Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
Open accessAbstract
TDP-43 is a predominantly nuclear RNA-binding protein that forms inclusion bodies in frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). The mRNA targets of TDP-43 in the human brain and its role in RNA processing are largely unknown. Using individual nucleotide-resolution ultraviolet cross-linking and immunoprecipitation (iCLIP), we found that TDP-43 preferentially bound long clusters of UG-rich sequences in vivo. Analysis of RNA binding by TDP-43 in brains from subjects with FTLD revealed that the greatest increases in binding were to the MALAT1 and NEAT1 noncoding RNAs. We also found that binding of TDP-43 to pre-mRNAs influenced alternative splicing in a similar position-dependent manner to Nova proteins. In addition, we identified unusually long clusters of TDP-43 binding at deep intronic positions downstream of silenced exons. A substantial proportion of alternative mRNA isoforms regulated by TDP-43 encode proteins that regulate neuronal development or have been implicated in neurological diseases, highlighting the importance of TDP-43 for the regulation of splicing in the brain.
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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 [174]
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 [174]
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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
Mechanisms of Alternative Pre-Messenger RNA Splicing
Black, D. L. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161720 · Cited by 2,704 · 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
Self-citationTripathi, V., Ellis, J. D., Shen, Z., Song, D. Y., Pan, Q., Watt, A. T., Freier, S. M., Bennett, C. F., Sharma, A., Bubulya, P. A., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.011 · Cited by 2,223 · see citing works
Clemson, C. M., Hutchinson, J. N., Sara, S. A., Ensminger, A. W., Fox, A. H., Chess, A., & Lawrence, J. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.026 · Cited by 1,445 · see citing works
From charcot to lou gehrig: deciphering selective motor neuron death in als
Cleveland, D. W., & Rothstein, J. D. (2001) · Nature reviews. Neuroscience · doi:10.1038/35097565 · Cited by 1,389 · see citing works
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
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., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335 · see citing works
Bim: a novel member of the Bcl‐2 family that promotes apoptosis
O’Connor, L., Strasser, A., O’Reilly, L. A., Hausmann, G., Adams, J. M., Cory, S., & Huang, D. C. S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.384 · Cited by 1,163 · see citing works
iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution
König, J., Zarnack, K., Rot, G., Curk, T., Kayikci, M., Zupan, B., Turner, D. J., Luscombe, N. M., & Ule, J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1838 · Cited by 1,126 · see citing works
Self-citationCLIP 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
Self-citationTDP-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
Buratti, E., & Baralle, F. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104236200 · Cited by 697 · see citing works
RNA recognition motifs: boring? Not quite
Cléry, A., Blatter, M., & Allain, F. H. ‐. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.04.002 · Cited by 637 · 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
Self-citationSimple sequence repeats as advantageous mutators in evolution
Kashi, Y., & King, D. G. (2006) · Trends in Genetics · doi:10.1016/j.tig.2006.03.005 · Cited by 588 · see citing works
Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
Buratti, E. (2007) · Frontiers in bioscience · doi:10.2741/2727 · Cited by 493 · 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
Johnson, B. S., McCaffery, J. M., Lindquist, S. L., & Gitler, A. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802082105 · Cited by 412 · see citing works
Abundant Raw Material for Cis-Regulatory Evolution in Humans
Rockman, M. V., & Wray, G. A. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004023 · Cited by 377 · see citing works
Ishiyama, N., Lee, S.-H., Liu, S., Li, G., Smith, M. J., Reichardt, L. F., & Ikura, M. (2010) · Cell · doi:10.1016/j.cell.2010.01.017 · Cited by 358 · see citing works
Igaz, L. M., Kwong, L. K., Chen‐Plotkin, A. S., Winton, M. J., Unger, T. L., Xu, Y., Neumann, M., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809462200 · Cited by 357 · 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
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
Kuo, P. H., Doudeva, L. G., Wang, Y.-T., Shen, C. ‐. J., & Yuan, H. S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp013 · Cited by 331 · see citing works
Regulation of Neuronal Survival Factor MEF2D by Chaperone-Mediated Autophagy
Yang, Q., She, H., Gearing, M., Colla, E., Lee, M. K., Shacka, J. J., & Mao, Z. (2009) · Science · doi:10.1126/science.1166088 · Cited by 304 · see citing works
