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 conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

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 …

The family of the human small Heat Shock Proteins (HSPBs) consists of ten members of
chaperones (HSPB1-HSPB10), characterized by a low molecular weight and capable of …

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 …

By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular
processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically …

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 …

The ability of cells to respond to stress is central to health. Stress can damage folded
proteins, which are vulnerable to even minor changes in cellular conditions. To maintain …

The small heat shock proteins (sHSPs), whose molecular weight ranges from 12∼ 43 kDa,
are members of the heat shock protein (HSP) family that are widely found in all organisms …

Small heat shock proteins (sHSPs) are a class of ATP-independent molecular chaperones
that play vital roles in maintaining protein solubility and preventing aberrant protein …