TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors

Powers, C. A., Mathur, M., Raaka, B. M., Ron, D., & Samuels, H. H. (1997) · Molecular Endocrinology · doi:10.1210/mend.12.1.0043 · Cited by 114

Pallidonigral TDP-43 pathology in Perry syndrome

Wider, C. W., Dickson, D. W., Stoessl, A. J., Tsuboi, Y., Chapon, F., Gutmann, L., Lechevalier, B., Calne, D. B., Personett, D. A., Hulihan, M., et al. (2008) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2008.07.005 · Cited by 113

Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry.

Calvio, C., Neubauer, G., Mann, M., & Lamond, A. I. (1995) · PubMed Central · Cited by 113

Identification and characterization of FUS/TLS as a new target of ATM

Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J. (2008) · Biochemical Journal · doi:10.1042/bj20081135 · Cited by 111

Proto-oncoprotein tls/fus is associated to the nuclear matrix and complexed with splicing factors ptb, srm160, and sr proteins

Meißner, M., Lopato, S., Gotzmann, J., Sauermann, G., & Barta, A. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00046-0 · Cited by 109

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

A Novel CpG-free Vertebrate Insulator Silences the Testis-specific SP-10 Gene in Somatic Tissues

Abhyankar, M. M., Urekar, C., & Reddi, P. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705811200 · Cited by 108

Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads

Belly, A., Moreau-Gachelin, F., Sadoul, R., & Goldberg, Y. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2004.12.071 · Cited by 107

Regional distribution of TDP‐43 inclusions in Alzheimer disease (AD) brains: Their relation to AD common pathology

Kadokura, A., Yamazaki, T., Lemere, C. A., Takatama, M., & Okamoto, K. (2009) · Neuropathology · doi:10.1111/j.1440-1789.2009.01017.x · Cited by 106

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

Multiple system degeneration with basophilic inclusions in Japanese ALS patients with FUS mutation

Tateishi, T., Hokonohara, T., Yamasaki, R., Miura, S., Kikuchi, H., Iwaki, A., Tashiro, H., Furuya, H., Nagara, Y., Ohyagi, Y., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0621-1 · Cited by 106

Genomic structure of the human RBP56/hTAF68 and FUS/TLS genes

Morohoshi, F., Ootsuka, Y., Arai, K., Ichikawa, H., Mitani, S., Munakata, N., & Ohki, M. (1998) · Gene · doi:10.1016/s0378-1119(98)00463-6 · Cited by 105

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

FUS‐Immunoreactive Intranuclear Inclusions in Neurodegenerative Disease

Woulfe, J., Gray, D. A., & Mackenzie, I. R. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00337.x · Cited by 99

FUS mutations in sporadic amyotrophic lateral sclerosis

Lai, S. L., Abramzon, Y. A., Schymick, J. C., Stephan, D. A., Dunckley, T. L., Dillman, A., Cookson, M., Calvo, A., Battistini, S., Giannini, F., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.12.020 · Cited by 98

Identification and Characterization of the Nuclear Localization/Retention Signal in the EWS Proto-oncoprotein

Zakaryan, R. P., & Gehring, H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.018 · Cited by 98

Chromosome 9p-linked families with frontotemporal dementia associated with motor neuron disease

Ber, I. L., Camuzat, A., Berger, É., Hannequin, D., Laquerrière, A., Golfier, V., Seilhean, D., Viennet, G., Couratier, P., Verpillat, P., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181a55f1c · Cited by 98

TDP-43 pathology in familial frontotemporal dementia and motor neuron disease without Progranulin mutations

Seelaar, H., Schelhaas, H. J., Azmani, A., Küsters, B., Rosso, S. M., Majoor‐Krakauer, D. F., de Rijk, M. C., Rizzu, P., ten Brummelhuis, M., van Doorn, P. A., et al. (2007) · Brain · doi:10.1093/brain/awm024 · Cited by 98

