, (2011) TDP-43 and FUS/TLS: Sending a complex message about messenger RNA in Amyotrophic Lateral Sclerosis? FEBS J 278, 3569-3577.
    • (2011) FEBS J , vol.278 , pp. 3569-3577
    • Strong, M.J.1    Volkening, K.2
  • 107
    • 80052963106 scopus 로고    scopus 로고
    • TDP-43: New aspects of autoregulation mechanisms in RNA binding proteins and their connection with human disease
    • Buratti E, &, Baralle FE, (2011) TDP-43: new aspects of autoregulation mechanisms in RNA binding proteins and their connection with human disease. FEBS J 278, 3530-3538.
    • (2011) FEBS J , vol.278 , pp. 3530-3538
    • Buratti, E.1    Baralle, F.E.2
  • 108
    • 34447119616 scopus 로고    scopus 로고
    • The exosome and RNA quality control in the nucleus
    • DOI 10.1038/sj.embor.7401005, PII 7401005
    • Vanacova S, &, Stefl R, (2007) The exosome and RNA quality control in the nucleus. EMBO Rep 8, 651-657. (Pubitemid 47033796)
    • (2007) EMBO Reports , vol.8 , Issue.7 , pp. 651-657
    • Vanacova, S.1    Stef, R.2
  • 109
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: Safeguarding cells from abnormal mRNA function
    • DOI 10.1101/gad.1566807
    • Isken O, &, Maquat LE, (2007) Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev 21, 1833-1856. (Pubitemid 47204924)
    • (2007) Genes and Development , vol.21 , Issue.15 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 112
    • 38949195105 scopus 로고    scopus 로고
    • Messenger RNA regulation: To translate or to degrade
    • DOI 10.1038/sj.emboj.7601977, PII 7601977
    • Shyu AB, Wilkinson MF, &, van Hoof A, (2008) Messenger RNA regulation: to translate or to degrade. EMBO J 27, 471-481. (Pubitemid 351225677)
    • (2008) EMBO Journal , vol.27 , Issue.3 , pp. 471-481
    • Shyu, A.-B.1    Wilkinson, M.F.2    Van Hoof, A.3
  • 113
    • 61849137222 scopus 로고    scopus 로고
    • Many roads to maturity: MicroRNA biogenesis pathways and their regulation
    • Winter J, Jung S, Keller S, Gregory RI, &, Diederichs S, (2009) Many roads to maturity: microRNA biogenesis pathways and their regulation. Nat Cell Biol 11, 228-234.
    • (2009) Nat Cell Biol , vol.11 , pp. 228-234
    • Winter, J.1    Jung, S.2    Keller, S.3    Gregory, R.I.4    Diederichs, S.5
  • 114
    • 60149088848 scopus 로고    scopus 로고
    • Origins and mechanisms of miRNAs and siRNAs
    • Carthew RW, &, Sontheimer EJ, (2009) Origins and mechanisms of miRNAs and siRNAs. Cell 136, 642-655.
    • (2009) Cell , vol.136 , pp. 642-655
    • Carthew, R.W.1    Sontheimer, E.J.2
  • 116
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • DOI 10.1083/jcb.136.4.761
    • Bashkirov VI, Scherthan H, Solinger JA, Buerstedde JM, &, Heyer WD, (1997) A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J Cell Biol 136, 761-773. (Pubitemid 27098734)
    • (1997) Journal of Cell Biology , vol.136 , Issue.4 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.-M.4    Heyer, W.-D.5
  • 119
    • 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
    • Moisse K, Volkening K, Leystra-Lantz C, Welch I, Hill T, &, Strong MJ, (2009) 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, 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
  • 124
    • 77958012134 scopus 로고    scopus 로고
    • Deletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism
    • Chiang PM, Ling J, Jeong YH, Price DL, Aja SM, &, Wong PC, (2010) Deletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism. Proc Natl Acad Sci USA 107, 16320-16324.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16320-16324
    • Chiang, P.M.1    Ling, J.2    Jeong, Y.H.3    Price, D.L.4    Aja, S.M.5    Wong, P.C.6
  • 127
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka T, Kametani F, Arai T, Akiyama H, &, Hasegawa M, (2009) Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum Mol Genet 18, 3353-3364.
    • (2009) Hum Mol Genet , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 128
    • 77958604956 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA
    • Kim SH, Shanware NP, Bowler MJ, &, Tibbetts RS, (2010) Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J Biol Chem 285, 34097-34105.