Understanding splicing regulation through RNA splicing maps
Witten, J. T., & Ule, J. (2011) · Trends in Genetics · doi:10.1016/j.tig.2010.12.001 · Cited by 276 · see citing works
Self-citationTDP‐43, a neuro‐pathosignature factor, is essential for early mouse embryogenesis
Wu, L., Cheng, W., Hou, S., Yan, Y., Jiang, S., & Shen, C. ‐. J. (2010) · genesis · doi:10.1002/dvg.20584 · Cited by 256 · see citing works
iCLIP Predicts the Dual Splicing Effects of TIA-RNA Interactions
Wang, Z., Kayikci, M., Briese, M., Zarnack, K., Luscombe, N. M., Rot, G., Zupan, B., Curk, T., & Ule, J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000530 · Cited by 242 · see citing works
Self-citationNuclear 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
Ayala, Y. M., Misteli, T., & Baralle, F. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800546105 · Cited by 232 · 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
Sequence-based estimation of minisatellite and microsatellite repeat variabilityPreprint
Legendre, M., Pochet, N. L. M. M., Pak, T. R., & Verstrepen, K. J. (2007) · Genome Research · doi:10.1101/gr.6554007 · Cited by 204 · see citing works
TDP-43-Mediated Neuron Loss In Vivo Requires RNA-Binding Activity
Voigt, A., Herholz, D., Fiesel, F. C., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012247 · Cited by 195 · see citing works
Diverse roles of hnRNP L in mammalian mRNA processing: A combined microarray and RNAi analysis
Hung, L.-H., Heiner, M., Hui, J., Schreiner, S., Beneš, V., & Bindereif, A. (2007) · RNA · doi:10.1261/rna.725208 · Cited by 159 · see citing works
Identification of casein kinase-1 phosphorylation sites on TDP-43
Kametani, F., Nonaka, T., Suzuki, T., Arai, T., Dohmae, N., Akiyama, H., & Hasegawa, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.038 · Cited by 121 · see citing works
δ-Catenin Is Required for the Maintenance of Neural Structure and Function in Mature Cortex In Vivo
Matter, C., Pribadi, M., Liu, X., & Trachtenberg, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.09.026 · Cited by 89 · see citing works
Selective involvement of BH3-only Bcl-2 family members Bim and Bad in neonatal hypoxia–ischemia
Ness, J., Harvey, C. R., Strasser, A., Bouillet, P., Klocke, B. J., & Roth, K. A. (2006) · Brain Research · doi:10.1016/j.brainres.2006.04.132 · Cited by 64 · see citing works
p120 Catenin Recruits Cadherins to γ-Secretase and Inhibits Production of Aβ Peptide
Kouchi, Z., Barthet, G., Şerban, G., Georgakopoulos, A., Shioi, J., & Robakis, N. K. R. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806250200 · Cited by 30 · see citing works
Becker, E. B. E., & Bonni, A. (2007) · Cell Cycle · doi:10.4161/cc.6.11.4316 · Cited by 24 · see citing works
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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
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
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., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335 · 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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Ferraiuolo, L., Kirby, J., Grierson, A. J., Sendtner, M., & Shaw, P. J. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.152 · Cited by 615 · 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
Raj, B., & Blencowe, B. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.05.004 · Cited by 475 · 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
ALS 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
Understanding 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
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
Self-citationThe 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
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
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
Self-citationMoore, 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
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
Self-citationAnalysis of alternative splicing associated with aging and neurodegeneration in the human brain
Tollervey, J. R., Wang, Z., Hortobágyi, T., Witten, J. T., Zarnack, K., Kayikci, M., Clark, T. A., Schweitzer, A. C., Rot, G., Curk, T., et al. (2011) · Genome Research · doi:10.1101/gr.122226.111 · Cited by 252 · see citing works
Self-citationNoncoding <scp>RNA</scp>s in disease
Lekka, E., & Hall, J. (2018) · FEBS Letters · doi:10.1002/1873-3468.13182 · Cited by 251 · see citing works
Analysis of CLIP and iCLIP methods for nucleotide-resolution studies of protein-RNA interactions
Sugimoto, Y., König, J., Hussain, S., Zupan, B., Curk, T., Frye, M., & Ule, J. (2012) · Genome Biology · doi:10.1186/gb-2012-13-8-r67 · Cited by 234 · see citing works
Self-citationLoss 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
“RNA binding protein CLIP analysis—Published TDP-43 iCLIP data from SH-SY5Y cells (Tollervey et al., 2011) was used to analyze TDP-43 binding sites.”
