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

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351

Autophagy in the Pathogenesis of Disease

Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062

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

Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria

Neary, D., Snowden, J. S., Gustafson, L., Passant, U., Stuss, D., Black, S., Freedman, M., Kertesz, A., Robert, P. H., Albert, M., et al. (1998) · Neurology · doi:10.1212/wnl.51.6.1546 · Cited by 5,047

Autophagy and Viruses: Adversaries or Allies?

Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,444

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882

Loss of autophagy in the central nervous system causes neurodegeneration in mice

Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500

Van Damme A.

Haine, M. M.-L., & Meeùs, N. (1986) · Cited by 3,464

The Microprocessor complex mediates the genesis of microRNAs

Gregory, R. I., Yan, K.-P., Amuthan, G., Chendrimada, T. P., Doratotaj, B., Cooch, N. S., & Shiekhattar, R. (2004) · Nature · doi:10.1038/nature03120 · Cited by 2,851

Biogenesis of small RNAs in animals

Kim, V. N., Han, J., & Siomi, M. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2632 · Cited by 2,814

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

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630

Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,625

Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,624

Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058

P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders

Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650

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

The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress

Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512

ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors

Boillée, S., Velde, C. V., & Cleveland, D. W. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.018 · Cited by 1,476

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391

HITS-CLIP yields genome-wide insights into brain alternative RNA processing

Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352 · cited 1×

HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.

Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234

Proteomic analysis of NMDA receptor–adhesion protein signaling complexes

Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., & Grant, S. G. N. (2000) · Nature Neuroscience · doi:10.1038/76615 · Cited by 1,194

Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration

Cairns, N. J., Bigio, E. H., Mackenzie, I. R. A., Neumann, M., Lee, V. M.-Y., Hatanpaa, K. J., White, C. L., Schneider, J. A., Grinberg, L. T., Halliday, G., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0237-2 · Cited by 1,110

Kinesin Transports RNA

Kanai, Y., Dohmae, N., & Hirokawa, N. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.022 · Cited by 1,109

Molecular biology of amyotrophic lateral sclerosis: insights from genetics

Pasinelli, P., & Brown, R. H. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1971 · Cited by 1,107

Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1

Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,017

Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update

Mackenzie, I. R. A., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I., Kril, J., Kovacs, G. G., Ghetti, B., Halliday, G., Holm, I. E., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0612-2 · Cited by 1,012

Non–cell autonomous toxicity in neurodegenerative disorders: ALS and beyond

Ilieva, H., Polymenidou, M., & Cleveland, D. W. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908164 · Cited by 1,008

Induced ncRNAs allosterically modify RNA-binding proteins in cis to inhibit transcription

Wang, X., Arai, S., Song, X., Reichart, D. R., Du, K., Pascual, G., Tempst, P., Rosenfeld, M. G., Glass, C. K., & Kurokawa, R. (2008) · Nature · doi:10.1038/nature06992 · Cited by 1,007

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

Large-Scale Proteomic Analysis of the Human SpliceosomePreprint

Rappsilber, J., Ryder, U., Lamond, A. I., & Mann, M. (2002) · Genome Research · doi:10.1101/gr.473902 · Cited by 945

TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease

Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916

Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma

Crozat, A., Åman, P., Mandahl, N., & Ron, D. (1993) · Nature · doi:10.1038/363640a0 · Cited by 897

RNA granules: post-transcriptional and epigenetic modulators of gene expression

Anderson, P., & Kedersha, N. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2694 · Cited by 885

Comprehensive proteomic analysis of the human spliceosome

Zhou, Z., Licklider, L. J., Gygi, S. P., & Reed, R. (2002) · Nature · doi:10.1038/nature01031 · Cited by 884

Prevalence and patterns of cognitive impairment in sporadic ALS

Ringholz, G. M., Appel, S. H., Bradshaw, M. R., Cooke, N., Mosnik, D. M., & Schulz, P. E. (2005) · Neurology · doi:10.1212/01.wnl.0000172911.39167.b6 · Cited by 843

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 812

Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., Beach, T. G., Buratti, E., Baralle, F., Morita, M., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21425 · Cited by 777

Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs

Ou, S.-H. I., Wu, F. K., Harrich, D., Garcı́a-Martı́nez, L. F., & Gaynor, R. B. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3584-3596.1995 · Cited by 762

HDAC6 controls autophagosome maturation essential for ubiquitin‐selective quality‐control autophagy

Lee, J., Koga, H., Kawaguchi, Y., Tang, W., Wong, E., Gao, Y., Pandey, U. B., Kaushik, S., Tresse, E., Lu, J., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.405 · Cited by 756

TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis

Van Deerlin, V. M., Leverenz, J. B., Bekris, L. M., Bird, T. D., Yuan, W., Elman, L. B., Clay, D., Wood, E. M., Chen-Plotkin, A. S., Martinez-Lage, M., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70071-1 · Cited by 723

A new subtype of frontotemporal lobar degeneration with FUS pathology

Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722

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

The overlap of amyotrophic lateral sclerosis and frontotemporal dementia

Lomen, C. E., Anderson, T. T., & Miller, B. L. (2002) · Neurology · doi:10.1212/wnl.59.7.1077 · Cited by 699

Characterization and Functional Implications of the RNA Binding Properties of Nuclear Factor TDP-43, a Novel Splicing Regulator ofCFTR Exon 9

Buratti, E., & Baralle, F. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104236200 · Cited by 697

Aberrant RNA Processing in a Neurodegenerative Disease: the Cause for Absent EAAT2, a Glutamate Transporter, in Amyotrophic Lateral Sclerosis

Lin, C.-L., Bristol, L. A., Jin, L., Dykes‐Hoberg, M., Crawford, T. O., Clawson, L., & Rothstein, J. D. (1998) · Neuron · doi:10.1016/s0896-6273(00)80997-6 · Cited by 672

Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation

Winton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800342200 · Cited by 660

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 643

Nuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping

Buratti, E., Dörk, T., Zuccato, E., Pagani, F., Romano, M., & Baralle, F. E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1774 · Cited by 633

TDP‐43 A315T mutation in familial motor neuron disease

Gitcho, M. A., Baloh, R. H., Chakraverty, S., Mayo, K., Norton, J. B., Levitch, D., Hatanpaa, K. J., White, C. L., Bigio, E. H., Caselli, R. J., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21344 · Cited by 633

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Zhang, Y., Xu, Y.-F., Cook, C. N., Gendron, T. F., Roettges, P. S., Link, C. D., Lin, W.-L., Tong, J., Castanedes‐Casey, M., Ash, P. E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900688106 · Cited by 614

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 608

TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration

Wils, H., Kleinberger, G., Janssens, J., Pereson, S., Joris, G., Cuijt, I., Smits, V., Groote, C. C., Broeckhoven, C. V., & Kumar‐Singh, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912417107 · Cited by 602

RNA polymerase II and the integration of nuclear eventsPreprint

Hirose, Y., & Manley, J. L. (2000) · Genes & Development · doi:10.1101/gad.14.12.1415 · Cited by 577

An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells

Yeo, G. W., Coufal, N. G., Liang, T. Y., Peng, G. E., Fu, X.-D., & Gage, F. H. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1545 · Cited by 572

Fusion of the dominant negative transcription regulator CHOP with a novel gene FUS by translocation t(12;16) in malignant liposarcoma

Rabbitts, T. H., Forster, A. M., Larson, R., & Nathan, P. (1993) · Nature Genetics · doi:10.1038/ng0693-175 · Cited by 559

TDP‐43 is recruited to stress granules in conditions of oxidative insult

Colombrita, C., Zennaro, E., Fallini, C., Weber, M., Sommacal, A., Buratti, E., Silani, V., & Ratti, A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06383.x · Cited by 557

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

TDP-43 in Familial and Sporadic Frontotemporal Lobar Degeneration with Ubiquitin Inclusions

Cairns, N. J., Neumann, M., Bigio, E. H., Holm, I. E., Troost, D., Hatanpaa, K. J., Foong, C., White, C. L., Schneider, J. A., Kretzschmar, H. A., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070182 · Cited by 545

RNA editing and death of motor neurons

Kawahara, Y., Ito, K., Sun, H. J., Aizawa, H., Kanazawa, I., & Kwak, S. (2004) · Nature · doi:10.1038/427801a · Cited by 536

Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery

Freibaum, B. D., Chitta, R. K., High, A. A., & Taylor, J. P. (2009) · Journal of Proteome Research · doi:10.1021/pr901076y · Cited by 529

Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease

Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494

Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease

Buratti, E. (2007) · Frontiers in bioscience · doi:10.2741/2727 · Cited by 493

Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice

Yin, F., Banerjee, R., Thomas, B., Zhou, P., Qian, L., Jia, T., Ma, X., Ma, Y., Iadecola, C., Beal, M. F., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20091568 · Cited by 480

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

Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases

Nakashima-Yasuda, H., Uryu, K., Robinson, J., Xie, S. X., Hurtig, H., Duda, J. E., Arnold, S. E., Siderowf, A., Grossman, M., Leverenz, J. B., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0261-2 · Cited by 468

Novel Mutations in TARDBP (TDP-43) in Patients with Familial Amyotrophic Lateral Sclerosis

