TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

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

hnRNP PROTEINS AND THE BIOGENESIS OF mRNA

Dreyfuss, G., Matunis, M. J., Piñol-Roma, S., & Burd, C. G. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.001445 · Cited by 1,558 · see citing works

TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease

Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916 · see citing works

Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs

Ou, S.-H. I., Wu, F. K., Harrich, D., Garcı́a-Martı́nez, L. F., & Gaynor, R. B. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3584-3596.1995 · Cited by 762 · see citing works

TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration

Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M., & Baloh, R. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908767106 · Cited by 706 · 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

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Zhang, Y., Xu, Y.-F., Cook, C. N., Gendron, T. F., Roettges, P. S., Link, C. D., Lin, W.-L., Tong, J., Castanedes‐Casey, M., Ash, P. E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900688106 · Cited by 604 · see citing works

Rethinking ALS: The FUS about TDP-43

Lagier‐Tourenne, C., & Cleveland, D. W. (2009) · Cell · doi:10.1016/j.cell.2009.03.006 · Cited by 590 · 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

Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases

Nakashima-Yasuda, H., Uryu, K., Robinson, J., Xie, S. X., Hurtig, H., Duda, J. E., Arnold, S. E., Siderowf, A., Grossman, M., Leverenz, J. B., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0261-2 · Cited by 468 · see citing works

TDP-43 Binds Heterogeneous Nuclear Ribonucleoprotein A/B through Its C-terminal Tail

Buratti, E., Brindisi, A., Giombi, M., Tisminetzky, S. G., Ayala, Y. M., & Baralle, F. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505557200 · Cited by 455 · see citing works

Glial specification in the vertebrate neural tube

Rowitch, D. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1389 · Cited by 432 · see citing works

Human, Drosophila, and C.elegans TDP43: Nucleic Acid Binding Properties and Splicing Regulatory Function

Ayala, Y. M., Pantano, S., D’Ambrogio, A., Buratti, E., Brindisi, A., Marchetti, C., Romano, M., & Baralle, F. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.038 · Cited by 372 · see citing works

Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies

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

Specification of dorsal spinal cord interneurons

Helms, A. W., & Johnson, J. E. B. (2003) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(03)00010-2 · 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 diversity and functional implications of the eukaryotic TDP gene family

Wang, H., Wang, I., Bose, J. K., & Shen, C. ‐. J. (2003) · Genomics · doi:10.1016/s0888-7543(03)00214-3 · Cited by 306 · see citing works

Depletion of TDP‐43 affects Drosophila motoneurons terminal synapsis and locomotive behavior

Feiguin, F. M., Godena, V. K., Romano, G., D’Ambrogio, A., Klima, R., & Baralle, F. E. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.04.019 · Cited by 303 · see citing works

Cocaine Regulates MEF2 to Control Synaptic and Behavioral Plasticity

Pulipparacharuvil, S., Renthal, W., Hale, C. F., Taniguchi, M., Xiao, G., Kumar, A., Russo, S. J., Sikder, D., Dewey, C. M., Davis, M. M., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.020 · Cited by 281 · see citing works

TDP‐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

ARE‐mRNA degradation requires the 5′–3′ decay pathway

Stoecklin, G., Mayo, T., & Anderson, P. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400572 · Cited by 237 · see citing works

TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression

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

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene

Mercado, P. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki897 · Cited by 226 · see citing works

TDP-43 Overexpression Enhances Exon 7 Inclusion during the Survival of Motor Neuron Pre-mRNA Splicing

Bose, J. K., Wang, I., Li, H., Tarn, W., & Shen, C. ‐. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805376200 · Cited by 172 · see citing works

TDP-43: a novel neurodegenerative proteinopathy

Forman, M. S., Trojanowski, J. Q., & Lee, V. M. ‐. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.08.005 · Cited by 127 · see citing works

TDP-43 Depletion Induces Neuronal Cell Damage through Dysregulation of Rho Family GTPases

Iguchi, Y., Katsuno, M., Niwa, J.-I., Yamada, S.-I., Sone, J., Waza, M., Adachi, H., Tanaka, F., Nagata, K., Arimura, N., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.012195 · Cited by 101 · see citing works

