Deubiquitinases (DUBs) are specialized proteases that remove ubiquitin from substrates or
cleave within ubiquitin chains to regulate ubiquitylation and therefore play important roles in …

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

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

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 …

The ubiquitin-proteasome system (UPS) is one of the major protein degradation pathways,
where abnormal UPS function has been observed in cancer and neurological diseases …

Ubiquitylation is a reversible protein modification that is implicated in many cellular
functions. Recently, much progress has been made in the characterization of a superfamily …

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 …

Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene
products, reverse the modification of proteins by a single ubiquitin (-like) protein, and …

Protein aggregation is a continuous process in our cells. Some proteins aggregate in a
regulated manner required for different vital functional processes in the cells whereas other …

The ubiquitin-proteasome system (UPS) has been implicated in neurodegenerative
diseases based on the presence of deposits consisting of ubiquitylated proteins in affected …