About this Research Topic
Neurodegeneration is a complex and multifaceted process leading to many chronic disease states. A key molecular pathway implicated in diverse neurodegenerative diseases, including Alzheimer’s and Parkinson’s, and other rarer as Hungtinton’s disease, spinocerebellar ataxia, prion diseases, and amyotrophic lateral sclerosis, is the misfolding of proteins whose physiological function is still elusive. In the last years, a great effort has been done for disclosing factors responsible for protein misfolding and aggregation. Metal ions, such as copper, zinc, iron and manganese, attracted researchers’ attention for their dual behavior in modulating physiological processes and affecting protein stability and folding, depending on their functional value. Noteworthy, proteins involved in neurodegenerative processes, such as α-synuclein, amyloid precursor protein, huntingtin and prion protein, present metal-binding sites and metal-dependent activity. Despite these considerations, the role of metal ions in modulating both physiological function(s) and pathological conversion of these key proteins is still unclear. To unravel their role and design new promising treatments against these incurable diseases, it is crucial to define physiological function(s) of these proteins as well as their role in preserving metal ions functional value.
This research topic will cover a broad range of topics related to metal-mediated physiological function(s) of proteins linked to neurodegeneration. It is hoped that this will inspire greater discussion and exchange of ideas in this crucial area of research and lead to positive outcomes both for researchers and patients.
- physiological function(s) of key proteins involved in neurodegeneration;
- metal-mediated neuronal function(s) of proteins such as α-synuclein, amyloid precursor protein, huntingtin and prion protein.
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