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

Neurodegenerative models in Drosophila: Polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis

Ambegaokar, S. S., Roy, B., & Jackson, G. R. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.026 · Cited by 80

Biology and Pathobiology of TDP-43 and Emergent Therapeutic StrategiesPreprint

Guo, L. E., & Shorter, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024554 · Cited by 85

Depletion of TDP-43 decreases fibril and plaque β-amyloid and exacerbates neurodegeneration in an Alzheimer’s mouse model

LaClair, K. D., Donde, A., Ling, J. P., Jeong, Y. H., Chhabra, R., Martin, L. J., & Wong, P. C. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1637-y · Cited by 76

RNA-binding proteins in neurological diseases

Zhou, H.-L., Mangelsdorf, M., Liu, J., Zhu, L., & Wu, J. Y. (2014) · Science China Life Sciences · doi:10.1007/s11427-014-4647-9 · Cited by 82

From molecule to molecule and cell to cell: Prion-like mechanisms in amyotrophic lateral sclerosis

Grad, L. I., Fernando, S. M., & Cashman, N. R. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.009 · Cited by 80

Neuronal Function and Dysfunction of Drosophila dTDP

Lin, M.-J., Cheng, C.-W., & Shen, C. ‐. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020371 · Cited by 77

Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS

Ito, D., & Suzuki, N. (2011) · Neurology · doi:10.1212/wnl.0b013e3182343365 · Cited by 78

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells

Appocher, C., Mohagheghi, F., Cappelli, S., Stuani, C., Romano, M., Feiguin, F. M., & Buratti, E. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx477 · Cited by 76

The role of altered protein acetylation in neurodegenerative disease

Kabir, F., Atkinson, R., Cook, A. L., Phipps, A. J., & King, A. E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1025473 · Cited by 75

TDP-43 Is a Transcriptional Repressor

Lalmansingh, A. S., Urekar, C., & Reddi, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166587 · Cited by 74

Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis

Ishihara, T., Ariizumi, Y., Shiga, A., Kato, T., Tan, C., Sato, T., Miki, Y., Yokoo, M., Fujino, T., Koyama, A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt262 · Cited by 74

TDP-43 dysfunction results in R-loop accumulation and DNA replication defects

Wood, M. D., Quinet, A., Lin, Y., Davis, A. A., Pasero, P., Ayala, Y. M., & Vindigni, A. (2020) · Journal of Cell Science · doi:10.1242/jcs.244129 · Cited by 72

TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Bright, F., Chan, G., van Hummel, A., Ittner, L. M., & Ke, Y. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157781 · Cited by 71

TDP‐1, the Caenorhabditis elegans ortholog of TDP‐43, limits the accumulation of double‐stranded RNA

Saldi, T. K., Ash, P. E., Wilson, G., Gonzales, P., Garrido‐Lecca, A., Roberts, C. M., Dostal, V., Gendron, T. F., Stein, L. D., Blumenthal, T., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488740 · Cited by 71

Caenorhabditis elegans RNA-processing Protein TDP-1 Regulates Protein Homeostasis and Life Span

Zhāng, T., Hwang, H., Hao, H., Talbot, C. C., & Wang, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311977 · Cited by 75

p62/sequestosome 1 binds to TDP‐43 in brains with frontotemporal lobar degeneration with TDP‐43 inclusions

Tanji, K., Zhang, H., Mori, F., Kakita, A., Takahashi, H., & Wakabayashi, K. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23081 · Cited by 72

Linking pathways in the developing and aging brain with neurodegeneration

Kovács, G. G., Adle‐Biassette, H., Milenković, I., Cipriani, S., van Scheppingen, J., & Aronica, E. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.03.045 · Cited by 69

Pleiotropic requirements for human TDP-43 in the regulation of cell and organelle homeostasis

Roczniak-Ferguson, A., & Ferguson, S. M. (2019) · Life Science Alliance · doi:10.26508/lsa.201900358 · Cited by 75

TDP‐43 and FUS/TLS: cellular functions and implications for neurodegeneration

Fiesel, F. C., & Kahle, P. J. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08258.x · Cited by 69