Rutherford, N. J., Zhang, Y., Baker, M. C., Gass, J. M., Finch, N. A., Xu, Y., Stewart, H. G., Kelley, B. J., Kuntz, K., Crook, R., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000193 · Cited by 465

VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD

Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437

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 437

Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations

Mackenzie, I. R., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I. I., Kril, J. J., Kovács, G. G., Ghetti, B. F., Halliday, G. M., Holm, I. E., et al. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0460-5 · Cited by 425

Concurrence of TDP-43, tau and α-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies

Higashi, S., Iseki, E., Yamamoto, R., Minegishi, M., Hino, H., Fujisawa, K., Togo, T., Katsuse, O., Uchikado, H., Furukawa, Y., et al. (2007) · Brain Research · doi:10.1016/j.brainres.2007.09.048 · Cited by 421

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity

Johnson, B. S., McCaffery, J. M., Lindquist, S. L., & Gitler, A. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802082105 · Cited by 416

HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregatesPreprint

Boyault, C., Zhang, Y., Fritah, S., Caron, C., Gilquin, B., Kwon, S. H., Garrido, C., Yao, T., Vourc’h, C., Matthias, P., et al. (2007) · Genes & Development · doi:10.1101/gad.436407 · Cited by 387

Human, Drosophila, and C.elegans TDP43: Nucleic Acid Binding Properties and Splicing Regulatory Function

Ayala, Y. M., Pantano, S., D’Ambrogio, A., Buratti, E., Brindisi, A., Marchetti, C., Romano, M., & Baralle, F. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.038 · Cited by 382

Concomitant TAR-DNA-Binding Protein 43 Pathology Is Present in Alzheimer Disease and Corticobasal Degeneration but Not in Other Tauopathies

Uryu, K., Nakashima-Yasuda, H., Forman, M. S., Kwong, L. K., Clark, C. M., Grossman, M., Miller, B. L., Kretzschmar, H. A., Lee, V. M.-Y., Trojanowski, J. Q., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31817713b5 · Cited by 382

TDP ‐ 43 mutation in familial amyotrophic lateral sclerosis

Yokoseki, A., Shiga, A., Tan, C., Tagawa, A., Kaneko, H., Koyama, A., Eguchi, H., Tsujino, A., Ikeuchi, T., Kakita, A., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21392 · Cited by 373

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

TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

Sephton, C. F., Good, S. K., Atkin, S., Dewey, C. M., Mayer, P., Herz, J., & Yu, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061846 · Cited by 370

Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies

Igaz, L. M., Kwong, L. K., Chen‐Plotkin, A. S., Winton, M. J., Unger, T. L., Xu, Y., Neumann, M., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809462200 · Cited by 367

hTAF(II)68, a novel RNA/ssDNA‐binding protein with homology to the pro‐oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II.

Bertolotti, A., Lutz, Y., Heard, D. J., Chambon, P., & Tora, L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00882.x · Cited by 363

TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein

Strong, M. J., Volkening, K., Hammond, R. R., Yang, W., Strong, W., Leystra‐Lantz, C., & Shoesmith, C. L. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.03.007 · Cited by 362

The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response

Andersson, M. K., Ståhlberg, A., Arvidsson, Y., Olofsson, A., Semb, H., Stenman, G., Nilsson, O., & Åman, P. (2008) · BMC Cell Biology · doi:10.1186/1471-2121-9-37 · Cited by 354

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

TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling

Zinszner, H., Sok, J., Immanuel, D., Yin, Y., & Ron, D. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.15.1741 · Cited by 350

SC35 autoregulates its expression by promoting splicing events that destabilize its mRNAs

Sureau, A., Gattoni, R., Dooghe, Y., Ste'venin, J., & Soret, J. (2001) · EMBO Journal · doi:10.1093/emboj/20.7.1785 · Cited by 347

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

TDP‐43, the signature protein of FTLD‐U, is a neuronal activity‐responsive factor

Wang, I., Wu, L., Chang, H., & Shen, C. ‐. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05190.x · Cited by 345

Structural insights into TDP-43 in nucleic-acid binding and domain interactions

Kuo, P. H., Doudeva, L. G., Wang, Y.-T., Shen, C. ‐. J., & Yuan, H. S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp013 · Cited by 339

TDP-43 in the Ubiquitin Pathology of Frontotemporal Dementia With VCP Gene Mutations

Neumann, M., Mackenzie, I. R., Cairns, N. J., Boyer, P. J., Markesbery, W. R., Smith, C. D., Taylor, J. P., Kretzschmar, H. A., Kimonis, V. E., & Forman, M. S. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31803020b9 · Cited by 334

Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Igaz, L. M., Kwong, L. K., Xu, Y., Truax, A. C., Uryu, K., Neumann, M., Clark, C. M., Elman, L. B., Miller, B. L., Grossman, M., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080003 · Cited by 332

