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February 9, 2024iScienceOpen Access

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

Sarah Lépine Angela Nauleau-Javaudin Éric Deneault Carol X.‐Q. Chen Narges Abdian Anna Krystina Franco-Flores Ghazal Haghi María José Castellanos‐Montiel Gilles Maussion Mathilde Chaineau Thomas M. Durcan

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Abstract

Cytoplasmic mislocalization and aggregation of the RNA-binding protein TDP-43 is a pathological hallmark of the motor neuron (MN) disease amyotrophic lateral sclerosis (ALS). Furthermore, while mutations in

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Cite This Study

Lépine et al. (2024) studied this question.

synapsesocial.com/papers/68e79c4cb6db64358770b893 https://doi.org/10.1016/j.isci.2024.109166

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral SclerosisOriginal Research · 2008 · 2,629 citations
2Mutant TDP-43 drives impairments in axonal transport and glycolysis in a mouse stem-cell-derived motor neuron model of amyotrophic lateral sclerosis (ALS)Original Research · 2026 · 5 citations
3Human iPSC-derived motor neurons as a platform for elucidating TDP-43-related amyotrophic lateral sclerosis pathogenesis: a mini reviewReview · 2026
4TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosisOriginal Research · 2026
5Transcriptome-based screening in TARDBP/TDP-43 knock-in motor neurons identifies the NEDD8-activating enzyme inhibitor MLN49242025 · 4 citations