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HDAC6 inhibition partially alleviates mitochondrial trafficking defects and restores motor function in human motor neuron and zebrafish models of Charcot-Marie-Tooth Disease Type 2APreprint

Butler, L., Adamson, K. I., Johnson, S. L., Jestice, L. H., Price, C. J., Stavish, D., Pooranachandran, N., Malicki, J. J., Tsakiridis, A., Grierson, A. J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.05.498819 · Cited by 4 · see citing works

TDP-43 nuclear retention is antagonized by hypo-phosphorylation of its C-terminus in the cytoplasm

Rabhi, C., Babault, N., Martin, C., Desforges, B., Maucuer, A., Joshi, V., Pankivskyi, S., Feng, Y., Bollot, G., Rattenbach, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07456-7 · Cited by 3 · see citing works

Advances and challenges in modeling Charcot-Marie-Tooth type 2A using iPSC-derived models

Rizzuti, M., Pagliari, E., D’Agostino, M., Ottoboni, L., Parente, V., Comi, G. P., Corti, S. P., Rizzo, F., & Abati, E. (2025) · Stem Cell Reports · doi:10.1016/j.stemcr.2025.102711 · Cited by 3 · see citing works

Modeling spastic paraplegia 4 with corticospinal motor neuron-enriched cortical organoids reveals genotype-phenotype and HDAC6-targetable pathology

Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117036 · Cited by 3 · see citing works

New developments in pre-clinical models of ALS to guide translation

Cock, L. D., Bercier, V., & Bosch, L. V. D. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.04.008 · Cited by 3 · see citing works

Distinct transcriptomic profile of satellite cells contributes to preservation of neuromuscular junctions in extraocular muscles of ALS mice

Li, A., Yi, J., Li, X., Dong, L., Ostrow, L. W., Ma, J., & Zhou, J. (2023) · eLife · doi:10.7554/elife.92644 · Cited by 3 · see citing works

The potential mechanism maintaining transactive response DNA binding protein 43 kDa in the mouse stroke model

Bian, Y., Fukui, Y., Ota-Elliott, R. S., Hu, X., Sun, H., Bian, Z., Zhai, Y., Yu, H., Hu, X., An, H., et al. (2025) · Neuroscience Research · doi:10.1016/j.neures.2025.01.006 · Cited by 3 · see citing works

The TDP-43I383V heterozygous mutation results in increased TDP-43 expression and altered neuronal activity in ALS patient-derived iPSC motor neurons

Chikuchi, R., Kato, Y., Tomatsu, A., Nishisaki, S., Kawakami, Y., Yoshimura, T., Li, J., Iguchi, Y., Onodera, K., Hashimoto, R., et al. (2025) · Neuroscience Research · doi:10.1016/j.neures.2025.105003 · Cited by 2 · see citing works

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 · see citing works

Epigenetic noise in the aging brain: tuning neuronal vulnerability to neurodegeneration

Yin, X., Zhang, H., Zhang, R., Xue, J., & Hou, Y. (2026) · Trends in Neurosciences · doi:10.1016/j.tins.2026.04.006 · Cited by 3 · see citing works

Biological networks and complexity in early-onset motor neuron diseases

Butchbach, M. E. R., & Scott, R. C. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.1035406 · Cited by 2 · see citing works

Histone Deacetylase 6 Brain PET in Amyotrophic Lateral Sclerosis‐Frontotemporal Spectrum Disorder

Vanderlinden, G., Carron, C. P., Weehaeghe, D. V., Vocht, J. D., Ombelet, F., Masrori, P., Weerdt, C. D., James, R. E., Evans, L. J., Schroeder, F. A., et al. (2025) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.70067 · Cited by 2 · see citing works

Distinct transcriptomic profile of satellite cells contributes to preservation of neuromuscular junctions in extraocular muscles of ALS micePreprint

Li, A., Yi, J., Li, X., Dong, L., Ostrow, L. W., Ma, J., & Zhou, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.12.528218 · Cited by 2 · see citing works

