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.
Search or browse funded studies
Previously funded studies appear chronologically, with the most recent appearing first.
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MJFF Research Grant, 2012Consortium to Identify LRRK2 Modifiers of Age of Onset
Objective/Rationale:
We propose to design and complete a collaborative study that will bring together data and samples from subjects with LRRK2 mutations with the express goal of... -
MJFF Research Grant, 2012Targeting the Unfolded Protein Response (UPR) Transcription Factor XBP1 to Alleviate Neurodegeneration Triggered by Alpha-synuclein
Objective/Rationale:
Our general aim is to investigate the role of a specific component of a cellular stress response, known as the Unfolded Protein Response, in the development of Parkinson's disease... -
MJFF Research Grant, 2012Mechanisms of Cellular Regulation and Post-translational Modification of LRRK2
Promising Outcomes of Original Grant:
We have identified methods to increase or decrease the ratio of cytosolic LRRK2 compared to membrane-localized LRRK2 as well as methods to increase or decrease the... -
Alpha-synuclein Biology Challenge, 2012Alpha-synuclein Aggregation Leads to Loss of Functional Forms of the Protein and Toxicity
Objective/Rationale:
The protein alpha-synuclein has been linked to Parkinson’s disease (PD). The prevailing hypotheses state that this protein is directly toxic to neurons and thus the removal of... -
LRRK2 Challenge, 2012Characterizing Region Specific Splice Isoforms of LRRK2
Objective/Rationale:
LRRK2 is one of the most important genetic risk factors that we know about for Parkinson’s disease: Tens of thousands of people in the US have mutations in this gene... -
Resource: Utilizing DATATOP Biospecimens, 2012Protein S-Nitrosylation as a Potential Biomarker for Parkinson’s Disease
Objective/Rationale:
Oxidative and nitrosatvie stress, related to reactive nitrogen (N) and oxygen (O) species, can cause protein misfolding, aggregation and dysfunction, and thus...
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