Emerging antisense oligonucleotide and viral therapies for amyotrophic lateral sclerosis

Ly, C. V., & Miller, T. M. (2018) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000594 · Cited by 70

Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration

Scialò, C., Cecco, E. D., Manganotti, P., & Legname, G. (2019) · Viruses · doi:10.3390/v11030261 · Cited by 69

TARDBP Mutation Analysis in TDP-43 Proteinopathies and Deciphering the Toxicity of Mutant TDP-43

Gendron, T. F., Rademakers, R., & Petrucelli, L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129036 · Cited by 70

TDP-43: A DNA and RNA binding protein with roles in neurodegenerative diseases

Warraich, S. T., Yang, S., Nicholson, G. A., & Blair, I. P. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.06.016 · Cited by 70

TDP-43 Loss-of-Function Causes Neuronal Loss Due to Defective Steroid Receptor-Mediated Gene Program Switching in Drosophila

Broeck, L. V., Naval-Sánchez, M., Adachi, Y., Diaper, D. C., Dourlen, P., Chapuis, J., Kleinberger, G., Gistelinck, M., Broeckhoven, C. V., Lambert, J., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2012.12.014 · Cited by 67

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

Cannon, A. D., Yang, B., Knight, J. A., Farnham, I. M., Zhang, Y., Wuertzer, C. A., D’Alton, S., Lin, W.-L., Castanedes‐Casey, M., Rousseau, L., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0979-3 · Cited by 68

RNA‐binding proteins in neurodegenerative disease: TDP‐43 and beyond

Hanson, K. A., Kim, S. H., & Tibbetts, R. S. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.111 · Cited by 68

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

Gendron, T. F., & Petrucelli, L. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9610-7 · Cited by 66

TDP43 and RNA instability in amyotrophic lateral sclerosis

Weskamp, K., & Barmada, S. J. (2018) · Brain Research · doi:10.1016/j.brainres.2018.01.015 · Cited by 68

Limbic-predominant age-related TDP43 encephalopathy (LATE) neuropathological change in neurodegenerative diseases

Nag, S., & Schneider, J. A. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00846-7 · Cited by 69

Pathogenic TARDBP Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia: Disease-Associated Pathways

Barmada, S. J., & Finkbeiner, S. M. (2010) · Reviews in the Neurosciences · doi:10.1515/revneuro.2010.21.4.251 · Cited by 63

Fishing for causes and cures of motor neuron disorders

Patten, S. A., Armstrong, G. A. B., Lissouba, A., Kabashi, E., Parker, J. A., & Drapeau, P. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.015719 · Cited by 70

TDP-43 induces p53-mediated cell death of cortical progenitors and immature neurons

Vogt, M. A., Ehsaei, Z., Knuckles, P., Higginbottom, A., Helmbrecht, M. S., Kunath, T., Eggan, K. C., Williams, L. A., Shaw, P. J., Wurst, W., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26397-2 · Cited by 61

ALS pathogenesis: Recent insights from genetics and mouse models

Swarup, V., & Julien, J. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.08.006 · Cited by 65

Heat Shock-induced Phosphorylation of TAR DNA-binding Protein 43 (TDP-43) by MAPK/ERK Kinase Regulates TDP-43 Function

Li, W., Reeb, A. N., Lin, B., Subramanian, P., Fey, E. E., Knoverek, C. R., French, R. L., Bigio, E. H., & Ayala, Y. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.753913 · Cited by 62

Synaptic dysfunction in ALS and FTD: anatomical and molecular changes provide insights into mechanisms of disease

Gelon, P. A., Dutchak, P. A., & Sephton, C. F. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1000183 · Cited by 64

Expansive Gene Transfer in the Rat CNS Rapidly Produces Amyotrophic Lateral Sclerosis Relevant Sequelae When TDP-43 is Overexpressed

Wang, D. B., Dayton, R. D., Henning, P. P., Cain, C. D., Zhao, L. R., Schrott, L. M., Orchard, E. A., Knight, D. S., & Klein, R. L. (2010) · Molecular Therapy · doi:10.1038/mt.2010.191 · Cited by 60