Chemical screens in aging-relevant human motor neurons identify MAP4Ks as therapeutic targets for amyotrophic lateral sclerosisPreprint

Liu, M., Ma, S., Tai, W., Zhong, X., Ni, H., Zou, Y., wang, J., & Zhang, C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.24.538014 · Cited by 2 · see citing works

Exploring epigenetic modifications as potential biomarkers and therapeutic targets in amyotrophic lateral sclerosis

Hou, X., Jiang, J., & Deng, M. (2025) · Journal of Neurology · doi:10.1007/s00415-025-13028-w · Cited by 2 · see citing works

Nucleocytoplasmic HDAC Inhibition Drives Acetylation-dependent TDP-43 Mislocalization and Disulfide-linked Oligomerization

Lukianenko, N., Kang, D. M., Bekci, A., Kim, Y. K., & Lim, S. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169318 · Cited by 1 · see citing works

Cytoskeletal disintegration in cardiovascular disease-related neurodegeneration

Atasever, E., Cebe, T., Turgut, Ş., Andican, G., & Çakatay, U. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.030 · Cited by 1 · see citing works

Fructose-2,6-bisphosphate restores TDP-43 pathology-driven genome repair deficiency in motor neuron diseases

Chakraborty, A., Mitra, J., Malojirao, V. H., Kodavati, M. M., Mandal, S. M., Gill, S. K., Sreenivasmurthy, S. G., Vasquez, V., Mankevich, M., Bosch, L. V. D., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-09787-5 · Cited by 1 · see citing works

Crosstalk between cysteine and lysine modifications: Integrating redox and metabolic regulation

Mitchem, E. C., Roede, J. R., & Fritz, K. S. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104357 · Cited by 1 · see citing works

What can we learn on ALS pathophysiology from iPSC-derived motor neurons harbouring TARBDP mutations: a systematic review

Pasho, E., Catanese, A., Kabashi, E., & Ciura, S. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00580-2 · Cited by 1 · see citing works

Effects of lysine deacetylation inhibition alone or in combination with arimoclomol on TDP-43 proteinopathyPreprint

Scozzari, S., Columbro, S. F., Favagrossa, M., Tortarolo, M., Cagnotto, A., Salmona, M., Marco, G. D., Bendotti, C., Calvo, A., Pasetto, L., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.15.628528 · Cited by 1 · see citing works

Transactive response DNA-binding Protein (TDP-43) regulates early HIV-1 entry and infectionPreprint

Cabrera-Rodríguez, R., Pérez-Yanes, S., González‐Montelongo, R., Lorenzo-Salazar, J. M., Estévez‐Herrera, J., García-Luis, J., Íñigo-Campos, A., Rubio‐Rodríguez, L. A., Muñoz‐Barrera, A., Trujillo‐González, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.06.471424

Mitochondrial bioenergetic dysfunction and cryptic splicing of stathmin-2 are neuropathological markers of disease duration in sporadic amyotrophic lateral sclerosisPreprint

Mehta, A. R., McDade, K., Newton, J. L., Ruepp, M., Pal, S., Chandran, S., Smith, C., & Selvaraj, B. T. (2022) · medRxiv · doi:10.1101/2022.09.01.22279305

A patient carrying a heterozygous p.Asn267Ser TARDBP missense mutation diagnosed as ALS and only involving lower motor neurons

Jin, S., Sun, Z., Fang, X., Chen, H., & Yang, W. (2022) · Neurological Sciences · doi:10.1007/s10072-022-06555-1

Distinct transcriptomic profile of satellite cells contributes to preservation of neuromuscular junctions in extraocular muscles of ALS micePreprint

Li, A., Yi, J., Li, X., Dong, L., Ostrow, L. W., Ma, J., & Zhou, J. (2024) · eLife · doi:10.7554/elife.92644.2

Distinct transcriptomic profile of satellite cells contributes to preservation of neuromuscular junctions in extraocular muscles of ALS micePreprint

