Live-cell imaging shows that replication-independent specialized polymerase action is a consequence of lesion processing via NER and impacts cellular survival under stress outside replicative phases of the cell cycle.

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

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.

Seven distinct cryo-electron microscopy structures delineate the elaborate mechanism for how E. coli Mfd, a transcription repair coupling factor, disassembles the RNA polymerase transcription elongation complex to initiate transcription-coupled repair.

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

The structure of human transcription factor IIH, a critical DNA repair and transcription initiation factor, has been determined by cryo-electron microscopy.

The ability of an enzyme called XPD helicase to unwind the double helix is influenced by the DNA sequence and the availability of energy.

Visualization of the sliding clamp in DNA mismatch repair shows how a transient complex is activated.

Genome-wide mapping of heteroduplex DNA (a recombination intermediate) formed during mitotic recombination in yeast demonstrates that the "classical" model of double-strand DNA break repair is inadequate to explain several aspects of mitotic recombination.

Bacterial exonuclease III exhibits underestimated enzymatic activities on single-stranded DNA, which may redefine its roles in relevant biological processes and biosensor development.