The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Protein homeostasis (proteostasis) is an essential pillar for correct cellular function.
Impairments in proteostasis are encountered both in aging and in several human disease …

The formation of insoluble inclusions in the cytosol and nucleus is associated with impaired
protein homeostasis and is a hallmark of several neurodegenerative diseases. Due to the …

Heat shock protein 70 (HSP70) chaperones play a central role in protein quality control and
are crucial for many cellular processes, including protein folding, degradation, and …

More than half of disease-causing missense variants are thought to lead to protein
degradation, but the molecular mechanism of how these variants are recognized by the cell …

Ubiquilin (UBQLN) proteins are a dynamic and versatile family of proteins found in all
eukaryotes that function in the regulation of proteostasis. Besides their canonical function as …

Chaperones of the 70 kDa heat shock protein (Hsp70) superfamily are key components of
the cellular proteostasis system. Together with its co-chaperones, Hsp70 forms proteostasis …

The cellular proteome performs highly varied functions to sustain life. Since most of these
functions require proteins to fold properly, they can be impaired by mutations that affect …

Proteins of the Hsp110 family are molecular chaperones that play important roles in protein
homeostasis in eukaryotes. The pathogenic fungus Candida albicans, which causes …

Defective mismatch repair leads to increased mutation rates, and germline loss-of-function
variants in the repair component MLH1 cause the hereditary cancer predisposition disorder …