Cellular redox homeostasis is precisely balanced by generation and elimination of reactive
oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and …

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 …

J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions.
Despite their essential role, the structure and function of many J-domain proteins remain …

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as
molecular chaperones that play a key role in intracellular protein homeostasis, regulation of …

Huntington's disease is a neurodegenerative disease caused by an expanded polyQ stretch
within Huntingtin (HTT) that renders the protein aggregation-prone, ultimately resulting in the …

Heat-shock proteins of 70 kDa (Hsp70s) are vital for all life and are notably important in
protein folding. Hsp70s use ATP binding and hydrolysis at a nucleotide-binding domain …

Hsp70 and Hsp90 chaperones provide protein quality control to the cytoplasm, endoplasmic
reticulum (ER), and mitochondria. Hsp90 activity is often enhanced by cochaperones that …

Abstract Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of
protein homeostasis (proteostasis). Paramount to this role is Hsp70's binding to client …

Single-molecule Förster resonance energy transfer (smFRET) inherits the strategy of
measurement from the effective “spectroscopic ruler” FRET and can be utilized to observe …

Molecular chaperones play central roles in sustaining protein homeostasis and preventing
protein aggregation. Most studies of these systems have been performed in bulk, providing …