Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration

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Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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

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Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

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

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Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

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Aggregation of Huntingtin in Neuronal Intranuclear Inclusions and Dystrophic Neurites in Brain

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

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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

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

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TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

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

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Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

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Alzheimer’s Disease: The Challenge of the Second Century

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

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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

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Mutations of optineurin in amyotrophic lateral sclerosis

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Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene

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Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia

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

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A mutation in the Amyloid Precursor Protein Associated with Hereditary Alzheimer's Disease

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

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A harmonized classification system for FTLD-TDP pathology

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

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

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

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Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

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α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells

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Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia

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

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

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

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

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

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

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

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Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles

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

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

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Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease

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TDP‐43 A315T mutation in familial motor neuron disease

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

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

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

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

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

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

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

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

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

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

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TDP-43 Binds Heterogeneous Nuclear Ribonucleoprotein A/B through Its C-terminal Tail

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

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Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS

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

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A mutation in sigma‐1 receptor causes juvenile amyotrophic lateral sclerosis

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

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TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

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Dementia lacking distinctive histologie features

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

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

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

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TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor

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

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

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

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

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

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

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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

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

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

Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: classification and relation to clinical phenotype

Mackenzie, I. R., Baborie, A., Pickering-Brown, S. M., du Plessis, D., Jaros, E., Perry, R. H., Neary, D., Snowden, J. S., & Mann, D. M. A. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0138-9 · Cited by 322 · see citing works

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 · see citing works

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

Guo, W., Chen, Y., Zhou, X., Kar, A. N., Ray, P., Chen, X., Rao, E. J., Yang, M., Ye, H., Zhu, L., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2053 · Cited by 317 · 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

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 · 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

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 · see citing works

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

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

Prion-like disorders: blurring the divide between transmissibility and infectivity

Cushman-Nick, M., Johnson, B. S., King, O. D., Gitler, A. D., & Shorter, J. (2010) · Journal of Cell Science · doi:10.1242/jcs.051672 · Cited by 288 · see citing works

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 &amp; Cellular Proteomics · doi:10.1074/mcp.m500255-mcp200 · Cited by 287 · see citing works

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 270 · see citing works

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

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

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

Nuclear factor TDP‐43 can affect selected microRNA levels

Buratti, E., Conti, L. D., Stuani, C., Romano, M., Baralle, M., & Baralle, F. E. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07643.x · Cited by 240 · see citing works

A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions*♦

Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K., & Nukina, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231209 · Cited by 235 · see citing works

Cellular toxicity of expanded RNA repeats: focus on RNA foci

Wojciechowska, M., & Krzyżosiak, W. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr299 · Cited by 235 · see citing works

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 232 · see citing works

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 · see citing works

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

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

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

Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change

Frost, B., Ollesch, J., Wille, H., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805627200 · Cited by 224 · 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

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

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

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 · 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

Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)

Volkening, K., Leystra‐Lantz, C., Yang, W., Jaffee, H., & Strong, M. J. (2009) · Brain Research · doi:10.1016/j.brainres.2009.09.105 · Cited by 209 · see citing works

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 · see citing works

A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43

Lanson, N. A., Maltare, A., King, H., Smith, R. B., Kim, J. H., Taylor, J. P., Lloyd, T. E., & Pandey, U. B. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr150 · Cited by 198 · see citing works

Sigma nonopioid intracellular receptor 1 mutations cause frontotemporal lobar degeneration–motor neuron disease

Luty, A. A., Kwok, J. B., Dobson‐Stone, C., Loy, C. T., Coupland, K., Karlström, H., Sobów, T., Tchorzewska, J., Maruszak, A., Barcikowska, M., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22274 · Cited by 196 · see citing works

TDP-43-Mediated Neuron Loss In Vivo Requires RNA-Binding Activity

Voigt, A., Herholz, D., Fiesel, F. C., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012247 · Cited by 195 · see citing works

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

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

The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

Yang, C., Tan, W., Whittle, C., Qiu, L., Cao, L.-C., Akbarian, S., & Xu, Z. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015878 · Cited by 187 · 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

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 · see citing works

The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span

Wang, J.-W., Brent, J. R., Tomlinson, A., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57883 · Cited by 170 · see citing works

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 · see citing works

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

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

Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43

Fuentealba, R. A., Udan-Johns, M., Bell, S., Wegorzewska, I., Shao, J., Diamond, M. I., Weihl, C. C., & Baloh, R. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125039 · Cited by 157 · see citing works

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

Dormann, D., Capell, A., Carlson, A. M., Shankaran, S. S., Rodde, R., Neumann, M., Kremmer, E., Matsuwaki, T., Yamanouchi, K., Nishihara, M., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06211.x · Cited by 156 · see citing works

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

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

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 · see citing works

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

Nishimoto, Y., Ito, D., Yagi, T., Nihei, Y., Tsunoda, Y., & Suzuki, N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022012 · Cited by 138 · see citing works

