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

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

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

α-Synuclein is phosphorylated in synucleinopathy lesions

Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M. S., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 2,174

Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 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

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 474

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

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

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

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

Increased cytoplasmicTARDBPmRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43

Koyama, A., Sugai, A., Kato, T., Ishihara, T., Shiga, A., Toyoshima, Y., Koyama, M., Konno, T., Hirokawa, S., Yokoseki, A., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw499 · Cited by 112

Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo

Scaramuzzino, C., Monaghan, J., Milioto, C., Lanson, N. A., Maltare, A., Aggarwal, T., Casci, I., Fackelmayer, F. O., Pennuto, M., & Pandey, U. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061576 · Cited by 108

Methylene blue and dimebon inhibit aggregation of TDP‐43 in cellular models

Yamashita, M., Nonaka, T., Arai, T., Kametani, F., Buchman, V. L., Ninkina, N. N., Бачурин, С. О., Akiyama, H., Goedert, M., & Hasegawa, M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.06.042 · Cited by 114

Mutant TDP-43 in motor neurons promotes the onset and progression of ALS in rats

Huang, C., Tong, J., Bi, F., Zhou, H., & Xia, X. (2011) · Journal of Clinical Investigation · doi:10.1172/jci59130 · Cited by 108

Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease

Fujishiro, H., Uchikado, H., Arai, T., Hasegawa, M., Akiyama, H., Yokota, O., Tsuchiya, K., Togo, T., Iseki, E., & Hirayasu, Y. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0463-2 · Cited by 106

Humoral factors in ALS patients during disease progression

Ehrhart, J. C., de Smith, A. J., Kuzmin‐Nichols, N., Zesiewicz, T., Jahan, I., Shytle, R. D., Kim, S.-H., Sanberg, C. D., Vu, T., Gooch, C. L., et al. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0350-4 · Cited by 106

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 102

Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation

Chiang, C.-H., Grauffel, C., Wu, L.-S., Kuo, P. H., Doudeva, L. G., Lim, C., Shen, C.-K. J., & Yuan, H. S. (2016) · Scientific Reports · doi:10.1038/srep21581 · Cited by 100

Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis

Walker, A. K., & Atkin, J. D. (2011) · IUBMB Life · doi:10.1002/iub.520 · Cited by 104

Implications of the prion-related Q/N domains in TDP-43 and FUS

Udan-Johns, M., & Baloh, R. H. (2011) · Prion · doi:10.4161/pri.5.1.14265 · Cited by 100

Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD

Wood, A., Gurfinkel, Y., Polain, N., Lamont, W. G., & Rea, S. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094705 · Cited by 105

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 102

Phase to Phase with TDP-43

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

Cytosolic TDP-43 expression following axotomy is associated with caspase 3 activation in NFL−/− mice: Support for a role for TDP-43 in the physiological response to neuronal injury

Moisse, K., Mepham, J., Volkening, K., Welch, I., Hill, T., & Strong, M. J. (2009) · Brain Research · doi:10.1016/j.brainres.2009.07.023 · Cited by 93

Genotype-phenotype relationship in hereditary amyotrophic lateral sclerosis

Yamashita, S., & Ando, Y. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0036-y · Cited by 105

Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation

Jiang, L.-L., Zhao, J., Yin, X.-F., He, W.-T., Yang, H., Che, M., & Hu, H.-Y. (2016) · Scientific Reports · doi:10.1038/srep23928 · Cited by 97

Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils

Shimonaka, S., Nonaka, T., Suzuki, G., Hisanaga, S.-I., & Hasegawa, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.713552 · Cited by 93

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

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

Broadening the phenotype of TARDBP mutations: the TARDBP Ala382Thr mutation and Parkinson’s disease in Sardinia

Quadri, M., Cossu, G., Saddi, V., Simons, E. J., Murgia, D., Melis, M., Ticca, A., Oostra, B. A., & Bonifati, V. (2011) · Neurogenetics · doi:10.1007/s10048-011-0288-3 · Cited by 90

Broad clinical phenotypes associated with TAR-DNA binding protein (TARDBP) mutations in amyotrophic lateral sclerosis

Kirby, J., Goodall, G., Smith, W., Highley, J. R., Masanzu, R., Hartley, J. A., Hibberd, R., Hollinger, H. C., Wharton, S. B., Morrison, K. E., et al. (2009) · Neurogenetics · doi:10.1007/s10048-009-0218-9 · Cited by 93

