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

Myopathic aggregation-prone variants in the TDP-43 prion-like domain: genetics paving the way

Pereira, P. E., Bleecker, J. D., Bogaert, E., & Dermaut, B. (2025) · Brain · doi:10.1093/brain/awaf076 · Cited by 3

In vivo self-assembled siRNAs ameliorate neurological pathology in TDP-43-associated neurodegenerative disease

Wu, J., Guo, J., Wu, J., Song, J., Xu, J., Lin, Y., Huang, C., Shi, C., Li, J., Li, C., et al. (2025) · Brain · doi:10.1093/brain/awaf330 · Cited by 5

Neurotrophic Therapy for ALS/MND

Rogers, M. (2014) · Springer eBooks · doi:10.1007/978-1-4614-5836-4_34 · Cited by 3

The prion-like effect and prion-like protein targeting strategy in amyotrophic lateral sclerosis

Wenzhi, Y., Xiangyi, L., & Dongsheng, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34963 · Cited by 3

TARDBP ( TDP ‐43) Knock‐in Zebrafish Display a Late‐Onset Motor Phenotype and Loss of Large Spinal Cord Motor Neurons

Harji, Z. A., Rampal, C. J., Rodríguez, E. C., Légaré, V. P., Lissouba, A., Semmler, S., Liao, M., Ross, J. P., Rouleau, G. A., Velde, C. V., et al. (2025) · Annals of Neurology · doi:10.1002/ana.78012 · Cited by 3

Temporal Expression of Mutant TDP-43 Correlates with Early Amyotrophic Lateral Sclerosis Phenotype and Motor Weakness

Chen, Q., Zhou, J., Huang, C., Huang, B., Bi, F., Zhou, H., & Xiao, B. (2018) · Current Neurovascular Research · doi:10.2174/1567202615666180109161541 · Cited by 3

Animal models of dementia

Roberson, E. D., & Kao, A. W. (2016) · Cambridge University Press eBooks · doi:10.1017/9781139924771.007 · Cited by 3

TDP-43: [GU]-ardian of the transcriptome

Sinha, I. R., Atkinson, A. L., Irwin, K. E., Ling, J. P., & Wong, P. C. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00944-2 · Cited by 2

The Use of Human Samples to Study Familial and Sporadic Amyotrophic Lateral Sclerosis: New Frontiers and Challenges

Ferraiuolo, L., Meyer, K., & Kaspar, B. K. (2013) · InTech eBooks · doi:10.5772/56487 · Cited by 3

Co-administration of Nanowired DL-3-n-Butylphthalide (DL-NBP) Together with Mesenchymal Stem Cells, Monoclonal Antibodies to Alpha Synuclein and TDP-43 (TAR DNA-Binding Protein 43) Enhance Superior Neuroprotection in Parkinson’s Disease Following Concussive Head Injury

Feng, L., Sharma, A., Wang, Z., Muresanu, D. F., Tian, Z. R., Lafuente, J. V., Buzoianu, A. D., Nozari, A., Wiklund, L., & Sharma, H. S. (2023) · Advances in neurobiology · doi:10.1007/978-3-031-32997-5_3 · Cited by 2

Molecular basis of the autoregulatory mechanism of motor neuron-related splicing factor 30

Izumikawa, K., Shida, T., Onodera, Y., Tashima, Y., Miyao, S., Suda, T., Suda, Y., Kamimura, R., Nagai, M., Sugihara, M., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110522 · Cited by 2

Importance of the Q/N-rich segment for protein stability of endogenous mouse TDP-43

Sato, T., Oda, K., Sakai, S., Kato, R., Yamamori, S., Itakura, M., Kodera, Y., Nishizawa, M., Sasaoka, T., Onodera, O., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-19153-0 · Cited by 2

An analysis of variants in TARDBP in the Korean population with amyotrophic lateral sclerosis: comparison with previous data

Sung, W., Kim, J.-A., Kim, Y. S., Park, J., Oh, K., Sung, J., Kim, Y.-E., Kim, Y.-E., & Kim, S. H. (2023) · Scientific Reports · doi:10.1038/s41598-023-45593-3 · Cited by 2

An Intramolecular Salt Bridge Linking TDP43's RNA Recognition Motifs Dictates RNA Binding and TDP43-Dependent NeurodegenerationPreprint