TDP-43 suppresses CGG repeat-induced neurotoxicity through interactions with HnRNP A2/B1

He, F., Krans, A., Freibaum, B. D., Taylor, J. P., & Todd, P. K. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu216 · Cited by 62

Brain-trait-associated variants impact cell-type-specific gene regulation during neurogenesis

Aygün, N., Elwell, A. L., Liang, D., Lafferty, M. J., Cheek, K. E., Courtney, K. P., Mory, J. T., Hadden-Ford, E., Krupa, O., de la Torre-Ubieta, L., et al. (2021) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2021.07.011 · Cited by 57

Progranulin and TDP-43: Mechanistic Links and Future Directions

Kumar‐Singh, S. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9625-0 · Cited by 56

RNA‐binding proteins implicated in neurodegenerative diseases

Cookson, M. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1397 · Cited by 58

An acridine derivative, [4,5-bis{(N-carboxy methyl imidazolium)methyl}acridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models

Prasad, A., Raju, G., Sivalingam, V., Girdhar, A., Verma, M., Vats, K., Taneja, V., Prabusankar, G., & Patel, B. K. (2016) · Scientific Reports · doi:10.1038/srep39490 · Cited by 56

Low-level overexpression of wild type TDP-43 causes late-onset, progressive neurodegeneration and paralysis in mice

Yang, C., Qiao, T., Yu, J. H., Wang, H., Guo, Y., Salameh, J. S., Metterville, J., Parsi, S., Yusuf, I. O., Brown, R. H., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0255710 · Cited by 55

A model of human neural networks reveals NPTX2 pathology in ALS and FTLD

Hruška-Plocháň, M., Wiersma, V. I., Betz, K. M., Mallona, I., Ronchi, S., Maniecka, Z., Hock, E., Tantardini, E., Laferrière, F., Sahadevan, S., et al. (2024) · Nature · doi:10.1038/s41586-024-07042-7 · Cited by 73

Amyotrophic lateral sclerosis: an update on recent genetic insights

Iguchi, Y., Katsuno, M., Ikenaka, K., Ishigaki, S., & Sobue, G. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7112-y · Cited by 56

Making sense of antisense oligonucleotides: A narrative review

Goyal, N., & Narayanaswami, P. (2017) · Muscle & Nerve · doi:10.1002/mus.26001 · Cited by 55

RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights

Rummens, J., & Cruz, S. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00851-y · Cited by 62

Accumulation of C-terminal fragments of transactive response DNA-binding protein 43 leads to synaptic loss and cognitive deficits in human TDP-43 transgenic mice

Medina, D. X., Orr, M. E., & Oddo, S. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.07.006 · Cited by 50

Sustained Expression of TDP-43 and FUS in Motor Neurons in Rodent's Lifetime

Huang, C., Xia, P. Y., & Zhou, H. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.396 · Cited by 51

Ascl1 controls the number and distribution of astrocytes and oligodendrocytes in the gray matter and white matter of the spinal cord

Vue, T. Y., Kim, E. J., Parras, C. M., Guillemot, F., & Johnson, J. E. B. (2014) · Development · doi:10.1242/dev.105270 · Cited by 49

Allele-Specific Knockdown of ALS-Associated Mutant TDP-43 in Neural Stem Cells Derived from Induced Pluripotent Stem Cells

Nishimura, A. L., Shum, C., Scotter, E. L., Abdelgany, A., Sardone, V., Wright, J. M., Lee, Y., Chen, H.-J., Bilican, B., Carrasco, M. A., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091269 · Cited by 52

Disease Animal Models of TDP-43 Proteinopathy and Their Pre-Clinical Applications

Liu, Y.-C., Chiang, P., & Tsai, K. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141020079 · Cited by 52

Stage-specific control of oligodendrocyte survival and morphogenesis by TDP-43

Heo, D., Ling, J. P., Molina-Castro, G. C., Langseth, A. J., Waisman, A., Nave, K., Möbius, W., Wong, P. C., & Bergles, D. E. (2022) · eLife · doi:10.7554/elife.75230 · Cited by 49

