Role of Hsp40 and Hsp70 in huntingtin misfolding, oligomerization and inclusion assembly

Funding Activity

Website
http://purl.org/au-research/grants/nhmrc/1049459

Funding Status
Closed

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Funded Activity Summary

Huntington disease results from a mutation that causes the Htt protein to become abnormally sticky and form toxic clusters in neurons. Cells have natural defences to clustering with proteins called chaperones, which are exciting therapeutic targets. This project will examine how chaperones defend against toxic Htt clustering with cutting-edge imaging technologies. The knowledge gained will aid in designing therapeutic strategies that stimulate the defence processes and suppress the clusters.

Funded Activity Details

Start Date: 01-01-2013

End Date: 01-01-2016

Funding Scheme: Project Grants

Funding Amount: $590,103.00

Funder: National Health and Medical Research Council

Research Topics

ANZSRC Field of Research (FoR)

Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)

ANZSRC Socio-Economic Objective (SEO)

There are no SEO codes available for this funding activity

Other Keywords

Huntington's disease | protein aggregation | protein conformation | protein localisation | protein-protein interaction

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