TAR DNA-Binding Protein 43 Accumulation in Protein Aggregate Myopathies

Olivé, M., Janué, A., Moreno, D., Gámez, J., Torrejón-Escribano, B., & Ferrer, I. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181996d8f · Cited by 94

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

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

Clinicopathological characterization of Pick’s disease versus frontotemporal lobar degeneration with ubiquitin/TDP-43-positive inclusions

Yokota, O., Tsuchiya, K., Arai, T., Yagishita, S., Matsubara, O., Mochizuki, A., Tamaoka, A., Kawamura, M., Yoshida, H., Terada, S., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0493-4 · Cited by 90

Hippocampal sclerosis dementia: a reappraisal

Probst, A., Taylor, K. I., & Tolnay, M. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0262-1 · Cited by 89

TDP43 depletion rescues aberrant CFTR exon 9 skipping

Ayala, Y. M., Pagani, F., & Baralle, F. E. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.01.052 · Cited by 88

Severe subcortical TDP-43 pathology in sporadic frontotemporal lobar degeneration with motor neuron disease

Brandmeir, N. J., Geser, F., Kwong, L. K., Zimmerman, E. A., Qian, J., Lee, V. M. ‐., & Trojanowski, J. Q. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0315-5 · Cited by 87

TLS Inhibits RNA Polymerase III Transcription

Tan, A. Y., & Manley, J. L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00884-09 · Cited by 87

The N-terminal domain of human TAFII68 displays transactivation and oncogenic properties

Bertolotti, A., Bell, B., & Tora, L. (1999) · Oncogene · doi:10.1038/sj.onc.1203207 · Cited by 87

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

Human POMp75 is identified as the pro-oncoprotein TLS/FUS: both POMp75 and POMp100 DNA homologous pairing activities are associated to cell proliferation

Bertrand, P., Akhmedov, A. T., Delacôte, F., Dürrbach, A., & López, B. S. (1999) · Oncogene · doi:10.1038/sj.onc.1203048 · Cited by 86

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

Transactive Response DNA-Binding Protein 43 Burden in Familial Alzheimer Disease and Down Syndrome

Lippa, C. F., Rosso, A. L., Stutzbach, L., Neumann, M., Lee, V. M. ‐., & Trojanowski, J. Q. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.277 · Cited by 83

TAR-DNA Binding Protein 43 in Pick Disease

Freeman, S. H., Spires‐Jones, T. L., Hyman, B. T., Growdon, J. H., & Frosch, M. P. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181609361 · Cited by 82

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

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

Enduring involvement of tau, β-amyloid, α-synuclein, ubiquitin and TDP-43 pathology in the amyotrophic lateral sclerosis/parkinsonism–dementia complex of Guam (ALS/PDC)

Judith Miklossy, A., Steele, J. C., Yu, S. Y., McCall, S. A., Sandberg, G. D., McGeer, E. G., & McGeer, P. L. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0439-2 · Cited by 81

TDP-43-negative FTLD-U is a significant new clinico-pathological subtype of FTLD

Roeber, S., Mackenzie, I. R., Kretzschmar, H. A., & Neumann, M. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0395-x · Cited by 80

cis-Requirement for the maintenance of round spermatid-specific transcription

Acharya, K. K., Govind, C. K., Shore, A. N., Stoler, M. H., & Reddi, P. P. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.04.443 · Cited by 79

Mimicking Aspects of Frontotemporal Lobar Degeneration and Lou Gehrig's Disease in Rats via TDP-43 Overexpression

Tatom, J. B., Wang, D. B., Dayton, R. D., Skalli, O., Hutton, M. L., Dickson, D. W., & Klein, R. L. (2009) · Molecular Therapy · doi:10.1038/mt.2009.3 · Cited by 78

Acta Neuropathologica

(1962) · Nature · doi:10.1038/1931136d0 · Cited by 76

FUS Mutations in Familial Amyotrophic Lateral Sclerosis in the Netherlands

Groen, E. J. N., van Es, M. A., van Vught, P. W. J., Spliet, W. G. M., Engelen-Lee, J.-Y., de Visser, M., Wokke, J. H. J., Schelhaas, H. J., Ophoff, R. A., Fumoto, K., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2009.329 · Cited by 75

