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 …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

Amyloid-forming proteins such α-synuclein and tau, which are implicated in Alzheimer's and
Parkinson's disease, can form different fibril structures or strains with distinct toxic properties …

Protein phase separation drives the assembly of membraneless organelles, but little is
known about how these membraneless organelles are maintained in a metastable liquid-or …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Heat shock proteins (Hsps) are a large family of molecular chaperones that are well-known
for their roles in protein maturation, re-folding and degradation. While some Hsps are …

A major role for the intracellular post-translational modification O-GlcNAc appears to be the
inhibition of protein aggregation. Most of the previous studies in this area focused on O …

Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …

Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

Parkinson's disease (PD) is a neurodegenerative disease characterized by progressive
death of dopaminergic neurons in the substantia nigra and the formation of Lewy bodies …