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 322

The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology

Fujii, R., Okabe, S., Urushido, T., Inoue, K., Yoshimura, A., Tachibana, T., Nishikawa, T., Hicks, G. G., & Takumi, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.01.058 · Cited by 322

Pathological Heterogeneity of Frontotemporal Lobar Degeneration with Ubiquitin-Positive Inclusions Delineated by Ubiquitin Immunohistochemistry and Novel Monoclonal Antibodies

Sampathu, D. M., Neumann, M., Kwong, L. K., Chou, T. T. T., Micsenyi, M. C., Truax, A. C., BRUCE, J. S., Grossman, M., Trojanowski, J. Q., & Lee, V. M. ‐. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060438 · Cited by 321

DCTN1 mutations in Perry syndrome

Farrer, M. J., Hulihan, M., Kachergus, J. M., Dächsel, J. C., Stoessl, A. J., Grantier, L. L., Calne, S. M., Calne, D. B., Lechevalier, B., Chapon, F., et al. (2009) · Nature Genetics · doi:10.1038/ng.293 · Cited by 320

Depletion of TDP‐43 affects Drosophila motoneurons terminal synapsis and locomotive behavior

Feiguin, F. M., Godena, V. K., Romano, G., D’Ambrogio, A., Klima, R., & Baralle, F. E. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.04.019 · Cited by 310

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 310

Evidence of Multisystem Disorder in Whole-Brain Map of Pathological TDP-43 in Amyotrophic Lateral Sclerosis

Geser, F., Brandmeir, N. J., Kwong, L. K., Martinez‐Lage, M., Elman, L. B., McCluskey, L. F., Xie, S. X., Lee, V. M. ‐., & Trojanowski, J. Q. (2008) · Archives of Neurology · doi:10.1001/archneur.65.5.636 · Cited by 308

Structural diversity and functional implications of the eukaryotic TDP gene family

Wang, H., Wang, I., Bose, J. K., & Shen, C. ‐. J. (2003) · Genomics · doi:10.1016/s0888-7543(03)00214-3 · Cited by 306

Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method

Hartmuth, K., Urlaub, H., Vornlocher, H., Will, C. L., Gentzel, M., Wilm, M. S., & Lührmann, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262483899 · Cited by 302

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 300

Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43

Davidson, Y. S., Kelley, T., Mackenzie, I. R., Pickering-Brown, S. M., du Plessis, D., Neary, D., Snowden, J. S., & Mann, D. M. A. (2007) · Acta Neuropathologica · doi:10.1007/s00401-006-0189-y · Cited by 299

Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death

Hicks, G. G., Singh, N., Nashabi, A., Mai, S., Bozek, G., Klewes, L., Arapovic, D., White, E. K., Koury, M. J., Oltz, E. M., et al. (2000) · Nature Genetics · doi:10.1038/72842 · Cited by 299

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

LINE-1 ORF1 Protein Localizes in Stress Granules with Other RNA-Binding Proteins, Including Components of RNA Interference RNA-Induced Silencing Complex

Goodier, J. L., Zhang, L., Vetter, M. R., & Kazazian, H. H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00332-07 · Cited by 292

Characterization of an RNA Granule from Developing Brain

Elvira, G., Wasiak, S., Blandford, V., Tong, X.-K., Serrano, A., Fan, X., del Rayo Sánchez-Carbente, M., Servant, F., Bell, A. W., Boismenu, D., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500255-mcp200 · Cited by 287

Genetics of familial amyotrophic lateral sclerosis

Valdmanis, P. N., & Rouleau, G. A. (2008) · Neurology · doi:10.1212/01.wnl.0000296811.19811.db · Cited by 286

The TET Family of Proteins: Functions and Roles in Disease

Tan, A. Y., & Manley, J. L. (2009) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjp025 · Cited by 282

HDAC6–p97/VCP controlled polyubiquitin chain turnover

Boyault, C., Gilquin, B., Zhang, Y., Rybin, V., Garman, E. F., Meyer‐Klaucke, W., Matthias, P., Müller, C. W., & Khochbin, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601210 · Cited by 280

A Drosophila model for TDP-43 proteinopathy

Li, Y., Ray, P., Rao, E. J., Chen, S., Guo, W., Chen, X., Woodruff, E. A., Fushimi, K., & Wu, J. Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913602107 · Cited by 279

Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease

Schwab, C., Arai, T., Hasegawa, M., Yu, S. Y., & McGeer, P. L. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e8951 · Cited by 277

EWS, but Not EWS-FLI-1, Is Associated with Both TFIID and RNA Polymerase II: Interactions between Two Members of the TET Family, EWS and hTAF II 68, and Subunits of TFIID and RNA Polymerase II Complexes