Pedigree with frontotemporal lobar degeneration – motor neuron disease and Tar DNA binding protein-43 positive neuropathology: genetic linkage to chromosome 9

Luty, A. A., Kwok, J. B., Thompson, E. M., Blumbergs, P. C., Brooks, W. S., Loy, C. T., Dobson‐Stone, C., Panegyres, P. K., Hecker, J. R., Nicholson, G. A., et al. (2008) · BMC Neurology · doi:10.1186/1471-2377-8-32 · Cited by 86

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

“Structural characterization of the minimal segment of TDP-43 competent for aggregation”

Mompeán, M., Buratti, E., Guarnaccia, C., Brito, R. M. M., Chakrabartty, A., Baralle, F. E., & Laurents, D. V. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.01.007 · Cited by 85

Premature death of TDP ‐43 ( A 315 T ) transgenic mice due to gastrointestinal complications prior to development of full neurological symptoms of amyotrophic lateral sclerosis

Esmaeili, M. A., Panahi, M., Yadav, S., Hennings, L. J., & Kiaei, M. (2013) · International Journal of Experimental Pathology · doi:10.1111/iep.12006 · Cited by 87

Amyotrophic lateral sclerosis mutant vesicle-associated membrane protein-associated protein-B transgenic mice develop TAR-DNA-binding protein-43 pathology

Tudor, E. L., Galtrey, C. M., Perkinton, M. S., Lau, K., Vos, K. J. D., Mitchell, J. C., Ackerley, S., Hortobágyi, T., Vámos, E., Leigh, P. N., et al. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.035 · Cited by 90

Phenotype and genotype analysis in amyotrophic lateral sclerosis with TARDBP gene mutations

Corcia, P., Valdmanis, P. N., Millecamps, S., Lionnet, C., Blasco, H., Mouzat, K., Daoud, H., Belzil, V., Morales, R. J., Pageot, N., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e3182553c88 · Cited by 92

The molecular link between inefficient GluA2 Q/R site-RNA editing and TDP-43 pathology in motor neurons of sporadic amyotrophic lateral sclerosis patients

Yamashita, T., & Kwak, S. (2013) · Brain Research · doi:10.1016/j.brainres.2013.12.011 · Cited by 84

TDP-43 transports ribosomal protein mRNA to regulate axonal local translation in neuronal axons

Nagano, S., Jinno, J., Abdelhamid, R. F., Jin, Y., Shibata, M., Watanabe, S., Hirokawa, S., Nishizawa, M., Sakimura, K., Onodera, O., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02205-y · Cited by 82

TDP-43 suppresses tau expression via promoting its mRNA instability

Gu, J., Wu, F., Xu, W., Shi, J., Hu, W. H., Jin, N., Qian, W., Wang, X., Iqbal, K., Gong, C., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx175 · Cited by 80

RNA binding mediates neurotoxicity in the transgenic Drosophila model of TDP-43 proteinopathy

Ihara, R., Matsukawa, K., Nagata, Y., Kunugi, H., Tsuji, S., Chihara, T., Kuranaga, E., Miura, M., Wakabayashi, T., Hashimoto, T., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt296 · Cited by 81

From molecule to molecule and cell to cell: Prion-like mechanisms in amyotrophic lateral sclerosis

Grad, L. I., Fernando, S. M., & Cashman, N. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.009 · Cited by 80

The molecular basis of frontotemporal dementia

Neumann, M., Tolnay, M., & Mackenzie, I. R. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001136 · Cited by 80

Super-Resolution Microscopy Reveals Presynaptic Localization of the ALS/FTD Related Protein FUS in Hippocampal Neurons

Schoen, M., Reichel, J. M., Demestre, M., Putz, S., Deshpande, D., Proepper, C., Liebau, S., Schmeißer, M. J., Ludolph, A. C., Michaelis, J., et al. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00496 · Cited by 80

RNA metabolism and the pathogenesis of motor neuron diseases

Lemmens, R., Moore, M. J., Al‐Chalabi, A., Brown, R. H., & Robberecht, W. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.02.003 · Cited by 80

Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS

Ito, D., & Suzuki, N. (2011) · Neurology · doi:10.1212/wnl.0b013e3182343365 · Cited by 78

Knockdown of the Drosophila Fused in Sarcoma (FUS) Homologue Causes Deficient Locomotive Behavior and Shortening of Motoneuron Terminal Branches

