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Article

RNA-binding properties orchestrate TDP-43 homeostasis through condensate formation in vivo.

Nucleic acids research - 22 May 2024

Scherer Natalie M, Maurel Cindy, Graus Matthew S, McAlary Luke, Richter Grant, Radford Rowan A W, Hogan Alison, Don Emily K, Lee Albert, Yerbury Justin, Francois Mathias, Chung Roger S, Morsch Marco

Abstract excerpt

Insoluble cytoplasmic aggregate formation of the RNA-binding protein TDP-43 is a major hallmark of neurodegenerative diseases including Amyotrophic Lateral Sclerosis. TDP-43 localizes predominantly in the nucleus, arranging itself into dynamic condensates through liquid-liquid phase separation (LLPS). Mutations and post-translational modifications can alter the condensation properties of TDP-43, contributing to...

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Identifiers

PMID: 38381071
DOI: 10.1093/nar/gkae112
PMCID: PMC11109982

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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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