β-Catenin Interacts With the FUS Proto-oncogene Product and Regulates Pre-mRNA Splicing

Sato, S., Idogawa, M., Honda, K., et al. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.07.025 · Cited by 74

No evidence for cognitive dysfunction or depression in patients with mild restless legs syndrome

Driver‐Dunckley, E. D., Connor, D. J., Hentz, J., Sabbagh, M., Silverberg, N. B., Hernández‐Davó, J. L., Vedders, L. J., Evidente, V. G. H., Shill, H. A., Caviness, J. N., et al. (2009) · Movement Disorders · doi:10.1002/mds.22701 · Cited by 73

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

TDP-43 accumulation is common in myopathies with rimmed vacuoles

Küsters, B., van Hoeve, B. J. A., Schelhaas, H. J., Laak, H. T., van Engelen, B. G. M., & Lammens, M. M. Y. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0471-2 · Cited by 72

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

TDP-43 Is Not a Common Cause of Sporadic Amyotrophic Lateral Sclerosis

Guerreiro, R. J., Schymick, J. C., Crews, C. K., Singleton, A., Hardy, J., & Traynor, B. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002450 · Cited by 71

FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion

Suzuki, N., Aoki, M., Warita, H., Kato, M., Mizuno, H., Shimakura, N., Akiyama, T., Furuya, H., Hokonohara, T., Iwaki, A., et al. (2010) · Journal of Human Genetics · doi:10.1038/jhg.2010.16 · Cited by 70

P68 RNA Helicase (DDX5) Alters Activity of Cis- and Trans-Acting Factors of the Alternative Splicing of H-Ras

Camats, M., Guil, S., Kokolo, M., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002926 · Cited by 68

Anterior horn cells with abnormal TDP-43 immunoreactivities show fragmentation of the Golgi apparatus in ALS

Fujita, Y., Mizuno, Y., Takatama, M., & Okamoto, K. (2008) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.12.016 · Cited by 67

Sporadic corticobasal syndrome due to FTLD-TDP

Tartaglia, M. C., Sidhu, M., Laluz, V., Racine, C. A., Rabinovici, G. D., Creighton, K., Karydas, A., Rademakers, R., Huang, E. J., Miller, B. L., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0605-1 · Cited by 67

Progranulin mutations in ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, M., Kumar-Singh, S., & Van Broeckhoven, C. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025251 · Cited by 67

A topogenic role for the oncogenic N-terminus of TLS: nucleolar localization when transcription is inhibited

Zinszner, H., Immanuel, D., Yin, Y., Liang, F., & Ron, D. (1997) · Oncogene · doi:10.1038/sj.onc.1200854 · Cited by 66

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

Mutational analysis of TARDBP in neurodegenerative diseases

Ticozzi, N., LeClerc, A. L., van Blitterswijk, M., Keagle, P. J., McKenna-Yasek, D. M., Sapp, P. C., Silani, V., Wills, A.-M. A., Brown, R. H., & Landers, J. E. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.11.018 · Cited by 64

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

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

TAR DNA-Binding Protein 43 Immunohistochemistry Reveals Extensive Neuritic Pathology in FTLD-U: A Midwest-Southwest Consortium for FTLD Study

Hatanpaa, K. J., Bigio, E. H., Cairns, N. J., Womack, K. B., Weıntraub, S., Morris, J. C., Foong, C., Xiao, G., Hladik, C. L., Mantanona, T. Y., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31816a12a6 · Cited by 62

Valosin containing protein associated inclusion body myopathy: abnormal vacuolization, autophagy and cell fusion in myoblasts

Vesa, J., Su, H., Watts, G. D. J., Krause, S., Walter, M. C., Martin, B., Smith, C. D., Wallace, D. C., & Kimonis, V. E. (2009) · Neuromuscular Disorders · doi:10.1016/j.nmd.2009.08.003 · Cited by 62

