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

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 …

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 …

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

A polyclonal antibody, R2, was raised against a fusion protein consisting of a portion of plant
hsp90 fused to the trpE protein of Escherichia coli. This antibody was found to be specific …

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 …

Hsp70 molecular chaperones have been shown to play an important role in helping cells to
cope with adverse environments, especially in response to high temperatures. The …

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 fifth Cold Spring Harbor heat shock meeting, organized by Costa Georgopoulos, Susan
Lindquist and Richard Morimoto, was held 1-5 May, 1996. Like the 1994 meeting, which had …

The subunit structure of Hsp80, the most abundant heat-shock protein of Neurospora crassa,
was examined by chemical cross-linking of the purified protein in vitro. Resolution of …