Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
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We used cross-linking and immunoprecipitation coupled with high-throughput sequencing to identify binding sites in 6,304 genes as the brain RNA targets for TDP-43, an RNA binding protein that, when mutated, causes amyotrophic lateral sclerosis. Massively parallel sequencing and splicing-sensitive junction arrays revealed that levels of 601 mRNAs were changed (including Fus (Tls), progranulin and other transcripts encoding neurodegenerative disease-associated proteins) and 965 altered splicing events were detected (including in sortilin, the receptor for progranulin) following depletion of TDP-43 from mouse adult brain with antisense oligonucleotides. RNAs whose levels were most depleted by reduction in TDP-43 were derived from genes with very long introns and that encode proteins involved in synaptic activity. Lastly, we found that TDP-43 autoregulates its synthesis, in part by directly binding and enhancing splicing of an intron in the 3' untranslated region of its own transcript, thereby triggering nonsense-mediated RNA degradation.
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Both ALS-associated mutations and changes in wild-type TDP43 expression alter a large programme of alternative exons in mutant mice.
“Both the ALS-associated mutations and the changes in wild-type TDP43 expression alter a large programme of alternative exons in mutant mice170,174,175.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [170]
Less than a quarter of affected exons are shared between the transgenic and RNA interference-depletion mouse models of TDP43.
“However, less than a quarter of affected exons are shared between the transgenic and RNA interference-depletion mouse models.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [170]
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Mapping and quantifying mammalian transcriptomes by RNA-Seq
Mortazavi, A., Williams, B. A., McCue, K., Schaeffer, L., & Wold, B. (2008) · Nature Methods · doi:10.1038/nmeth.1226 · Cited by 13,696 · see citing works
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366 · see citing works
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works
Alternative isoform regulation in human tissue transcriptomes
Wang, E. T., Sandberg, R., Luo, S., Khrebtukova, I., Zhang, L., Mayr, C., Kingsmore, S. F., Schroth, G. P., & Burge, C. B. (2008) · Nature · doi:10.1038/nature07509 · Cited by 5,181 · see citing works
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works
A gene atlas of the mouse and human protein-encoding transcriptomes
Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475 · see citing works
Shah, M. A., Datson, N. A., Srinidhi, L., Stanton, V. P., MacDonald, M. E., Allard, M. W., Youngman, S., Am, F., Mott, R., Draths, K., et al. (1993) · Cell · Cited by 3,055 · see citing works
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630 · see citing works
Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,531 · see citing works
Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,526 · see citing works
Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058 · see citing works
Argonaute HITS-CLIP decodes microRNA–mRNA interaction maps
Chi, S. W., Zang, J. B., Mele, A., & Darnell, R. B. (2009) · Nature · doi:10.1038/nature08170 · Cited by 1,791 · see citing works
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Velde, C. V., Bouchard, J.-P., Lacomblez, L., Pochigaeva, K., Salachas, F., et al. (2008) · Nature Genetics · doi:10.1038/ng.132 · Cited by 1,544 · see citing works
Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512 · see citing works
HITS-CLIP yields genome-wide insights into brain alternative RNA processing
Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352 · cited 1× · see citing works
“Moreover, cross-linking, immunoprecipitation and high-throughput sequencing (CLIP-seq or HITS-CLIP) experiments have found that a single RNA-binding protein can have previously unrecognized roles in RNA processing and affect many alternatively spliced transcript”
BackgroundCharacterizing the RNA targets and position-dependent splicing regulation by TDP-43
Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2778 · Cited by 1,165 · see citing works
Cooper, T. A., Wan, L., & Dreyfuss, G. (2009) · Cell · doi:10.1016/j.cell.2009.02.011 · Cited by 1,160 · see citing works
CLIP Identifies Nova-Regulated RNA Networks in the Brain
Ule, J., Jensen, K. B., Ruggiu, M., Mele, A., Ule, A., & Darnell, R. B. (2003) · Science · doi:10.1126/science.1090095 · Cited by 1,120 · see citing works
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · see citing works
Self-citationTranscriptome analysis by strand-specific sequencing of complementary DNA
Parkhomchuk, D., Borodina, T. A., Amstislavskiy, V. S., Banaru, M., Hallen, L., Krobitsch, S., Lehrach, H. R., & Солдатов, А. В. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp596 · Cited by 934 · see citing works
Van Deerlin, V. M., Leverenz, J. B., Bekris, L. M., Bird, T. D., Yuan, W., Elman, L. B., Clay, D., Wood, E. M., Chen-Plotkin, A. S., Martinez-Lage, M., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70071-1 · Cited by 723 · see citing works
Nuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
Buratti, E., Dörk, T., Zuccato, E., Pagani, F., Romano, M., & Baralle, F. E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1774 · Cited by 633 · see citing works
TDP‐43 A315T mutation in familial motor neuron disease
Gitcho, M. A., Baloh, R. H., Chakraverty, S., Mayo, K., Norton, J. B., Levitch, D., Hatanpaa, K. J., White, C. L., Bigio, E. H., Caselli, R. J., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21344 · Cited by 619 · see citing works
TDP‐43 regulates its mRNA levels through a negative feedback loop
Ayala, Y. M., Conti, L. D., Avendaño-Vázquez, S. E., Dhir, A., Romano, M., D’Ambrogio, A., Tollervey, J. R., Ule, J., Baralle, M., Buratti, E., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.310 · Cited by 618 · see citing works
Yeo, G. W., Coufal, N. G., Liang, T. Y., Peng, G. E., Fu, X.-D., & Gage, F. H. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1545 · Cited by 572 · see citing works
Self-citationXu, Y.-F., Gendron, T. F., Zhang, Y., Lin, W.-L., D’Alton, S., Sheng, H., Casey, M. C., Tong, J., Knight, J. A., Yu, X., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1630-10.2010 · Cited by 555 · see citing works
Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin
Hu, F., Padukkavidana, T., Vægter, C. B., Brady, O. A., Zheng, Y., Mackenzie, I. R., Feldman, H., Nykjær, A., & Strittmatter, S. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.034 · Cited by 545 · see citing works
ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
Ling, S., de Albuquerque, C. P., Han, J. S., Lagier‐Tourenne, C., Tokunaga, S., Zhou, H., & Cleveland, D. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008227107 · Cited by 450 · see citing works
Self-citationDysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
Igaz, L. M., Kwong, L. K., Lee, E. B., Chen‐Plotkin, A. S., Swanson, E., Unger, T. L., Malunda, J. A., Xu, Y., Winton, M. J., Trojanowski, J. Q., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44867 · Cited by 434 · see citing works
Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes
Sephton, C. F., Cenik, C., Küçükural, A., Dammer, E. B., Cenik, B., Han, Y., Dewey, C. M., Roth, F. P., Herz, J., Peng, J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190884 · Cited by 429 · see citing works
Wollerton, M., Gooding, C., Wagner, E. J., García-Blanco, M. A., & Smith, C. W. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00502-1 · Cited by 409 · see citing works
Mili, S., & STEITZ, J. A. (2004) · RNA · doi:10.1261/rna.7151404 · Cited by 369 · see citing works
The splicing factor SC35 has an active role in transcriptional elongation
Lin, S., Coutinho-Mansfield, G., Wang, D., Pandit, S., & Fu, X. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1461 · Cited by 363 · see citing works
TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein
Strong, M. J., Volkening, K., Hammond, R. R., Yang, W., Strong, W., Leystra‐Lantz, C., & Shoesmith, C. L. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.03.007 · Cited by 349 · see citing works
SC35 autoregulates its expression by promoting splicing events that destabilize its mRNAs
Sureau, A., Gattoni, R., Dooghe, Y., Ste'venin, J., & Soret, J. (2001) · EMBO Journal · doi:10.1093/emboj/20.7.1785 · Cited by 347 · see citing works
