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 …

The impact of molecular dynamics (MD) simulations in molecular biology and drug discovery
has expanded dramatically in recent years. These simulations capture the behavior of …

Many intrinsically disordered proteins (IDPs) may undergo liquid–liquid phase separation
(LLPS) and participate in the formation of membraneless organelles in the cell, thereby …

α-Synuclein (α-syn) phosphorylation at serine 129 (pS129–α-syn) is substantially increased
in Lewy body disease, such as Parkinson's disease (PD) and dementia with Lewy bodies …

Abstract α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …

Aberrant aggregation of the misfolded presynaptic protein, α-Synuclein (α-Syn) into Lewy
body (LB) and Lewy neuritis (LN) is a major pathological hallmark of Parkinson's disease …

The formation and viscoelastic properties of condensates of intrinsically disordered proteins
(IDPs) is dictated by amino acid sequence and solution conditions. Because of the …

Cells chemically isolate molecules in compartments to both facilitate and regulate their
interactions. In addition to membrane-encapsulated compartments, cells can form …

The Alzheimer's disease (AD) afflicted brain is neuropathologically defined by extracellular
amyloid-β (Aβ) plaques and intraneuronal neurofibrillary tangles composed of …

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 …