Li, A., Yi, J., Li, X., Dong, L., Ostrow, L. W., Ma, J., & Zhou, J. (2024) · eLife · doi:10.7554/elife.92644.3

Dianas moleculares en la detección clínica de la Esclerosis Lateral Amiotrófica

Peralta, G. S., & Naranjo, D. (2024) · Polo del Conocimiento · doi:10.23857/pc.v9i8.7788

Nucleocytoplasmic Hdac Inhibition Drives Acetylation-Dependent Tdp43 Mislocalization and Disulfide-Linked AggregationPreprint

Lim, S., Lukianenko, N., Bekci, A., & Kim, Y. K. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5217747

Human iPSC-Derived Cardiomyocytes from ALS Patients with C9ORF72 Mutation Exhibit Cellular Hallmarks of ALS PathologyPreprint

Nebol, A., Yorukoglu, G., Uraz, H., King, M. C., Azzouz, M., Ferraiuolo, L., & Çağavi, E. (2025) · Research Square · doi:10.21203/rs.3.rs-6782801/v1

RNA helicase maheshvara interacts with TDP-43 and exacerbates neurodegeneration in Drosophila model of amyotrophic lateral sclerosis

Pandey, P., Das, R., Yadav, H., Mukherjee, A., & Mutsuddi, M. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107036

Study on the Correlation between TDP-43, HDAC6, Prdx1 Proteins and Brain Oxygen Levels and Cognitive Function in SchizophreniaPreprint

Tang, Z., Zhang, H., Lin, Y., Hu, R., Hu, X., Jin, X., Wen, G., & Xiong, P. (2025) · Research Square · doi:10.21203/rs.3.rs-7125132/v1

Genotype–Phenotype Distinctions in Spastic Paraplegia 4 Reveal HDAC6 as a Therapeutic TargetPreprint

Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T. M., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.15.664947

Additional file 1 of Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Ueda, T., Takeuchi, T., Fujikake, N., Suzuki, M., Minakawa, E. N., Ueyama, M., Fujino, Y., Kimura, N., Nagano, S., Yokoseki, A., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26676047

TARDBP as a regulator of HIV-1 assembly and infection: a review of targeting the viral capsid precursor Pr55Gag and limiting viral core entry

Cabrera-Rodríguez, R., Pons-Grífols, A., Pernas, M., Casado, C., Trujillo‐González, R., Lorenzo-Sánchez, I., Reyes-Castañeda, I., Trinité, B., Blanco, J., & Valenzuela-Fernández, A. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02762-x

Therapeutic potential of HDAC6 in amyotrophic lateral sclerosis

Guo, W., & Bosch, L. V. D. (2018) · Cell Stress · doi:10.15698/cst2018.01.120 · Cited by 15 · see citing works

The Role of HDAC6 in TDP-43-Induced Neurotoxicity and UPS Impairment

Lee, S., Kwon, Y., Kim, S., Jo, M., Jeon, Y., Cheon, M., Lee, S., Kim, S. R., Kim, K., & Kim, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.581942 · Cited by 25 · see citing works

Mutant Induced Pluripotent Stem Cell Lines Recapitulate Aspects of TDP-43 Proteinopathies and Reveal Specific Vulnerability

Shaw, C. E., Chandran, S., Bilican, B., Serio, A., Barmada, S. J., Nishimura, A. L., Sullivan, G. J., Carrasco, M., Phatnani, P., Friedman, B. A., et al. (2012) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specific vulnerability

Bilican, B., Serio, A., Barmada, S. J., Nishimura, A. L., Sullivan, G. J., Carrasco, M., Phatnani, H. P., Puddifoot, C. A., Story, D., Fletcher, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202922109 · Cited by 328 · see citing works

TDP-43: A Key Therapeutic Target beyond Amyotrophic Lateral Sclerosis

Palomo, V., Tosat‐Bitrián, C., Nozal, V., Nagaraj, S., Martín‐Requero, Á., & Martı́nez, A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00026 · Cited by 45 · see citing works