In recent years, due to the aging of the population and the development of diagnostic
medicine, the number of identified diseases associated with the accumulation of amyloid …

Metal ions stabilize protein–protein interactions and can modulate protein aggregation.
Here, using liquid-based atomic force microscopy and molecular dynamics simulations, we …

Summary α-Synuclein plays an important role in synaptic functions by interacting with
synaptic vesicle membrane, while its oligomers and fibrils are associated with several …

The protein α-synuclein, a key player in Parkinson's disease (PD) and other
synucleinopathies, exists in different physiological conformations: cytosolic unfolded …

N-acetylated α-synuclein (αSyn) has long been established as an intrinsically disordered
protein associated with a dysfunctional role in Parkinson's disease. In recent years, a …

Many studies report a higher risk for Parkinson's disease (PD) and younger age of onset in
men. This, and the fact that the neuropathological process underlying PD symptoms may …

The presence of partially structured helices in natively unfolded amyloid-β42 (Aβ42) and α-
synuclein (αS) has been shown to accelerate fibrillation in the onset of Alzheimer's and …

The formation of amyloid fibrils by α-synuclein (αS) protein inside the Lewy bodies and Lewy
neurites is the prominent pathological hallmark of Parkinson's disease (PD). The fibrillation …

α-Synuclein (αSyn), a 140-residue intrinsically disordered protein, comprises the primary
proteinaceous component of pathology-associated Lewy body inclusions in Parkinson's …

The experimental finding that α-synuclein (αS) occurs physiologically as a helically folded
tetramer begs the question: why are helical tetramers the most populated multimers? While …