Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

Protein semisynthesis—defined herein as the assembly of a protein from a combination of
synthetic and recombinant fragments—is a burgeoning field of chemical biology that has …

SUMOylation is a reversible post-translational modification that regulates protein function
through covalent attachment of small ubiquitin-like modifier (SUMO) proteins. The process of …

Site-selective chemical conjugation of synthetic molecules to proteins expands their
functional and therapeutic capacity. Current protein modification methods, based on …

The small ubiquitin-like modifier (SUMO) signaling cascade is critical for gene expression,
genome integrity, and cell cycle progression. In this review, we discuss the important role …

Post-translational modifications of cellular substrates with ubiquitin and ubiquitin-like
proteins (UBLs), including ubiquitin, SUMOs, and neural precursor cell–expressed …

Autophagy is an evolutionarily conserved mechanism for protein degradation that is critical
for the maintenance of homeostasis in man. Autophagy has unexpected pleiotropic functions …

Simple Summary The small ubiquitin-like modifier (SUMO) pathway regulates the hallmark
properties of cancer cells. Moreover, alterations in activity and in levels of SUMO machinery …

E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two steps by carboxy-
terminal adenylation and thioester bond formation to a conserved catalytic cysteine in the E1 …

Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regulates
numerous cellular processes including transcription, the cell cycle, stress responses, DNA …