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

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

hnRNP PROTEINS AND THE BIOGENESIS OF mRNA

Dreyfuss, G., Matunis, M. J., Piñol-Roma, S., & Burd, C. G. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.001445 · Cited by 1,558

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

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

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

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

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

Rethinking ALS: The FUS about TDP-43

Lagier‐Tourenne, C., & Cleveland, D. W. (2009) · Cell · doi:10.1016/j.cell.2009.03.006 · Cited by 596

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

Therapeutic and diagnostic challenges for frontotemporal dementia

Dâ€TMAlton, S., & Lewis, J. M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00204 · Cited by 26

Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43

Vivoli, M., Guri, P., Chiti, F., & Bemporad, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176259 · Cited by 26

Identification of a subnuclear body involved in sequence-specific cytokine RNA processing

Lee, S., Lee, T. A., Lee, E., Kang, S., Park, A., Kim, S. W., Park, H., Yoon, J., Ha, S., Park, T., et al. (2015) · Nature Communications · doi:10.1038/ncomms6791 · Cited by 27

Robustness and Vulnerability of the Autoregulatory System That Maintains Nuclear TDP-43 Levels: A Trade-off Hypothesis for ALS Pathology Based on in Silico Data

Sugai, A., Kato, T., Koyama, A., Koike, Y. M., Kasahara, S., Konno, T., Ishihara, T., & Onodera, O. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00028 · Cited by 23

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 27

Serum total TDP-43 levels are decreased in frontotemporal dementia patients with C9orf72 repeat expansion or concomitant motoneuron disease phenotype

Katisko, K., Huber, N., Kokkola, T., Hartikainen, P. H., Krüger, J., Heikkinen, A.-L., Paananen, V., Leinonen, V., Korhonen, V. E., Helisalmi, S., et al. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01091-8 · Cited by 24

Human TDP-43 and FUS selectively affect motor neuron maturation and survival in a murine cell model of ALS by non-cell-autonomous mechanisms

Wächter, N., Storch, A., & Hermann, A. (2015) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2015.1055275 · Cited by 24

Disease-Associated Mutations of TDP-43 Promote Turnover of the Protein Through the Proteasomal Pathway

Araki, W., Minegishi, S., Motoki, K., Kume, H., Hohjoh, H., Araki, Y. M., & Tamaoka, A. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8644-6 · Cited by 26

Elevated nuclear TDP-43 induces constitutive exon skipping

Carmen-Orozco, R. P., Tsao, W., Ye, Y., Sinha, I. R., Chang, K., Trinh, V. T., Chung, W., Bowden, K., Troncoso, J. C., Blackshaw, S., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00732-w · Cited by 27

Endothelial TDP-43 controls sprouting angiogenesis and vascular barrier integrity, and its deletion triggers neuroinflammation

Arribas, V., Onetti, Y., Ramiro‐Pareta, M., Villacampa, P., Beck, H., Alberola, M., Esteve‐Codina, A., Merkel, A., Sperandio, M., Martínez-Estrada, O. M., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.177819 · Cited by 21

Structural Transition, Function and Dysfunction of TDP-43 in Neurodegenerative Diseases

Afroz, T., Pérez‐Berlanga, M., & Polymenidou, M. (2019) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2019.380 · Cited by 22

TDP-43 maximizes nerve conduction velocity by repressing a cryptic exon for paranodal junction assembly in Schwann cells

Chang, K.-J., Agrawal, I., Vainshtein, A., Ho, W. Y., Xin, W., Tucker‐Kellogg, G., Susuki, K., Peles, E., Ling, S., & Chan, J. R. (2021) · eLife · doi:10.7554/elife.64456 · Cited by 22

Cryptic splicing: common pathological mechanisms involved in male infertility and neuronal diseases

Aldalaqan, S., Dalgliesh, C., Luzzi, S., Siachisumo, C., Reynard, L. N., Ehrmann, I. E., & Elliott, D. J. (2021) · Cell Cycle · doi:10.1080/15384101.2021.2015672 · Cited by 26

Transcriptional targets of amyotrophic lateral sclerosis/frontotemporal dementia protein TDP-43 – meta-analysis and interactive graphical database

Cao, M. C., & Scotter, E. L. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049418 · Cited by 25

Maternal TDP-43 interacts with RNA Pol II and regulates zygotic genome activation

Nie, X., Xu, Q., Xu, C., Chen, F., Wang, Q., Qin, D., Wang, R., Gao, Z., Lu, X., Yang, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39924-1 · Cited by 25

