Due to the present scenario of climate change, plants have to evolve strategies to survive
and perform under a plethora of biotic and abiotic stresses, which restrict plant productivity …

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 …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually
ubiquitous proteins that are strongly induced by a variety of stresses, but that also function …

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 …

Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …

Accumulation of aggregation‐prone misfolded proteins disrupts normal cellular function and
promotes ageing and disease. Bacteria, fungi and plants counteract this by solubilizing and …

Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of
chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with …