Fernando Moreno‐Herrero

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.

This study shows FBH1 reverses replication forks through sequential unwinding of nascent strands without forming four-way junctions, distinct from other reversal factors.

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

This study reveals how SCFFBH1 promotes fork reversal and regulates RAD51 through DNA binding and ubiquitination, using cryo-EM structures and in vitro experiments.

This study identifies RPA as a direct interactor of Mer3/HFM1 helicase, showing its role in enhancing helicase processivity and crossover formation during meiosis.

This study identifies a CTP-independent ParABS system in Streptomyces coelicolor that segregates plasmid SCP2 through a ParT protein that diffuses on DNA without CTP binding or hydrolysis.

This study investigates the real-time kinetics of Twinkle, a human mitochondrial helicase, and identifies regulatory roles of its N-terminal ZBD and C-terminal tail, along with mtSSB interactions.

The paper shows that KorB, a DNA-sliding clamp, switches to a repressor role with KorA to mediate long-range gene silencing on plasmid RK2.

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 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.