Sasayama, H., Shimamura, M., Tokuda, T., Azuma, Y., Yoshida, T., Mizuno, T., Nakagawa, M., Fujikake, N., Nagai, Y., & Yamaguchi, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039483 · Cited by 80

Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis

Ishihara, T., Ariizumi, Y., Shiga, A., Kato, T., Tan, C., Sato, T., Miki, Y., Yokoo, M., Fujino, T., Koyama, A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt262 · Cited by 74

Accumulation of TDP-43 and α-actin in an amyotrophic lateral sclerosis patient with the K17I ANG mutation

Seilhean, D., Cazeneuve, C., Thuriès, V., Russaouen, O., Millecamps, S., Salachas, F., Meininger, V., LeGuern, E., & Duyckaerts, C. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0545-9 · Cited by 71

Neurodegeneration the RNA way

Renoux, A. J., & Todd, P. K. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.10.006 · Cited by 75

Recent advances in motor neuron disease

Damme, P. V., & Robberecht, W. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832ffbe3 · Cited by 76

Review: Transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration

Gendron, T. F., Josephs, K. A., & Petrucelli, L. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01060.x · Cited by 76

TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander

Banks, G. T., Kuta, A., Isaacs, A. M., & Fisher, E. (2008) · Mammalian Genome · doi:10.1007/s00335-008-9117-x · Cited by 73

Mutant FUS and ELAVL4 (HuD) Aberrant Crosstalk in Amyotrophic Lateral Sclerosis

De Santis, R., Alfano, V., de Turris, V., Colantoni, A., Santini, L., Garone, M. G., Antonacci, G., Peruzzi, G., Sudria-Lopez, E., Wyler, E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.085 · Cited by 70

Coexistence of Huntington’s disease and amyotrophic lateral sclerosis: a clinicopathologic study

Tada, M., Coon, E. A., Osmand, A. P., Kirby, P., Martin, W. R. W., Wieler, M., Shiga, A., Shirasaki, H., Tada, M., Makifuchi, T., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1005-5 · Cited by 69

TARDBP Mutation Analysis in TDP-43 Proteinopathies and Deciphering the Toxicity of Mutant TDP-43

Gendron, T. F., Rademakers, R., & Petrucelli, L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129036 · Cited by 70

Cytoplasmic accumulation of TDP-43 in circulating lymphomonocytes of ALS patients with and without TARDBP mutations

Marco, G. D., Lupino, E., Calvo, A., Moglia, C., Buccinnà, B., Grifoni, S., Ramondetti, C., Lomartire, A., RINAUDO, M. T., Piccinini, M., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0786-7 · Cited by 68

A novel mutation P112H in the TARDBP gene associated with frontotemporal lobar degeneration without motor neuron disease and abundant neuritic amyloid plaques

Moreno, F., Rabinovici, G. D., Karydas, A., Miller, Z., Hsu, S. C., Legati, A., Fong, J. C., Schonhaut, D. R., Esselmann, H., Watson, C., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0190-6 · Cited by 69

Prion-like mechanisms and potential therapeutic targets in neurodegenerative disorders

Hasegawa, M., Nonaka, T., & Masuda‐Suzukake, M. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.11.010 · Cited by 71

Genetic Rodent Models of Amyotrophic Lateral Sclerosis

Bosch, L. V. D. (2011) · BioMed Research International · doi:10.1155/2011/348765 · Cited by 70

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

Gendron, T. F., & Petrucelli, L. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9610-7 · Cited by 66

Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons

Sato, T., Takeuchi, S., Saito, A., Ding, W., Bamba, H., Matsuura, H., Hisa, Y., Tooyama, I., & Urushitani, M. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.09.050 · Cited by 63

Amyotrophic Lateral Sclerosis–Frontotemporal Lobar Dementia in 3 Families With p.Ala382Thr TARDBP Mutations

Chiò, A., Calvo, A., Moglia, C., Restagno, G., Ossola, I., Brunetti, M., Montuschi, A., Cistaro, A., Ticca, A., Traynor, B. J., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.173 · Cited by 66

TDP-43 Regulates the Microprocessor Complex Activity During In Vitro Neuronal Differentiation

Carlo, V. D., Grossi, E., Laneve, P., Morlando, M., Modigliani, S. D., Ballarino, M., Bozzoni, I., & Caffarelli, E. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8564-x · Cited by 67

Pathogenic TARDBP Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia: Disease-Associated Pathways