Hir, H. L., Moore, M. J., & Maquat, L. E. (2000) · Genes & Development · doi:10.1101/gad.14.9.1098 · Cited by 337 · see citing works
Du, H., Cline, M. S., Osborne, R. J., Tuttle, D. L., Clark, T. A., Donohue, J. P., Hall, M. P., Shiue, L., Swanson, M. S., Thornton, C. A., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1720 · Cited by 332 · see citing works
Self-citationComprehensive discovery of endogenous Argonaute binding sites in Caenorhabditis elegans
Zisoulis, D. G., Lovci, M., Wilbert, M. L., Hutt, K. R., Liang, T. Y., Pasquinelli, A. E., & Yeo, G. W.-M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1745 · Cited by 290 · see citing works
Self-citationSchwab, C., Arai, T., Hasegawa, M., Yu, S. Y., & McGeer, P. L. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e8951 · Cited by 271 · see citing works
Nuclear factor TDP‐43 can affect selected microRNA levels
Buratti, E., Conti, L. D., Stuani, C., Romano, M., Baralle, M., & Baralle, F. E. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07643.x · Cited by 240 · see citing works
Mercado, P. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki897 · Cited by 226 · see citing works
Knockdown of transactive response DNA‐binding protein (TDP‐43) downregulates histone deacetylase 6
Fiesel, F. C., Voigt, A., Weber, S. S., den Haute, C. V., Waldenmaier, A., Görner, K., Walter, M. J., Anderson, M. L., Kern, J. V., Rasse, T. M., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.324 · Cited by 226 · see citing works
Bergeron, C., Berić-Maskarel, K., Muntasser, S., Weyer, L., Somerville, M. J., & Percy, M. E. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199405000-00002 · Cited by 164 · see citing works
Discovery and Analysis of Evolutionarily Conserved Intronic Splicing Regulatory Elements
Yeo, G. W.-M., Nostrand, E. L. V., & Liang, T. Y. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030085 · Cited by 158 · see citing works
Self-citationRNAdb--a comprehensive mammalian noncoding RNA database
Pang, K. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki089 · Cited by 155 · see citing works
Carrasquillo, M. M., Nicholson, A. M., Finch, N. A., Gibbs, J. R., Baker, M. C., Rutherford, N. J., Hunter, T. A., DeJesus‐Hernandez, M., Bisceglio, G. D., Mackenzie, I. R., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.11.002 · Cited by 138 · see citing works
Mammalian orthologues of a yeast regulator of nonsense transcript stability.
Perlick, H. A., Medghalchi, S. M., Spencer, F. A., Kendzior, R. J., & Dietz, H. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10928 · Cited by 137 · see citing works
Antagonistic factors control the unproductive splicing of SC35 terminal intron
Dreumont, N., Hardy, S., Behm‐Ansmant, I., Kister, L., Branlant, C., Stévenin, J., & Bourgeois, C. F. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1086 · Cited by 45 · see citing works
A Mutation that Creates a Pseudoexon in SOD1 Causes Familial ALS
Valdmanis, P. N., Belzil, V., Lee, J., Dion, P. A., St‐Onge, J., Hince, P., Funalot, B., Couratier, P., Clavelou, P., Camu, W., et al. (2009) · Annals of Human Genetics · doi:10.1111/j.1469-1809.2009.00546.x · Cited by 38 · see citing works
A novel SOD1 splice site mutation associated with familial ALS revealed by SOD activity analysis
Birve, A., Neuwirth, C., Weber, M., Marklund, S. L., Nilsson, A.-C., Jonsson, P. A., & Andersen, P. M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq338 · Cited by 30 · see citing works
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Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,047 · see citing works
Self-citationConverging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · see citing works
Self-citationCharacterizing the RNA targets and position-dependent splicing regulation by TDP-43
Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2778 · Cited by 1,165 · see citing works
Scotti, M. M., & Swanson, M. S. (2015) · Nature Reviews Genetics · doi:10.1038/nrg.2015.3 · Cited by 1,130 · see citing works
Overcoming cellular barriers for RNA therapeutics
Dowdy, S. F. (2017) · Nature Biotechnology · doi:10.1038/nbt.3802 · Cited by 1,139 · see citing works
The changing scene of amyotrophic lateral sclerosis
Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957 · see citing works
Stress granules as crucibles of ALS pathogenesis
Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., & Patel, B. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00025 · Cited by 770 · see citing works
Tripathi, V., Shen, Z., Chakraborty, A., Giri, S., Freier, S. M., Wu, X., Zhang, Y., Gorospe, M., Prasanth, S. G., Lal, A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003368 · Cited by 753 · see citing works
Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs
Lagier‐Tourenne, C., Polymenidou, M., Hutt, K. R., Vu, A. Q., Baughn, M. W., Huelga, S. C., Clutario, K. M., Ling, S., Liang, T. Y., Mazur, C., et al. (2012) · Nature Neuroscience · doi:10.1038/nn.3230 · Cited by 730 · see citing works
Self-citationMALAT1 — a paradigm for long noncoding RNA function in cancer
Gutschner, T., Hämmerle, M., & Diederichs, S. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1028-y · Cited by 722 · see citing works
TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
Ling, J. P., Pletniková, O., Troncoso, J. C., & Wong, P. C. (2015) · Science · doi:10.1126/science.aab0983 · Cited by 673 · see citing works
Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations
Alami, N. H., Smith, R. B., Carrasco, M. A., Williams, L. A., Winborn, C. S., Han, S. S. W., Kiskinis, E., Winborn, B., Freibaum, B. D., Kanagaraj, A., et al. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.018 · Cited by 660 · see citing works
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659 · see citing works
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Klim, J. R., Williams, L. A., Limone, F., Guerra San Juan, I., Davis-Dusenbery, B. N., Mordes, D. A., Burberry, A., Steinbaugh, M. J., Gamage, K. K., Kirchner, R., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0300-4 · Cited by 653 · see citing works
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Melamed, Z., López-Erauskin, J., Baughn, M. W., Zhang, O., Drenner, K., Sun, Y., Freyermuth, F., McMahon, M. A., Beccari, M. S., Artates, J. W., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0293-z · Cited by 635 · see citing works
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Blokhuis, A. M., Groen, E. J. N., Koppers, M., van den Berg, L. H., & Pasterkamp, R. J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1125-6 · Cited by 573 · see citing works
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Ma, X. R., Prudencio, M., Koike, Y., Vatsavayai, S. C., Kim, G., Harbinski, F., Briner, A., Rodriguez, C. M., Guo, C., Akiyama, T., et al. (2022) · Nature · doi:10.1038/s41586-022-04424-7 · Cited by 574 · see citing works
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Lagier‐Tourenne, C., Baughn, M. W., Rigo, F., Sun, S., Liu, P., Li, H., Jiang, J., Watt, A. T., Chun, S. J., Katz, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318835110 · Cited by 555 · see citing works
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Gałgański, Ł., Urbanek-Trzeciak, M. O., & Krzyżosiak, W. J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx759 · Cited by 489 · see citing works
Arnold, E. S., Ling, S., Huelga, S. C., Lagier‐Tourenne, C., Polymenidou, M., Ditsworth, D., Kordasiewicz, H. B., McAlonis‐Downes, M., Platoshyn, O., Parone, P. A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222809110 · Cited by 494 · see citing works
Self-citationHuelga, S. C., Vu, A. Q., Arnold, J. D., Liang, T. Y., Liu, P. P., Yan, B. Y., Donohue, J. P., Shiue, L., Hoon, S., Brenner, S., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.02.001 · Cited by 470 · see citing works
Self-citationThe inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity
Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4130 · Cited by 462 · see citing works
Pre-mRNA splicing in disease and therapeutics
Singh, R. K., & Cooper, T. A. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.06.006 · Cited by 456 · see citing works
The role of TDP-43 mislocalization in amyotrophic lateral sclerosis
Suk, T. R., & Rousseaux, M. W. C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00397-1 · Cited by 456 · see citing works
TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes
Kawahara, Y., & Mieda-Sato, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112427109 · Cited by 449 · see citing works
Long Noncoding RNAs with snoRNA Ends
Yin, Q.-F., Yang, L. C., Zhang, Y., Xiang, J., Wu, Y., Carmichael, G., & Chen, L. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.033 · Cited by 444 · see citing works
GFOLD: a generalized fold change for ranking differentially expressed genes from RNA-seq data
Feng, J., Meyer, C. A., Wang, Q., Liu, J. S., Liu, X. S., & Zhang, Y. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts515 · Cited by 426 · see citing works
Cytoplasmic functions of long noncoding RNAs
Noh, J. H., Kim, K. M., McClusky, W. G., Abdelmohsen, K., & Gorospe, M. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1471 · Cited by 428 · see citing works
RNA-binding proteins with prion-like domains in health and disease
Harrison, A. F., & Shorter, J. (2017) · Biochemical Journal · doi:10.1042/bcj20160499 · Cited by 415 · see citing works
Olney, N. T., Spina, S., & Miller, B. L. (2017) · Neurologic Clinics · doi:10.1016/j.ncl.2017.01.008 · Cited by 419 · see citing works
Advances in understanding the molecular basis of frontotemporal dementia
Rademakers, R., Neumann, M., & Mackenzie, I. R. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.117 · Cited by 414 · see citing works
Mapping in vivo protein-RNA interactions at single-nucleotide resolution from HITS-CLIP data
Zhang, C., & Darnell, R. B. (2011) · Nature Biotechnology · doi:10.1038/nbt.1873 · Cited by 405 · see citing works
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
Lukavsky, P. J., Daujotyte, D., Tollervey, J. R., Ule, J., Stuani, C., Buratti, E., Baralle, F. E., Damberger, F. F., & Allain, F. H. ‐. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2698 · Cited by 408 · see citing works
Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges
Lovci, M. T., Ghanem, D., Marr, H., Arnold, J., Gee, S., Parra, M., Liang, T. Y., Stark, T. J., Gehman, L. T., Hoon, S., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2699 · Cited by 385 · see citing works
Self-citationPhysiological functions and pathobiology of TDP ‐43 and FUS / TLS proteins
Ratti, A., & Buratti, E. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13625 · Cited by 384 · see citing works
TDP-43 proteinopathies: a new wave of neurodegenerative diseases
de Boer, E. M. J., Orie, V. K., Williams, T. L., Baker, M. R., Oliveira, H. M. D., Polvikoski, T. M., Silsby, M., Menon, P., van den Bos, M. A. J., Halliday, G. M., et al. (2020) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2020-322983 · Cited by 373 · see citing works
Mackenzie, I. R., & Neumann, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13588 · Cited by 374 · see citing works
Wang, I.-F., Guo, B.-S., Liu, Y.-C., Wu, C.-C., Yang, C.-H., Tsai, K.-J., & Shen, C.-K. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206362109 · Cited by 377 · see citing works
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases
Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00254 · Cited by 375 · see citing works
The Seeds of Neurodegeneration: Prion-like Spreading in ALS
Polymenidou, M., & Cleveland, D. W. (2011) · Cell · doi:10.1016/j.cell.2011.10.011 · Cited by 370 · see citing works
Self-citationALS Genetics: Gains, Losses, and Implications for Future Therapies
Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370 · see citing works
An acetylation switch controls TDP-43 function and aggregation propensity
Cohen, T. J., Hwang, A. W., Restrepo, C. R., Yuan, C., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Nature Communications · doi:10.1038/ncomms6845 · Cited by 357 · see citing works
Exosome secretion is a key pathway for clearance of pathological TDP-43
Iguchi, Y., Eid, L., Parent, M., Soucy, G., Bareil, C., Riku, Y., Kawai, K., Takagi, S., Yoshida, M., Katsuno, M., et al. (2016) · Brain · doi:10.1093/brain/aww237 · Cited by 360 · see citing works
TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets
Scotter, E. L., Chen, H.-J., & Shaw, C. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0338-x · Cited by 356 · see citing works
HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells
