The deubiquitylating enzymes (DUBs, also known as deubiquitylases or deubiquitinases)
maintain the dynamic state of the cellular ubiquitome by releasing conjugated ubiquitin from …

Mammalian development demands precision. Millions of molecules must be properly
located in temporal order, and their function regulated, to orchestrate important steps in cell …

Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …

Ubiquitylation is a critical post-translational modification that controls a wide variety of
processes in eukaryotes. Ubiquitin chains of different topologies are specialized for different …

Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases
regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry …

The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the
metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate …

Posttranslational modification with ubiquitin chains controls cell fate in all eukaryotes.
Depending on the connectivity between subunits, different ubiquitin chain types trigger …

Proteolysis in eukaryotic cells is mainly mediated by the ubiquitin (Ub)-proteasome system
(UPS) and the autophagylysosome system (hereafter autophagy). The UPS is a selective …

Sample purity is central to in vitro studies of protein function and regulation, and to the
efficiency and success of structural studies using techniques such as x-ray crystallography …