Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can
prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of …

Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

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

Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …

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 …

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 …

Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental
roles in cell biology. sHSPs are key components of the cellular protein quality control …

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 …

Misfolded protein aggregates formed by the same (homologous) or different
(heterologous/cross) sequences are the pathological hallmarks of many protein misfolding …