The prion-like nature of amyotrophic lateral sclerosis

McAlary, L., Yerbury, J. J., & Cashman, N. R. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.002 · Cited by 21

Downregulation of glutamic acid decarboxylase in Drosophila TDP-43-null brains provokes paralysis by affecting the organization of the neuromuscular synapses

Romano, G., Holodkov, N., Klima, R., Grilli, F., Guarnaccia, C., Nizzardo, M., Rizzo, F., Garcia, R. C., & Feiguin, F. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-19802-3 · Cited by 21

Tau tubulin kinases in proteinopathy

Taylor, L. M., McMillan, P. J., Kraemer, B. C., & Liachko, N. F. (2019) · FEBS Journal · doi:10.1111/febs.14866 · Cited by 20

Modeling of Neurodegenerative Diseases: ‘Step by Step’ and ‘Network’ Organization of the Complexes of Model Systems

Pasko, V. I., Churkina, A. S., Shakhov, A. S., Kotlobay, A. A., & Alieva, I. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010604 · Cited by 21

Neuronal TDP-43 depletion affects activity-dependent plasticity

Koza, P., Beroun, A., Konopka, A., Górkiewicz, T., Bijoch, Ł., Torres-Elguera, J. C., Bulska, E., Knapska, E., Kaczmarek, L., & Konopka, W. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104499 · Cited by 20

TDP-43 Is Efficiently Transferred Between Neuron-Like Cells in a Manner Enhanced by Preservation of Its N-Terminus but Independent of Extracellular Vesicles

Sackmann, C., Sackmann, V., & Hallbeck, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00540 · Cited by 21

Neuromuscular junction denervation and terminal Schwann cell loss in the hTDP‐43 overexpression mouse model of amyotrophic lateral sclerosis

Alhindi, A., Shand, M., Smith, H. L., Leite, A. S., Huang, Y., van der Hoorn, D., Ridgway, Z., Faller, K. M. E., Jones, R. A., Gillingwater, T. H., et al. (2023) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12925 · Cited by 18

A Nonsense Mutation in Mouse Tardbp Affects TDP43 Alternative Splicing Activity and Causes Limb-Clasping and Body Tone Defects

Ricketts, T., McGoldrick, P., Fratta, P., Oliveira, H. M. D., Kent, R., Phatak, V. M., Brandner, S., Blanco, G., Greensmith, L., Acevedo‐Arozena, A., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085962 · Cited by 19

Changes in TDP-43 expression in development, aging, and in the neurofilament light protein knockout mouse

Liu, Y., Atkinson, R. A. K., Fernández-Martos, C. M., Kirkcaldie, M., Cui, H., Vickers, J. C., & King, A. E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.10.001 · Cited by 19

Simple animal models for amyotrophic lateral sclerosis drug discovery

Patten, S. A., Parker, J. A., Wen, X., & Drapeau, P. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2016.1196183 · Cited by 20

TDP-43: multiple targets, multiple disease mechanisms?

Sendtner, M. (2011) · Nature Neuroscience · doi:10.1038/nn.2784 · Cited by 17

Akirin2 is essential for the formation of the cerebral cortex

Bösch, P., Fuller, L. C., Sleeth, C. M., & Weiner, J. A. (2016) · Neural Development · doi:10.1186/s13064-016-0076-8 · Cited by 19

Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins

Buratti, E. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_15 · Cited by 19

Genetic strategies to study TDP-43 in rodents and to develop preclinical therapeutics for amyotrophic lateral sclerosis

Wang, D. B., Gitcho, M. A., Kraemer, B. C., & Klein, R. L. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07803.x · Cited by 18

The Role of TAR DNA Binding Protein 43 (TDP-43) as a CandiDate Biomarker of Amyotrophic Lateral Sclerosis: A Systematic Review and Meta-Analysis

Gambino, C. M., Ciaccio, A. M., Sasso, B. L., Giglio, R. V., Vidali, M., Agnello, L., & Ciaccio, M. (2023) · Diagnostics · doi:10.3390/diagnostics13030416 · Cited by 17

Physical exercise modulates the microglial complement pathway in mice to relieve cortical circuitry deficits induced by mutant human TDP-43

Wei, J., Liu, L., Song, X., Lin, B., Cui, J., Luo, L., Liu, Y., Li, S., Li, X., So, K., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112240 · Cited by 18