Chapter 1 The Molecular Links Between TDP‐43 Dysfunction and Neurodegeneration

Buratti, E., & Baralle, F. E. (2009) · Advances in genetics · doi:10.1016/s0065-2660(09)66001-6 · Cited by 96 · see citing works

TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons

Casafont, Í., Bengoechea, R., Tapia, O., Berciano, M. T., & Lafarga, M. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2009.06.006 · Cited by 81 · see citing works

Specificity of Ca2+-Dependent Protein Interactions Mediated by the C2A Domains of Synaptotagmins

Sugita, S., & Südhof, T. C. (2000) · Biochemistry · doi:10.1021/bi9920984 · Cited by 59 · see citing works

Synaptic expression of the high-affinity kainate receptor subunit KA2 in hippocampal cultures

Roche, K. W., & Huganir, R. L. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00253-f · Cited by 53 · see citing works

Converging 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

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

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 977 · 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

ALS Genetics, Mechanisms, and Therapeutics: Where Are We Now?

Mejzini, R., Flynn, L. L., Pitout, I. L., Fletcher, S., Wilton, S. D., & Akkari, P. A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01310 · Cited by 755 · 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

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

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

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

Protein aggregation in amyotrophic lateral sclerosis

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

Animal models of neurodegenerative diseases

Dawson, T. M., Golde, T. E., & Lagier-Tourenne, C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0236-8 · Cited by 576 · see citing works

Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains

Nonaka, T., Masuda‐Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., Yoshida, M., Murayama, S., Mann, D. M. A., Akiyama, H., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.007 · Cited by 520 · see citing works

ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

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

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

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

Dysregulation 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

Physiological 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

TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor

Dewey, C. M., Cenik, B., Sephton, C. F., Dries, D. R., Mayer, P. R., Rich, S. K., Johnson, B. A., Herz, J., & Yu, G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01279-10 · Cited by 366 · 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 334 · 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

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

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Kraemer, B. C., Schuck, T., Wheeler, J. M., Robinson, L. C., Trojanowski, J. Q., Lee, V. M. Y., & Schellenberg, G. D. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0659-0 · Cited by 350 · see citing works

Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor κB–mediated pathogenic pathways

Swarup, V., Phaneuf, D., Dupré, N., Petri, S., Strong, M. J., Križ, J., & Julien, J. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20111313 · Cited by 338 · see citing works

Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43

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

Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice

Shan, X., Chiang, P., Price, D. L., & Wong, P. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003459107 · Cited by 312 · see citing works

Deletion of TDP-43 down-regulates Tbc1d1 , a gene linked to obesity, and alters body fat metabolism

Chiang, P., Ling, J. P., Jeong, Y. H., Price, D. L., Aja, S. M., & Wong, P. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002176107 · Cited by 303 · see citing works

A cellular model for sporadic ALS using patient-derived induced pluripotent stem cells

Burkhardt, M. F., Martinez, F. J., Wright, S., Ramos, C., Volfson, D., Mason, M. J., Garnes, J., Dang, V., Lievers, J., Shoukat-Mumtaz, U., et al. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.07.007 · Cited by 300 · see citing works

The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation

Buratti, E., & Baralle, F. E. (2010) · RNA Biology · doi:10.4161/rna.7.4.12205 · Cited by 284 · 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

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

Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease

March, Z. M., King, O. D., & Shorter, J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.037 · Cited by 215 · see citing works

Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA*

Kim, S. H., Shanware, N. P., Bowler, M. J., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154831 · Cited by 213 · see citing works

TDP-43 and FUS: a nuclear affair

Dormann, D., & Haass, C. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.05.002 · Cited by 214 · see citing works

TDP-43 aggregation in neurodegeneration: Are stress granules the key?

Dewey, C. M., Cenik, B., Sephton, C. F., Johnson, B. A., Herz, J., & Yu, G. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.032 · Cited by 211 · see citing works

Progressive motor weakness in transgenic mice expressing human TDP-43

Stallings, N. R., Puttaparthi, K., Luther, C. M., Burns, D. K., & Elliott, J. L. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.06.017 · Cited by 209 · see citing works

The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?

