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 …

Protein modification by ubiquitin is a central regulatory mechanism in eukaryotic cells.
Recent proteomics developments in mass spectrometry enable systematic analysis of …

Ubiquitin signaling plays an essential role in controlling cellular processes in eukaryotes,
and the impairment of ubiquitin regulation contributes to the pathogenesis of a wide range of …

Functional consequences of protein ubiquitination have gone far beyond the degradation
regulation as was initially imagined during its discovery 40 years back. The state-of-the-art …

Mass-spectrometry-based proteomics has become an essential tool for the qualitative and
quantitative analysis of cellular systems. The biochemical complexity and functional diversity …

The ubiquitin‐proteasome system (UPS) was discovered about 40 years ago and is known
to regulate a multitude of cellular processes including protein homeostasis. Ubiquitylated …

Ubiquitin is an essential, highly-conserved small regulatory protein in eukaryotic cells. It
covalently modifies a wide variety of targeted proteins in the forms of monomer and …

Human neurodegenerative and infectious diseases and tumorigenesis are associated with
alterations in ubiquitin pathways. Over 10% of the genome encode for genes that either bind …

The diversity of ubiquitin modifications is immense. A protein can be monoubiquitylated,
multi-monoubiquitylated, and polyubiquitylated with chains varying in size and shape …

Protein ubiquitination is a powerful modulator of cellular functions. Classically linked to the
degradation of proteins, it also plays a role in intracellular localization, DNA damage …