The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

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 …

Small heat shock proteins (sHSPs) are an ubiquitous protein family found in archaea,
bacteria and eukaryotes. In plants, as in other organisms, sHSPs are upregulated by stress …

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 …

Insect heat shock proteins include ATP-independent small heat shock proteins and the
larger ATP-dependent proteins, Hsp70, Hsp90, and Hsp60. In concert with cochaperones …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Heat stress events are major factors limiting crop productivity. During summer days, land
plants must anticipate in a timely manner upcoming mild and severe temperature. They …

Small heat shock proteins are a diverse, ancient, and important family of proteins. All
organisms possess small heat shock proteins (sHSPs), indicating that these proteins …

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