Yu, H., Lu, S., Gasior, K. I., Singh, D., Vazquez‐Sanchez, S., Tapia, O., Toprani, D., Beccari, M. S., Yates, J. R., Cruz, S. D., et al. (2021) · Science · doi:10.1126/science.abb4309 · Cited by 355 · see citing works
Self-citationUnderstanding the role of TDP-43 and FUS/TLS in ALS and beyond
Da Cruz, S., & Cleveland, D. W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.05.029 · Cited by 351 · see citing works
Self-citationAfroz, T., Hock, E., Ernst, P. J., Foglieni, C., Jambeau, M., Gilhespy, L. A. B., Laferrière, F., Maniecka, Z., Plückthun, A., Mittl, P. R. E., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00062-0 · Cited by 351 · see citing works
Self-citationMALAT1: a druggable long non-coding RNA for targeted anti-cancer approaches
Amodio, N., Raimondi, L., Juli, G., Stamato, M. A., Caracciolo, D., Tagliaferri, P., & Tassone, P. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0606-4 · Cited by 351 · see citing works
Shen, W., Hoyos, C. L. D., Migawa, M. T., Vickers, T. A., Sun, H., Low, A., Bell, T. A., Rahdar, M., Mukhopadhyay, S., Hart, C. E., et al. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0106-2 · Cited by 350 · see citing works
The neurogenetics of alternative splicing
Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340 · see citing works
Walker, A. K., Spiller, K. J., Ge, G., Zheng, A., Xu, Y., Zhou, M. S., Tripathy, K., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1460-x · Cited by 338 · see citing works
Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization
West, J. A., Mito, M., Kurosaka, S., Takumi, T., Tanegashima, C., Chujo, T., Yanaka, K., Kingston, R. E., Hirose, T., Bond, C. S., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601071 · Cited by 331 · see citing works
Bilican, B., Serio, A., Barmada, S. J., Nishimura, A. L., Sullivan, G. J., Carrasco, M., Phatnani, H. P., Puddifoot, C. A., Story, D., Fletcher, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202922109 · Cited by 328 · see citing works
Tam, O. H., Rozhkov, N. V., Shaw, R., Kim, D., Hubbard, I., Fennessey, S., Propp, N., Phatnani, H., Kwan, J., Sareen, D., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.066 · Cited by 327 · see citing works
Genetics of amyotrophic lateral sclerosis: an update
Chen, S., Sayana, P., Zhang, X., & Le, W. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-28 · Cited by 323 · see citing works
Site identification in high-throughput RNA–protein interaction data
Uren, P. J., Bahrami‐Samani, E., Burns, S. C., Qiao, M., Karginov, F. V., Hodges, E. C., Hannon, G. J., Sanford, J. R., Penalva, L. O. F., & Smith, A. D. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts569 · Cited by 324 · see citing works
Ameur, A., Zaghlool, A., Halvardson, J., Wetterbom, A., Gyllensten, U., Cavelier, L., & Feuk, L. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2143 · Cited by 323 · see citing works
Mitra, J., Guerrero, E. N., Hegde, P. M., Liachko, N. F., Wang, H., Vasquez, V., Gao, J., Pandey, A., Taylor, J. P., Kraemer, B. C., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818415116 · Cited by 305 · see citing works
Colombrita, C., Onesto, E., Megiorni, F., Pizzuti, A., Baralle, F. E., Buratti, E., Silani, V., & Ratti, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333450 · Cited by 291 · see citing works
Local RNA Translation at the Synapse and in Disease: Figure 1.
Liu‐Yesucevitz, L., Bassell, G. J., Gitler, A. D., Hart, A. C., Klann, E., Richter, J. D., Warren, S. T., & Wolozin, B. L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4105-11.2011 · Cited by 289 · see citing works
Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain
Rogelj, B., Easton, L. E., Bogu, G. K., Stanton, L. W., Rot, G., Curk, T., Zupan, B., Sugimoto, Y., Modic, M., Haberman, N., et al. (2012) · Scientific Reports · doi:10.1038/srep00603 · Cited by 278 · see citing works
Bentmann, E., Neumann, M., Tahirović, S., Rodde, R., Dormann, D., & Haass, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328757 · Cited by 277 · see citing works
Duan, Y., Du, A., Gu, J., Duan, G., Wang, C., Gui, X., Ma, Z., Qian, B., Deng, X., Zhang, K., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0141-z · Cited by 271 · see citing works
MALAT1 Long Non-Coding RNA: Functional Implications