Bertolotti, A., Melot, T., Acker, J., Vigneron, M., Delattre, O., & Tora, L. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1489 · Cited by 265

FUS mutations in amyotrophic lateral sclerosis: clinical, pathological, neurophysiological and genetic analysis

Blair, I. P., Williams, K. L., Warraich, S. T., Durnall, J. C., Thoeng, A., Manavis, J., Blumbergs, P. C., Vucic, S., Kiernan, M. C., & Nicholson, G. A. (2009) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2009.194399 · Cited by 264

A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP.Preprint

Zinszner, H., Albalat, R., & Ron, D. (1994) · Genes & Development · doi:10.1101/gad.8.21.2513 · Cited by 263

RNA and RNA Binding Proteins Participate in Early Stages of Cell Spreading through Spreading Initiation Centers

de Hoog, C. L., Foster, L. J., & Mann, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00456-8 · Cited by 262

FUS pathology in basophilic inclusion body disease

Muñoz, D. G., Neumann, M., Kusaka, H., Yokota, O., Ishihara, K., Terada, S., Kuroda, S., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0598-9 · Cited by 259

Abnormal TDP-43 immunoreactivity in AD modifies clinicopathologic and radiologic phenotype

Josephs, K. A., Whitwell, J. L., Knopman, D. S., Hu, W. T., Stroh, D. A., Baker, M., Rademakers, R., Boeve, B. F., Parisi, J. E., Smith, G. E., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000304041.09418.b1 · Cited by 258

Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

Neumann, M., Roeber, S., Kretzschmar, H. A., Rademakers, R., Baker, M. C., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0581-5 · Cited by 257

TDP‐43, a neuro‐pathosignature factor, is essential for early mouse embryogenesis

Wu, L., Cheng, W., Hou, S., Yan, Y., Jiang, S., & Shen, C. ‐. J. (2010) · genesis · doi:10.1002/dvg.20584 · Cited by 256

Mutation within TARDBP leads to Frontotemporal Dementia without motor neuron disease

Borroni, B., Bonvicini, C., Alberici, A., Buratti, E., Agosti, C., Archetti, S., Papetti, A., Stuani, C., Luca, M. D., Gennarelli, M., et al. (2009) · Human Mutation · doi:10.1002/humu.21100 · Cited by 254

TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines

Fujii, R., & Takumi, T. (2005) · Journal of Cell Science · doi:10.1242/jcs.02692 · Cited by 253

Male sterility and enhanced radiation sensitivity in TLS−/− mice

Kuroda, M., Sok, J., Webb, L., Baechtold, H., Urano, F., Yin, Y., Chung, P., de Rooij, D. G., Akhmedov, A., Ashley, T., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.3.453 · Cited by 248

TDP-43 is deposited in the Guam parkinsonism-dementia complex brains

Hasegawa, M., Arai, T., Akiyama, H., Nonaka, T., Mori, H., Hashimoto, T., Yamazaki, M., & Oyanagi, K. (2007) · Brain · doi:10.1093/brain/awm065 · Cited by 242

TDP-43-Positive White Matter Pathology in Frontotemporal Lobar Degeneration With Ubiquitin-Positive Inclusions

Neumann, M., Kwong, L. K., Truax, A. C., Vanmassenhove, B., Kretzschmar, H. A., Deerlin, V. M. V., Clark, C. M., Grossman, M., Miller, B. L., Trojanowski, J. Q., et al. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000248554.45456.58 · Cited by 238

TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression

Ayala, Y. M., Misteli, T., & Baralle, F. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800546105 · Cited by 235

Knockdown of transactive response DNA‐binding protein (TDP‐43) downregulates histone deacetylase 6

Fiesel, F. C., Voigt, A., Weber, S. S., den Haute, C. V., Waldenmaier, A., Görner, K., Walter, M. J., Anderson, M. L., Kern, J. V., Rasse, T. M., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.324 · Cited by 232

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene

Mercado, P. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki897 · Cited by 226

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 226

Genetic contribution of FUS to frontotemporal lobar degeneration

Langenhove, T. V., van der Zee, J., Sleegers, K., Engelborghs, S., Vandenberghe, R. R., Gijselinck, I., den Broeck, M. V., Mattheijssens, M., Peeters, K., Deyn, P. P. D., et al. (2010) · Neurology · doi:10.1212/wnl.0b013e3181ccc732 · Cited by 225

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 221

Rapidly progressive aphasic dementia and motor neuron disease

Caselli, R. J., Windebank, A., Petersen, R. C., Komori, T., Parisi, J. E., Okazaki, H., Kokmen, E., Iverson, R. A., Dinapoli, R., Graff-Radford, N., et al. (1993) · Annals of Neurology · doi:10.1002/ana.410330210 · Cited by 214

