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Article

Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes.

Proceedings of the National Academy of Sciences of the United States of America - 19 Feb 2013

Sontag Emily M, Joachimiak Lukasz A, Tan Zhiqun, Tomlinson Anthony, Housman David E, Glabe Charles G, Potkin Steven G, Frydman Judith, Thompson Leslie M

Abstract excerpt

Aggregation of misfolded proteins is characteristic of a number of neurodegenerative diseases, including Huntington disease (HD). The CCT/TRiC (chaperonin containing TCP-1/TCP-1 ring) chaperonin complex can inhibit aggregation and cellular toxicity induced by expanded repeat Huntingtin (mHtt) fragments. The substrate-binding apical domain of CCT/TRiC subunit CCT1, ApiCCT1, is sufficient to inhibit aggregation of...

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Identifiers

PMID: 23365139
DOI: 10.1073/pnas.1222663110
PMCID: PMC3581981

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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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