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Article

Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.

Scientific reports - 1 Jan 2012

Sahl Steffen J, Weiss Lucien E, Duim Whitney C, Frydman Judith, Moerner W E

Abstract excerpt

The identities of toxic aggregate species in Huntington's disease pathogenesis remain ambiguous. While polyQ-expanded huntingtin (Htt) is known to accumulate in compact inclusion bodies inside neurons, this is widely thought to be a protective coping response that sequesters misfolded conformations or aggregated states of the mutated protein. To define the spatial distributions of fluorescently-labeled Htt-exon1...

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Identifiers

PMID: 23193437
DOI: 10.1038/srep00895
PMCID: PMC3508451

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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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