Dear Colleagues,

Many neurodegenerative diseases including Parkinson’s disease (PD), Alzheimer’s disease (AD), and amyotrophic lateral sclerosis (ALS) belong to the large category of proteinopathies, conditions characterized by the presence of proteinaceous inclusions within and/or outside the degenerating neurons. The identification of such aggregates supports the view that misfolded proteins represent a basic requirement for the neurodegenerative process and provides input to verify the existence of possible dysfunctions of the biological systems influencing protein homeostasis.

In neurodegenerative diseases, both environmental and genetic factors contribute to altering the physiological processes involved in the synthesis of disease-specific proteins, resulting in a protein overproduction or in the generation of post-translationally modified protein forms more prone to aggregation. Furthermore, the impairment of intracellular protein catabolic systems plays a crucial role in proteotoxicity, and the prion-like spreading of pathological proteins further amplifies neuronal damage.

A better comprehension of the molecular mechanisms responsible for proteotoxicity in neurodegenerative diseases can allow the identification of both new therapeutic targets and useful biomarkers for these devastating disorders.

Prof. Dr. Lucio Tremolizzo
Dr. Gessica Sala
Guest Editors

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• Parkinson’s disease
• amyotrophic lateral sclerosis
• Alzheimer’s disease
• neurodegenerative diseases
• alpha-synuclein
• TDP-43
• beta-amyloid
• tau
• genetics
• catabolism
• proteotoxicity