Genetic architecture of amyotrophic lateral sclerosis: a comprehensive review

Yuan, L., Yang, Y., Guo, Y., & Deng, H. (2025) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2025.05.008 · Cited by 18

The identification of high-performing antibodies for TDP-43 for use in Western Blot, immunoprecipitation and immunofluorescence

Worrall, D., Ayoubi, R., Fotouhi, M., Southern, K., McPherson, P. S., Laflamme, C., & NeuroSGC/YCharOS/EDDU collaborative group (2023) · F1000Research · doi:10.12688/f1000research.131852.1 · Cited by 15

Augmented quantal release of acetylcholine at the vertebrate neuromuscular junction following tdp-43 depletion

Dzieciolowska, S., Drapeau, P., & Armstrong, G. A. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177005 · Cited by 16

Protonation–Deprotonation Switch Controls the Amyloid-like Misfolding of Nucleic-Acid-Binding Domains of TDP-43

Patni, D., & Jha, S. K. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c03262 · Cited by 15

Promise of Nucleic Acid Therapeutics for Amyotrophic Lateral Sclerosis

Ito, D. (2021) · Annals of Neurology · doi:10.1002/ana.26259 · Cited by 15

Effect of TDP43-CTFs35 on Brain Endothelial Cell Functions in Cerebral Ischemic Injury

Xu, X., Zhang, C., Jiang, J., Xin, M., & Hao, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02869-5 · Cited by 15

Motor Neuron Diseases

Wong, P. C., Chiang, P., Martin, L. J., Koliatsos, V. E., & Price, D. L. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374947-5.00045-6 · Cited by 15

Computational Insights of Unfolding of N-Terminal Domain of TDP-43 Reveal the Conformational Heterogeneity in the Unfolding Pathway

Li, R., Singh, R., Kashav, T., Yang, C., Sharma, R. D., Lynn, A. M., Prasad, R., Prakash, A., & Kumar, V. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.822863 · Cited by 14

Optineurin Deficiency and Insufficiency Lead to Higher Microglial TDP-43 Protein Levels

Prtenjača, N., Rob, M., Alam, M. S., Markovinović, A., Stuani, C., Buratti, E., & Munitić, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126829 · Cited by 13

Allele-specific silencing as therapy for familial amyotrophic lateral sclerosis caused by the p.G376D TARDBP mutation

Romanò, R., Luca, M. D., Fiore, V. S. D., Pecoraro, M., Lattante, S., Sabatelli, M., Bella, V. L., & Bucci, C. (2022) · Brain Communications · doi:10.1093/braincomms/fcac315 · Cited by 15

TDP-43 Epigenetic Facets and Their Neurodegenerative Implications

Gimenez, J., Spalloni, A., Cappelli, S., Ciaiola, F., Orlando, V., Buratti, E., & Longone, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813807 · Cited by 15

Mis-localization of endogenous TDP-43 leads to ALS-like early-stage metabolic dysfunction and progressive motor deficits

Hu, Y., Hruscha, A., Pan, C., Schifferer, M., Schmidt, M. K., Nuscher, B., Giera, M. A., Kostidis, S., Burhan, Ö. P., van Bebber, F., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00735-7 · Cited by 16

TDP43 autoregulation gives rise to dominant negative isoforms that are tightly controlled by transcriptional and post-translational mechanisms

Dykstra, M. M., Weskamp, K., Gómez, N., Waksmacki, J., Tank, E. M. H., Glineburg, M. R., Snyder, A. G., Pinarbasi, E. S., Bekier, M. E., Li, X., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115113 · Cited by 19

Aberrant expression of TAR DNA binding protein-43 is associated with spermatogenic disorders in men

Varghese, D. S., Chandran, U., Soumya, A., Pillai, S. M., Jayakrishnan, K., Reddi, P. P., & Kumar, P. G. (2014) · Reproduction Fertility and Development · doi:10.1071/rd14090 · Cited by 13

Physiological tissue-specific and age-related reduction of mouse TDP-43 levels is regulated by epigenetic modifications

Pacetti, M., Conti, L. D., Marasco, L. E., Romano, M., Rashid, M. M., Nubiè, M., Baralle, F. E., & Baralle, M. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049032 · Cited by 15

Reduced TDP-43 Expression Improves Neuronal Activities in a Drosophila Model of Perry Syndrome

Hosaka, Y., Inoshita, T., Shiba‐Fukushima, K., Cui, C., Arano, T., Imai, Y., & Hattori, N. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.06.002 · Cited by 13

