Role of Hsp40 and Hsp70 in huntingtin misfolding, oligomerization and inclusion assembly [ 2013 - 2016 ]

Also known as: Chaperone defenders against toxic clusters in Huntington's disease

Research Grant

[Cite as]

Researchers: A/Pr Daniel Hatters (Principal investigator) ,  A/Pr Till Boecking

Brief description 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.

Funding Amount $AUD 590,103.59

Funding Scheme Project Grants

Notes Standard Project Grant

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