Energy metabolism (encompassing energy assimilation, conversion and utilization) plays a
central role in all life processes and serves as a link between the organismal physiology …

The 70-kDa heat shock protein (HSP70) family of molecular chaperones represents one of
the most ubiquitous classes of chaperones and is highly conserved in all organisms …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …

Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the
generation of misfolded proteins exceeds the cellular refolding and degradative capacity …

RNA sequencing (RNA-seq) is a sensitive and accurate method for quantifying gene
expression. Small samples or those whose RNA is degraded, such as formalin-fixed paraffin …

The sensitivity of the protein-folding environment to chaperone disruption can be highly
tissue-specific. Yet, the organization of the chaperone system across physiological human …

Members of the HSP70/HSP110 family (HSP70s) form a central hub of the chaperone
network controlling all aspects of proteostasis in bacteria and the ATP-containing …

The heat shock response is a universal transcriptional response to proteotoxic stress
orchestrated by heat shock transcription factor Hsf1 in all eukaryotic cells. Despite over 40 …

Molecular chaperones control the cellular folding, assembly, unfolding, disassembly,
translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989 …