Transactivation Response DNA-Binding Protein 43 Microvasculopathy in Frontotemporal Degeneration and Familial Lewy Body Disease

Lin, W.-L., Castanedes‐Casey, M., & Dickson, D. W. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181baacec · Cited by 61

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

Absence of FUS-immunoreactive pathology in frontotemporal dementia linked to chromosome 3 (FTD-3) caused by mutation in the CHMP2B gene

Holm, I. E., Isaacs, A. M., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0593-1 · Cited by 60

Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy

Thorpe, J. R., Tang, H., Atherton, J., & Cairns, N. J. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0137-1 · Cited by 57

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

Absence of heterogeneous nuclear ribonucleoproteins and survival motor neuron protein in TDP-43 positive inclusions in frontotemporal lobar degeneration

Neumann, M., Igaz, L. M., Kwong, L. K., Nakashima‐Yasuda, H., Kolb, S. J., Dreyfuss, G., Kretzschmar, H. A., Trojanowski, J. Q., & Lee, V. M. ‐. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0221-x · 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

Clinical and pathological characteristics of patients with Leucine‐rich repeat kinase‐2 mutations

Covy, J. P., Yuan, W., Waxman, E. A., Hurtig, H. I., Deerlin, V. M. V., & Giasson, B. I. (2008) · Movement Disorders · doi:10.1002/mds.22096 · Cited by 55

C-terminal FUS/TLS mutations in familial and sporadic ALS in Germany

Drepper, C., Herrmann, T., Wessig, C., Beck, M., & Sendtner, M. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.11.017 · Cited by 55

Phosphorylation-dependent TDP-43 antibody detects intraneuronal dot-like structures showing morphological characters of granulovacuolar degeneration

Kadokura, A., Yamazaki, T., Kakuda, S., Makioka, K., Lemere, C. A., Fujita, Y., Takatama, M., & Okamoto, K. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.06.024 · Cited by 54

Elucidating the genetics and pathology of Perry syndrome

Wider, C. W., Dächsel, J. C., Farrer, M. J., et al. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.08.044 · Cited by 53

Frontotemporal lobar degeneration with ubiquitin-positive, but TDP-43-negative inclusions

Josephs, K. A., Lin, W.-L., Ahmed, Z., Stroh, D. A., Graff‐Radford, N. R., & Dickson, D. W. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0397-8 · Cited by 53

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

Wobbler mice modeling motor neuron disease display elevated transactive response DNA binding protein

Dennis, J. S., & Citron, B. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.10.030 · Cited by 49

TDP-43 in neurodegenerative disorders

Cook, C. N., Zhang, Y., Xu, Y.-F., Dickson, D. W., & Petrucelli, L. (2008) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.8.7.969 · 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

Identification of a human protein that recognizes the 3′ splice site during the second step of pre‐mRNA splicing

Wu, S., & Green, M. R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.14.4421 · Cited by 49

Antagonistic factors control the unproductive splicing of SC35 terminal intron

Dreumont, N., Hardy, S., Behm‐Ansmant, I., Kister, L., Branlant, C., Stévenin, J., & Bourgeois, C. F. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1086 · Cited by 48

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

Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation

Haapasalo, A., Viswanathan, J., Bertram, L., Soininen, H. S., Tanzi, R. E., & Hiltunen, M. O. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380150 · Cited by 46

The occurrence of mutations in FUS in a Belgian cohort of patients with familial ALS

Damme, P. V., Goris, A., Race, V., Hersmus, N., Dubois, B., Bosch, L. V. D., Matthijs, G., & Robberecht, W. (2009) · European Journal of Neurology · doi:10.1111/j.1468-1331.2009.02859.x · 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

An in vitro enzymatic assay coupled to proteomics analysis reveals a new DNA processing activity for Ewing sarcoma and TAF(II)68 proteins

