Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

Ubiquitination is crucial for a plethora of physiological processes, including cell survival and
differentiation and innate and adaptive immunity. In recent years, considerable progress has …

Mitochondria are essential organelles that execute and coordinate various metabolic
processes in the cell. Mitochondrial dysfunction severely affects cell fitness and contributes …

Huntington's disease is a progressive, fatal, neurodegenerative disorder caused by an
expanded CAG repeat in the huntingtin gene, which encodes an abnormally long …

Deubiquitinating enzymes (Dubs) function to remove covalently attached ubiquitin from
proteins, thereby controlling substrate activity and/or abundance. For most Dubs, their …

In living cells, both newly made and preexisting polypeptide chains are at constant risk for
misfolding and aggregation. In accordance with the wide diversity of misfolded forms …

Cells possess an extensive network of components to safeguard proteome integrity and
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

The ubiquitin proteasome system (UPS) degrades individual proteins in a highly regulated
fashion and is responsible for the degradation of misfolded, damaged, or unneeded cellular …

Protein aggregation and dysfunction of the ubiquitin-proteasome system are hallmarks of
many neurodegenerative diseases. Here, we address the elusive link between these …