Understanding the role of TDP-43 and FUS/TLS in ALS and beyond

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

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

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

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The Microprocessor complex mediates the genesis of microRNAs

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TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

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

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

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Transgenic strategies for combinatorial expression of fluorescent proteins in the nervous system

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Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia

Boillée, S., Yamanaka, K., Lobsiger, C. S., Copeland, N. G., Jenkins, N. A., Kassiotis, G., Kollias, G., & Cleveland, D. W. (2006) · Science · doi:10.1126/science.1123511 · Cited by 1,623 · see citing works

TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Velde, C. V., Bouchard, J.-P., Lacomblez, L., Pochigaeva, K., Salachas, F., et al. (2008) · Nature Genetics · doi:10.1038/ng.132 · Cited by 1,544 · see citing works

ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors

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ALS-Linked SOD1 Mutant G85R Mediates Damage to Astrocytes and Promotes Rapidly Progressive Disease with SOD1-Containing Inclusions

Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., et al. (1997) · Neuron · doi:10.1016/s0896-6273(00)80272-x · Cited by 1,341 · see citing works

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

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Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Elden, A. C., Kim, H.-J., Hart, M. P., Chen‐Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R. A., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,327 · see citing works

Mutations of optineurin in amyotrophic lateral sclerosis

Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265 · see citing works

Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS

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Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2778 · Cited by 1,165 · see citing works

Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis

Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140 · see citing works

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

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · see citing works

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 · see citing works

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 977 · see citing works

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

Rosen, D. (1993) · Nature · doi:10.1038/364362c0 · Cited by 922 · see citing works

A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)

Ong, S., & Mann, M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.427 · Cited by 898 · see citing works

Wild-type microglia extend survival in PU.1 knockout mice with familial amyotrophic lateral sclerosis

Beers, D. R., Henkel, J. S., Xiao, Q., Zhao, W., Wang, J., Yen, A. A., Siklos, L., McKercher, S. R., & Appel, S. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607423103 · Cited by 733 · see citing works

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 · see citing works

TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration

Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M., & Baloh, R. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908767106 · Cited by 706 · see citing works

ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis

Greenway, M. J., Andersen, P. M., Russ, C., Ennis, S., Cashman, S., Donaghy, C. G., Patterson, V., Swingler, R. J., Kieran, D., Prehn, J. H. M., et al. (2006) · Nature Genetics · doi:10.1038/ng1742 · Cited by 668 · see citing works

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 619 · see citing works

TDP‐43 regulates its mRNA levels through a negative feedback loop

Ayala, Y. M., Conti, L. D., Avendaño-Vázquez, S. E., Dhir, A., Romano, M., D’Ambrogio, A., Tollervey, J. R., Ule, J., Baralle, M., Buratti, E., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.310 · Cited by 618 · see citing works

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 592 · see citing works

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

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

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules

Bosco, D. A., Lemay, N., Ko, H. K., Zhou, H., Burke, C., Kwiatkowski, T. J., Sapp, P. C., McKenna-Yasek, D. M., Brown, R. H., & Hayward, L. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq335 · Cited by 520 · see citing works

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 514 · see citing works

ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS

Ling, S., de Albuquerque, C. P., Han, J. S., Lagier‐Tourenne, C., Tokunaga, S., Zhou, H., & Cleveland, D. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008227107 · Cited by 450 · see citing works

Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice

Igaz, L. M., Kwong, L. K., Lee, E. B., Chen‐Plotkin, A. S., Swanson, E., Unger, T. L., Malunda, J. A., Xu, Y., Winton, M. J., Trojanowski, J. Q., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44867 · Cited by 434 · see citing works

Identification of Neuronal RNA Targets of TDP-43-containing Ribonucleoprotein Complexes

Sephton, C. F., Cenik, C., Küçükural, A., Dammer, E. B., Cenik, B., Han, Y., Dewey, C. M., Roth, F. P., Herz, J., Peng, J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190884 · Cited by 429 · see citing works

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

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

Atomic structure and chemistry of human serum albumin

He, X. M., & Carter, D. C. (1993) · Nature · doi:10.1038/364362b0 · Cited by 415 · see citing works

Deleterious Variants of FIG4, a Phosphoinositide Phosphatase, in Patients with ALS

Chow, C. Y., Landers, J. E., Bergren, S. K., Sapp, P. C., Grant, A. E., Jones, J. M., Everett, L., Lenk, G. M., McKenna-Yasek, D. M., Weisman, L. S., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.12.010 · Cited by 407 · see citing works

Familial amyotrophic lateral sclerosis with frontotemporal dementia is linked to a locus on chromosome 9p13.2–21.3

Vance, C. A., Al‐Chalabi, A., Ruddy, D., Smith, B. N., Hu, X., Sreedharan, J., Siddique, T., Schelhaas, H. J., Küsters, B., Troost, D., et al. (2006) · Brain · doi:10.1093/brain/awl030 · Cited by 392 · see citing works

