Transcription factor proteins play an important role in modulating base damage formation and excision repair at the binding sites in the genome.

Accumulation of mutations in some cancers is correlated with an aberration of DNA repair and access of a DNA deaminase to normal genomic DNA.

The repair of spontaneous DNA damage can introduce mutators that lead to further genetic changes, which could underlie evolutionary change, disease and aging.

Uracil/adenine base pairs in HIV-1 DNA are attacked by the uracil base excision repair machinery in macrophages, which leads to HIV restriction and viral genome diversification by transcription-associated mutagenesis.

NEIL DNA glycosylases are required to counteract oxidative base damages within the mitochondrial genome to safeguard neural crest cell differentiation.

Structural, biochemical, and cellular data reveal the mechanism by which the clamp loader attaches sliding clamps at gapped and nicked DNA to support DNA damage repair.

DNA lesions formed by alkylating agents trigger double-strand breaks, in the absence of replication, by the action of MMR and BER at nearby O-alkyl and N-alkyl adducts, respectively.

A structural investigation reveals details of the mechanism by which the nuclease RecJ processes DNA ends to repair double strand breaks.

Biochemical analysis in Xenopus egg extracts reveals that the MutSα mismatch sensor retains the DNA-bound replication clamp to maintain a post-replicative temporal window permissive to strand-specific repair of mismatches.

Cryo-EM shows a 5’ DNA site on the RFC clamp loader, in addition to the 3’ site, and biochemical study shows the 5’ site facilitates PCNA loading onto gaps, consistent with genetics indicating the 5’ DNA site facilitates gap repair.