The post-translational modification of proteins with ubiquitin plays a central role in nearly all
aspects of eukaryotic biology. Historically, studies have focused on the conjugation of …

Ubiquitination regulates nearly all cellular processes by coordinated activity of ubiquitin
writers (E1, E2, and E3 enzymes), erasers (deubiquitinating enzymes) and readers (proteins …

Ubiquitination is a post-translational modification (PTM) that is essential for balancing
numerous physiological processes. To enable delineation of protein ubiquitination at a site …

The ubiquitin-proteasome axis has been extensively explored at a system-wide level, but the
impact of deubiquitinating enzymes (DUBs) on the ubiquitinome remains largely unknown …

The development of modern high-throughput instrumentation and improved core facility
infrastructures leads to an accumulation of large amounts of scientific data. However, for a …

Ubiquitination is a versatile post-translational modification (PTM), which regulates diverse
fundamental features of protein substrates, including stability, activity, and localization …

The Ddi1/DDI2 proteins are ubiquitin shuttling factors, implicated in a variety of cellular
functions. In addition to ubiquitin-binding and ubiquitin-like domains, they contain a …

The fetal development of organs and functions is vulnerable to perturbation by maternal
inflammation which may increase susceptibility to disorders after birth. Because it is not well …

Maintenance of genome integrity requires tight control of DNA damage response (DDR)
signalling and repair, with phosphorylation and ubiquitination representing key elements …

As originally described some 40 years ago, protein ubiquitination was thought to serve
primarily as a static mark for protein degradation. In the ensuing years, it has become clear …