Barmada, S. J., & Finkbeiner, S. M. (2010) · Reviews in the Neurosciences · doi:10.1515/revneuro.2010.21.4.251 · Cited by 63

Heterogeneity of cerebral TDP-43 pathology in sporadic amyotrophic lateral sclerosis: Evidence for clinico-pathologic subtypes

Takeuchi, R., Tada, M., Shiga, A., Toyoshima, Y., Konno, T., Sato, T., Nozaki, H., Kato, T., Horie, M., Shimizu, H., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0335-2 · Cited by 66

miR-129-5p: A key factor and therapeutic target in amyotrophic lateral sclerosis

Loffreda, A., Nizzardo, M., Arosio, A., Ruepp, M., Calogero, R., Volinia, S., Galasso, M., Bendotti, C., Ferrarese, C., Lunetta, C., et al. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101803 · Cited by 58

Sporadic amyotrophic lateral sclerosis of long duration is associated with relatively mild TDP-43 pathology

Nishihira, Y., Tan, C., Hoshi, Y., Iwanaga, K., Yamada, M., Kawachi, I., Tsujihata, M., Hozumi, I., Morita, T., Onodera, O., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0443-6 · Cited by 61

Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport

Štalekar, M., Yin, X., Rebolj, K., Darovic, S., Troakes, C., Mayr, M., Shaw, C. E., & Rogelj, B. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.02.046 · Cited by 64

From nucleation to widespread propagation: A prion-like concept for ALS

Maniecka, Z., & Polymenidou, M. (2015) · Virus Research · doi:10.1016/j.virusres.2014.12.032 · Cited by 65

Reversible Behavioral Phenotypes in a Conditional Mouse Model of TDP-43 Proteinopathies

Alfieri, J. A., Pino, N. S., & Igaz, L. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1918-14.2014 · Cited by 60

Increased expression of TDP-43 in the skin of amyotrophic lateral sclerosis

Suzuki, M., Mikami, H., Watanabe, T., Yamano, T., Yamazaki, T., Nomura, M., Yasui, K., Ishikawa, H., & Ono, S. (2010) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2010.01321.x · Cited by 62

TDP-43 expression in mouse models of amyotrophic lateral sclerosis and spinal muscular atrophy

Turner, B. J., Bäumer, D., Parkinson, N., Scaber, J., Ansorge, O., & Talbot, K. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-104 · Cited by 65

Synaptic dysfunction in ALS and FTD: anatomical and molecular changes provide insights into mechanisms of disease

Gelon, P. A., Dutchak, P. A., & Sephton, C. F. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1000183 · Cited by 64

The ALS/FTLD‐related RNA‐binding proteins TDP‐43 and FUS have common downstream RNA targets in cortical neurons

Honda, D., Ishigaki, S., Iguchi, Y., Fujioka, Y., Udagawa, T., Masuda, A., Ohno, K., Katsuno, M., & Sobue, G. (2013) · FEBS Open Bio · doi:10.1016/j.fob.2013.11.001 · Cited by 61

Aggresome formation and liquid–liquid phase separation independently induce cytoplasmic aggregation of TAR DNA-binding protein 43

Watanabe, S., Inami, H., Oiwa, K., Murata, Y., Sakai, S., Komine, O., Sobue, A., Iguchi, Y., Katsuno, M., & Yamanaka, K. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03116-2 · Cited by 59

Mitochondria, a Key Target in Amyotrophic Lateral Sclerosis Pathogenesis

Genin, E. C., Abou-Ali, M., & Paquis‐Flucklinger, V. (2023) · Genes · doi:10.3390/genes14111981 · Cited by 64

On the development of markers for pathological TDP-43 in amyotrophic lateral sclerosis with and without dementia

Geser, F., Prvulovic, D., O’Dwyer, L., Hardiman, O. M., Bede, P., Bokde, A. L. W., Trojanowski, J. Q., & Hampel, H. J. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.08.011 · Cited by 58

Primary fibroblasts cultures reveal TDP-43 abnormalities in amyotrophic lateral sclerosis patients with and without SOD1 mutations

Sabatelli, M., Zollino, M., Conte, A., Grande, A. D., Marangi, G., Lucchini, M., Massimiliano Mirabella, A., Romano, Â., Piacentini, R., Bisogni, G., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.009 · Cited by 57

Identification of 2 Loci at Chromosomes 9 and 14 in a Multiplex Family With Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Gijselinck, I., Engelborghs, S., Maes, G., Cuijt, I., Peeters, K., Mattheijssens, M., Joris, G., Cras, P. P., Martin, J., Deyn, P. P. D., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.82 · Cited by 55

