As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …

The ubiquitin proteasome pathway is responsible for most of the protein degradation in
mammalian cells. Rates of degradation by this pathway have generally been assumed to be …

The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is
responsible for selective protein degradation in eukaryotic cells. Here we present cryo …

The ubiquitin proteasome system (UPS) degrades misfolded proteins including those
implicated in neurodegenerative diseases. We investigated the effects of tau accumulation …

The ability of ubiquitin to form up to eight different polyubiquitin chain linkages generates
complexity within the ubiquitin proteasome system, and accounts for the diverse roles of …

All eukaryotes rely on selective proteolysis to control the abundance of key regulatory
proteins and maintain a healthy and properly functioning proteome. Most of this turnover is …

Languishing antibiotic discovery and flourishing antibiotic resistance have prompted the
development of alternative untapped sources for antibiotic discovery, including previously …

To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and
unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP …

ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform
mechanical work during targeted protein degradation within cells. ClpXP consists of …

The 26S proteasome is at the executive end of the ubiquitin-proteasome pathway for the
controlled degradation of intracellular proteins. While the structure of its 20S core particle …