TDP ‐ 43 mutation in familial amyotrophic lateral sclerosis

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works

α-Synuclein is phosphorylated in synucleinopathy lesions

Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 1,906 · see citing works

Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with <i>SOD1</i> mutations

Mackenzie, I. R. A., Bigio, E. H., Ince, P. G., Geser, F., Neumann, M., Cairns, N. J., Kwong, L. K., Forman, M. S., Ravits, J., Stewart, H., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21147 · Cited by 992 · 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 454 · see citing works

Progranulin Mediates Caspase-Dependent Cleavage of TAR DNA Binding Protein-43

Zhang, Y., Xu, Y.-F., Dickey, C. A., Buratti, E., Baralle, F. E., Bailey, R. M., Pickering-Brown, S. M., Dickson, D. W., & Petrucelli, L. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3421-07.2007 · Cited by 371 · see citing works

UBIQUITIN-IMMUNOREACTIVE INTRANEURONAL INCLUSIONS IN AMYOTROPHIC LATERAL SCLEROSIS

Leigh, P. N., Whitwell, H., Garofalo, O., Buller, J., Swash, M., Martin, J., Gallo, J., Weller, R. O., & Anderton, B. H. (1991) · Brain · doi:10.1093/brain/114.2.775 · Cited by 331 · see citing works

TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation

Tan, C., Eguchi, H., Tagawa, A., Onodera, O., Iwasaki, T., Tsujino, A., Nishizawa, M., Kakita, A., & Takahashi, H. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0206-9 · Cited by 298 · see citing works

TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease

Kwong, L. K., Neumann, M., Sampathu, D. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0226-5 · Cited by 231 · see citing works

Neuropathology with Clinical Correlations of Sporadic Amyotrophic Lateral Sclerosis: 102 Autopsy Cases Examined Between 1962 and 2000

Piao, Y., Wakabayashi, K., Kakita, A., Yamada, M., Hayashi, S., Morita, T., Ikuta, F., Oyanagi, K., & Takahashi, H. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00002.x · Cited by 210 · see citing works

Higher order arrangement of the eukaryotic nuclear bodies

Wang, I., Reddy, N. M., & Shen, C.-K. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212483099 · Cited by 190 · see citing works

Neuronal inclusion protein TDP-43 has no primary genetic role in FTD and ALS

Gijselinck, I., Sleegers, K., Engelborghs, S., Robberecht, W., Martin, J., Vandenberghe, R. R., Sciot, R., Dermaut, B., Goossens, D., van der Zee, J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.11.002 · Cited by 85 · see citing works

Familial amyotrophic lateral sclerosis: a SOD1-unrelated Japanese family of bulbar type with Bunina bodies and ubiquitin-positive skein-like inclusions in lower motor neurons

Tagawa, A., Tan, C., Kikugawa, K., Fukase, M., Nakano, R., Onodera, O., Nishizawa, M., & Takahashi, H. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0151-z · Cited by 14 · 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

Amyotrophic lateral sclerosis

Wijesekera, L. C., & Leigh, P. N. (2009) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-4-3 · Cited by 1,051 · 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

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., & Gitler, A. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010264 · Cited by 789 · 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 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

Animal models of Alzheimer's disease and frontotemporal dementia

Götz, J., & Ittner, L. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2420 · Cited by 676 · see citing works

Structural determinants of the cellular localization and shuttling of TDP-43

Ayala, Y. M., Zago, P., D’Ambrogio, A., Xu, Y.-F., Petrucelli, L., Buratti, E., & Baralle, F. E. (2008) · Journal of Cell Science · doi:10.1242/jcs.038950 · Cited by 633 · see citing works

Clinical, genetic and pathological heterogeneity of frontotemporal dementia: A review

Seelaar, H., Rohrer, J. D., Pijnenburg, Y. A. L., Fox, N. C., & van Swieten, J. C. (2011) · Journal of Neurology, Neurosurgery &amp; Psychiatry · doi:10.1136/jnnp.2010.212225 · Cited by 609 · 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

Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

Neumann, M., Kwong, L. K., Lee, E. B., Kremmer, E., Flatley, A., Xu, Y., Forman, M. S., Troost, D., Kretzschmar, H. A., Trojanowski, J. Q., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0477-9 · Cited by 604 · see citing works

Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis

Barmada, S. J., Skibinski, G., Korb, E., Rao, E. J., Wu, J. Y., & Finkbeiner, S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4988-09.2010 · Cited by 554 · see citing works

Wild-Type Human TDP-43 Expression Causes TDP-43 Phosphorylation, Mitochondrial Aggregation, Motor Deficits, and Early Mortality in Transgenic Mice