BackgroundMethodInce-Dunn, G., Okano, H. J., Jensen, K. B., Park, W.-Y., Zhong, R., Ule, J., Mele, A., Fak, J. J., Yang, C., Zhang, C., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.07.009 · Cited by 212 · see citing works
Self-citationFunctional roles and networks of non-coding RNAs in the pathogenesis of neurodegenerative diseases
Wu, Y.-Y., & Kuo, H.-C. (2020) · Journal of Biomedical Science · doi:10.1186/s12929-020-00636-z · Cited by 213 · see citing works
Licatalosi, D. D., Yano, M., Fak, J. J., Mele, A., Grabinski, S. E., Zhang, C., & Darnell, R. B. (2012) · Genes & Development · doi:10.1101/gad.191338.112 · Cited by 193 · see citing works
Transposable Elements in TDP-43-Mediated Neurodegenerative Disorders
Li, W., Jin, Y., Prazak, L., Hammell, M., & Dubnau, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044099 · Cited by 195 · see citing works
Misregulated RNA processing in amyotrophic lateral sclerosis
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Bennett, C. F., Cleveland, D. W., & Yeo, G. W. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.059 · Cited by 169 · see citing works
RNA Protein Interaction in Neurons
Darnell, R. B. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062912-114322 · Cited by 181 · see citing works
Alternative splicing: decoding an expansive regulatory layer
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Regulation of Autophagy by Neuropathological Protein TDP-43
Bose, J. K., Huang, C.-C., & Shen, C.-K. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237115 · Cited by 165 · see citing works
Review: neuropathology of non-tau frontotemporal lobar degeneration
Neumann, M., & Mackenzie, I. R. A. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12526 · Cited by 144 · see citing works
Troakes, C., Maekawa, S., Wijesekera, L., Rogelj, B., Siklós, L., Bell, C., Smith, B., Newhouse, S., Vance, C., Johnson, L., et al. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2011.01286.x · Cited by 124 · see citing works
Self-citationMcMillan, M., Gomez, N., Hsieh, C., Bekier, M., Li, X., Miguez, R., Tank, E. M. H., & Barmada, S. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2022.12.019 · Cited by 112 · see citing works
Wei, Y.-N., Hu, H.-Y., Xie, G.-C., Fu, N., Ning, Z.-B., Zeng, R., & Khaitovich, P. (2015) · Genome Biology · doi:10.1186/s13059-015-0608-2 · Cited by 117 · see citing works
RNA-binding proteins in neurodegeneration: Seq and you shall receive
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Mutation of a U2 snRNA Gene Causes Global Disruption of Alternative Splicing and Neurodegeneration
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Pun, F. W., Liu, B. H. M., Long, X., Leung, H. W., Leung, G. H. D., Mewborne, Q. T., Gao, J., Shneyderman, A., Ozerov, I. V., Wang, J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.914017 · Cited by 115 · see citing works
De Santis, R., Santini, L., Colantoni, A., Peruzzi, G., de Turris, V., Alfano, V., Bozzoni, I., & Rosa, A. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.09.004 · Cited by 91 · see citing works
Garcia Morato, J., Hans, F., von Zweydorf, F., Feederle, R., Elsässer, S. J., Skodras, A. A., Gloeckner, C. J., Buratti, E., Neumann, M., & Kahle, P. J. (2022) · Nature Communications · doi:10.1038/s41467-022-28822-7 · Cited by 94 · see citing works
Sephton, C. F., Cenik, B., Cenik, B. K., Herz, J., & Yu, G. (2012) · bchm · doi:10.1515/hsz-2012-0115 · Cited by 86 · see citing works
Guerrero, E. N., Mitra, J., Wang, H., Rangaswamy, S., Hegde, P. M., Basu, P., Rao, K. S., & Hegde, M. L. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz062 · Cited by 68 · see citing works
del Campo, M., Zetterberg, H., Gandy, S., Onyike, C. U., Oliveira, F., Udeh‐Momoh, C., Lleó, A., Teunissen, C. E., & Pijnenburg, Y. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12643 · Cited by 52 · see citing works
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Yang, H.-S., White, C. C., Klein, H.-U., Yu, L., Gaiteri, C., Ma, Y., Felsky, D., Mostafavi, S., Petyuk, V. A., Sperling, R. A., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.05.010 · Cited by 47 · see citing works
Bajc Česnik, A., Motaln, H., & Rogelj, B. (2020) · Cells · doi:10.3390/cells9081791 · Cited by 17 · see citing works
Self-citationHe, J., Zhou, T., Hu, L.-F., Jiao, Y., Wang, J., Yan, S., Jia, S., Chen, Q., Zhu, W., Zhang, J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72351-6
- Authors
- Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., Patani, R., Chandran, S., Rot, G., Zupan, B., Shaw, C. E., & Ule, J.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Ljubljana (SI)
- King's College London (GB)
- University of Cambridge (GB)
- Corresponding author
- Ule, Jernej
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2011-02-27
- Volume
- 14
- Issue
- 4
- Pages
- 452-458
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC3108889
- OpenAlex
- W2136949432
- Cited by
- 1,165
- References
- 38
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- FWCI
- 34.71
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
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- HAL (submittedVersion, other-oa)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Portal (King's College London) (submittedVersion)
- Queen Mary Research Online (Queen Mary University of London) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Funders
- Wellcome Trust (089701, 089701/Z/09/Z)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- TDP-43, alternative splicing, RNA-binding proteins, pre-mRNA, MALAT1, NEAT1, amyotrophic lateral sclerosis, frontotemporal lobar degeneration, iCLIP, neuronal development, RNA processing
- MeSH terms
- Brain Chemistry, Cell Line, DNA-Binding Proteins, Gene Expression Regulation, Humans, RNA Splicing, RNA, Messenger, RNA-Binding Proteins, Alternative Splicing, Protein Isoforms, RNA, Untranslated, Cell Line, Tumor
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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