To study the altered functions of protein quality control system under exposure of environmental toxin and their implications in induction of neurodegenerative protein aggregation diseases.

Summary of research:

The dysfunction protein quality control system is key feature in protein aggregation diseases. Molecular chaperone network and protein degradation pathway has also been implicated to play a role in these disorders. Our research interest is in pursuing studies aimed at investigating the role of both the chaperone and the proteasomal degradation pathways in Parkinson''''s disease. In particular, we want to study the role of alpha-synuclein, a protein that misfolds and aggregates in the brain regions that are critically involved in Parkinson’s disease. Molecular chaperone proteins are used by cells to promote correct protein folding or to target misfolded proteins for degradation. Our interest is to investigate the role of chaperone proteins on alpha-synuclein-induced toxicity, aggregation and clearance, which includes studies to investigate the effect of novel inhibitors or inducers that alter levels of molecular chaperones in the brain for their ability to stop alpha-synuclein toxicity and aggregation.