Xu, Y.-F., Gendron, T. F., Zhang, Y., Lin, W.-L., D’Alton, S., Sheng, H., Casey, M. C., Tong, J., Knight, J. A., Yu, X., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1630-10.2010 · Cited by 555 · see citing works

TAR DNA-binding protein 43 in neurodegenerative disease

Chen‐Plotkin, A. S., Lee, V. M. ‐., & Trojanowski, J. Q. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.18 · Cited by 469 · see citing works

Risk factors for amyotrophic lateral sclerosis

Fang, F., Ingre, C., Roos, P. M., Kamel, F., & Piehl, F. (2015) · Clinical Epidemiology · doi:10.2147/clep.s37505 · Cited by 470 · see citing works

Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo

Kabashi, E., Lin, L., Tradewell, M. L., Dion, P. A., Bercier, V., Bourgouin, P., Rochefort, D. L., Hadj, S. B., Durham, H. D., Velde, C. V., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp534 · Cited by 416 · see citing works

Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death

Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414 · see citing works

The genetics and neuropathology of amyotrophic lateral sclerosis

Al‐Chalabi, A., Jones, A., Troakes, C., King, A., Al‐Sarraj, S., & van den Berg, L. H. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1022-4 · Cited by 396 · see citing works

The Seeds of Neurodegeneration: Prion-like Spreading in ALS

Polymenidou, M., & Cleveland, D. W. (2011) · Cell · doi:10.1016/j.cell.2011.10.011 · Cited by 370 · see citing works

TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets

Scotter, E. L., Chen, H.-J., & Shaw, C. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0338-x · Cited by 356 · see citing works

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

Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specific vulnerability

Bilican, B., Serio, A., Barmada, S. J., Nishimura, A. L., Sullivan, G. J., Carrasco, M., Phatnani, H. P., Puddifoot, C. A., Story, D., Fletcher, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202922109 · Cited by 328 · see citing works

Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis

Pesiridis, G. S., Lee, V. M.-Y., & Trojanowski, J. Q. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp303 · Cited by 324 · see citing works

Phosphorylated TDP-43 in Alzheimer’s disease and dementia with Lewy bodies

Arai, T., Mackenzie, I. R. A., Hasegawa, M., Nonoka, T., Niizato, K., Tsuchiya, K., Iritani, S., Onaya, M., & Akiyama, H. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0480-1 · Cited by 345 · see citing works

Amyotrophic Lateral Sclerosis: An Update for 2018

Oskarsson, B., Gendron, T. F., & Staff, N. P. (2018) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2018.04.007 · Cited by 315 · see citing works

Use of Caenorhabditis elegans as a model to study Alzheimer’s disease and other neurodegenerative diseases

Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310 · see citing works

SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype–phenotype correlations

Millecamps, S., Salachas, F., Cazeneuve, C., Gordon, P., Bricka, B., Camuzat, A., Guillot‐Noël, L., Russaouen, O., Bruneteau, G., Pradat, P., et al. (2010) · Journal of Medical Genetics · doi:10.1136/jmg.2010.077180 · Cited by 310 · see citing works

TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia

Weihl, C. C., Temız, P., Miller, S. E., Watts, G., Smith, C., Forman, M. S., Hanson, P. I., Kimonis, V. E., & Pestronk, A. (2008) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2007.131334 · Cited by 306 · see citing works

TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration

Benajiba, L., Ber, I. L., Camuzat, A., Lacoste, M., Thomas-Antérion, C., Couratier, P., Legallic, S., Salachas, F., Hannequin, D., Décousus, M., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21612 · Cited by 302 · see citing works

Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43

Nonaka, T., Kametani, F., Arai, T., Akiyama, H., & Hasegawa, M. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp275 · Cited by 295 · see citing works

Neuropathology of amyotrophic lateral sclerosis and its variants

Saberi, S., Stauffer, J. E., Schulte, D. J., & Ravits, J. (2015) · Neurologic Clinics · doi:10.1016/j.ncl.2015.07.012 · Cited by 282 · see citing works

The RNA-binding Protein Fused in Sarcoma (FUS) Functions Downstream of Poly(ADP-ribose) Polymerase (PARP) in Response to DNA Damage

Mastrocola, A. S., Kim, S. H., Trinh, A. T., Rodenkirch, L. A., & Tibbetts, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497974 · Cited by 262 · see citing works

ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules

Vance, C. A., Scotter, E. L., Nishimura, A. L., Troakes, C., Mitchell, J. C., Kathe, C., Urwin, H., Manser, C., Miller, C. C. J., Hortobágyi, T., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt117 · Cited by 266 · 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

Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments

Swarup, V., Phaneuf, D., Bareil, C., Robertson, J., Rouleau, G. A., Križ, J., & Julien, J. (2011) · Brain · doi:10.1093/brain/awr159 · Cited by 264 · see citing works