Flores, B. N., Li, X., Martinez, J., Beg, A. A., & Barmada, S. J. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3236488 · Cited by 1

The TDP43 CFTS Affect Brain Endothelial Cell Functions by Regulating YAP and Tight Junction Proteins in Cerebral Ischemic Injury.Preprint

Xu, X., Zhang, C., Jiang, J., Xin, M., & Hao, J. (2021) · Research Square · doi:10.21203/rs.3.rs-762288/v1 · Cited by 2

The post-translational modification SUMO affects TDP-43 phase separation, compartmentalization, and aggregation in a zebrafish modelPreprint

Maurel, C., Scherer, N. M., Hogan, A. L., Vidal-Itriago, A., Don, E. K., Radford, R. A. W., Chapman, T. R., Cull, S., Vourc’h, P., Chung, R. S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.14.503569 · Cited by 2

Barriers to Novel Therapeutics in Amyotrophic Lateral Sclerosis

Kobeleva, X., & Petri, S. (2013) · Neurodegenerative Disease Management · doi:10.2217/nmt.13.66 · Cited by 1

Uncovering Critical Roles for RNA in Neurodegeneration.

Ayala, Y. M. (2023) · PubMed Central · Cited by 1

A partial deletion of the Tardbp 3’UTR affects TDP-43 regulation and leads to motor dysfunction in mice

Dinh, T. T. H., IMURA, C., Shiokawa, M., Ayabe, S., Yoshiki, A., Inoue, H., & Amano, T. (2025) · EXPERIMENTAL ANIMALS · doi:10.1538/expanim.25-0061 · Cited by 1

On the potential roles of TDP-43 in the formation of membraneless organelles and their transformation into toxic aggregates

Sergeeva, O. S., Neklesova, M. V., Reushev, V. A., Artemov, A. V., Константинович, Т. К., Константинович, Т. К., Uversky, V. N., & Fonin, A. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152808 · Cited by 2

Splicing the narrative: alternative TARDBP splicing and its relation to neurodegeneration in ALS and FTD

Miller, M. R., Dykstra, M. M., & Barmada, S. J. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199846 · Cited by 1

Enhancer RNA-mediated transcriptional regulation of TDP-43 during early neural lineage specification

Jang, Y., Lee, H., Oh, M., Moon, J., Kim, S. S., Han, J., Park, J.-L., & Kim, S.-K. (2026) · Animal Cells and Systems · doi:10.1080/19768354.2026.2643998 · Cited by 1

Targeting TDP-43 in sporadic amyotrophic lateral sclerosis

Estevez‐Fraga, C., Álvarez‐Velasco, R., Afroz, T., Costa, M. R., Jovičić, A., Yeh, F. L., McColgan, P., Malaspina, A., & McCampbell, A. (2026) · Journal of Neurology · doi:10.1007/s00415-026-14023-5 · Cited by 1

Neurotoxicity and ALS: Insights into Pathogenesis

Vucic, S., & Kiernan, M. C. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_138-1 · Cited by 1

Heterogeneous Nuclear Ribonucleoproteins In Amyotrophic Lateral Sclerosis: What Do We Know?

Moujalled, D., & White, A. R. (2014) · Future Neurology · doi:10.2217/fnl.14.7 · Cited by 1

TDP-43 is essential for Eph receptor-class-specific spinal motor axon trajectory into the limb

Kao, T., Wang, C., Hsu, T., Wu, Y., Chuang, J.-Y., Huang, C.-C. S., & Hsieh, C. T. (2021) · Neuroscience Research · doi:10.1016/j.neures.2021.10.006 · Cited by 1

Amyotrophic Lateral Sclerosis: From Mechanisms to Current, Emerging, and Alternative Therapeutics

Kioutchoukova, I. P. (2023) · Med Discoveries · doi:10.52768/2993-1142/1059 · Cited by 1

Mechanisms of FUS-mediated motor neuron degeneration in amyotrophic lateral sclerosis

Lyashchenko, A. K. (2015) · doi:10.7916/d8jq0zv1 · Cited by 1

TDP-43 Depletion: Mechanism of Neuronal Cell Death in ALS

Kitamura, A. (2018) · Future Neurology · doi:10.2217/fnl-2018-0010 · Cited by 1

TDP-43 y su incidencia en demencias degenerativas

Ure, J. A. (2020) · Neurología Argentina · doi:10.1016/j.neuarg.2020.07.001 · Cited by 1

