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Article

The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins.

PloS one - 1 Jan 2018

Higgins Ryan, Kabbaj Marie-Helene, Hatcher Alexa, Wang Yanchang

Abstract excerpt

The functionality of a protein depends on its correct folding, but newly synthesized proteins are susceptible to aberrant folding and aggregation. Heat shock proteins (HSPs) function as molecular chaperones that aid in protein folding and the degradation of misfolded proteins. Trinucleotide (CAG) repeat expansion in the Huntingtin gene (HTT) results in the expression of misfolded Huntingtin protein (Htt), which...

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Identifiers

PMID: 29346421
DOI: 10.1371/journal.pone.0191490
PMCID: PMC5773196

Genes

HTT

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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