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Mechanisms of toxicity in C9FTLD/ALS

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The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity

Chang, C., Wu, T.-H., Wu, C.-Y., Chiang, M.-H., Toh, E. K.-W., Hsu, Y.-C., Lin, K.-F., Liao, Y.-H., Huang, T.-H., & Huang, J. J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.071 · Cited by 142

ALS mutant FUS proteins are recruited into stress granules in induced Pluripotent Stem Cells (iPSCs) derived motoneurons

Lenzi, J., Santis, R. D., de Turris, V., Morlando, M., Laneve, P., Calvo, A., Caliendo, V., Chiò, A., Rosa, A., & Bozzoni, I. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.020099 · Cited by 140

Characterization of Alternative Isoforms and Inclusion Body of the TAR DNA-binding Protein-43

Nishimoto, Y., Ito, D., Yagi, T., Nihei, Y., Tsunoda, Y., & Suzuki, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022012 · Cited by 145

Parkin Ubiquitinates Tar-DNA Binding Protein-43 (TDP-43) and Promotes Its Cytosolic Accumulation via Interaction with Histone Deacetylase 6 (HDAC6)

Hebron, M. L., Lonskaya, I., Sharpe, K., Weerasinghe, P. P. K., Algarzae, N. K., Shekoyan, A. R., & Moussa, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419945 · Cited by 147

Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia

Mori, F., Tanji, K., Zhang, H., Nishihira, Y., Tan, C., Takahashi, H., & Wakabayashi, K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0396-9 · Cited by 135

Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy

Arai, T., Hasegawa, M., Nonoka, T., Kametani, F., Yamashita, M., Hosokawa, M., Niizato, K., Tsuchiya, K., Kobayashi, Z., Ikeda, K., et al. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01089.x · Cited by 134

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

Cytoplasmic accumulation and aggregation of TDP-43 upon proteasome inhibition in cultured neurons.

van Eersel, J., Ke, Y. D., Gladbach, A., Bi, M., Götz, J., Kril, J. J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022850 · Cited by 130

An MND/ALS phenotype associated with C9orf72 repeat expansion: Abundant p62‐positive, TDP‐43‐negative inclusions in cerebral cortex, hippocampus and cerebellum but without associated cognitive decline

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

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

TDP‐43 is consistently co‐localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations

Maekawa, S., Leigh, P. N., King, A., Jones, E. R. L., Steele, J. C., Bódi, I., Shaw, C. E., Hortobágyi, T., & Al‐Sarraj, S. (2009) · Neuropathology · doi:10.1111/j.1440-1789.2009.01029.x · Cited by 125

Phenotypic Heterogeneity of Monogenic Frontotemporal Dementia

Benussi, A., Padovani, A., & Borroni, B. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00171 · Cited by 129

Multiplex SILAC Analysis of a Cellular TDP-43 Proteinopathy Model Reveals Protein Inclusions Associated with SUMOylation and Diverse Polyubiquitin Chains

Seyfried, N. T., Gozal, Y. M., Dammer, E. B., Xia, Q., Duong, D. M., Cheng, D., Lah, J. J., Levey, A. I., & Peng, J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800390-mcp200 · Cited by 127

TDP-43: an emerging new player in neurodegenerative diseases

Wang, I., Wu, L., & Shen, C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.09.001 · Cited by 123

Recent advances in the genetics of amyotrophic lateral sclerosis

Valdmanis, P. N., Daoud, H., Dion, P. A., & Rouleau, G. A. (2009) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-009-0030-9 · Cited by 121

Linking hnRNP Function to ALS and FTD Pathology

Purice, M. D., & Taylor, J. P. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00326 · Cited by 128

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 126

Phosphorylated TDP-43 pathology and hippocampal sclerosis in progressive supranuclear palsy

Yokota, O., Davidson, Y. S., Bigio, E. H., Ishizu, H., Terada, S., Arai, T., Hasegawa, M., Akiyama, H., Sikkink, S. K., Pickering-Brown, S. M., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0702-1 · Cited by 121

Non-human primate model of amyotrophic lateral sclerosis with cytoplasmic mislocalization of TDP-43

Uchida, A., Sasaguri, H., Kimura, N., Tajiri, M., Ohkubo, T., Ono, F., Sakaue, F., Kanai, K., Hirai, T., Sano, T., et al. (2012) · Brain · doi:10.1093/brain/awr348 · Cited by 125

Hyperphosphorylation as a Defense Mechanism to Reduce TDP-43 Aggregation

Li, H.-Y., Yeh, P.-A., Chiu, H.-C., Tang, C., & Tu, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023075 · Cited by 121

TDP‐43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Baloh, R. H. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08256.x · Cited by 121

Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell

Duan, W., Li, X., Shi, J., Guo, Y., Li, Z., & Li, C. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.06.018 · Cited by 122

TDP-43 pathology in sporadic ALS occurs in motor neurons lacking the RNA editing enzyme ADAR2

Aizawa, H., Sawada, J., Hideyama, T., Yamashita, T., Katayama, T., Hasebe, N., Kimura, T., Yahara, O., & Kwak, S. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0678-x · Cited by 119

Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP‐43

Urushitani, M., Sato, T., Bamba, H., Hisa, Y., & Tooyama, I. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22243 · Cited by 114

Inflammation Induces TDP-43 Mislocalization and Aggregation

Correia, A. S., Patel, P., Dutta, K., & Julien, J.-P. (2015) · PLOS ONE · doi:10.1371/journal.pone.0140248 · Cited by 114

Cytoplasmic dynein in neurodegeneration

Eschbach, J., & Dupuis, L. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.03.004 · Cited by 117

The clinical and pathological spectrum of TDP-43 associated ALS

Onodera, O., Yokoseki, A., Tan, C., Ishihara, T., Nishiira, Y., Toyoshima, Y., Kakita, A., Nishizawa, M., & Takahashi, H. (2010) · Rinsho Shinkeigaku · doi:10.5692/clinicalneurol.50.940

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

TDP-43 M311V mutation in familial amyotrophic lateral sclerosis

Lemmens, R., Race, V., Hersmus, N., Matthijs, G., Bosch, L. V. D., Damme, P. V., Dubois, B., Boonen, S. E., Goris, A., & Robberecht, W. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2008.157677 · Cited by 57

Correspondence to:

Williams, K. L., Durnall, J. C., Thoeng, A., Warraich, S. T., Nicholson, G. A., Blair, I. P., Neuroscience, N., Australia, S. S., Blair, D. I. P., Laboratory, N., et al. (2009)

TARDBP (TDP‐43) sequence analysis in patients with familial and sporadic ALS: identification of two novel mutations

Bo, R. D., Ghezzi, S., Corti, S. P., Pandolfo, M., Ranieri, M., Santoro, D., Ghione, I., Prelle, A. C., Orsetti, V., Mancuso, M., et al. (2009) · European Journal of Neurology · doi:10.1111/j.1468-1331.2009.02574.x · Cited by 108