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 213

Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: Implications for TDP-43 in the physiological response to neuronal injury

Moisse, K., Volkening, K., Leystra-Lantz, C., Welch, I., Hill, T., & Strong, M. J. (2009) · Brain Research · doi:10.1016/j.brainres.2008.10.021 · Cited by 210

Transgenic Rat Model of Neurodegeneration Caused by Mutation in the TDP Gene

Zhou, H., Huang, C., Chen, H., Wang, D., Landel, C. P., Xia, P. Y., Bowser, R. P., Liu, Y.-J., & Xia, X. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000887 · Cited by 209

Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system

Wang, X., Fan, H., Ying, Z., Li, B., Wang, H., & Wang, G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.055 · Cited by 207

TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea

Kovács, G. G., Murrell, J. R., Horvath, S., Haraszti, L., Majtényi, K., Molnár, M. J., Budka, H., Ghetti, B. F., & Spina, S. (2009) · Movement Disorders · doi:10.1002/mds.22697 · Cited by 207

Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone

Custer, S. K., Neumann, M., Lu, H., Wright, A. C., & Taylor, J. P. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq050 · Cited by 204

TLS, EWS and TAF15: a model for transcriptional integration of gene expression

Law, W. J. (2006) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/ell015 · Cited by 203

Sarcoplasmic redistribution of nuclear TDP‐43 in inclusion body myositis

Salajegheh, M. K., Pinkus, J. L., Taylor, J. P., Amato, A. A., Nazareno, R., Baloh, R. H., & Greenberg, S. A. (2009) · Muscle & Nerve · doi:10.1002/mus.21386 · Cited by 203

Cognitive change in motor neurone disease/amyotrophic lateral sclerosis (MND/ALS)

Neary, D., Snowden, J. S., & Mann, D. M. A. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00425-1 · Cited by 198

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 198

Identification of an RNA Binding Specificity for the Potential Splicing Factor TLS

Lerga, A., Hallier, M., Delva, L., Orvain, C., Gallais, I., Marie, J., & Moreau-Gachelin, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008304200 · Cited by 193

The role of hypothermia in the management of severe brain injury: a meta-analysis.

Harris, O. A., Colford, J. M., Good, M. C., et al. (2002) · PubMed · doi:10.1001/archneur.59.7.1077 · Cited by 192

Pathological TDP-43 in parkinsonism–dementia complex and amyotrophic lateral sclerosis of Guam

Geser, F., Winton, M. J., Kwong, L. K., Xu, Y., Xie, S. X., Igaz, L. M., Garruto, R. M., Perl, D. P., Galasko, D. R., Lee, V. M. ‐., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0257-y · Cited by 190

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 189

Myosin-Va Facilitates the Accumulation of mRNA/Protein Complex in Dendritic Spines

Yoshimura, A., Fujii, R., Watanabe, Y., Okabe, S., Fukui, K., & Takumi, T. (2006) · Current Biology · doi:10.1016/j.cub.2006.10.024 · Cited by 187

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

p54nrb associates with the 5′ splice site within large transcription/splicing complexes

Kameoka, S., Duque, P., & Konarska, M. M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600187 · Cited by 186

Molecular Neuropathology of TDP-43 Proteinopathies

Neumann, M. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10010232 · Cited by 172

TDP-43 Overexpression Enhances Exon 7 Inclusion during the Survival of Motor Neuron Pre-mRNA Splicing

Bose, J. K., Wang, I., Li, H., Tarn, W., & Shen, C. ‐. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805376200 · Cited by 172

Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation

Baechtold, H., Kuroda, M., Sok, J. C., Ron, D., López, B. S., & Akhmedov, A. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34337 · Cited by 171

Mutations of FUS gene in sporadic amyotrophic lateral sclerosis

Corrado, L., Bo, R. D., Castellotti, B., Ratti, A., Cereda, C., Penco, S., Sorarú, G., Carlomagno, Y., Ghezzi, S., Pensato, V., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.071027 · Cited by 170

Rapamycin Rescues TDP-43 Mislocalization and the Associated Low Molecular Mass Neurofilament Instability

Caccamo, A., Majumder, S., Deng, J. J., Bai, Y., Thornton, F. B., & Oddo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031278 · Cited by 169

Missense Mutations in the Progranulin Gene Linked to Frontotemporal Lobar Degeneration with Ubiquitin-immunoreactive Inclusions Reduce Progranulin Production and Secretion

Shankaran, S. S., Capell, A., Hruscha, A., Fellerer, K., Neumann, M., Schmid, B., & Haass, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705115200 · Cited by 168

TARDBP 3′-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy

Gitcho, M. A., Bigio, E. H., Mishra, M., Johnson, N., Weıntraub, S., Mesulam, M. M., Rademakers, R., Chakraverty, S., Cruchaga, C., Morris, J. C., et al. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0571-7 · Cited by 168

Domain Architectures and Characterization of an RNA-binding Protein, TLS

Iko, Y., Kodama, T. S., Kasai, N., Oyama, T., Morita, E. H., Muto, T., Okumura, M., Fujii, R., Takumi, T., Tate, S.-I., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408552200 · Cited by 168

Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein.

