Gergő Gógl

The paper analyzes the structural and functional interactions of HERC2/UBE3A and HERC2/DOCK10 complexes to understand their role in Angelman and Dup15q Syndromes.

The paper identifies an NR2F1-dependent retinoic acid network in mice that regulates retinal specialization and links its disruption to foveal hypoplasia in BBSOAS patients.

This study quantifies how mutations in GATA1 affect DNA binding affinity using a new assay, revealing that certain mutations reduce binding while others increase it.

The paper identifies DGKκ as a key target of FMRP regulation through m⁶A modification, showing its role in FXS phenotypes.

This study identifies POLE2 as a general NPF-motif receptor, revealing its role in recruiting proteins involved in replication, DNA repair, and transcription through SLiM-mediated interactions.

The paper introduces a high-throughput mass-spectrometry-based assay to measure protein-ligand affinity constants, demonstrating its application to 14-3-3 isoforms and phosphopeptides.

The paper identifies functional differences in PDZ-binding motifs among DGK enzyme types using interactomic and evolutionary analyses.

The paper introduces nHU, a method to quantify binding affinities from cell extracts, showing agreement between in vitro and in-cell measurements.

The paper measures affinities of 65,000 PDZ domain interactions using quantitative fragmentomics, revealing viral interference hotspots and system-wide impacts of interactome hijacking.

The paper investigates how phosphorylation of a PDZ-binding linear motif alters interactions with PDZ domains, showing widespread modulation of binding affinities rather than discrete on/off switches.