The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
Open accessAbstract
Mutations in TARDBP, encoding TAR DNA-binding protein-43 (TDP-43), are associated with TDP-43 proteinopathies, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). We compared wild-type TDP-43 and an ALS-associated mutant TDP-43 in vitro and in vivo. The A315T mutant enhances neurotoxicity and the formation of aberrant TDP-43 species, including protease-resistant fragments. The C terminus of TDP-43 shows sequence similarity to prion proteins. Synthetic peptides flanking residue 315 form amyloid fibrils in vitro and cause neuronal death in primary cultures. These data provide evidence for biochemical similarities between TDP-43 and prion proteins, raising the possibility that TDP-43 derivatives may cause spreading of the disease phenotype among neighboring neurons. Our work also suggests that decreasing the abundance of neurotoxic TDP-43 species, enhancing degradation or clearance of such TDP-43 derivatives and blocking the spread of the disease phenotype may have therapeutic potential for TDP-43 proteinopathies.
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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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Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
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Principles and Properties of Stress Granules
Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,728
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Jain, S., Wheeler, J. R., Walters, R. W., Agrawal, A., Barsic, A., & Parker, R. (2016) · Cell · doi:10.1016/j.cell.2015.12.038 · Cited by 1,590
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
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
Chou, C.-C., Zhang, Y., Umoh, M. E., Vaughan, S. W., Lorenzini, I., Liu, F., Sayegh, M., Donlin-Asp, P. G., Chen, Y. H., Duong, D. M., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0047-3 · Cited by 600
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Metadata
- Authors
- Guo, W., Chen, Y., Zhou, X., Kar, A., Ray, P., Chen, X., Rao, E. J., Yang, M., Ye, H., Zhu, L., Liu, J., Xu, M., Yang, Y., Wang, C., Zhang, D., Bigio, E. H., Mesulam, M., Shen, Y., Xu, Q., Fushimi, K., & Wu, J. Y.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2011-06-12
- Volume
- 18
- Issue
- 7
- Pages
- 822-830
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2143612940
- Cited by
- 317
- References
- 48
- FWCI
- 13.17
- Type
- journal article
- Language
- en
- Open access
- green
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- Guo, W., Chen, Y., Zhou, X., Kar, A., Ray, P., Chen, X., Rao, E. J., Yang, M., Ye, H., Zhu, L., Liu, J., Xu, M., Yang, Y., Wang, C., Zhang, D., Bigio, E. H., Mesulam, M., Shen, Y., Xu, Q., . . . Wu, J. Y. (2011). An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2053
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
