The seven members of the 90-kDa heat shock protein (Hsp90) family encode highly
conserved molecular chaperones essential for cell survival in Arabidopsis thaliana. Hsp90 …

The 90-kDa heat shock protein (Hsp90) is an essential molecular chaperone in eukaryotic
cells, with key roles in the folding and activation of proteins involved in signal transduction …

Members of the HSP70 family function as molecular chaperones to maintain cellular
homeostasis and help plants cope with environmental stimuli. However, due to functional …

The Hsp70 molecular chaperones of plants are encoded by a multi‐gene family whose
members are developmentally regulated and differentially expressed in response to …

The genome of Arabidopsis thaliana contains seven Hsp90 family genes. Three organellar
and two cytosolic AtHsp90 isoforms were characterized by functionally expressing them in a …

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential
for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle …

Heat shock protein AtHSP90–2 is one of the three constitutive cytosolic HSP90s of
Arabidopsis thaliana, which are highly homologous and show mild expression activation in …

Small heat shock proteins (sHSPs) are virtually ubiquitous stress proteins that are also found
in many normal tissues and accumulate in diseases of protein folding. They generally act as …

Summary NtHSP18P (HSP18), a cytosolic class I small heat‐shock protein from tobacco
pollen grains, was expressed in Escherichia coli. The viability of these cells was improved …

Small heat-stress proteins (sHsps) are the most abundant stress-induced proteins with up to
20 different members in higher plants. In the cytoplasm, two different classes can be …