Ontology highlight
ABSTRACT:
SUBMITTER: Lotz GP
PROVIDER: S-EPMC2992252 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Lotz Gregor P GP Legleiter Justin J Aron Rebecca R Mitchell Emily J EJ Huang Shao-Yi SY Ng Cheping C Glabe Charles C Thompson Leslie M LM Muchowski Paul J PJ
The Journal of biological chemistry 20100923 49
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 and atomic force microscopy, we found that mutant htt fragments assemble into soluble ...[more]