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Article

Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle.

The Journal of biological chemistry - 3 Dec 2010

Lotz Gregor P, Legleiter Justin, Aron Rebecca, Mitchell Emily J, Huang Shao-Yi, Ng Cheping, Glabe Charles, Thompson Leslie M, Muchowski Paul J

Abstract excerpt

Inclusion bodies of aggregated mutant huntingtin (htt) fragments are a neuropathological hallmark of Huntington disease (HD). The molecular chaperones Hsp70 and Hsp40 colocalize to inclusion bodies and are neuroprotective in HD animal models. How these chaperones suppress mutant htt toxicity is unclear but might involve direct effects on mutant htt misfolding and aggregation. Using size exclusion chromatography...

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Identifiers

PMID: 20864533
DOI: 10.1074/jbc.M110.160218
PMCID: PMC2992252

Genes

DNAJB1

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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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