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 …

Alpha-synuclein (αSyn) is a highly expressed and conserved protein, typically found in the
presynaptic terminals of neurons. The misfolding and aggregation of αSyn into amyloid …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

The misfolding and pathological aggregation of α-synuclein forming insoluble amyloid
deposits is associated with Parkinson's disease, the second most common …

Parkinson's disease (PD) is the second most common neurodegenerative disorder caused
due to loss of dopaminergic neurons in substantia nigra pars compacta, which occurs the …

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 …

We report accelerated molecular dynamics simulations of α-Synuclein and its complex with
two Cu (II) ions bound to experimentally determined binding sites. Adding two Cu (II) ions …

Aggregates of α-synuclein are thought to be the disease-causing agent in Parkinson's
disease. Various case studies have hinted at a correlation between COVID-19 and the onset …

Polyalanine (polyA) disease-causative proteins with an expansion of alanine repeats can be
aggregated. Although curative treatments for polyA diseases have not been explored, the …