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Article

Aggregation of ALS-linked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation.

Biochemical and biophysical research communications - 26 Sept 2014

Takanashi Keisuke, Yamaguchi Atsushi

Abstract excerpt

Protein aggregate/inclusion is one of hallmarks for neurodegenerative disorders including amyotrophic lateral sclerosis (ALS). FUS/TLS, one of causative genes for familial ALS, encodes a multifunctional DNA/RNA binding protein predominantly localized in the nucleus. C-terminal mutations in FUS/TLS cause the retention and the inclusion of FUS/TLS mutants in the cytoplasm. In the present study, we examined the...

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Share to Heterogeneous Nuclear Ribonucleoprotein A1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25173930
DOI: 10.1016/j.bbrc.2014.08.115

Genes

FUS
SMN1

Variants

Provenance

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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