R. Ferreira de Freitas

The paper develops a chemical probe, UNC6934, that targets the PWWP1 domain of NSD2, revealing cooperative control of NSD2 localization through chromatin reader domains.

This study identifies small-molecule antagonists of the NSD2 PWWP domain that block its interaction with H3K36me2, providing a tool for further investigation of NSD2's role in disease.

The paper identifies small molecule fragments that bind to the tudor domain of SETDB1 and describes their binding modes and biophysical properties.

The paper identifies small molecule antagonists targeting the USP5 ZnF-UBD, providing a framework for developing chemical probes to study its role in ubiquitin signaling.

The paper identifies HDAC6 ZnF-UBD inhibitors and describes their structure-activity relationships, revealing key binding features and potential for further optimization.

The paper analyzes atomic protein-ligand interactions in the PDB, finding that hydrophobic interactions are common in high-efficiency ligands while polar interactions are over-represented in fragment inhibitors.