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Article

Conformational switch of polyglutamine-expanded huntingtin into benign aggregates leads to neuroprotective effect.

Scientific reports - 9 Oct 2015

Sun Chia-Sui, Lee Chi-Chang, Li Yi-Ni, Yao-Chen Yang Sunny, Lin Chih-Hsiang, Chang Yi-Che, Liu Po-Fan, He Ruei-Yu, Wang Chih-Hsien, Chen Wenlung, Chern Yijuang, Jen-Tse Huang Joseph

Abstract excerpt

The abundant accumulation of inclusion bodies containing polyglutamine-expanded mutant huntingtin (mHTT) aggregates is considered as the key pathological event in Huntington's disease (HD). Here, we demonstrate that FKBP12, an isomerase that exhibits reduced expression in HD, decreases the amyloidogenicity of mHTT, interrupts its oligomerization process, and structurally promotes the formation of amorphous...

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Identifiers

PMID: 26450664
DOI: 10.1038/srep14992
PMCID: PMC4598856

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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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