Hergesheimer, R. C., Chami, A. A., de Assis, D. R., Vourc’h, P., Andres, C. R., Corcia, P., Lanznaster, D., & Blasco, H. (2019) · Brain · doi:10.1093/brain/awz078 · Cited by 198 · see citing works

Expression of ALS‐linked TDP‐43 mutant in astrocytes causes non‐cell‐autonomous motor neuron death in rats

Tong, J., Huang, C., Bi, F., Wu, Q., Huang, B., Liu, X., Li, F., Zhou, H., & Xia, X. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.122 · Cited by 196 · see citing works

Loss of TDP-43 causes age-dependent progressive motor neuron degeneration

Iguchi, Y., Katsuno, M., Niwa, J.-I., Takagi, S., Ishigaki, S., Ikenaka, K., Kawai, K., Watanabe, H., Yamanaka, K., Takahashi, R., et al. (2013) · Brain · doi:10.1093/brain/awt029 · Cited by 195 · see citing works

The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD

Berning, B. A., & Walker, A. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00335 · Cited by 183 · see citing works

Autophagy and ALS: mechanistic insights and therapeutic implications

Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works

The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

Yang, C., Tan, W., Whittle, C., Qiu, L., Cao, L.-C., Akbarian, S., & Xu, Z. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015878 · Cited by 187 · 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

Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis

Yang, C., Wang, H., Qiao, T., Yang, B., Aliaga, L., Qiu, L., Tan, W., Salameh, J. S., McKenna-Yasek, D. M., Smith, T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322641111 · Cited by 185 · see citing works

Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains

Kametani, F., Obi, T., Shishido, T., Akatsu, H., Murayama, S., Saito, Y., Yoshida, M., & Hasegawa, M. (2016) · Scientific Reports · doi:10.1038/srep23281 · Cited by 172 · see citing works

Mice with endogenous TDP‐43 mutations exhibit gain of splicing function and characteristics of amyotrophic lateral sclerosis

Fratta, P., Sivakumar, P., Humphrey, J., Lo, K., Ricketts, T., Oliveira, H. M. D., Armas, J. M. B., Kalmár, B., Ule, A. M., Yu, Y., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798684 · Cited by 171 · see citing works

Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization

Pinarbasi, E. S., Çağatay, T., Fung, H. Y. J., Li, Y. C., Chook, Y. M., & Thomas, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-25008-4 · Cited by 168 · see citing works

Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth

Schmid, B., Hruscha, A., Hogl, S., Banzhaf‐Strathmann, J., Strecker, K., van der Zee, J., Teucke, M., Eimer, S., Hegermann, J., Kittelmann, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218311110 · Cited by 170 · see citing works

TDP ‐43 and FUS en route from the nucleus to the cytoplasm

Ederle, H., & Dormann, D. (2017) · FEBS Letters · doi:10.1002/1873-3468.12646 · Cited by 169 · see citing works

RNA targets of TDP-43 identified by UV-CLIP are deregulated in ALS

Xiao, S., Sanelli, T. R., Dib, S., Sheps, D., Findlater, J., Bilbao, J. M., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.02.013 · Cited by 163 · see citing works

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

Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43

Fuentealba, R. A., Udan-Johns, M., Bell, S., Wegorzewska, I., Shao, J., Diamond, M. I., Weihl, C. C., & Baloh, R. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125039 · Cited by 154 · see citing works

Rodent models of amyotrophic lateral sclerosis

McGoldrick, P., Joyce, P. I., Fisher, E., & Greensmith, L. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.012 · Cited by 156 · 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

Molecular pathology and genetic advances in amyotrophic lateral sclerosis: an emerging molecular pathway and the significance of glial pathology

Ince, P. G., Highley, J. R., Kirby, J., Wharton, S. B., Takahashi, H., Strong, M. J., & Shaw, P. J. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0913-0 · Cited by 154 · see citing works

