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 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 virtually ubiquitous molecular chaperones that can
prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of …

Plants have evolved a variety of responses to elevated temperatures that minimize damage
and ensure protection of cellular homeostasis. New information about the structure and …

Small heat-shock proteins (sHsps) are a widespread and diverse class of molecular
chaperones. Recent evidence suggests that they maintain protein homeostasis by binding …

Small heat shock proteins (sHSPs) associate with nuclei, cytoskeleton and membranes, and
as molecular chaperones they bind partially denatured proteins, thereby preventing …

Aim To investigate if rhizosphere bacteria can improve heat tolerance of wheat. Methods
Wheat (Triticum aestivum) seeds of the cultivars Olivin and Sids1 were treated with Bacillus …

The ubiquitous small heat shock proteins (sHSPs) are well documented to act in vitro as
molecular chaperones to prevent the irreversible aggregation of heat-sensitive proteins …

The small heat shock proteins (sHsps), which are ubiquitous stress proteins proposed to act
as chaperones, are encoded by an unusually complex gene family in plants. Plant sHsps …

Small heat shock proteins (sHSPs) have been thought to function as chaperones, protecting
their targets from denaturation and aggregation when organisms are subjected to various …