Although the discovery of the critical role of α-synuclein (α-syn) in the pathogenesis of
Parkinson's disease (PD) is now twenty-five years old, it still represents a milestone in PD …

Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Alpha-synuclein (αS) is a conformationally plastic protein that reversibly binds to cellular
membranes. It aggregates and is genetically linked to Parkinson's disease (PD). Here, we …

The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key
characteristic of Parkinson's disease. To define the nature of the species giving rise to …

Oligomeric species populated during the aggregation process of α-synuclein have been
linked to neuronal impairment in Parkinson's disease and related neurodegenerative …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Intracellular aggregation of the human amyloid protein α-synuclein is causally linked to
Parkinson's disease. While the isolated protein is intrinsically disordered, its native structure …

The two main pathological hallmarks of Parkinson's disease are loss of dopamine neurons
in the substantia nigra pars compacta and proteinaceous amyloid fibrils composed mostly of …

Abstract α-Synuclein is an abundant neuronal protein which localizes predominantly to
presynaptic terminals, and is strongly linked genetically and pathologically to Parkinson's …