The protein quality control (PQC) system maintains protein homeostasis by counteracting
the accumulation of misfolded protein conformers. Substrate degradation and refolding …

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 …

Small heat shock proteins are ubiquitously expressed chaperones, yet mutations in some of
them cause tissue-specific diseases. Here, we will discuss how small heat shock proteins …

Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of
harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for …

Skeletal muscle and the nervous system depend on efficient protein quality control, and they
express chaperones and cochaperones at high levels to maintain protein homeostasis …

α-Crystallins are small heat-shock proteins that act as holdase chaperones. In humans, αA-
crystallin is expressed only in the eye lens, while αB-crystallin is found in many tissues. α …

Molecular chaperones play important roles in preventing protein misfolding and its
potentially harmful consequences. Deterioration of molecular chaperone systems upon …

Small heat shock proteins (sHSPs) are nature's 'first responders' to cellular stress, interacting
with affected proteins to prevent their aggregation. Little is known about sHSP structure …

In vivo, small heat-shock proteins (sHsps) are key players in maintaining a healthy
proteome. αB-crystallin (αB-c) or HspB5 is one of the most widespread and populous of the …