    • (2010) J Biol Chem , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.P.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 130
    • 33646366933 scopus 로고    scopus 로고
    • Two catalytic domains are required for protein deacetylation
    • DOI 10.1074/jbc.C500241200
    • Zhang Y, Gilquin B, Khochbin S, &, Matthias P, (2006) Two catalytic domains are required for protein deacetylation. J Biol Chem 281, 2401-2404. (Pubitemid 43845699)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2401-2404
    • Zhang, Y.1    Gilquin, B.2    Khochbin, S.3    Matthias, P.4
  • 134
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated Huntingtin
    • DOI 10.1074/jbc.M508786200
    • Iwata A, Riley BE, Johnston JA, &, Kopito RR, (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280, 40282-40292. (Pubitemid 41779165)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 135
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, &, Yao TP, (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738. (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 143
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • DOI 10.1128/MCB.21.23.8035-8044.2001
    • Seigneurin-Berny D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, &, Khochbin S, (2001) Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol Cell Biol 21, 8035-8044. (Pubitemid 33051794)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 144
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • DOI 10.1038/35087056
    • Dai RM, &, Li CC, (2001) Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat Cell Biol 3, 740-744. (Pubitemid 32734252)
    • (2001) Nature Cell Biology , vol.3 , Issue.8 , pp. 740-744
    • Dai, R.M.1    Li, C.-C.H.2
  • 145
    • 57649198447 scopus 로고    scopus 로고
    • Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease
    • Ju JS, Miller SE, Hanson PI, &, Weihl CC, (2008) Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease. J Biol Chem 283, 30289-30299.
    • (2008) J Biol Chem , vol.283 , pp. 30289-30299
    • Ju, J.S.1    Miller, S.E.2    Hanson, P.I.3    Weihl, C.C.4
  • 147
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, Dantuma NP, &, Taylor JP, (2010) VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6, 217-227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 148
    • 66449134941 scopus 로고    scopus 로고
    • VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death
    • Gitcho MA, Strider J, Carter D, Taylor-Reinwald L, Forman MS, Goate AM, &, Cairns NJ, (2009) VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem 284, 12384-12398.
    • (2009) J Biol Chem , vol.284 , pp. 12384-12398
    • Gitcho, M.A.1    Strider, J.2    Carter, D.3    Taylor-Reinwald, L.4    Forman, M.S.5    Goate, A.M.6    Cairns, N.J.7
  • 151
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura S, Noda T, &, Yoshimori T, (2008) Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct Funct 33, 109-122.
    • (2008) Cell Struct Funct , vol.33 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 152
    • 33644507718 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin function and dysfunction in motor neurons
    • DOI 10.1016/j.ijdevneu.2005.11.013, PII S0736574805001449, Neural Signal Transduction in Health and Disease - Cytokinesd, Mitochondrial Dysfunction and Transport Processes
    • Levy JR, &, Holzbaur EL, (2006) Cytoplasmic dynein/dynactin function and dysfunction in motor neurons. Int J Dev Neurosci 24, 103-111. (Pubitemid 43294616)
    • (2006) International Journal of Developmental Neuroscience , vol.24 , Issue.2-3 , pp. 103-111
    • Levy, J.R.1    Holzbaur, E.L.F.2
  • 153
    • 74949114469 scopus 로고    scopus 로고
    • The effects of dynein inhibition on the autophagic pathway in glioma cells
    • Yamamoto M, Suzuki SO, &, Himeno M, (2010) The effects of dynein inhibition on the autophagic pathway in glioma cells. Neuropathology 30, 1-6.
    • (2010) Neuropathology , vol.30 , pp. 1-6
    • Yamamoto, M.1    Suzuki, S.O.2    Himeno, M.3
  • 156
    • 76549101965 scopus 로고    scopus 로고
    • Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43
    • Urushitani M, Sato T, Bamba H, Hisa Y, &, Tooyama I, (2010) Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43. J Neurosci Res 88, 784-797.
    • (2010) J Neurosci Res , vol.88 , pp. 784-797
    • Urushitani, M.1    Sato, T.2    Bamba, H.3    Hisa, Y.4    Tooyama, I.5
  • 157
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)
    • Crippa V, Sau D, Rusmini P, Boncoraglio A, Onesto E, Bolzoni E, Galbiati M, Fontana E, Marino M, Carra S, et al. (2010) The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet 19, 3440-3456.
    • (2010) Hum Mol Genet , vol.19 , pp. 3440-3456
    • Crippa, V.1    Sau, D.2    Rusmini, P.3    Boncoraglio, A.4    Onesto, E.5    Bolzoni, E.6    Galbiati, M.7    Fontana, E.8    Marino, M.9    Carra, S.10
  • 158
    • 70350454798 scopus 로고    scopus 로고
    • Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability
    • Caccamo A, Majumder S, Deng JJ, Bai Y, Thornton FB, &, Oddo S, (2009) Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability. J Biol Chem 284, 27416-27424.
    • (2009) J Biol Chem , vol.284 , pp. 27416-27424
    • Caccamo, A.1    Majumder, S.2    Deng, J.J.3    Bai, Y.4    Thornton, F.B.5    Oddo, S.6
  • 159
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • Wang X, Fan H, Ying Z, Li B, Wang H, &, Wang G, (2010) Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci Lett 469, 112-116.
    • (2010) Neurosci Lett , vol.469 , pp. 112-116
    • Wang, X.1    Fan, H.2    Ying, Z.3    Li, B.4    Wang, H.5    Wang, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.