U6 snRNA expression prevents toxicity in TDP-43-knockdown cells

Yahara, M., Kitamura, A., & Kinjo, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0187813 · Cited by 14

Transactive response DNA-binding protein 43 is enriched at the centrosome in human cells

Bodin, A., Greibill, L., Gouju, J., Letournel, F., Pozzi, S., Julien, J., Renaud, L., Bohl, D., Millecamps, S., Verny, C., et al. (2023) · Brain · doi:10.1093/brain/awad228 · Cited by 13

Implications of TDP-43 in non-neuronal systems

Hao, K., Liu, K., Jiao, B., & Zhao, L. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01336-5 · Cited by 13

The progress inC9orf72research: ALS/FTD pathogenesis, functions and structure

Jiang, L., Zhang, T., Lu, K., & Qi, S. (2021) · Small GTPases · doi:10.1080/21541248.2021.1892443 · Cited by 13

InFUSing antisense oligonucleotides for treating ALS

Codron, P., Cassereau, J., & Vourc’h, P. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.02.006 · Cited by 12

A restricted level of PQBP1 is needed for the best longevity of Drosophila

Tamura, T., Sone, M., Nakamura, Y., Shimamura, T., Imoto, S., Miyano, S., & Okazawa, H. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.07.015 · Cited by 11

Dynamic duo – FMRP and TDP-43: Regulating common targets, causing different diseases

Ferro, D., Yao, S., & Zarnescu, D. C. (2018) · Brain Research · doi:10.1016/j.brainres.2018.04.034 · Cited by 14

Challenges of modelling TDP-43 pathology in mice

Armas, J. M. B., Taoro‐González, L., Fisher, E., & Acevedo‐Arozena, A. (2025) · Mammalian Genome · doi:10.1007/s00335-025-10131-1 · Cited by 12

Animal Models for the Study of Human Neurodegenerative Diseases

Colpo, G. D., Ribeiro, F. M., Rocha, N. P., & Teixeira, A. L. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809468-6.00042-5 · Cited by 12

TDP-43 is Required for Mammary Gland Repopulation and Proliferation of Mammary Epithelial Cells

Zhao, L., Li, L., Xu, H., Hao, K., Zou, L., Yang, Q., Shen, C.-K. J., Nie, J., & Jiao, B. (2019) · Stem Cells and Development · doi:10.1089/scd.2019.0011 · Cited by 10

Liquid-liquid phase separation in human diseases: Functions, mechanisms and treatments

Yue, T., Zhang, F., Wei, Y., & Wang, Z. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102521 · Cited by 11

Clinical, Genetic and Neuropathological Features of Frontotemporal Dementia: An Update and Guide

Paulos, J. P., & Massano, J. (2013) · Acta Médica Portuguesa · doi:10.20344/amp.1226 · Cited by 9

Thermodynamic modulation of folding and aggregation energy landscape by DNA binding of functional domains of TDP-43

Patni, D., & Jha, S. K. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140916 · Cited by 10

Similar dose-dependence of motor neuron cell death caused by wild type human TDP-43 and mutants with ALS-associated amino acid substitutions

Wu, L.-S., Cheng, W.-C., & Shen, C.-K. J. (2013) · Journal of Biomedical Science · doi:10.1186/1423-0127-20-33 · Cited by 10

Molecular Mechanisms of Amyotrophic Lateral Sclerosis

Collins, M. A., & Bowser, R. P. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-802257-3.00004-3 · Cited by 10

Thioridazine reverts the phenotype in cellular and Drosophila models of amyotrophic lateral sclerosis by enhancing TDP-43 aggregate clearance

Cragnaz, L., Spinelli, G., Conti, L. D., Bureau, E. A., Brownlees, J., Feiguin, F. M., Romano, V. C., Skoko, N., Klima, R., Kettleborough, C. A., et al. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105515 · Cited by 12

Developmental anatomy of the primary olfactory pathway in the opossum Monodelphis domestica.

