Heat shock factor 1 is involved in estrogen-induced chromatin remodeling in estrogen receptor-positive breast cancer cells.

Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

Helitron transposable elements, by providing high density transcription factor binding sites upstream of host genes, have diversified the heat shock response within and among Caenorhabditis species.

In response to ethanol stress, the yeast transcription factor Hsf1 forms nuclear condensates and drives the coalescence of target genes prior to their transcriptional activation while in response to thermal stress these three phenomena are tightly coordinated.

Quantitative dissection of the roles of chaperone binding and phosphorylation in regulating heat shock factor 1 leads to a predictive model of the dynamics of the yeast heat shock response.

Host protein homeostasis is a critical force shaping influenza evolution, impacting both the nature of selection on the influenza genome and the accessibility of specific mutational trajectories.

When translation stops, cells require intracellular acidification to turn on the conserved heat shock response during stress, and stress-triggered acidification (common in eukaryotes) is adaptive, promoting cell and population fitness.

Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.

A genome-wide screen in yeast reveals that key proteins in ribosome quality control also regulate mutant Huntingtin aggregation and toxicity.