The stress 70 molecular chaperones of plants are localized and function in all of the major
subcellular compartments of the cell. Collectively, all of the various forms are encoded by a …

Stress 70 molecular chaperones are found in all the major subcellular compartments of plant
cells, and they are encoded by a multigene family. Twelve members of this family have been …

Molecular chaperones of the stress 70 family reversibly bind and release nonnative proteins
in a nucleotide-dependent cycle. Purified monoclonal antibodies prepared against spinach …

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 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 …

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 …

The 70-kD heat-shock proteins (HSP70s) are encoded by a multigene family in eukaryotes.
In plants, the 70-kD heat-shock cognate (HSC70) proteins are located in organellar and …

The essential cellular functions of the molecular chaperone HSP90 have been intensively
investigated in fungal and mammalian model systems. Several recent publications have …

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 …

Arabidopsis thaliana, the first plant for which the entire genome sequence is available, was
also among the first plant species from which Hsp100 proteins were characterized. The …