Altered astrocytic expression of TDP-43 does not influence motor neuron survival

Haidet-Phillips, A. M., Gross, S. K., Williams, T. L., Tuteja, A., Sherman, A., Ko, M., Jeong, Y. H., Wong, P. C., & Maragakis, N. J. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.10.004 · Cited by 51

TDP-43 drives synaptic and cognitive deterioration following traumatic brain injury

Gao, F., Hu, M., Zhang, J., Hashem, J., & Chen, C. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02449-w · Cited by 49

TDP-43 PrionsPreprint

Nonaka, T., & Hasegawa, M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024463 · Cited by 50

Evolutionarily Conserved Heterogeneous Nuclear Ribonucleoprotein (hnRNP) A/B Proteins Functionally Interact with Human and Drosophila TAR DNA-binding Protein 43 (TDP-43)

Romano, M., Buratti, E., Romano, G., Klima, R., Belluz, L. D. B., Stuani, C., Baralle, F. E., & Feiguin, F. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.548859 · Cited by 47

Linking RNA Dysfunction and Neurodegeneration in Amyotrophic Lateral Sclerosis

Barmada, S. J. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0340-3 · Cited by 52

FUS contributes to mTOR-dependent inhibition of translation

Sévigny, M., Bourdeau‐Julien, I., Venkatasubramani, J. P., Hui, J. B., Dutchak, P. A., & Sephton, C. F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013801 · Cited by 49

Tardbpl splicing rescues motor neuron and axonal development in a mutant tardbp zebrafish

Hewamadduma, C., Grierson, A. J., Ma, T. P., Pan, L., Moens, C. B., Ingham, P. W., Ramesh, T., & Shaw, P. J. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt082 · Cited by 55

Distinct pathways leading to TDP-43-induced cellular dysfunctions

Yamashita, M., Nonaka, T., Hirai, S., Miwa, A., Okado, H., Arai, T., Hosokawa, M., Akiyama, H., & Hasegawa, M. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu152 · Cited by 46

TDP-43 as a possible biomarker for frontotemporal lobar degeneration: a systematic review of existing antibodies

Goossens, J., Vanmechelen, E., Trojanowski, J. Q., Lee, V. M. ‐., Broeckhoven, C. V., van der Zee, J., & Engelborghs, S. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0195-1 · Cited by 43

The FTD/ALS-associated RNA-binding protein TDP-43 regulates the robustness of neuronal specification through microRNA-9a in Drosophila

Li, Z., Lu, Y., Xu, X., & Gao, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds420 · Cited by 45

Regulation of nuclear TDP-43 by NR2A-containing NMDA receptors and PTEN

Zheng, M., Liao, M., Cui, T.-Y., Tian, H., Fan, D., & Wan, Q. (2012) · Journal of Cell Science · doi:10.1242/jcs.095729 · Cited by 42

RNA as the stone guest of protein aggregation

Louka, A., Zacco, E., Temussi, P. A., Tartaglia, G. G., & Pastore, A. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa822 · Cited by 37

Isolation and characterization of soluble human full‐length TDP‐43 associated with neurodegeneration

Vivoli, M., Nigro, A., Luti, S., Capitini, C., Fani, G., Gonnelli, L., Boscaro, F., & Chiti, F. (2019) · The FASEB Journal · doi:10.1096/fj.201900474r · Cited by 40

RNA binding proteins: a common denominator of neuronal function and dysfunction

Doxakis, E. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-014-1443-7 · Cited by 40

An Early Onset Progressive Motor Neuron Disorder inScyl1-Deficient Mice Is Associated with Mislocalization of TDP-43

Pelletier, S. W., Gingras, S., Howell, S. R., Vogel, P., & Ihle, J. N. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1787-12.2012 · Cited by 39

A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43

Furukawa, Y., Suzuki, Y., Fukuoka, M., Nagasawa, K., Nakagome, K., Shimizu, H., Mukaiyama, A., & Akiyama, S. (2016) · Scientific Reports · doi:10.1038/srep20576 · Cited by 45

