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Article

Suppression of mutant Huntingtin aggregate formation by Cdk5/p35 through the effect on microtubule stability.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 27 Aug 2008

Kaminosono Sayuko, Saito Taro, Oyama Fumitaka, Ohshima Toshio, Asada Akiko, Nagai Yoshitaka, Nukina Nobuyuki, Hisanaga Shin-Ichi

Abstract excerpt

Huntington's disease (HD) is a polyglutamine [poly(Q)] disease with an expanded poly(Q) stretch in the N terminus of the huntingtin protein (htt). A major pathological feature of HD neurons is inclusion bodies, detergent-insoluble aggregates composed of poly(Q)-expanded mutant htt (mhtt). Misfolding of mhtt is thought to confer a toxic property via formation of aggregates. Although toxic molecular species are...

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Identifiers

PMID: 18753376
DOI: 10.1523/JNEUROSCI.0973-08.2008
PMCID: PMC6670830

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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