Protein Aggregations and Parkinson's Disease Pathogenesis, Progression and Treatments

Dear Colleagues,

An introduction about the Special Issue

The number of patients living with Parkinson’s disease (PD) has been estimated at over 6 million. PD is the most prevalent neurodegenerative disease that involves a movement disorder, with patients typically displaying a clinical triad of rigidity, bradykinesia, and resting tremor. PD is characterized histopathologically by the loss of dopaminergic neurons from the substantia nigra pars compacta. Akin to some of the other major neurodegenerative diseases, the brains of PD patients are interspersed with aggregated proteins. Protein aggregates are detected in both familial and sporadic forms of PD and include oligomers and fibrils of α-synuclein within Lewy bodies. Collectively, specific mutations as well as protein post-translational modifications can promote oligomerization and formation of protein aggregation, and these aggregates may themselves limit the activity or overwhelm the capacity of protein clearance systems such as the proteasome, sustaining their accumulation. Protein oligomers and aggregates can be neurotoxic and trigger neuronal death and loss of function; hence, therapies directed towards limiting aberrant protein aggregation are emerging as potential disease treatments. In this Special Issue, we want to bring together research articles and reviews that are focused on the proteins that form aggregates in PD, papers that cover the molecular triggers for aggregation such as protein post-translational modifications, the potential consequences of protein aggregation and how that contributes to disease pathogenesis and/or progression, and finally, studies that consider reducing the propensity of proteins to aggregate as a strategy to combat disease.

Dr. Wayne Carter
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

• Parkinson’s disease
• protein oligomers
• protein aggregates
• protein misfolding
• protein post-translational modifications
• proteasomal degradation
• Lewy bodies
• α-synuclein
• neurotoxicity