Ubiquitin signaling is a conserved, widespread, and dynamic process in which protein
substrates are rapidly modified by ubiquitin to impact protein activity, localization, or stability …

Ubiquitylation is essential for signal transduction as well as cell division and differentiation in
all eukaryotes. Substrate modifications range from a single ubiquitin molecule to complex …

PRIMPOL repriming allows DNA replication to skip DNA lesions, leading to ssDNA gaps.
These gaps must be filled to preserve genome stability. Using a DNA fiber approach to …

BRCA1/2 mutant tumor cells display an elevated mutation burden, the etiology of which
remains unclear. Here, we report that these cells accumulate ssDNA gaps and spontaneous …

Posttranslational modifications (PTMs) of proteins, the major mechanism of protein function
regulation, play important roles in regulating a variety of cellular physiological and …

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 …

Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates
governs numerous eukaryotic cellular processes, including apoptosis, cell division and …

Ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes
responsible for the attachment of ubiquitin (Ub) to cellular proteins. Humans have∼ 40 E2s …

Ubiquitination is a reversible post-translational modification based on the chemical addition
of ubiquitin to proteins with regulatory effects on various signaling pathways. Ubiquitination …

Sumoylation is an essential post‐translational modification intimately involved in a diverse
range of eukaryotic cellular mechanisms. Small ubiquitin‐like modifier (SUMO) protein …