Roles for RNA-binding proteins in development and disease

Brinegar, A. E., & Cooper, T. A. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.050 · Cited by 151 · see citing works

Abnormal RNA stability in amyotrophic lateral sclerosis

Tank, E., Figueroa‐Romero, C., Hinder, L. M., Bedi, K., Archbold, H. C., Li, X., Weskamp, K., Safren, N., Paez-Colasante, X., Pacut, C. M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05049-z · Cited by 144 · see citing works

Activity-dependent FUS dysregulation disrupts synaptic homeostasis

Sephton, C. F., Tang, A. A., Kulkarni, A., West, J. D., Brooks, M., Stubblefield, J. J., Liu, Y., Zhang, M. Q., Green, C. B., Huber, K. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406162111 · Cited by 145 · see citing works

Downregulation of MicroRNA-9 in iPSC-Derived Neurons of FTD/ALS Patients with TDP-43 Mutations

Zhang, Z., Almeida, S., Lu, Y., Nishimura, A. L., Peng, L., Sun, D., Wu, B., Karydas, A. M., Tartaglia, M. C., Fong, J. C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076055 · Cited by 142 · see citing works

TDP-43/FUS in motor neuron disease: Complexity and challenges

Guerrero, E. N., Wang, H., Mitra, J., Hegde, P. M., Stowell, S. E., Liachko, N. F., Kraemer, B. C., Garruto, R. M., Rao, K. S. J., & Hegde, M. L. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.09.004 · Cited by 144 · see citing works

Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders

Janssens, J., & Broeckhoven, C. V. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt349 · Cited by 140 · see citing works

Mitochondrial Dysfunction and Decrease in Body Weight of a Transgenic Knock-in Mouse Model for TDP-43

Stribl, C., Samara, A., Trümbach, D., Peis, R., Neumann, M., Fuchs, H., Gailus‐Durner, V., de Angelis, M. H., Rathkolb, B., Wolf, E., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515940 · Cited by 137 · see citing works

Cross-Regulation between TDP-43 and Paraspeckles Promotes Pluripotency-Differentiation Transition

Modic, M., Grosch, M., Rot, G., Schirge, S., Lepko, T., Yamazaki, T., Lee, F. C. Y., Rusha, E., Shaposhnikov, D., Palo, M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.041 · Cited by 135 · see citing works

Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1

Barmada, S. J., Ju, S., Arjun, A., Batarse, A., Archbold, H. C., Peisach, D., Li, X., Zhang, Y., Tank, E. M. H., Qiu, H., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509744112 · Cited by 125 · see citing works

RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy

Chen, H.-J., Topp, S. D., Hui, H. S., Zacco, E., Katarya, M., McLoughlin, C., King, A., Smith, B. N., Troakes, C., Pastore, A., et al. (2019) · Brain · doi:10.1093/brain/awz313 · Cited by 133 · see citing works

SOD1 and TDP-43 animal models of amyotrophic lateral sclerosis: recent advances in understanding disease toward the development of clinical treatments

Joyce, P. I., Fratta, P., Fisher, E., & Acevedo‐Arozena, A. (2011) · Mammalian Genome · doi:10.1007/s00335-011-9339-1 · Cited by 130 · see citing works

TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis?

Broeck, L. V., Callaerts, P., & Dermaut, B. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.11.003 · Cited by 130 · see citing works

Shortened TDP43 isoforms upregulated by neuronal hyperactivity drive TDP43 pathology in ALS

Weskamp, K., Tank, E. M. H., Miguez, R., McBride, J. P., Gómez, N., White, M. A., Lin, Z., Moreno-Gonzalez, C., Serio, A., Sreedharan, J., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci130988 · Cited by 127 · see citing works

Rodent models of TDP-43: Recent advances

Tsao, W., Jeong, Y. H., Lin, S. Z., Ling, J. P., Price, D. L., Chiang, P., & Wong, P. C. (2012) · Brain Research · doi:10.1016/j.brainres.2012.04.031 · Cited by 126 · see citing works

TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signaling

Zhang, T., Mullane, P., Periz, G., & Wang, J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr076 · Cited by 125 · see citing works

