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Article

Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation.

Scientific reports - 17 Feb 2016

Chiang Chien-Hao, Grauffel Cédric, Wu Lien-Szu, Kuo Pan-Hsien, Doudeva Lyudmila G, Lim Carmay, Shen Che-Kun James, Yuan Hanna S

Abstract excerpt

The RNA-binding protein TDP-43 forms intracellular inclusions in amyotrophic lateral sclerosis (ALS). While TDP-43 mutations have been identified in ALS patients, how these mutations are linked to ALS remains unclear. Here we examined the biophysical properties of six ALS-linked TDP-43 mutants and found that one of the mutants, D169G, had higher thermal stability than wild-type TDP-43 and that it was cleaved by...

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Identifiers

PMID: 26883171
DOI: 10.1038/srep21581
PMCID: PMC4756693

Genes

RRM1

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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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Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation.PMID 26883171Read ↗

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