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Atomistic Insights into A315E Mutation-Enhanced Pathogenicity of TDP-43 Core Fibrils.

ACS chemical neuroscience - 21 Sept 2022

Li Fangying, Chen Yujie, Liu Xianshi, Tang Yiming, Dong Xuewei, Wei Guanghong

Abstract excerpt

The aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) into fibrillary deposits is implicated in amyotrophic lateral sclerosis (ALS), and some hereditary mutations localized in the low complexity domain (LCD) facilitate the formation of pathogenic TDP-43 fibrils. A recent cryo-EM study reported the atomic-level structures of the A315E TDP-43 LCD (residues 288-319, TDP-43288-319) core fibril in which the...

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PMID: 36053560
DOI: 10.1021/acschemneuro.2c00416

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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