Accelerated Disease Onset with Stabilized Familial Amyotrophic Lateral Sclerosis (ALS)-linked Mutant TDP-43 Proteins

Watanabe, S., Kaneko, K., & Yamanaka, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433615 · Cited by 124 · see citing works

Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2

Guenther, E. L., Ge, P., Trinh, H., Sawaya, M. R., Cascio, D., Boyer, D. R., Gonen, T., Zhou, Z. H., & Eisenberg, D. S. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0045-5 · Cited by 121 · see citing works

The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis

Bampton, A., Gittings, L. M., Fratta, P., Lashley, T., & Gatt, A. P. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02203-0 · Cited by 118 · see citing works

Wild type human TDP-43 potentiates ALS-linked mutant TDP-43 driven progressive motor and cortical neuron degeneration with pathological features of ALS

Mitchell, J. C., Constable, R., So, E., Vance, C. A., Scotter, E. L., Glover, L., Hortobágyi, T., Arnold, E. S., Ling, S., McAlonis‐Downes, M., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0212-4 · Cited by 118 · see citing works

Amyotrophic lateral sclerosis: Current perspectives from basic research to the clinic

Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 116 · see citing works

Tdp-43 cryptic exons are highly variable between cell types

Jeong, Y. H., Ling, J. P., Lin, S. Z., Donde, A., Braunstein, K. E., Majounie, E., Traynor, B. J., LaClair, K. D., Lloyd, T. E., & Wong, P. C. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0144-x · Cited by 113 · see citing works

Progranulin Does Not Bind Tumor Necrosis Factor (TNF) Receptors and Is Not a Direct Regulator of TNF-Dependent Signaling or Bioactivity in Immune or Neuronal Cells

Chen, X., Chang, J., Deng, Q., Xu, J., Nguyen, T. A., Martens, L. H., Cenik, B., Taylor, G., Hudson, K. F., Chung, J., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5336-12.2013 · Cited by 108 · see citing works

Mutant TDP-43 Causes Early-Stage Dose-Dependent Motor Neuron Degeneration in a TARDBP Knockin Mouse Model of ALS

Ebstein, S. Y., Yagudayeva, I., & Shneider, N. A. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.045 · Cited by 106 · see citing works

Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies

Cascella, R., Capitini, C., Fani, G., Dobson, C. M., Cecchi, C., & Chiti, F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737726 · Cited by 105 · see citing works

FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention

Humphrey, J., Birsa, N., Milioto, C., McLaughlin, M., Ule, A. M., Robaldo, D., Eberle, A. B., Kräuchi, R., Bentham, M. P., Brown, A., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa410 · Cited by 103 · see citing works

Splicing repression is a major function of TDP-43 in motor neurons

Donde, A., Sun, M., Ling, J. P., Braunstein, K. E., Pang, B., Wen, X., Cheng, X., Chen, L., & Wong, P. C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02042-8 · Cited by 100 · see citing works

Extensive cryptic splicing upon loss of RBM17 and TDP43 in neurodegeneration models

Tan, Q., Yalamanchili, H. K., Park, J., Maio, A. D., Lu, H., Wan, Y., White, J. J., Bondar, V. V., Sayegh, L. S., Liu, X., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw337 · Cited by 96 · see citing works

TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR

Fiesel, F. C., Weber, S. S., Supper, J., Zell, A., & Kahle, P. J. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1082 · Cited by 99 · see citing works

Controlling the Regional Identity of hPSC-Derived Neurons to Uncover Neuronal Subtype Specificity of Neurological Disease Phenotypes

Imaizumi, K., Sone, T., Ibata, K., Fujimori, K., Yuzaki, M., Akamatsu, W., & Okano, H. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.10.005 · Cited by 99 · see citing works

Mouse models of frontotemporal dementia

Roberson, E. D. (2012) · Annals of Neurology · doi:10.1002/ana.23722 · Cited by 97 · see citing works

Biomarker-based dissection of neurodegenerative diseases

Olsson, B., Zetterberg, H., Hampel, H. J., & Blennow, K. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.04.006 · Cited by 96 · see citing works