Arun, G., Aggarwal, D., & Spector, D. L. (2020) · Non-Coding RNA · doi:10.3390/ncrna6020022 · Cited by 276 · see citing works
Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions
Nussbacher, J. K., Tabet, R., Yeo, G. W.-M., & Lagier‐Tourenne, C. (2019) · Neuron · doi:10.1016/j.neuron.2019.03.014 · Cited by 264 · see citing works
Self-citationTDP-43 gains function due to perturbed autoregulation in a Tardbp knock-in mouse model of ALS-FTD
White, M. A., Kim, E., Duffy, A., Adalbert, R., Phillips, B. U., Peters, O. M., Stephenson, J., Yang, S., Massenzio, F., Lin, Z., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0113-5 · Cited by 267 · see citing works
TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
Cohen, T. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.06.004 · Cited by 271 · see citing works
LIN28 Binds Messenger RNAs at GGAGA Motifs and Regulates Splicing Factor Abundance
Wilbert, M. L., Huelga, S. C., Kapeli, K., Stark, T. J., Liang, T. Y., Chen, S., Yan, B. Y., Nathanson, J. L., Hutt, K. R., Lovci, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.004 · Cited by 269 · see citing works
Self-citationTriad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Tziortzouda, P., Bosch, L. V. D., & Hirth, F. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00431-1 · Cited by 270 · see citing works
Ribosomal Protein s15 Phosphorylation Mediates LRRK2 Neurodegeneration in Parkinson’s Disease
Martin, I., Kim, J. W., Lee, B. D., Kang, H. C., Xu, J.-C., Jia, H., Stankowski, J., Kim, M.-S., Zhong, J., Kumar, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.064 · Cited by 265 · see citing works
Mobile DNA elements in the generation of diversity and complexity in the brain
Erwin, J. A., Marchetto, M. C., & Gage, F. H. (2014) · Nature reviews. Neuroscience · doi:10.1038/nrn3730 · Cited by 264 · see citing works
TARDBP and FUS Mutations Associated with Amyotrophic Lateral Sclerosis: Summary and Update
Lattante, S., Rouleau, G. A., & Kabashi, E. (2013) · Human Mutation · doi:10.1002/humu.22319 · Cited by 262 · see citing works
Swarup, V., Phaneuf, D., Bareil, C., Robertson, J., Rouleau, G. A., Križ, J., & Julien, J. (2011) · Brain · doi:10.1093/brain/awr159 · Cited by 264 · see citing works
Gopal, P. P., Nirschl, J., Klinman, E., & Holzbaur, E. L. F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614462114 · Cited by 261 · see citing works
Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models
Armakola, M., Higgins, M., Figley, M. D., Barmada, S. J., Scarborough, E. A., Diaz, Z., Fang, X., Shorter, J., Krogan, N. J., Finkbeiner, S. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2434 · Cited by 250 · see citing works
Aulas, A., & Velde, C. V. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00423 · Cited by 256 · see citing works
Moore, M. J., Zhang, C., Gantman, E. C., Mele, A., Darnell, J. C., & Darnell, R. B. (2014) · Nature Protocols · doi:10.1038/nprot.2014.012 · Cited by 251 · see citing works
Smith, B. N., Topp, S. D., Fallini, C., Shibata, H., Chen, H.-J., Troakes, C., King, A., Ticozzi, N., Kenna, K. P., Gkazi, S. A., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aad9157 · Cited by 249 · see citing works
Fallini, C., Bassell, G. J., & Rossoll, W. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds205 · Cited by 247 · see citing works
Scekic‐Zahirovic, J., Sendscheid, O., Oussini, H. E., Jambeau, M., Sun, Y., Mersmann, S., Wagner, M., Dieterle, S., Sinniger, J., Dirrig‐Grosch, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201592559 · Cited by 239 · see citing works
Self-citationMechanism of STMN2 cryptic splice-polyadenylation and its correction for TDP-43 proteinopathies
Baughn, M. W., Melamed, Z., López‐Erauskin, J., Beccari, M. S., Ling, K., Zuberi, A. R., Presa, M. F., Gonzalo-Gil, E., Maimon, R., Vazquez‐Sanchez, S., et al. (2023) · Science · doi:10.1126/science.abq5622 · Cited by 236 · see citing works
Self-citationNon-coding RNAs with essential roles in neurodegenerative disorders
Salta, E., & Strooper, B. D. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70286-1 · Cited by 244 · see citing works
Secreted PD-L1 variants mediate resistance to PD-L1 blockade therapy in non–small cell lung cancer