TDP-43 Regulates Drosophila Neuromuscular Junctions Growth by Modulating Futsch/MAP1B Levels and Synaptic Microtubules Organization

Godena, V. K., Romano, G., Romano, M., Appocher, C., Klima, R., Buratti, E., Baralle, F. E., & Feiguin, F. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017808 · Cited by 137 · see citing works

Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments

Zhang, Y., Gendron, T. F., Xu, Y.-F., Ko, L., Yen, S.-H. C., & Petrucelli, L. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-33 · Cited by 134 · see citing works

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

Mori, F., Tanji, K., Zhang, H., Nishihira, Y., Tan, C., Takahashi, H., & Wakabayashi, K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0396-9 · Cited by 133 · see citing works

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

Phosphorylated and ubiquitinated TDP‐43 pathological inclusions in ALS and FTLD‐U are recapitulated in SH‐SY5Y cells

Nonaka, T., Arai, T., Buratti, E., Baralle, F. E., Akiyama, H., & Hasegawa, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.12.031 · Cited by 118 · see citing works

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 117 · see citing works

A “Two-hit” Hypothesis for Inclusion Formation by Carboxyl-terminal Fragments of TDP-43 Protein Linked to RNA Depletion and Impaired Microtubule-dependent Transport

Pesiridis, G. S., Tripathy, K., Tanik, S. A., Trojanowski, J. Q., & Lee, V. M. ‐. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231118 · Cited by 114 · see citing works

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

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

A90V TDP‐43 variant results in the aberrant localization of TDP‐43 in vitro

Winton, M. J., Deerlin, V. M. V., Kwong, L. K., Yuan, W., McCarty-Wood, E., Yu, C., Schellenberg, G. D., Rademakers, R., Caselli, R. J., Karydas, A., et al. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.05.024 · Cited by 113 · see citing works

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 · see citing works

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 101 · see citing works

Neurotoxic 43-kDa TAR DNA-binding Protein (TDP-43) Triggers Mitochondrion-dependent Programmed Cell Death in Yeast

Braun, R. J., Sommer, C., Carmona‐Gutiérrez, D., Khoury, C. M., Ring, J., Büttner, S., & Madeo, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194852 · Cited by 101 · see citing works

PolyQ Repeat Expansions in ATXN2 Associated with ALS Are CAA Interrupted Repeats

Yu, Z., Zhu, Y., Chen‐Plotkin, A. S., Clay-Falcone, D., McCluskey, L. F., Elman, L. B., Kalb, R. G., Trojanowski, J. Q., Lee, V. M. ‐., Deerlin, V. M. V., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017951 · Cited by 99 · 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

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 · see citing works

Dementia lacking distinctive histology (DLDH) revisited

Mackenzie, I. R., Shi, J., Shaw, C. L., DuPlessis, D., Neary, D., Snowden, J. S., & Mann, D. M. A. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0123-3 · Cited by 87 · see citing works

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 85 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 55 · see citing works

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 · see citing works

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 45 · see citing works

AMSH is required to degrade ubiquitinated proteins in the central nervous system

Suzuki, S., Tamai, K., Watanabe, M., Kyuuma, M., Ono, M., Sugamura, K., & Tanaka, N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.065 · Cited by 29 · see citing works

Potential Mechanisms of Progranulin-deficient FTLD

Ward, M. E., & Miller, B. L. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9622-3 · Cited by 24 · see citing works

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 · see citing works

Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways

Cirulli, E. T., Lasseigne, B. N., Petrovski, S., Sapp, P. C., Dion, P. A., Leblond, C. S., Couthouis, J., Lu, Y.-F., Wang, Q., Krueger, B. J., et al. (2015) · Science · doi:10.1126/science.aaa3650 · Cited by 966 · see citing works

Impact of multiple pathologies on the threshold for clinically overt dementia

Kapasi, A., DeCarli, C., & Schneider, J. A. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1717-7 · Cited by 739 · see citing works

The neurogenetics of alternative splicing

Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340 · see citing works

Loss of function of C9orf72 causes motor deficits in a zebrafish model of amyotrophic lateral sclerosis

Ciura, S., Lattante, S., Le Ber, I., Latouche, M., Tostivint, H., Brice, A., & Kabashi, E. (2013) · Annals of Neurology · doi:10.1002/ana.23946 · Cited by 333 · see citing works

Loss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons

Liu, E. Y., Russ, J., Cali, C. P., Phan, J. M., Amlie-Wolf, A., & Lee, E. B. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.003 · Cited by 231 · see citing works

The neuropathology associated with repeat expansions in the C9ORF72 gene

Mackenzie, I. R. A., Frick, P., & Neumann, M. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1232-4 · Cited by 206 · see citing works

TDP‐43 loss of function increases TFEB activity and blocks autophagosome–lysosome fusion

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Misregulated RNA processing in amyotrophic lateral sclerosis

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LATE to the PART-y

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