Melike Çağlayan

This study characterizes LIG1's structural and biochemical interactions with oxidatively damaged DNA during the final steps of base excision repair.

This study examines how the K845N mutation in LIG1 affects nick binding and sealing using biochemical, structural, and single-molecule approaches, revealing reduced ligation efficiency and altered binding dynamics.

This study uses single-molecule techniques to compare how LIG1 and LIG3 bind and ligate gap and nick DNA substrates, revealing differences in binding dynamics and efficiency.

This study investigates how LIG1 and LIG3α handle nick sealing after polβ inserts dATP or dCTP during 8-oxoG bypass, showing ribonucleotide insertions disrupt repair coordination.

This study characterizes LIG1 active site mutants to show F635 and F872 residues are critical for accurate nick ligation and DNA repair.

This study investigates how LIG1 binds to nick DNA at the single-molecule level, revealing specific and non-specific binding dynamics and the role of the N-terminal region in nick search.