The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis
Open accessAbstract
Significance: Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease that causes paralysis and death. TDP-43 is a protein that regulates gene expression. TDP-43 aggregation and depletion from cell nucleus are found in ALS. Therefore, TDP-43 may cause neurodegeneration by generating toxicity from its aggregation or by a loss of its function. Our experiments test the consequence of a partial loss of TDP-43 function in mice. The results demonstrate that a partial loss of TDP-43 function is sufficient to cause neurodegeneration and ALS symptoms. In addition, we have found evidence for TDP-43 dysfunction in human ALS. Therefore, we propose that TDP-43 dysfunction causes neurodegeneration in the human disease, and future therapy should aim to restore the normal function of TDP-43.
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Citations
Cites
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
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TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
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“Overexpression of both mutant and wild-type TDP-43 can cause neurodegeneration in vitro and in vivo (9, 15), suggesting that an amplification of wild-type TDP-43 function can be toxic.”
BackgroundConverging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 4×
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BackgroundInfluentialFatality in mice due to oversaturation of cellular microRNA/short hairpin RNA pathways
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Oligodendroglia metabolically support axons and contribute to neurodegeneration
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Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia
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Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
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Cited by
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., & Patel, B. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00025 · Cited by 774
TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
Ling, J. P., Pletnikova, O., Troncoso, J. C., & Wong, P. C. (2015) · Science · doi:10.1126/science.aab0983 · Cited by 688
ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair
Klim, J. R., Williams, L. A., Limone, F., Guerra San Juan, I., Davis-Dusenbery, B. N., Mordes, D. A., Burberry, A., Steinbaugh, M. J., Gamage, K. K., Kirchner, R., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0300-4 · Cited by 653
Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice
Becker, L. A., Huang, B., Bieri, G., Ma, R., Knowles, D. A., Jafar-Nejad, P., Messing, J., Kim, H. J., Soriano, A., Auburger, G., et al. (2017) · Nature · doi:10.1038/nature22038 · Cited by 571
The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity
Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4130 · Cited by 459
Metadata
- Authors
- Yang, C., Wang, H., Qiao, T., Yang, B., Aliaga, L., Qiu, L., Tan, W., Salameh, J., McKenna-Yasek, D. M., Smith, T., Peng, L., Moore, M. J., Brown, R. H., Cai, H., & Xu, Z.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-03-10
- Volume
- 111
- Issue
- 12
- Pages
- E1121-9
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2131198526
- Cited by
- 185
- References
- 23
- FWCI
- 10.87
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yang, C., Wang, H., Qiao, T., Yang, B., Aliaga, L., Qiu, L., Tan, W., Salameh, J., McKenna-Yasek, D. M., Smith, T., Peng, L., Moore, M. J., Brown, R. H., Cai, H., & Xu, Z. (2014). Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1322641111
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