Single-copy expression of an amyotrophic lateral sclerosis-linked TDP-43 mutation (M337V) in BAC transgenic mice leads to altered stress granule dynamics and progressive motor dysfunction

Gordon, D., Dafinca, R., Scaber, J., Alegre‐Abarrategui, J., Farrimond, L. E., Scott, C., Biggs, D., Kent, L., Oliver, P. L., Davies, B., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.09.024 · Cited by 96 · see citing works

Phase to Phase with TDP-43

Sun, Y., & Chakrabartty, A. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01088 · Cited by 96 · see citing works

Review: Prion‐like mechanisms of transactive response DNA binding protein of 43 kDa ( TDP ‐43) in amyotrophic lateral sclerosis ( ALS )

Smethurst, P., Sidle, K. C. L., & Hardy, J. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12206 · Cited by 94 · see citing works

TDP-43, an ALS Linked Protein, Regulates Fat Deposition and Glucose Homeostasis

Stallings, N. R., Puttaparthi, K., Dowling, K. J., Luther, C. M., Burns, D. K., Davis, K. E., & Elliott, J. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071793 · Cited by 94 · see citing works

The function of RNA-binding proteins at the synapse: implications for neurodegeneration

Sephton, C. F., & Yu, G. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1943-x · Cited by 91 · see citing works

TDP-43-Based Animal Models of Neurodegeneration: New Insights into ALS Pathology and Pathophysiology

Wegorzewska, I., & Baloh, R. H. (2010) · Neurodegenerative Diseases · doi:10.1159/000321547 · Cited by 93 · see citing works

RNA binding proteins and the pathological cascade in ALS/FTD neurodegeneration

Ito, D., Hatano, M., & Suzuki, N. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aah5436 · Cited by 92 · see citing works

An Intramolecular Salt Bridge Linking TDP43 RNA Binding, Protein Stability, and TDP43-Dependent Neurodegeneration

Flores, B. N., Li, X., Malik, A. M., Martinez, J., Beg, A. A., & Barmada, S. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.093 · Cited by 92 · see citing works

Does a loss of TDP-43 function cause neurodegeneration?

Xu, Z. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-27 · Cited by 91 · see citing works

Alteration of POLDIP3 Splicing Associated with Loss of Function of TDP-43 in Tissues Affected with ALS

Shiga, A., Ishihara, T., Miyashita, A., Kuwabara, M., Kato, T., Watanabe, N., Yamahira, A., Kondo, C., Yokoseki, A., Takahashi, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043120 · Cited by 89 · see citing works

TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration

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

RNA-mediated toxicity in neurodegenerative disease

Belzil, V., Gendron, T. F., & Petrucelli, L. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.12.006 · Cited by 86 · see citing works

The neurobiology of amyotrophic lateral sclerosis

Bento‐Abreu, A., Damme, P. V., Bosch, L. V. D., & Robberecht, W. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07260.x · Cited by 85 · see citing works

C9orf72-FTD/ALS pathogenesis: evidence from human neuropathological studies

Vatsavayai, S. C., Nana, A. L., Yokoyama, J. S., & Seeley, W. W. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1921-0 · Cited by 78 · see citing works

TDP‐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

P3‐006: Neurons during early development are highly vulnerable to TDP‐43 dysregulation

Cannon, A. D., Yang, B., Knight, J. A., Farnham, M., Zhang, Y., Wuertzer, C. A., D’Alton, S., Howard, J. C., Lin, W.-L., Scott, B., et al. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1445

TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration

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

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Kraemer, B. C., Schuck, T., Wheeler, J. M., Robinson, L. C., Trojanowski, J. Q., Lee, V. M. Y., & Schellenberg, G. D. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0659-0 · Cited by 350 · see citing works

ORIGINAL PAPER Neuronal sensitivity to TDP-43 overexpression is dependent on timing of induction

Cannon, A., Yang, B., Knight, J., Farnham, I. M., Zhang, Y., Wuertzer, C. A., Lin, W.-L., Rousseau, L., Scott, B., Jurasic, M., et al. (2016)