Chansky, H. A., Hu, M., Hickstein, D. D., & Yang, L. (2001) · PubMed · Cited by 166

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 166

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 166

Expression Patterns of the Human Sarcoma-Associated GenesFUSandEWSand the Genomic Structure ofFUS

Åman, P., Panagopoulos, I., Lassen, C., Fioretos, T., Mencinger, M., Toresson, H., Höglund, M., Forster, A., Rabbitts, T. H., Ron, D., et al. (1996) · Genomics · doi:10.1006/geno.1996.0513 · Cited by 165

Frequency of ubiquitin and FUS-positive, TDP-43-negative frontotemporal lobar degeneration

Seelaar, H., Klijnsma, K. Y., de Koning, I., van der Lugt, A., Chiu, W. Z., Azmani, A., Rozemüller, A. J. M., & Swieten, J. C. V. (2009) · Journal of Neurology · doi:10.1007/s00415-009-5404-z · Cited by 165

Early or late appearance of "dropped head syndrome" in amyotrophic lateral sclerosis

Gourie‐Devi, M. (2003) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.74.5.683 · Cited by 164

Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort

Ticozzi, N., Silani, V., LeClerc, A. L., Keagle, P. J., Gellera, C., Ratti, A., Taroni, F., Kwiatkowski, T. J., McKenna‐Yasek, D., Sapp, P. C., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181bbff05 · Cited by 163

Two German Kindreds With Familial Amyotrophic Lateral Sclerosis Due to TARDBP Mutations

Kühnlein, P., Sperfeld, A., Vanmassenhove, B., Deerlin, V. M. V., Lee, V. M. ‐., Trojanowski, J. Q., Kretzschmar, H. A., Ludolph, A. C., & Neumann, M. (2008) · Archives of Neurology · doi:10.1001/archneur.65.9.1185 · Cited by 161

Involvement of the Pro-oncoprotein TLS (Translocated in Liposarcoma) in Nuclear Factor-κB p65-mediated Transcription as a Coactivator

Uranishi, H., Tetsuka, T., Yamashita, M., Asamitsu, K., Shimizu, M., Itoh, M., & Okamoto, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011176200 · Cited by 158

De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis

DeJesus‐Hernandez, M., Kocerha, J., Finch, N. A., Crook, R., Baker, M. C., Desaro, P., Johnston, A., Rutherford, N. J., Wojtas, A., Kennelly, K. D., et al. (2010) · Human Mutation · doi:10.1002/humu.21241 · Cited by 158

Detection of Arginine Dimethylated Peptides by Parallel Precursor Ion Scanning Mass Spectrometry in Positive Ion Mode

Rappsilber, J., Friesen, W. J., Paushkin, S. V., Dreyfuss, G., & Mann, M. (2003) · Analytical Chemistry · doi:10.1021/ac026283q · Cited by 153

TLS/FUS fusion domain of TLS/FUS-erg chimeric protein resulting from the t(16;21) chromosomal translocation in human myeloid leukemia functions as a transcriptional activation domain.

Prasad, D. D. K., Ouchida, M., Lee, L., Rao, V. N., & Reddy, E. S. P. (1994) · PubMed · Cited by 147

Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis

Chen, A. K.-H., Lin, R. Y., Hsieh, E. Z.-J., Tu, P., Chen, R. P. ‐., Liao, T., Chen, W., Wang, C., & Huang, J. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9066207 · Cited by 145

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

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

Atypical frontotemporal lobar degeneration with ubiquitin-positive, TDP-43-negative neuronal inclusions

Mackenzie, I. R., Foti, D. J., Woulfe, J., & Hurwitz, T. A. (2008) · Brain · doi:10.1093/brain/awn061 · Cited by 144

p97: The Cell's Molecular Purgatory?