Amyotrophic lateral sclerosis: an update on recent genetic insights

Iguchi, Y., Katsuno, M., Ikenaka, K., Ishigaki, S., & Sobue, G. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7112-y · Cited by 56

Screening for TARDBP mutations in Japanese familial amyotrophic lateral sclerosis

Kamada, M., Maruyama, H., Tanaka, E. I., Morino, H., Wate, R., Ito, H., Kusaka, H., Kawano, Y., Miki, T., Nodera, H., et al. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.04.017 · Cited by 55

TARDBP pathogenic mutations increase cytoplasmic translocation of TDP-43 and cause reduction of endoplasmic reticulum Ca2+ signaling in motor neurons

Mutihac, R., Alegre‐Abarrategui, J., Gordon, D., Farrimond, L. E., Yamasaki-Mann, M., Talbot, K., & Wade‐Martins, R. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.12.010 · Cited by 55

Research Advances in Amyotrophic Lateral Sclerosis, 2009 to 2010

Traub, R., Mitsumoto, H., & Rowland, L. P. (2010) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-010-0160-0 · Cited by 54

Skeletal Muscle in Motor Neuron Diseases: Therapeutic Target and Delivery Route for Potential Treatments

Dupuis, L., & Echaniz‐Laguna, A. (2010) · Current Drug Targets · doi:10.2174/1389450111007011250 · Cited by 53

Molecular Dissection of TDP-43 Proteinopathies

Hasegawa, M., Nonaka, T., Tsuji, H., Tamaoka, A., Yamashita, M., Kametani, F., Yoshida, M., Arai, T., & Akiyama, H. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9571-x · Cited by 56

A Review of the Potential Role of Nano-Enabled Drug Delivery Technologies in Amyotrophic Lateral Sclerosis: Lessons Learned from Other Neurodegenerative Disorders

Mazibuko, Z., Choonara, Y. E., Kumar, P., du Toit, L. C., Modi, G., Naidoo, D., & Pillay, V. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24322 · Cited by 51

TDP-43 M337V Mutation in Familial Amyotrophic Lateral Sclerosis in Japan

Tamaoka, A., Arai, M., Itokawa, M., Arai, T., Hasegawa, M., Tsuchiya, K., Takuma, H., Tsuji, H., Ishii, A., Watanabe, M., et al. (2010) · Internal Medicine · doi:10.2169/internalmedicine.49.2915 · Cited by 49

Genome-Wide Approaches to Dissect the Roles of RNA Binding Proteins in Translational Control: Implications for Neurological Diseases

Kapeli, K., & Yeo, G. W.-M. (2012) · Frontiers in Neuroscience · doi:10.3389/fnins.2012.00144 · Cited by 50

Endothelial and Astrocytic Support by Human Bone Marrow Stem Cell Grafts into Symptomatic ALS Mice towards Blood-Spinal Cord Barrier Repair

Garbuzova-Davis, S. N., Kurien, C., Thomson, A., Falco, D., Ahmad, S., Staffetti, J. F., Steiner, G. A., Abraham, S., James, G. V., Mahendrasah, A., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-00993-0 · Cited by 49

Selective occurrence of TDP-43-immunoreactive inclusions in the lower motor neurons in Machado–Joseph disease

Tan, C., Yamada, M., Toyoshima, Y., Yokoseki, A., Miki, Y., Hoshi, Y., Kaneko, H., Ikeuchi, T., Onodera, O., Kakita, A., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0552-x · Cited by 49

TDP‐43 neuropathology is similar in sporadic amyotrophic lateral sclerosis with or without TDP‐43 mutations

Pamphlett, R., Luquin, N., McLean, C., Jew, S. K., & Adams, L. (2008) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2008.00982.x · Cited by 47

Imbalance of mitochondrial dynamics in Drosophila models of amyotrophic lateral sclerosis

Altanbyek, V., Cha, S.-J., Kang, G.-U., Im, D. S., Lee, S., Kim, H., & Kim, K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.134 · Cited by 47

Amyotrophic lateral sclerosis mutant TDP-43 may cause synaptic dysfunction through altered dendritic spine function

Jiang, T., Handley, E. E., Brizuela, M., Dawkins, E., Lewis, K. E. A., Clark, R. M., Dickson, T. C., & Blizzard, C. A. (2019) · Disease Models & Mechanisms · doi:10.1242/dmm.038109 · Cited by 48

