Associated Papers
Myopathic aggregation-prone variants in the TDP-43 prion-like domain: genetics paving the way.
Ervilha Pereira P et al.
Brain : a Journal of Neurology, 2025
Comprehensive mapping of mutations in TDP-43 and α-Synuclein that affect stability and binding.
Alamri SH et al.
Journal of Biomolecular Structure & Dynamics, 2025
38126188 (PubMed )
Supplement: supplement_1.xlsx › Table_S8
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP.
Arseni D et al.
Nature, 2023
37532939 (PubMed )
Supplement: 41586_2023_6405_MOESM1_ESM.pdf
Structure of pathological TDP-43 filaments from ALS with FTLD.
Arseni D et al.
Nature, 2022
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions.
Versluys L et al.
Frontiers in Neuroscience, 2022
Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43.
Li Q et al.
Nature Communications, 2021
The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?
Hergesheimer RC et al.
Brain : a Journal of Neurology, 2019
30938443 (PubMed )
Supplement: awz078_supplementary_data.pdf
TDP-43 post-translational modifications in health and disease.
Buratti E
Expert Opinion on Therapeutic Targets, 2018
Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.
Lauranzano E et al.
Brain : a Journal of Neurology, 2015
Absence of mutations in exon 6 of the TARDBP gene in 207 Chinese patients with sporadic amyotrohic lateral sclerosis.
Ye CH et al.
Plos One, 2013
[Study of mutations in 5'-noncoding region of BCL-6 gene in B-cell non-Hodgkin's lymphomas].
Min DL et al.
Zhonghua Bing Li Xue Za Zhi = Chinese Journal of Pathology, 2004
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