Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Neuroscience
Link
http://www.nature.com/articles/s41583-021-00431-1.pdf
Reference139 articles.
1. Ou, S. H., Wu, F., Harrich, D., García-Martínez, L. F. & Gaynor, R. B. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 69, 3584–3596 (1995).
2. Buratti, E. et al. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J. 20, 1774–1784 (2001). This paper was the first to describe splicing regulation as a major function of TDP43 activity.
3. Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130–133 (2006).
4. Arai, T. et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 351, 602–611 (2006). Together with Neumann et al. (2006), this paper identifies TDP43 as the main component of proteinaceous inclusions in ALS and FTD, and describes nuclear depletion and cytoplasmic accumulation as major hallmarks of disease.
5. Heyburn, L. & Moussa, C. E.-H. TDP-43 in the spectrum of MND-FTLD pathologies. Mol. Cell. Neurosci. 83, 46–54 (2017).
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