The evolving biology of cell reprogramming

Wilmut, I., Sullivan, G. J., & Chambers, I. (2011) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0051 · Cited by 47

Targeting angiogenin in therapy of amyotropic lateral sclerosis

Kishikawa, H., Wu, D., & Hu, G.-F. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.10.1229 · Cited by 47

Identification of compounds protective against G93A-SOD1 toxicity for the treatment of amyotrophic lateral sclerosis

Benmohamed, R., Arvanites, A. C., Kim, J., Ferrante, R. J., Silverman, R. B., Morimoto, R. I., & Kirsch, D. R. (2010) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2010.522586 · Cited by 46

Identification of ter94, Drosophila VCP, as a strong modulator of motor neuron degeneration induced by knockdown of Caz, Drosophila FUS

Azuma, Y., Tokuda, T., Shimamura, M., Kyotani, A., Sasayama, H., Yoshida, T., Mizuta, I., Mizuno, T., Nakagawa, M., Fujikake, N., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu055 · Cited by 45

The Genetic Diagnosis of Neurodegenerative Diseases and Therapeutic Perspectives

Casallas, J. C. G., & Bustos, R. (2018) · Brain Sciences · doi:10.3390/brainsci8120222 · Cited by 49

Motor neuron expression of the voltage-gated calcium channel cacophony restores locomotion defects in a Drosophila, TDP-43 loss of function model of ALS

Chang, J., Hazelett, D. J., Stewart, J. A., & Morton, D. B. (2013) · Brain Research · doi:10.1016/j.brainres.2013.11.019 · Cited by 44

Large-scale screening of TARDBP mutation in amyotrophic lateral sclerosis in Japanese

Iida, A., Kamei, T., Sano, M., Oshima, S., Tokuda, T., Nakamura, Y., & Ikegawa, S. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.017 · Cited by 44

Association between novel TARDBP mutations and Chinese patients with amyotrophic lateral sclerosis

Xiong, H.-L., Wang, J.-Y., Sun, Y., Wu, J.-J., Chen, Y., Qiao, K., Zheng, Q.-J., Zhao, G., & Wu, Z. (2010) · BMC Medical Genetics · doi:10.1186/1471-2350-11-8 · Cited by 44

Identification of Genetic Modifiers of TDP-43 Neurotoxicity in Drosophila

Zhan, L., Hanson, K. A., Kim, S. H., Tare, A., & Tibbetts, R. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057214 · Cited by 43

When Does ALS Start? ADAR2?GluA2 Hypothesis for the Etiology of Sporadic ALS

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Ultrastructural studies of ALS mitochondria connect altered function and permeability with defects of mitophagy and mitochondriogenesis

Ruffoli, R., Bartalucci, A., Frati, A., & Fornai, F. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00341 · Cited by 42

Single-cell RNA-sequencing reveals early mitochondrial dysfunction unique to motor neurons shared across FUS- and TARDBP-ALS

Schweingruber, C., Nijssen, J., Mechtersheimer, J., Reber, S., Lebœuf, M., O’Brien, N. L., Mei, I., Hedges, E. C., Keuper, M., Benitez, J. A., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59679-1 · Cited by 43

Role of selected mutations in the Q/N rich region of TDP-43 in EGFP-12xQ/N-induced aggregate formation

Budini, M., Romano, V. C., Avendaño-Vázquez, S. E., Bembich, S., Buratti, E., & Baralle, F. E. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.031 · Cited by 41

Sporadic ALS with compound heterozygous mutations in the SQSTM1 gene

Shimizu, H., Toyoshima, Y., Shiga, A., Yokoseki, A., Arakawa, K., Sekine, Y., Shimohata, T., Ikeuchi, T., Nishizawa, M., Kakita, A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1150-5 · Cited by 42

Localization of fused in sarcoma (FUS) protein to the post-synaptic density in the brain

Aoki, N., Higashi, S., Kawakami, I., Kobayashi, Z., Hosokawa, M., Katsuse, O., Togo, T., Hirayasu, Y., & Akiyama, H. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0984-6 · Cited by 45

High-content RNAi screening identifies the Type 1 inositol triphosphate receptor as a modifier of TDP-43 localization and neurotoxicity

Kim, S. H., Zhan, L., Hanson, K. A., & Tibbetts, R. S. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds321 · Cited by 37

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