SUMO, a small ubiquitin-related modifier, is known to covalently attach to a number of
nuclear regulatory proteins such as p53, IκB, promyelocytic leukemia protein and c-Jun. The …

Abundance and activity of the tumor suppressor p53 are regulated by many different
posttranslational modifications. These include phosphorylation, acetylation, ribosylation, O …

During the development of multicellular organisms, transcriptional regulation plays an
important role in the control of cell growth, differentiation and morphogenesis. SUMOylation …

SUMOylation is a highly transient post‐translational protein modification. Attachment of
SUMO to target proteins occurs via a number of specific activating and ligating enzymes that …

Small ubiquitin-like modifier (SUMO) regulates diverse cellular processes through its
reversible, covalent attachment to target proteins. Many SUMO substrates are involved in …

Reversible post-translational modification is a rapid and efficient system to control the
activity of pre-existing proteins. Modifiers range from small chemical moieties, such as …

SUMO ylation is a post‐translational modification that regulates a multitude of cellular
processes, including replication, cell‐cycle progression, protein transport and the DNA …

The dynamic and reversible post-translational modification of proteins and protein
complexes with the ubiquitin-related SUMO modifier regulates a wide variety of nuclear …

Protein SUMOylation has emerged as an important regulatory event, particularly in nuclear
processes such as transcriptional control and DNA repair. In this context, small ubiquitin-like …

Small ubiquitin-like modifier (SUMO) family proteins regulate target-protein functions by post-
translational modification. However, a potent and selective inhibitor targeting the SUMO …