Mark Simon Dillingham

This paper identifies two structural elements in HELB essential for its interaction with RPA-coated ssDNA, showing how they facilitate RPA displacement and DNA loop formation.

OT-Curtains enables real-time observation of DNA-end interactions using optical tweezers and microscopy, demonstrating applications in DNA repair and telomere biology.

The paper investigates how the bacterial SMC complex MukBEF loads DNA and how a viral protein inhibits this process through DNA mimicry.

This study investigates the DNA binding and bridging activities of CtIP in healthy and diseased states, identifying a C-terminal DNA-binding domain and showing that tetramerization is required for DNA bridging.

This paper develops a baculovirus-based system for delivering large DNA cargoes for CRISPR-based genome editing in human cells, achieving up to 30% correct interventions.

This study characterizes human HELB as a monomeric helicase that binds ssDNA, hydrolyzes ATP, and clears RPA from ssDNA through translocation.

The paper uses force-fluorescence measurements to show that the CTD of ParB blocks network formation by heterodimerizing with DNA-bound ParB.