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Funded Studies

The Foundation supports research across basic, translational and clinical science to speed breakthroughs that can lead to the creation of new treatments and a better quality of life for people with Parkinson's disease.

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Previously funded studies appear chronologically, with the most recent appearing first.

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  • Target Advancement Program, 2016
    Role of GTPase Activity in Neurodegenerative Phenotypes Induced by G2019S LRRK2 in a Pre-clinical Model of Parkinson’s Disease

    Study Rationale:
    Mutations in the LRRK2 gene cause familial (inherited) Parkinson's disease (PD). Familial mutations tend to lead to increased kinase (protein regulation) activity or impaired GTPase...

  • Target Advancement Program, 2016
    Validation of a Protein, Transglutaminase 2, as a Way to Reduce Alpha-synuclein Clumping and Toxicity in Parkinson's Disease

    Study Rationale:

    Accumulation of abnormal aggregates (clumps) of the protein alpha-synuclein is a key feature of Parkinson's disease (PD) and plays a role in neuron degeneration (cell loss)...

  • Research Grant, 2016
    Further Validation of SIRT3 in a Parkinsonian Model

    Objective/Rationale:
    Dysfunctional mitochondria (powerhouses of the cell) are central to the pathology of Parkinson's Disease (PD). Sirtuins are a group of proteins that increase energetic processes...

  • Research Grant, 2016
    Validation of Uncharacterized LRRK2 Phosphorylation Sites

    Study Rationale:
    The Parkinson's disease (PD) protein kinase (enzyme) LRRK2 is regulated by a chemical process called phosphorylation. To date, only a handful of the sites of phosphorylation have been...

  • Target Advancement Program, 2016
    Characterization of TNIK as a LRRK2 Kinase

    Study Rationale:
    The LRRK2 protein undergoes chemical modification called phosphorylation, which can alter its function, and is carried out by enzymes called kinases (LRRK2 is also a kinase)...

  • Target Advancement Program, 2016
    High-throughput LRRK2 Ubiquitination Assay

    Study Rationale:
    The LRRK2 protein is regulated by modifications called phosphorylation, which occurs at several specific sites on the protein (Serines910, 935, 955, 973) and can alter the biology of...

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