TDP-43 Mediates Degeneration in a Novel Drosophila Model of Disease Caused by Mutations in VCP/p97

Ritson, G. P., Custer, S. K., Freibaum, B. D., Guinto, J. B., Geffel, D., Moore, J., Tang, W., Winton, M. J., Neumann, M., Trojanowski, J. Q., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5894-09.2010 · Cited by 256 · see citing works

Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models

Armakola, M., Higgins, M., Figley, M. D., Barmada, S. J., Scarborough, E. A., Diaz, Z., Fang, X., Shorter, J., Krogan, N. J., Finkbeiner, S. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2434 · Cited by 250 · see citing works

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo

D’Ambrogio, A., Buratti, E., Stuani, C., Guarnaccia, C., Romano, M., Ayala, Y. M., & Baralle, F. E. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp342 · Cited by 225 · see citing works

Functional Significance of TDP-43 Mutations in Disease

Buratti, E. (2015) · Advances in genetics · doi:10.1016/bs.adgen.2015.07.001 · Cited by 225 · see citing works

Genetic mutations in RNA-binding proteins and their roles in ALS

Kapeli, K., Martinez, F. J., & Yeo, G. W.-M. (2017) · Human Genetics · doi:10.1007/s00439-017-1830-7 · Cited by 221 · see citing works

Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1: Regulation of TDP-43 aggregation by phosphorylation and p62

Brady, O. A., Meng, P., Zheng, Y., Mao, Y., & Hu, F. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07098.x · Cited by 215 · see citing works

Dysregulated molecular pathways in amyotrophic lateral sclerosis–frontotemporal dementia spectrum disorder

Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works

Abnormal phosphorylation of Ser409/410 of TDP‐43 in FTLD‐U and ALS

Inukai, Y., Nonaka, T., Arai, T., Yoshida, M., Hashizume, Y., Beach, T. G., Buratti, E., Baralle, F. E., Akiyama, H., Hisanaga, S., et al. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.07.027 · Cited by 217 · 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

Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis

Kasai, T., Tokuda, T., Ishigami, N., Sasayama, H., Foulds, P., Mitchell, D. J., Mann, D. M. A., Allsop, D., & Nakagawa, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0456-1 · Cited by 211 · see citing works

Frameshift and novel mutations in FUS in familial amyotrophic lateral sclerosis and ALS/dementia

Yan, J., Deng, H., Siddique, N. A., Fecto, F., Chen, W., Yang, Y., Liu, E., Donkervoort, S. C., Zheng, J. G., Shi, Y., et al. (2010) · Neurology · doi:10.1212/wnl.0b013e3181f07e0c · Cited by 208 · see citing works

High frequency ofTARDBPgene mutations in Italian patients with amyotrophic lateral sclerosis

Corrado, L., Ratti, A., Gellera, C., Buratti, E., Castellotti, B., Carlomagno, Y., Ticozzi, N., Mazzini, L., Testa, L., Taroni, F., et al. (2009) · Human Mutation · doi:10.1002/humu.20950 · Cited by 207 · see citing works

FUS Transgenic Rats Develop the Phenotypes of Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration

Huang, C., Zhou, H., Tong, J., Chen, H., Liu, Y., Wang, D., Wei, X., & Xia, X. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002011 · Cited by 206 · see citing works

RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations

Daigle, J. G., Lanson, N. A., Smith, R. B., Casci, I., Maltare, A., Monaghan, J., Nichols, C. D., Kryndushkin, D. S., Shewmaker, F. P., & Pandey, U. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds526 · Cited by 206 · 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

Angiogenin variants in Parkinson disease and amyotrophic lateral sclerosis

van Es, M. A., Schelhaas, H. J., van Vught, P. W. J., Ticozzi, N., Andersen, P. M., Groen, E. J. N., Schulte, C., Blauw, H. M., Koppers, M., Diekstra, F. P., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22611 · Cited by 201 · see citing works

The role of TDP-43 in amyotrophic lateral sclerosis and frontotemporal dementia

Mackenzie, I., & Rademakers, R. (2008) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3283168d1d · Cited by 160 · see citing works

The molecular basis of the frontotemporal lobar degeneration–amyotrophic lateral sclerosis spectrum

Langenhove, T. V., van der Zee, J., & Broeckhoven, C. V. (2012) · Annals of Medicine · doi:10.3109/07853890.2012.665471 · Cited by 192 · see citing works

Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies

Geser, F., Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01091.x · Cited by 195 · 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

Contribution of TARDBP mutations to sporadic amyotrophic lateral sclerosis

Daoud, H., Valdmanis, P. N., Kabashi, E., Dion, P. A., Dupré, N., Camu, W., Meininger, V., & Rouleau, G. A. (2008) · Journal of Medical Genetics · doi:10.1136/jmg.2008.062463 · Cited by 194 · see citing works

Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases

Geser, F., Martinez‐Lage, M., Kwong, L. K., Lee, V. M. ‐., & Trojanowski, J. Q. (2009) · Journal of Neurology · doi:10.1007/s00415-009-5069-7 · Cited by 190 · 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

Sporadic amyotrophic lateral sclerosis: two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions

Nishihira, Y., Tan, C.-F., Onodera, O., Toyoshima, Y., Yamada, M., Morita, T., Nishizawa, M., Kakita, A., & Takahashi, H. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0385-z · Cited by 187 · see citing works

The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS)

Strong, M. J. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.09.029 · Cited by 185 · 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

The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation

Zhang, Y., Caulfield, T. R., Xu, Y., Gendron, T. F., Hubbard, J., Stetler, C. T., Sasaguri, H., Whitelaw, E. C., Cai, S., Lee, C. W., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt166 · Cited by 185 · see citing works

Expression of mutant TDP-43 induces neuronal dysfunction in transgenic mice

Xu, Y.-F., Zhang, Y., Lin, W.-L., Cao, X., Stetler, C. T., Dickson, D. W., Lewis, J. M., & Petrucelli, L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-73 · Cited by 179 · see citing works

The Complex Molecular Biology of Amyotrophic Lateral Sclerosis (ALS)

Redler, R. L., & Dokholyan, N. V. (2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00002-3 · Cited by 172 · see citing works

Molecular Neuropathology of TDP-43 Proteinopathies

Neumann, M. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10010232 · Cited by 169 · see citing works

Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion

Jiang, L.-L., Che, M., Zhao, J., Zhou, C.-J., Xie, M.-Y., Li, H.-Y., He, J.-H., & Hu, H.-Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463828 · Cited by 162 · see citing works

RNA-binding proteins with prion-like domains in ALS and FTLD-U

Gitler, A. D., & Shorter, J. (2011) · Prion · doi:10.4161/pri.5.3.17230 · Cited by 161 · see citing works

Loss and gain of Drosophila TDP-43 impair synaptic efficacy and motor control leading to age-related neurodegeneration by loss-of-function phenotypes

Diaper, D. C., Adachi, Y., Sutcliffe, B., Humphrey, D. M., Elliott, C. J. H., Stepto, A., Ludlow, Z. N., Broeck, L. V., Callaerts, P., Dermaut, B., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt005 · Cited by 160 · 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 157 · see citing works

Proteolytic processing of TAR DNA binding protein‐43 by caspases produces C‐terminal fragments with disease defining properties independent of progranulin

Dormann, D., Capell, A., Carlson, A. M., Shankaran, S. S., Rodde, R., Neumann, M., Kremmer, E., Matsuwaki, T., Yamanouchi, K., Nishihara, M., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06211.x · Cited by 157 · see citing works

TDP‐43 Redistribution is an Early Event in Sporadic Amyotrophic Lateral Sclerosis

Giordana, M. T., Piccinini, M., Grifoni, S., Marco, G. D., Vercellino, M., Magistrello, M., Pellerino, A., Buccinnà, B., Lupino, E., & RINAUDO, M. T. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00284.x · Cited by 156 · see citing works

Frontotemporal Dementia: Implications for Understanding Alzheimer DiseasePreprint

Goedert, M., Ghetti, B. F., & Spillantini, M. G. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006254 · Cited by 148 · see citing works

Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones

Udan-Johns, M., Bengoechea, R., Bell, S., Shao, J., Diamond, M. I., True, H. L., Weihl, C. C., & Baloh, R. H. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt408 · Cited by 149 · see citing works

Mechanisms of toxicity in C9FTLD/ALS

Gendron, T. F., Belzil, V., Zhang, Y., & Petrucelli, L. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1237-z · Cited by 144 · see citing works

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 · see citing works

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 · see citing works

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 138 · see citing works

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 138 · see citing works

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 133 · see citing works

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 132 · 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

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 · see citing works

An MND/ALS phenotype associated with <i>C9orf72</i> 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 · 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

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 · see citing works

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 122 · see citing works

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 119 · see citing works

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 121 · see citing works

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 122 · see citing works

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 121 · 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

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 120 · see citing works

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 119 · see citing works

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 119 · see citing works

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 118 · see citing works

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 117 · see citing works

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 117 · see citing works

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 · see citing works

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 · see citing works

Cytoplasmic dynein in neurodegeneration

Eschbach, J., & Dupuis, L. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.03.004 · Cited by 114 · see citing works

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 · see citing works

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 56 · see citing works

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 106 · see citing works