Chuah, M. I., Tennent, R., & Teague, R. (1997) · PubMed · Cited by 10

Human neural networks with sparse TDP-43 pathology reveal NPTX2 misregulation in ALS/FTLDPreprint

Hruška-Plocháň, M., Betz, K. M., Ronchi, S., Wiersma, V. I., Maniecka, Z., Hock, E., Laferrière, F., Sahadevan, S., Hoop, V., Delvendahl, I., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.08.471089 · Cited by 10

ATXN2L primarily interacts with NUFIP2, the absence of ATXN2L results in NUFIP2 depletion, and the ATXN2-polyQ expansion triggers NUFIP2 accumulation

Key, J., Almaguer-Mederos, L. E., Kandi, A. R., Şen, N.-E., Gispert, S., Koepf, G., Meierhofer, D., & Auburger, G. W. J. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106903 · Cited by 10

Aberrant neural activity in prefrontal pyramidal neurons lacking TDP-43 precedes neuron loss

Liang, B., Thapa, R., Zhang, G., Moffitt, C. M., Zhang, Y., Zhang, L., Johnston, A., Ruby, H. P., Barbera, G., Wong, P. C., et al. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102297 · Cited by 9

Toxicity in ALS: TDP-43 modifiers and C9orf72

Martin, J. L. S., Wang, L., & Kaprielian, Z. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134621 · Cited by 10

hnRNP A1B, a Splice Variant of HNRNPA1, Is Spatially and Temporally Regulated

Gagné, M., Deshaies, J.-E., Sidibé, H., Benchaar, Y., Arbour, D., Dubinski, A. F., Litt, G., Peyrard, S., Robitaille, R., Sephton, C. F., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.724307 · Cited by 9

A postzygotic de novo NCDN mutation identified in a sporadic FTLD patient results in neurochondrin haploinsufficiency and altered FUS granule dynamics

Nicolas, G., Sévigny, M., Lecoquierre, F., Marguet, F., Deschênes, A., Pelaez, M. C., Feuillette, S., Audebrand, A., Lecourtois, M., Rousseau, S., et al. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01314-x · Cited by 9

Multiple knockout mouse and embryonic stem cell models reveal the role of miR-124a in neuronal maturation

Chaya, T., Maeda, Y., Sugimura, R., Okuzaki, D., Watanabe, S., Varner, L. R., Motooka, D., Gyoten, D., Yamamoto, H., Kato, H., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102293 · Cited by 9

Loss of TDP-43 causes ectopic endothelial sprouting and migration defects through increased fibronectin, vcam 1 and integrin α4/β1

Hipke, K., Pitter, B., Hruscha, A., van Bebber, F., Modic, M., Bansal, V., Lewandowski, S. A., Orozco, D., Edbauer, D., Bonn, S., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1169962 · Cited by 8

DNA-Mediated Formation of Phase-Separated Coacervates of the Nucleic Acid-Binding Domain of TAR DNA-Binding Protein (TDP-43) Prevents Its Amyloid-Like Misfolding

Patni, D., Patil, A. D., Kirmire, M. S., Jha, A., & Jha, S. K. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00117 · Cited by 8

Critical impact of lysine 136 in TDP-43 phase separation, compartmentalization, and aggregation in living vertebrates

Maurel, C., Scherer, N. M., Luu, L., Radford, R. A. W., Hogan, A. L., Merjane, J., Vidal-Itriago, A., Don, E. K., Chapman, T. R., Cull, S., et al. (2025) · iScience · doi:10.1016/j.isci.2025.112761 · Cited by 11

Targeting lipid droplets in FUS-linked amyotrophic lateral sclerosis mitigates neuronal and astrocytic lipotoxicity

Marcadet, L., Pelaez, M. C., Desmeules, A., Serrano, J., Cheng, Z., Khademullah, C. S., Parham, E., Kennedy, J., Troakes, C., Vance, C. A., et al. (2025) · Brain · doi:10.1093/brain/awaf328 · Cited by 8

Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands

Rao, P. P. N., Shakeri, A., Zhao, Y., & Calon, F. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113753 · Cited by 8

5-Hydroxytryptamine: a potential therapeutic target in amyotrophic lateral sclerosis

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CRISPR screen for protein inclusion formation uncovers a role for SRRD in the regulation of intermediate filament dynamics and aggresome assembly

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Unmasking the skiptic task of TDP‐43

Rouaux, C., de Aguilar, J. G., & Dupuis, L. (2018) · The EMBO Journal · doi:10.15252/embj.201899645 · Cited by 9

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TDP ‐43 proteinopathies and neurodegeneration: insights from Caenorhabditis elegans models

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Novel monoclonal antibodies targeting the RRM2 domain of human TDP-43 protein

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FUS ALS-causative mutations impact FUS autoregulation and the processing of RNA-binding proteins through intron retentionPreprint

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

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P3‐006: Neurons during early development are highly vulnerable to TDP‐43 dysregulation

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ORIGINAL PAPER Neuronal sensitivity to TDP-43 overexpression is dependent on timing of induction

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