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 · see citing works

A locus on chromosome 9p confers susceptibility to ALS and frontotemporal dementia

Morita, M., Al‐Chalabi, A., Andersen, P. M., Hosler, B. A., Sapp, P. C., Englund, E. M., Mitchell, J. E., Habgood, J., de Belleroche, J., Xi, J., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000200048.53766.b4 · Cited by 356 · see citing works

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Kraemer, B. C., Schuck, T., Wheeler, J. M., Robinson, L. C., Trojanowski, J. Q., Lee, V. M. Y., & Schellenberg, G. D. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0659-0 · Cited by 350 · see citing works

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 349 · see citing works

Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice

Shan, X., Chiang, P., Price, D. L., & Wong, P. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003459107 · Cited by 312 · see citing works

Deletion of TDP-43 down-regulates Tbc1d1 , a gene linked to obesity, and alters body fat metabolism

Chiang, P., Ling, J. P., Jeong, Y. H., Price, D. L., Aja, S. M., & Wong, P. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002176107 · Cited by 303 · see citing works

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 303 · see citing works

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

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A Drosophila model for TDP-43 proteinopathy

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Chromosome 9p21 in amyotrophic lateral sclerosis in Finland: a genome-wide association study

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

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

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 · see citing works

Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase

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Neurotoxic effects of TDP-43 overexpression in C. elegans

Ash, P. E. A., Zhang, Y., Roberts, C. M., Saldi, T. K., Hutter, H., Buratti, E., Petrucelli, L., & Link, C. D. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq230 · Cited by 248 · see citing works

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 245 · see citing works

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

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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 226 · see citing works

Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U

Tsai, K., Yang, C.-H., Fang, Y.-H., Cho, K.-H., Chien, W., Wang, W., Wu, T., Lin, C., Fu, W., & Shen, C.-K. J. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20092164 · Cited by 226 · see citing works

Phosphorylation Promotes Neurotoxicity in aCaenorhabditis elegansModel of TDP-43 Proteinopathy

Liachko, N. F., Guthrie, C. R., & Kraemer, B. C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2911-10.2010 · Cited by 222 · see citing works

Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA*

Kim, S. H., Shanware, N. P., Bowler, M. J., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154831 · Cited by 213 · see citing works

Progressive motor weakness in transgenic mice expressing human TDP-43

Stallings, N. R., Puttaparthi, K., Luther, C. M., Burns, D. K., & Elliott, J. L. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.06.017 · Cited by 209 · see citing works

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

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

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 200 · see citing works

Astrocyte loss of mutant SOD1 delays ALS disease onset and progression in G85R transgenic mice

Wang, L., Gutmann, D. H., & Roos, R. P. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq463 · Cited by 192 · see citing works

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

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

Nuclear Factor TDP-43 Binds to the Polymorphic TG Repeats in CFTR Intron 8 and Causes Skipping of Exon 9: A Functional Link with Disease Penetrance

Buratti, E., Brindisi, A., Pagani, F., & Baralle, F. E. (2004) · The American Journal of Human Genetics · doi:10.1086/420978 · Cited by 187 · see citing works

RNA targets of TDP-43 identified by UV-CLIP are deregulated in ALS

Xiao, S., Sanelli, T. R., Dib, S., Sheps, D., Findlater, J., Bilbao, J. M., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.02.013 · Cited by 163 · see citing works

Progranulin is Neurotrophic In Vivo and Protects against a Mutant TDP-43 Induced Axonopathy

Laird, A. S., Hoecke, A. V., Muynck, L. D., Timmers, M., Bosch, L. V. D., Damme, P. V., & Robberecht, W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013368 · Cited by 147 · see citing works

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 134 · see citing works

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 128 · see citing works

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 126 · see citing works

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

Seyfried, N. T., Gozal, Y. M., Dammer, E. B., Xia, Q., Duong, D. M., Cheng, D., Lah, J. J., Levey, A. I., & Peng, J. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800390-mcp200 · Cited by 119 · see citing works

Both cytoplasmic and nuclear accumulations of the protein are neurotoxic in Drosophila models of TDP-43 proteinopathies

Miguel, L., Frébourg, T., Campion, D., & Lecourtois, M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.007 · Cited by 94 · see citing works

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 93 · see citing works

Analysis of IFT74as a candidate gene for chromosome 9p-linked ALS-FTD

Momeni, P., Schymick, J. C., Jain, S., Cookson, M., Cairns, N. J., Greggio, E., Greenway, M. J., Berger, S. L., Pickering-Brown, S. M., Chiò, A., et al. (2006) · BMC Neurology · doi:10.1186/1471-2377-6-44 · Cited by 74 · see citing works

No Effect on SOD1 Splicing by TARDP or FUS Mutations

Belzil, V., Daoud, H., Dion, P. A., & Rouleau, G. A. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.1 · Cited by 4 · see citing works

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 · see citing works

Stress granules as crucibles of ALS pathogenesis

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The changing scene of amyotrophic lateral sclerosis

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