DNA double strand break (DSB) responses depend on the sequential actions of the E3
ubiquitin ligases RNF8 and RNF168 plus E2 ubiquitin-conjugating enzyme Ubc13 to …

Nonproteolytic ubiquitylation of chromatin surrounding deoxyribonucleic acid double-strand
breaks (DSBs), mediated by the RNF8/RNF168 ubiquitin ligases, plays a key role in …

DNA double-strand breaks (DSBs) not only interrupt the genetic information, but also disrupt
the chromatin structure, and both impairments require repair mechanisms to ensure genome …

DNA double-strand breaks (DSBs) are highly cytolethal DNA lesions. In response to DSBs,
cells initiate a complex response that minimizes their deleterious impact on cellular and …

Ubiquitin signals emanating from DNA double-strand breaks (DSBs) trigger the ordered
assembly of DNA damage mediator and repair proteins. This highly orchestrated process is …

The mammalian E3 ubiquitin ligases RNF8 and RNF168 facilitate recruitment of the DNA
damage response protein 53BP1 to sites of DNA double-strand breaks (DSBs). The …

The E3 ubiquitin (Ub) ligase RNF168 plays a critical role in the initiation of the DNA damage
response to double-strand breaks (DSBs). The recruitment of RNF168 by ubiquitylated …

Ubiquitylation plays key roles in DNA damage signal transduction. The current model
envisions that lysine63-linked ubiquitin chains, via the concerted action of E3 ubiquitin …

Ubiquitylation is crucial for proper cellular responses to DNA double-strand breaks (DSBs). If
unrepaired, these highly cytotoxic lesions cause genome instability, tumorigenesis …

Protein recruitment to DNA double-strand breaks (DSBs) relies on ubiquitylation of the
surrounding chromatin by the RING finger ubiquitin ligases RNF8 and RNF168. Flux through …