David S. Libich

This study identifies DNA binding and RAD51 interaction interfaces in BRCA1's disordered region and shows their distinct roles in homologous recombination and DNA repair.

This paper identifies SERBP1 as a G4-binding protein that regulates translation through topology-driven recognition of G-quadruplex structures in RNA, with implications for cancer therapy.

This paper investigates how EWS's RNA-binding domains interact with its low-complexity domain to influence condensate formation, revealing electrostatic and residue-specific interactions that underlie EWS self-association.

The paper investigates how RAD52 and RPA interact to promote inverse RNA strand exchange in DNA repair using NMR and biochemical methods.

This study identifies distinct roles of BRCA2's two DNA binding domains in DNA repair and replication fork stability using genetic and biochemical methods.

The paper identifies SERBP1 as a protein involved in PARylation-dependent complexes that regulate splicing, cell division, and ribosome biogenesis, with implications for neurodegenerative diseases.

This study investigates the phase separation mechanism of the EWSLCD domain using biophysical methods, revealing tyrosine residues as key drivers of condensate formation.