Protein folding in vivo is mediated by an array of proteins that act either as 'foldases' or
'molecular chaperones'. Foldases include protein disulfide isomerase and peptidyl prolyl …

Heat shock proteins (hsps) are among the most abundant intracellular proteins. Their
synthesis is rapidly up-regulated by various 'stressors' including temperature, glucose …

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 heat shock protein (Hsp) sequences, because of their ubiquity and high degree of
conservation, provide useful models for phylogenetic analysis. In this paper I have carried …

The Arabidopsis shepherd (shd) mutant shows expanded shoot apical meristems (SAM) and
floral meristems (FM), disorganized root apical meristems, and defects in pollen tube …

The promoter region of the Arabidopsis AtHsp90-1 gene is congested with heat shock
elements and stress response elements, as well as with other potential transcriptional …

Rice seedlings accumulate stainable amounts of the 104 and 90 kDa polypeptides in
response to high temperature stress. We have purified and raised highly specific polyclonal …

A PCR-based approach was used to isolate cDNAs for cinnamate 4-hydroxylase (C4H) from
Catharanthus roseus cell cultures. The protein shared 75.9% identity with C4H from other …

Abstract Three AtHsp90 isoforms, cytosolic AtHsp90. 2, chloroplast-located AtHsp90. 5, and
endoplasmic reticulum (ER)-located AtHsp90. 7, were characterized by constitutive …

The green fluorescent protein (GFP) was targeted to the endoplasmic reticulum (ER) of living
plant cells using a virus‐based expression system. The signal peptide from the storage …