Protein ubiquitination is a dynamic multifaceted post-translational modification involved in
nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid …

Ubiquitylation is essential for signal transduction as well as cell division and differentiation in
all eukaryotes. Substrate modifications range from a single ubiquitin molecule to complex …

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 …

Hundreds of E3 ligases play a critical role in recognizing specific substrates for modification
by ubiquitin (Ub). Separating genuine targets of E3s from E3-interactors remains a …

Muscle RING finger 1 (MuRF1) and muscle atrophy F-box (MAFbx)/atrogin-1 were identified
more than 10 years ago as two muscle-specific E3 ubiquitin ligases that are increased …

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

The posttranslational modification with ubiquitin, a process referred to as ubiquitylation,
controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a …

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 …

Control of protein levels by nucleic-acid-based technologies has proven to be a useful
research tool but lacks the advantages of small molecules with respect to cell permeability …

Posttranslational modification of cell-cycle regulators with ubiquitin chains is essential for
eukaryotic cell division. Such chains can be connected through seven lysine residues or the …