Complex processes are involved in the protection of cells and organisms by heat shock
proteins (hsps). Aberrant protein production due to high temperatures is prevented by the …

A continuous threat to cell function and viability is the contain components of the ubiquitin-
proteasome degraaccumulation in cells of proteins with highly abnormal dative pathway and …

PERK and IRE1 are type-I transmembrane protein kinases that reside in the endoplasmic
reticulum (ER) and transmit stress signals in response to perturbation of protein folding …

ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor
that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 …

The existence of multiple heat shock factor (HSF) genes in higher eukaryotes has promoted
questions regarding the functions of these HSF family members, especially with respect to …

▪ Abstract Proteolysis in Escherichia coli serves to rid the cell of abnormal and misfolded
proteins and to limit the time and amounts of availability of critical regulatory proteins. Most …

The rapid yet transient transcriptional activation of heat shock genes is mediated by the
reversible conversion of HSF1 from an inert negatively regulated monomer to a …

The heat-shock response is a mechanism of cellular protection against sudden adverse
environmental growth conditions and results in the prompt production of various heat-shock …

Members of the conserved Hsp70 chaperone family are assumed to constitute a main
cellular system for the prevention and the amelioration of stress‐induced protein damage …

Hsp33, a member of a newly discovered heat shock protein family, was found to be a very
potent molecular chaperone. Hsp33 is distinguished from all other known molecular …