The abnormal aggregation of α-synulcein is associated with multiple neurodegenerative
diseases such as Parkinson's disease. The hydrophobic non-amyloid component (NAC) …

The presence of intracellular filamentous α-synuclein (αS) aggregates is a common feature
in Parkinson's disease. Recombinant expressed and purified human αS is also capable of …

Oligomeric aggregates are widely suspected as toxic agents in diseases caused by protein
aggregation, yet they remain poorly characterized, partly because they are challenging to …

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 …

The heterogeneity of the synucleinopathies, neurological disorders that include Parkinson's
disease (PD), indicates that toxicity, seeding/cross-seeding ability, and propagation of α …

A 140-residue intrinsically disordered protein (IDP), α-synuclein (αS), is known to adopt
conformations that are vastly plastic and susceptible to environmental cues and crowders …

Aggregation of intrinsically disordered proteins have long been recognized as central to
amyloid diseases. However, recent research has illuminated the significance of liquid-liquid …

Amyloid formation by the intrinsically disordered α-synuclein protein is the hallmark of
Parkinson's disease. We present atomistic Molecular Dynamics simulations of the core of α …

The pathogenesis of Parkinson's disease is closely associated with the aggregation of the α-
synuclein protein. Several familial mutants have been identified and shown to affect the …

Aggregation of α-synuclein is central to the pathogenesis of Parkinson's disease. The most
toxic familial mutation E46K accelerates the aggregation process by an unknown …