Guipaud, O., Guillonneau, F., Labas, V., Praseuth, D., Rossier, J., López, B. S., & Bertrand, P. (2006) · PROTEOMICS · doi:10.1002/pmic.200600259 · Cited by 42

Absence of ubiquitinated inclusions in hypocretin neurons of patients with narcolepsy

Honda, M., Arai, T., Fukazawa, M., Honda, Y., Tsuchiya, K., Salehi, A., Akiyama, H., & Mignot, E. J.-M. (2009) · Neurology · doi:10.1212/wnl.0b013e3181b2a6af · Cited by 40

Sporadic amyotrophic lateral sclerosis: Widespread multisystem degeneration with TDP‐43 pathology in a patient after long‐term survival on a respirator

Nishihira, Y., Tan, C., Toyoshima, Y., Yonemochi, Y., Kondo, H., Nakajima, T., & Takahashi, H. (2009) · Neuropathology · doi:10.1111/j.1440-1789.2008.00999.x · Cited by 39

RNA splicing mediated by YB‐1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells

Rapp, T. B., Yang, L., Conrad, E. U., Mandahl, N., & Chansky, H. A. (2002) · Journal of Orthopaedic Research® · doi:10.1016/s0736-0266(02)00006-2 · Cited by 37

TDP-43 in ubiquitinated inclusions in the inferior olives in frontotemporal lobar degeneration and in other neurodegenerative diseases: a degenerative process distinct from normal ageing

Davidson, Y. S., Amin, H., Kelley, T., Shi, J., Tian, J., Kumaran, R., Lashley, T., Lees, A. J., DuPlessis, D., Neary, D., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0526-z · Cited by 32

Enlarging clinical spectrum of FALS with TARDBP gene mutations: S393L variant in an Italian family showing phenotypic variability and relevance for genetic counselling

Origone, P., Caponnetto, C., Poggio, M., Ghiglione, E., Bellone, E., Ferrandes, G., Mancardi, G., & Mandich, P. (2010) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482960903165039 · Cited by 30

A novel TARDBP mutation in an Australian amyotrophic lateral sclerosis kindred

Williams, K. L., Durnall, J. C., Thoeng, A., Warraich, S. T., Nicholson, G. A., & Blair, I. P. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2008.163261 · Cited by 30

TDP-43 in skeletal muscle of patients affected with amyotrophic lateral sclerosis

Sorarú, G., Orsetti, V., Buratti, E., Baralle, F. E., Cima, V., Volpe, M., D’Ascenzo, C., Palmieri, A., Koutsikos, K., Pegoraro, E., et al. (2009) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482960902810890 · Cited by 29

TDP-43 pathology in familial British dementia

Schwab, C., Arai, T., Hasegawa, M., Akiyama, H., Yu, S. Y., & McGeer, P. L. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0514-3 · Cited by 29

TARDBP in amyotrophic lateral sclerosis: identification of a novel variant but absence of copy number variation

Bäumer, D., Parkinson, N., & Talbot, K. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2008.166512 · Cited by 28

Genetic variants in the promoter of TARDBP in sporadic amyotrophic lateral sclerosis

Luquin, N., Yu, B., Saunderson, R. B., Trent, R. J., & Pamphlett, R. (2009) · Neuromuscular Disorders · doi:10.1016/j.nmd.2009.07.005 · Cited by 26

Lack of TAR‐DNA binding protein‐43 (TDP‐43) pathology in human prion diseases

Isaacs, A. M., Powell, C., Webb, T., Linehan, J. M., Collinge, J., & Brandner, S. (2008) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2008.00963.x · Cited by 26

A protein–protein interaction of stress‐responsive myosin VI endowed to inhibit neural progenitor self‐replication with RNA binding protein, TLS, in murine hippocampus

Takarada, T., Tamaki, K., Takumi, T., Ogura, M., Ito, Y., Nakamichi, N., & Yoneda, Y. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06225.x · Cited by 25

TDP-43 inclusions do not protect motor neurons from sporadic ALS

Pamphlett, R., & Jew, S. K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0392-0 · Cited by 22