Tar DNA-binding protein-43 (TDP-43) regulates axon growth in vitro and in vivo

Tripathi, V. B., Baskaran, P., Shaw, C. E., & Guthrie, S. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.004 · Cited by 41

TDP-43 causes differential pathology in neuronal versus glial cells in the mouse brain

Yan, S., Wang, C.-E., Wei, W., Gaertig, M. A., Lai, L., Li, S., & Li, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt662 · Cited by 38

Translational regulation in the brain by TDP-43 phase separation

Gao, J., Wang, L., Ren, X., Dunn, J., Peters, A., Miyagi, M., Fujioka, H., Zhao, F., Askwith, C. C., Liang, J., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202101019 · Cited by 42

Advances and challenges in understanding the multifaceted pathogenesis of amyotrophic lateral sclerosis

Laferrière, F., & Polymenidou, M. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14054 · Cited by 43

The amyloidogenicity of a C-terminal region of TDP-43 implicated in Amyotrophic Lateral Sclerosis can be affected by anions, acetylation and homodimerization

Prasad, A., Sivalingam, V., Bharathi, V., Girdhar, A., & Patel, B. K. (2018) · Biochimie · doi:10.1016/j.biochi.2018.05.003 · Cited by 36

Neuromuscular junction abnormalities in a zebrafish loss-of-function model of TDP-43

Bose, P., Armstrong, G. A. B., & Drapeau, P. (2018) · Journal of Neurophysiology · doi:10.1152/jn.00265.2018 · Cited by 37

Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions

Versluys, L., Pereira, P. E., Schuermans, N., Paepe, B. D., Bleecker, J. D., Bogaert, E., & Dermaut, B. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.815765 · Cited by 34

Disturb mitochondrial associated proteostasis: Neurodegeneration and imperfect ageing

Jagtap, Y. A., Kumar, P., Kinger, S., Dubey, A. R., Choudhary, A., Gutti, R. K., Singh, S., Jha, H. C., Poluri, K. M., & Mishra, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1146564 · Cited by 36

Sustained therapeutic benefits by transient reduction of TDP-43 using ENA-modified antisense oligonucleotides in ALS/FTD mice

Takeuchi, T., Maeta, K., Ding, X., Oe, Y., Takeda, A., Inoue, M., Nagano, S., Fujihara, T., Matsuda, S., Ishigaki, S., et al. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.01.006 · Cited by 34

Homozygous ALS-linked mutations in TARDBP/TDP-43 lead to hypoactivity and synaptic abnormalities in human iPSC-derived motor neurons

Lépine, S., Nauleau-Javaudin, A., Deneault, É., Chen, C. X. ‐., Abdian, N., Franco-Flores, A. K., Haghi, G., Castellanos‐Montiel, M. J., Maussion, G., Chaineau, M., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109166 · Cited by 40

TDP-43 high throughput screening analyses in neurodegeneration: Advantages and pitfalls

Buratti, E., Romano, M., & Baralle, F. E. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.03.001 · Cited by 32

TDP-43 and HERV-K Envelope-Specific Immunogenic Epitopes Are Recognized in ALS Patients

Simula, E. R., Arru, G., Zarbo, I. R., Solla, P., & Sechi, L. A. (2021) · Viruses · doi:10.3390/v13112301 · Cited by 33

Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses

Verde, E. M., Secco, V., Ghezzi, A., Mandrioli, J., & Carra, S. (2025) · Cells · doi:10.3390/cells14100680 · Cited by 35

How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?

Baloh, R. H. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a269b · Cited by 33

Dysregulation of Translation in TDP-43 Proteinopathies: Deficits in the RNA Supply Chain and Local Protein Production

Bjork, R. T., Mortimore, N. P., Loganathan, S., & Zarnescu, D. C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.840357 · Cited by 36

Altered TDP-43 Structure and Function: Key Insights into Aberrant RNA, Mitochondrial, and Cellular and Systemic Metabolism in Amyotrophic Lateral Sclerosis

Jiang, L., & Ngo, S. T. (2022) · Metabolites · doi:10.3390/metabo12080709 · Cited by 35

Cytoplasmic TDP43 Binds microRNAs: New Disease Targets in Amyotrophic Lateral Sclerosis

