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Article

Inhibition of 26S proteasome activity by huntingtin filaments but not inclusion bodies isolated from mouse and human brain.

Journal of neurochemistry - 1 Sept 2006

Díaz-Hernández Miguel, Valera Adriana G, Morán María A, Gómez-Ramos Pilar, Alvarez-Castelao Beatriz, Castaño José G, Hernández Félix, Lucas José J

Abstract excerpt

In Huntington's disease (HD), as in the rest of CAG triplet-repeat disorders, the expanded polyglutamine (polyQ)-containing proteins form intraneuronal fibrillar aggregates that are gathered into inclusion bodies (IBs). Since IBs contain ubiquitin and proteasome subunits, it was proposed that inhibition of proteasome activity might underlie pathogenesis of polyQ disorders. Recent in vitro enzymatic studies...

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Identifiers

PMID: 16787406
DOI: 10.1111/j.1471-4159.2006.03968.x

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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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Inhibition of 26S proteasome activity by huntingtin filaments but not inclusion bodies isolated from mouse and human brain.PMID 16787406Read ↗

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