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

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

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

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

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

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

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 614

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 596

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

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

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

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 1,012

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 817

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 803

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 697

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

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

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 649

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 607

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

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 547

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 508

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 483

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 448

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 448

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 417

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 390

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 370

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 382

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

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

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

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 346

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 343

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 323

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 313

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 316

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 286

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

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 285

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 223

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 221

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 222

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 223

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 225

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 211

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 194

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 202

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 193

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

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

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

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 188

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 176

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 176

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 180

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 178

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 172

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 175

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

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 161

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 162

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

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

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 153

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 153

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 156

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

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 146

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 148

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 139

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 136

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

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 132

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 139

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 134

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 131

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 129

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 127

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 123

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 125

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 116

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 122

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 125

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 120

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 110

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 102

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 101

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 107

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 109

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 99

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 101

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 101

Mouse models of frontotemporal dementia

Roberson, E. D. (2012) · Annals of Neurology · doi:10.1002/ana.23722 · Cited by 103

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 102

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 94

Phase to Phase with TDP-43

Sun, Y., & Chakrabartty, A. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01088 · Cited by 105

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 99

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 103

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 97

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 97

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 88

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 90

Does a loss of TDP-43 function cause neurodegeneration?

Xu, Z. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-27 · Cited by 95

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 94

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

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 90

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 89

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 82

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

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

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

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)