The self-association of amylogenic proteins to the fibril form is considered a pivotal factor in
the pathogenesis of neurodegenerative diseases, including Parkinson's disease (PD). PD …

The second most prevalent neurodegenerative disease, Parkinson's disease (PD), is
caused by the accumulation and deposition of fibrillar aggregates of the α-Syn into the Lewy …

The aggregation of alpha-synuclein (α-Syn) is closely related to the occurrence of some
neurodegenerative diseases such as Parkinson's disease. The misfolding of α-Syn …

The mechanisms of dimerization of α-synuclein from full-length monomers and their
structural features have been investigated through molecular dynamics simulations in this …

Parkinson's disease (PD) is the second most common neurodegenerative diseases with no
cure yet and its major hallmark is α-synuclein fibrillary aggregates. The crucial role of α …

Self-association of α-synuclein (αS) into pathogenic oligomeric species and subsequent
formation of highly ordered amyloid fibrils is linked to the Parkinson's disease. So most of the …

The α-synuclein is a major component of amyloid fibrils found in Lewy bodies, the
characteristic intracellular proteinaceous deposits which are pathological hallmarks of …

Amyloid-β (Aβ) aggregation is recognized to be a key toxic factor in the pathogenesis of
Alzheimer disease, which is the most common progressive neurodegenerative disorder. In …

The fibrillary aggregates of α-synuclein (α-syn) are closely associated with the etiology of
Parkinson's disease (PD). Mounting evidence shows that the interaction of α-syn with …

Parkinson's disease, originating from the intrinsically disordered peptide α-synuclein, is a
common neurodegenerative disorder that affects more than 5% of the population above age …