Paez-Colasante, X., Figueroa‐Romero, C., Rumora, A. E., Hur, J., Mendelson, F. E., Hayes, J. M., Backus, C., Taubman, G. F., Heinicke, L. A., Walter, N. G., et al. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00117 · Cited by 33

TDP-43—The key to understanding amyotrophic lateral sclerosis

Xu, Z., & Yang, C. (2014) · Rare Diseases · doi:10.4161/21675511.2014.944443 · Cited by 36

Cytoplasmic localization of amyotrophic lateral sclerosis‐related TDP‐43 proteins modulates stress granule formation

Besnard‐Guérin, C. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14762 · Cited by 28

Mechanisms Associated with TDP-43 Neurotoxicity in ALS/FTLD

Shenouda, M., Zhang, A. B., Weichert, A., & Robertson, J. (2018) · Advances in neurobiology · doi:10.1007/978-3-319-89689-2_9 · Cited by 31

TDP-43 safeguards the embryo genome from L1 retrotransposition

Li, T. D., Murano, K., Kitano, T., Guo, Y., Negishi, L., & Siomi, H. (2022) · Science Advances · doi:10.1126/sciadv.abq3806 · Cited by 32

RNA binding proteins in senescence: A potential common linker for age-related diseases?

Varesi, A., Campagnoli, L. I. M., Barbieri, A., Rossi, L., Ricevuti, G., Esposito, C., Chirumbolo, S., Marchesi, N., & Pascale, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101958 · Cited by 29

TDP‐43 and FUS/TLS: sending a complex message about messenger RNA in amyotrophic lateral sclerosis?

Strong, M. J., & Volkening, K. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08277.x · Cited by 28

Pathogenic Mutation of TDP-43 Impairs RNA Processing in a Cell Type-Specific Manner: Implications for the Pathogenesis of ALS/FTLD

Imaizumi, K., Ideno, H., Sato, T., Morimoto, S., & Okano, H. (2022) · eNeuro · doi:10.1523/eneuro.0061-22.2022 · Cited by 27

ALS/FTLD-linked TDP-43 regulates neurite morphology and cell survival in differentiated neurons

Han, J. H., Yu, T.-H., Ryu, H.-H., Jun, M.-H., Ban, B.-K., Jang, D., & Lee, J. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.05.025 · Cited by 28

TDP-43: A new player on the AD field?

Youmans, K. L., & Wolozin, B. L. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.05.018 · Cited by 28

Development of a Novel Nonradiometric Assay for Nucleic Acid Binding to TDP-43 Suitable for High-Throughput Screening Using AlphaScreen® Technology

Cassel, J. A., Blass, B. E., Reitz, A. B., & Pawlyk, A. C. (2010) · SLAS DISCOVERY · doi:10.1177/1087057110382778 · Cited by 27

Drosophila lines with mutant and wild type human TDP-43 replacing the endogenous gene reveals phosphorylation and ubiquitination in mutant lines in the absence of viability or lifespan defects

Chang, J., & Morton, D. B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180828 · Cited by 27

Abnormal Regenerative Responses and Impaired Axonal Outgrowth after Nerve Crush in TDP-43 Transgenic Mouse Models of Amyotrophic Lateral Sclerosis

Swarup, V., Audet, J., Phaneuf, D., Križ, J., & Julien, J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2267-12.2012 · Cited by 26

TDP-43 in the spectrum of MND-FTLD pathologies

Heyburn, L., & Moussa, C. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.07.001 · Cited by 27

Prion-like properties of disease-relevant proteins in amyotrophic lateral sclerosis

Bräuer, S., Zimyanin, V. L., & Hermann, A. (2018) · Journal of Neural Transmission · doi:10.1007/s00702-018-1851-y · Cited by 29

Delineating the effect of mutations on the conformational dynamics of N-terminal domain of TDP-43

Kumar, V., Pandey, P., Idrees, D., Prakash, A., & Lynn, A. M. (2019) · Biophysical Chemistry · doi:10.1016/j.bpc.2019.106174 · Cited by 26

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)