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 …

Protein ubiquitination is one of the most powerful posttranslational modifications of proteins,
as it regulates a plethora of cellular processes in distinct manners. Simple …

Sixteen ovarian tumor (OTU) family deubiquitinases (DUBs) exist in humans, and most
members regulate cell-signaling cascades. Several OTU DUBs were reported to be ubiquitin …

Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that
regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics …

The ubiquitin proteasome system maintains protein homeostasis by regulating the
breakdown of misfolded proteins, thereby preventing misfolded protein aggregates. The …

Ubiquitylation is a major posttranslational modification that controls most complex aspects of
cell physiology. It is reversed through the action of a large family of deubiquitylating …

The protein kinase PINK 1 was recently shown to phosphorylate ubiquitin (Ub) on Ser65,
and phosphoUb activates the E3 ligase Parkin allosterically. Here, we show that PINK 1 can …

Several ubiquitin chain types have remained unstudied, mainly because tools and
techniques to detect these posttranslational modifications are scarce. Linkage-specific …

Protein ubiquitination regulates many cellular processes via attachment of structurally and
functionally distinct ubiquitin (Ub) chains. Several atypical chain types have remained poorly …