Temperature-Dependent Localization of TLS?CHOP to Splicing Factor Compartments

Göransson, M. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5566 · Cited by 20

Frontotemporal lobar degeneration with ubiquitinated tau‐negative inclusions and additional α‐synuclein pathology but also unusual cerebellar ubiquitinated p62‐positive, TDP‐43‐negative inclusions

King, A., Al‐Sarraj, S., & Shaw, C. E. (2008) · Neuropathology · doi:10.1111/j.1440-1789.2008.00966.x · Cited by 20

Translocated in liposarcoma (TLS) is a substrate for fibroblast growth factor receptor-1

Klint, P., Hellman, U., Wernstedt, C., Åman, P., Ron, D., & Claesson, L. (2003) · Cellular Signalling · doi:10.1016/j.cellsig.2003.09.007 · Cited by 11

TLS interaction with NMDA R1 splice variant in retinal ganglion cell line RGC-5

Selamat, W., Jamari, I., Wang, Y., Takumi, T., Wong, F., & Fujii, R. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.12.014 · Cited by 10

TDP-43 is not present in brain tissue of patients with schizophrenia

Mateen, F. J., & Josephs, K. A. (2008) · Schizophrenia Research · doi:10.1016/j.schres.2008.08.033 · Cited by 8

Identification of RNA Binding Specificity for the TET-family Proteins

Takahama, K., Kino, K., Arai, S., et al. (2008) · Nucleic Acids Symposium Series · doi:10.1093/nass/nrn108 · Cited by 7

Identification of DNA binding specificity for TLS

Takahama, K., Arai, S., Kurokawa, R., et al. (2009) · Nucleic Acids Symposium Series · doi:10.1093/nass/nrp124 · Cited by 7

Frontotemporal lobar degeneration: toward the end of conFUSion

Frank, S., & Tolnay, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0602-4 · Cited by 6

Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409

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

Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335

A large-scale binding and functional map of human RNA-binding proteins

Van Nostrand, E. L., Freese, P., Pratt, G. A., Wang, X., Wei, X., Xiao, R., Blue, S. M., Chen, J.-Y., Cody, N. A. L., Dominguez, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2077-3 · Cited by 1,317

Phenotype of Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia with ALS (FTD/ALS) Associated with the GGGGCC Repeat Expansion in C9ORF72 (c9FTD/ALS) (S05.003)

Boylan, K. A., DeJesus-Hernandez, M., Rush, B., Desaro, P., Johnston, A., Kryston, T., Rutherford, N., Baker, M., Wszolek, Z., Dickson, D. W., et al. (2012) · Neurology · doi:10.1212/wnl.78.1_meetingabstracts.s05.003

Nutritional and metabolic status at diagnosis and survival of patients with Amyotrophic Lateral Sclerosis (ALS) and frontotemporal dementia (FTD) compared to patients with ALS alone

Jésus, P., Sourisseau, H., Lautrette, G., et al. (2020) · HAL (Le Centre pour la Communication Scientifique Directe)

Half of the patients with amyotrophic lateral sclerosis after ventilation had apparent frontotemporal lobar atrophy: A Quantitative survey of 92 patients by CT imaging

Sugano, K., Yoshino, H., Nakazato, T., et al. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.08.2007

Current Concepts in the Classification and Diagnosis of Frontotemporal Lobar Degenerations: A Practical Approach

Rohan, Z., & Matěj, R. (2013) · Archives of Pathology & Laboratory Medicine · doi:10.5858/arpa.2012-0510-rs · Cited by 18

Genetic analysis of matrin 3 gene in French amyotrophic lateral sclerosis patients and frontotemporal lobar degeneration with amyotrophic lateral sclerosis patients

Millecamps, S., de Septenville, A. L., Teyssou, E., Daniau, M., Camuzat, A., Albert, M., Leguern, É., Galimberti, D., Brice, A., Marie, Y., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.016 · Cited by 40