A systems biology approach to understand the role of TDP-43 in amyotrophic lateral sclerosis

Haque, M. M. U., Anwar, M. S., Malik, M. Z., Singh, R. K. B., Verma, N., & Sharma, S. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.00006-0 · Cited by 1

Neurotrophic Therapy for ALS/MND

Fowler, M., Shepheard, S. R., & Rogers, M. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_34 · Cited by 1

Neurotoxicity and ALS: Insights into Pathogenesis

Vucic, S., & Kiernan, M. C. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_138 · Cited by 1

Frontotemporal Lobar Degeneration with TDP‐43 Pathology

Mackenzie, I. R., & Neumann, M. (2011) · Wiley eBooks · doi:10.1002/9781444341256.ch41 · Cited by 1

TDP43 autoregulation gives rise to shortened isoforms that are tightly controlled by both transcriptional and post-translational mechanismsPreprint

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. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.02.601776 · Cited by 1

Elucidating the Role of TDP-43 in the Pathogenesis of Amyotrophic Lateral Sclerosis

Jauregui, M. (2012) · TSpace (University of Toronto)

From Neurodegeneration to Infertility and Back - Exploring Functions of Two Genes: ARMC4 and TARDBP: A Dissertation

Cheng, W. (2014) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2js4j

Genetic characterization of patients with frontotemporal dementia and amyotrophic lateral sclerosis in the Nordic countries

Chiang, H. (2012) · Figshare

Involvement of endoplasmic reticulum stress in TDP-43-linked neurodegenerative disease

Walker, A. K. (2014) · Postdoc Journal · doi:10.14304/surya.jpr.v2n6.2

A survey of axonal transport function and motor behaviour in Drosophila models of amyotrophic lateral sclerosis

Baldwin, K. R. (2015) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Electrophysiological biomarkers for the study of new therapeutic strategies for motoneuron disease

Mancuso, R. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

The role of ALS associated genes and c-Jun in neurodegeneration

Acosta‐Saltos, A. (2016) · UCL Discovery (University College London)

R O L E O F A U T O P H A G Y A N D I TS E N H A N C I N G I N T H E C L E A R A N C E O F T DP-43 A G G R E G A T ES

Gorica, N. (2014)

Autonomous and motor disorders

Pietropaolo, S., Sluyter, F., & Crusio, W. E. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781107360556.005

TDP-43 Pathology: Elucidation of Mechanisms and Treatment with Tyrosine Kinase Inhibition

Heyburn, L. (2017) · DigitalGeorgetown (Georgetown University Library)

Investigation of the intercellular transmission of α-synuclein, amyloid-β and TDP-43

Sackmann, C. (2019) · Linköping University medical dissertations · doi:10.3384/diss.diva-160318

Relationship Between TDP-43 Toxicity and Aggregation in Saccharomyces Cerevisiae

Aguilar, M. A. (2018) · Digital Commons - DU (University of Denver)

New lessons on TDP-43 from the killifish N. furzeriPreprint

Louka, A., Bagnoli, S., Rupert, J., Esapa, B., Tartaglia, G. G., Cellerino, A., Pastore, A., & Tozzini, E. T. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.04.429704

m6A RNA methylation and TARDBP, a gene implicated in amyotrophic lateral sclerosis

Quoibion, A. (2017) · doi:10.82308/31337

Structural dissection of TDP-43

Kumar, V. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.00001-1

Importance of the Q/N-rich Segment for Protein Stability and Activity of Endogenous Mouse TDP-43Preprint

Sato, T., Oda, K., Sakai, S., Kato, R., Yamamori, S., Itakura, M., Kodera, Y., Nishizawa, M., Sasaoka, T., Onodera, O., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-1113360/v1

Neurotrophic Therapy for ALS/MND

Fowler, M., Shepheard, S. R., & Rogers, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_34-1

Characterization of the Human TARDBP Gene PromoterPreprint

Baralle, M., & Romano, M. (2020) · Research Square · doi:10.21203/rs.3.rs-110373/v1

Motor disorders

Gordon, D., & Talbot, K. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781107360556.008

Theme 07 - Pre-Clinical Therapeutic Strategies

(2022) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2022.2120683

Translational control of furina by an RNA regulon is important for left-right patterning, heart morphogenesis and cardiac valve function

