English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Since 1962, when Ferruccio Ritossa discovered new puffing patterns in the polytene chromosomes of Drosophila incubated at an elevated temperature (153), we have been aware that stress at the cellular level is answered by the production of specific gene products. These products are variously termed heat shock proteins (Hsps) or cell stress proteins and were originally identified as molecules that are produced in response to the presence of unfolded proteins within the cell (2). How- ever, it was not until the pioneering work of the groups of Laskey, Ellis, and Georgopoulos that the relationship between the generation of correctly assembled macromolecules and the proteins that function to ensure correct assembly was estab- lished. Laskey and coworkers studied the nuclear protein nucleoplasmin, which ensures correct assembly of histones and DNA into nucleosomes. Laskey termed nucleoplasmin a mo- lecular chaperone as it mimicked the function of a human chaperone who ensures correct interactions between people (98). Ellis and Georgopoulos studied the protein which even- tually was known as chaperonin 60 (Cpn60) and which was responsible for initiating the vast flood of papers on molecular chaperones over the past two decades (58). Currently, a mo- lecular chaperone is defined by Ellis as "one of a large and diverse group of proteins that share the property of assisting the non-covalent assembly/disassembly of other macromolec- ular structures, but which are not permanent components of these structures when they are performing their normal bio- logical functions" (58). A further refinement of terminology is necessary as certain molecular chaperones are produced con- stitutively and the concentrations within the cell do not in- crease in response to stress. These proteins are defined as molecular chaperones but are not Hsps or stress proteins. Molecular chaperones, whose concentrations increase in re- sponse to stress, are both chaperones and stress proteins/heat shock proteins. The first protein-folding molecular chaperone to be discov- ered was Cpn60 (58). Since the identification of this protein as a molecular chaperone in 1988, many more proteins with ac- tual or putative molecular chaperone functions have been dis- covered, and the term currently applies to 25 families of pro-

Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection