[1]. Diana Arseni, et al. TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP. Article. 2023.[2]. Diana Arseni, et al.Structure of pathological TDP-43 filaments from ALS with FTLD. Article. 2021.[3]. Ariel Ionescu1, Topaz Altman1 and Eran Perlson. Looking for ...
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). 5. Arseni, D. et al. S...
Diana Arseni, et al.Structure of pathological TDP-43 filaments from ALS with FTLD. Article. 2021. Ariel Ionescu1, Topaz Altman1 and Eran Perlson. Looking for answers far away from the soma—the (un)known axonal functions of TDP-43, and their contribution to early NMJ disruption in ALS. M...
8 Conicella, A. E., Zerze, G. H., Mittal, J. & Fawzi, N. L. ALS Mutations Disrupt Phase Separation Mediated by alpha-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.Structure24, 1537-1549...
An abundance of glycine and neutral polar residues facilitates numerous turns and restricts 尾-strand length, which results in an absence of 尾-sheet stacking that is associated with cross-尾 amyloid structure. An uneven distribution of residues gives rise to structurally and chemically distinct ...
Fig. 1 Structure of TDP-43.(A)Domain Structure: The top panel (A) shows a schematic representation of TDP-43’s linear domain structure. From left to right: NTD: N-Terminal Domain; NLS: Nuclear Localization Signal; RRM1 and RRM2: RNA Recognition Motifs 1 and 2; NES: Nuclear Export Sig...
Structure of TDP-43.(A)Domain Structure: The top panel (A) shows a schematic representation of TDP-43’s linear domain structure. From left to right: NTD: N-Terminal Domain; NLS: Nuclear Localization Signal; RRM1 and RRM2: RNA Recognition Motifs 1 and 2; NES: Nuclear Export Signal; Garo...
Fig. 1 Structure of TDP-43 protein. Numbers represent amino acid lengths of TDP-43. NLS: nuclear localization signal, RRM: RNA recognition motifs, NES: nuclear export signal, Q/N: glutamine/asparagine-rich domain, M1–M5: five putative mitochondrial localization signals ...
domain10. This NTD forms functional but non-pathological homo-oligomers under physiological conditions and is resistant to cellular stress11. The extent to which the structure of the NTD and the mechanism of its assembly in isolation affects the misfolding and aggregation of the FL TDP-43 remains...
By performing systematic energy calculations, we reveal a prevailing trend of destabilizing effects induced by these mutations in the amyloid structure, challenging the traditionally assumed correlation between pathogenicity and amyloidogenic propensity. Understanding the molecular basis of this discrepancy ...