Gong, B., Kiyotani, K., Sakata, S., Nagano, S., Kumehara, S., Baba, S., Besse, B., Yanagitani, N., Friboulet, L., Nishio, M., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20180870 · Cited by 243 · see citing works
TDP-43 condensation properties specify its RNA-binding and regulatory repertoire
Hallegger, M., Chakrabarti, A. M., Lee, F. C. Y., Lee, B. L., Amalietti, A. G., Odeh, H. M., Copley, K. E., Rubien, J. D., Portz, B., Kuret, K., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.018 · Cited by 240 · see citing works
TDP-43 depletion in microglia promotes amyloid clearance but also induces synapse loss
Paolicelli, R. C., Jawaid, A., Henstridge, C. M., Valeri, A., Merlini, M., Robinson, J. L., Lee, E. B., Rose, J., Appel, S., Lee, V. M.-Y., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.05.037 · Cited by 239 · see citing works
SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination
Zhao, D. Y., Gish, G. D., Braunschweig, U., Li, Y., Ni, Z., Schmitges, F. W., Zhong, G., Liu, K., Li, W., Moffat, J., et al. (2015) · Nature · doi:10.1038/nature16469 · Cited by 238 · see citing works
Wang, C., Duan, Y., Duan, G., Wang, Q., Zhang, K., Deng, X., Qian, B., Gu, J., Ma, Z., Zhang, S., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.019 · Cited by 227 · see citing works
Truncated stathmin-2 is a marker of TDP-43 pathology in frontotemporal dementia
Prudencio, M., Humphrey, J., Pickles, S., Brown, A.-L., Hill, S. E., Kachergus, J. M., Shi, J., Heckman, M. G., Spiegel, M. R., Cook, C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci139741 · Cited by 231 · see citing works
Loss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons
Liu, E. Y., Russ, J., Cali, C. P., Phan, J. M., Amlie-Wolf, A., & Lee, E. B. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.003 · Cited by 231 · see citing works
“Alterations specifically affected long genes including transcripts with TDP-43 binding sites, concor-dant with prior experimental data showing the preferential binding of TDP-43 to long introns (LagierTourenne et al., 2012; Polymenidou et al., 2011; Tollervey et al., 2011).”
BackgroundSmola, M. J., Christy, T. W., Inoue, K., Nicholson, C. O., Friedersdorf, M. B., Keene, J. D., Lee, D. M., Calabrese, J. M., & Weeks, K. M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600008113 · Cited by 230 · see citing works
Pathomechanisms of TDP‐43 in neurodegeneration
Gao, J., Wang, L., Huntley, M. L., Perry, G. L., & Wang, X. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14327 · Cited by 230 · see citing works
- Authors
- Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., Kordasiewicz, H., Sedaghat, Y., Donohue, J. P., Shiue, L., Bennett, C. F., Yeo, G. W., & Cleveland, D. W.
- Affiliations
- University of California San Diego (US)
- Ionis Pharmaceuticals (United States) (US)
- University of California, Santa Cruz (US)
- Corresponding author
- Yeo, Gene W
- Cleveland, Don W
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2011-02-27
- Volume
- 14
- Issue
- 4
- Pages
- 459-468
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC3094729
- OpenAlex
- W2101042581
- Cited by
- 1,335
- References
- 51
- Citations by year
- 2026: 71 · 2025: 112 · 2024: 116 · 2023: 84 · 2022: 76 · 2021: 85 · 2020: 74 · 2019: 85 · 2018: 84 · 2017: 83 · 2016: 72 · 2015: 78 · 2014: 79 · 2013: 86 · 2012: 99
- FWCI
- 63.46
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wellcome Trust (089701)
- National Human Genome Research Institute (HG004659, R01HG004659)
- National Institute of General Medical Sciences (R01GM084317, GM084317)
- National Institute of Neurological Disorders and Stroke (R37 NS 27036, R37NS027036)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- TDP-43, amyotrophic lateral sclerosis, RNA-binding proteins, RNA splicing, long introns, neuronal vulnerability, nonsense-mediated mRNA decay, 3' untranslated region, progranulin, sortilin, FUS, synaptic proteins, antisense oligonucleotides, brain transcriptome, neurodegeneration
- MeSH terms
- Amyotrophic Lateral Sclerosis, Animals, DNA-Binding Proteins, Female, Homeostasis, Humans, Mice, Inbred C57BL, Mice, Transgenic, Nerve Degeneration, Neurons, RNA Precursors, RNA, Messenger, Oligonucleotides, Antisense, Alternative Splicing, 3' Untranslated Regions, Mice
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