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Article

[FUS/TLS as a polyglutamine aggregate interacting protein].

Rinsho shinkeigaku = Clinical neurology - 1 Nov 2010

Nukina Nobuyuki

Abstract excerpt

Formation of intracellular aggregates is the hallmark of polyglutamine (polyQ) diseases. We analyzed the components of purified nuclear polyQ aggregates by mass spectrometry. As a result, we found that the RNA-binding protein translocated in liposarcoma (TLS) was one of the major components of nuclear polyQ aggregate-interacting proteins in a Huntington disease cell model and was also associated with neuronal...

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Source

Identifiers

PMID: 21921521
DOI: 10.5692/clinicalneurol.50.945

Genes

FUS

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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[FUS/TLS as a polyglutamine aggregate interacting protein].PMID 21921521Read ↗

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