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Article

Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 3 Sept 2008

Southwell Amber L, Khoshnan Ali, Dunn Denise E, Bugg Charles W, Lo Donald C, Patterson Paul H

Abstract excerpt

Although expanded polyglutamine (polyQ) repeats are inherently toxic, causing at least nine neurodegenerative diseases, the protein context determines which neurons are affected. The polyQ expansion that causes Huntington's disease (HD) is in the first exon (HDx-1) of huntingtin (Htt). However, other parts of the protein, including the 17 N-terminal amino acids and two proline (polyP) repeat domains, regulate the...

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Source

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Identifiers

PMID: 18768695
DOI: 10.1523/JNEUROSCI.2747-08.2008
PMCID: PMC2633448

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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Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity.PMID 18768695Read ↗

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Toxic effects of mutant huntingtin in axons are mediated by its proline-rich domain.Semantic proximity Read ↗

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