Nagorska, A., Zaucker, A., Lambert, F. R. P., Inman, A., Toral-Pérez, S., Gorodkin, J., Wan, Y., Smutny, M., & Sampath, K. (2023) · Development · doi:10.1242/dev.201657

Assessment of an allelic series of mouse TDP43 mutations

Ricketts, T. C. (2012) · UCL Discovery (University College London)

Implication des macrophages périphériques dans la Sclérose latérale Amyotrophique

Chiot, A. (2018) · theses.fr (ABES) · doi:10.70675/e3d90f5az237az4722zbff2z9c99590e826b

Novel FUS and CHCHD10 models to investigate pathogenic mechanisms in Amyotrophic Lateral Sclerosis

Bourefis, A.-R. (2019) · theses.fr (ABES) · doi:10.70675/45ab8515z9859z430fzb472z306dd61206c8

Etude du continuum mécanistique et physiopathologique entre la Sclérose Latérale Amyotrophique et la Démence FrontoTemporale

Waegaert, R. (2019) · theses.fr (ABES) · doi:10.70675/ff848a6ez0d22z4e0cz9e04z0511c3f18730

Agrégation de la protéine TDP-43 dans la sclérose latérale amyotrophique : sélection d’intracorps ciblant la protéine et étude de modifications post-traductionnelles.

Chami, A. A. (2020) · theses.fr (ABES) · doi:10.70675/d7bfa972z9f99z4e0bza8fbz24483ea92753

Analyses génétiques et fonctionnelles de nouveaux gènes incriminés dans la Sclérose Latérale Amyotrophique (SLA)

Teyssou, E. (2017) · theses.fr (ABES) · doi:10.70675/6b2c9ef9z3766z4be8z8030zea731dbce4f3

Comprendre et modéliser la Sclérose Latérale Amyotrophique à début précoce

Muratet, F. (2022) · theses.fr (ABES) · doi:10.70675/9a7778aaz88c7z40b1z92d3zaf5699b86a09

Liaison et impact du zinc sur deux protéines associées aux maladies neuro-dégénératives : tau et TDP-43

Yatoui, D. (2022) · theses.fr (ABES) · doi:10.70675/e3620ccez2ea7z43f2za0dcz257a72021b17

Etude de la dynamique de la protéine TDP-43 en conditions physiologique et pathologique : implication et perspectives en recherche sur la Sclérose Latérale Amyotrophique

Bodin, A. (2024) · theses.fr (ABES) · doi:10.70675/14330e52z0bddz4f9bza10fzfd1b2ddc9736

TDP-43–Associated Neurodegenerative Disease Conceptualization and Integrated Staging

Benatar, M., Barmada, S., Jicha, G. A., Lagier‐Tourenne, C., Gregory, J., Al‐Chalabi, A., Boeve, B. F., Jack, C. R., Seeley, W. W., Maragakis, N. J., et al. (2026) · JAMA Neurology · doi:10.1001/jamaneurol.2026.2812 · Cited by 1

TDP-43 overexpression induces cellular dysfunction and ALS-associated transcriptional changes

DeSando, S. A., McClay, K., Banks, A. N., Cheung, M., Reitz, A. B., & Freeman, K. B. (2026) · Discover Neuroscience · doi:10.1186/s13064-026-00324-y

TDP-43 and ALS - what's wrong with my membranes?

Dahlhaus, R., Yalcin, I., Tischer, J., & Braun, R. J. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107630

RNA –Protein Reciprocity and the Limits of RBP Buffering

Doxakis, E. (2026) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70065

HeLa-S3 RNA-seq Dataset for Training - chr11 only based on GSE136366

Umer, H. (2026) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.18462431

Interrogating the role of splicing factors in Huntington’s Disease

Kooner, G. S. (2015) · Leicester Research Archive (University of Leicester)

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

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

Cannon, A. D., Yang, B., Knight, J. A., Farnham, M., Zhang, Y., Wuertzer, C. A., D’Alton, S., Howard, J. C., Lin, W.-L., Scott, B., et al. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1445

TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration

Sephton, C. F., Cenik, B., Cenik, B. K., Herz, J., & Yu, G. (2012) · bchm · doi:10.1515/hsz-2012-0115 · Cited by 86

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

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

Cannon, A., Yang, B., Knight, J., Farnham, I. M., Zhang, Y., Wuertzer, C. A., Lin, W.-L., Rousseau, L., Scott, B., Jurasic, M., et al. (2016)