Halawani, D., & Latterich, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.003 · Cited by 143

TDP-43 in differential diagnosis of motor neuron disorders

Dickson, D. W., Josephs, K. A., & Amador, C. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0234-5 · Cited by 143

A Reassessment of the Neuropathology of Frontotemporal Dementia Linked to Chromosome 3

Holm, I. E., Englund, E. M., Mackenzie, I. R., Johannsen, P., & Isaacs, A. M. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181567f02 · Cited by 141

Impaired Protein Aggregate Handling and Clearance Underlie the Pathogenesis of p97/VCP-associated Disease

Ju, J.-S., Miller, S., Hanson, P. I., & Weihl, C. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805517200 · Cited by 140

Sporadic ALS has compartment-specific aberrant exon splicing and altered cell–matrix adhesion biology

Rabin, S. J., Kim, J. M., Baughn, M. W., Libby, R. T., Kim, Y. J., Fan, Y., Libby, R. T., Spada, A. R. L., Stone, B. C., & Ravits, J. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp498 · Cited by 137

The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS

Hallier, M., Lerga, A., Barnache, S., Tavitian, A., & Moreau-Gachelin, F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4838 · Cited by 136

Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease

Hu, W. T., Josephs, K. A., Knopman, D. S., Boeve, B. F., Dickson, D. W., Petersen, R. C., & Parisi, J. E. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0400-4 · Cited by 136

Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases

Lin, W.-L., & Dickson, D. W. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0408-9 · Cited by 135

Two Italian kindreds with familial amyotrophic lateral sclerosis due to FUS mutation

Chiò, A., Restagno, G., Brunetti, M., Ossola, I., Calvo, A., Mora, G., Sabatelli, M., Monsurrò, M. R., Battistini, S., Mandrioli, J., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.001 · Cited by 135

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

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

p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis

Nogalska, A., Terracciano, C., D’Agostino, C., King Engel, W., & Askanas, V. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0564-6 · Cited by 134

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

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

Ubiquilin Modifies TDP-43 Toxicity in a Drosophila Model of Amyotrophic Lateral Sclerosis (ALS)

Hanson, K. A., Kim, S. H., Wassarman, D. A., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.078527 · Cited by 133

Mutations in FUS cause FALS and SALS in French and French Canadian populations

Belzil, V., Valdmanis, P. N., Dion, P. A., Daoud, H., Kabashi, E., Noreau, A., Gauthier, J., Hince, P., Desjarlais, A., Bouchard, J. P., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181bbfeef · Cited by 133

Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching

Lu, Y., Ferris, J., & Gao, F. (2009) · Molecular Brain · doi:10.1186/1756-6606-2-30 · Cited by 130

TLS-ERG Leukemia Fusion Protein Inhibits RNA Splicing Mediated by Serine-Arginine Proteins

Yang, L., Embree, L. J., & Hickstein, D. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3345-3354.2000 · Cited by 130

A novel progranulin mutation associated with variable clinical presentation and tau, TDP43 and alpha-synuclein pathology

Leverenz, J. B., Yu, C. E., Montine, T. J., Steinbart, E., Bekris, L. M., Zabetian, C., Kwong, L. K., Lee, V. M.-Y., Schellenberg, G. D., & Bird, T. D. (2007) · Brain · doi:10.1093/brain/awm069 · Cited by 129

TLS/FUS, a pro‐oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL‐mediated leukemogenesis

Perrotti, D., Bonatti, S., Trotta, R., Martinez, R., Skorski, T., Salomoni, P., Grassilli, E., Iozzo, R. V., Cooper, D. R., & Calabretta, B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4442 · Cited by 128

Evaluation of subcortical pathology and clinical correlations in FTLD-U subtypes

Josephs, K. A., Stroh, A., Dugger, B. N., & Dickson, D. W. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0547-7 · Cited by 126

Lack of TDP-43 abnormalities in mutant SOD1 transgenic mice shows disparity with ALS

Robertson, J., Sanelli, T. R., Xiao, S., Yang, W., Horne, P., Hammond, R. R., Pioro, E. P., & Strong, M. J. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.03.066 · Cited by 125

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

TDP-43: an emerging new player in neurodegenerative diseases

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

The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases

Doi, H., Koyano, S., Suzuki, Y., et al. (2009) · Neuroscience Research · doi:10.1016/j.neures.2009.10.004 · Cited by 122

TDP-43 Dimerizes in Human Cells in Culture

Shiina, Y., Arima, K., Tabunoki, H., et al. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9489-9 · Cited by 122

Potentiation of Amyotrophic Lateral Sclerosis (ALS)-associated TDP-43 Aggregation by the Proteasome-targeting Factor, Ubiquilin 1

Kim, S. H., Shi, Y., Hanson, K. A., Williams, L. M., Sakasai, R., Bowler, M. J., & Tibbetts, R. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808064200 · Cited by 120

RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells

Doi, H., Okamura, K., Bauer, P. O., Furukawa, Y., Shimizu, H., Kurosawa, M., Machida, Y., Miyazaki, H., Mitsui, K., Kuroiwa, Y., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705306200 · Cited by 119

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

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

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