Fabien Durbesson

The paper reports a large-scale quantitative interactome of human PDZ domains and bacterial PDZ-binding motifs, showing bacteria tailor effector sequences to bind with similar or higher affinity than human PBMs to hijack host functions.

The paper investigates the role of RomRX and MglB in regulating cell polarity in Myxococcus xanthus, showing RomRX acts as an effector of MglAGTP and competes with MglB to modulate complex stability.

This study introduces in vitro assays to quantify actin-binding protein (ABP) activity in actin turnover and identifies conditions that maximize turnover efficiency.

This paper develops a high-throughput screening pipeline to identify carbohydrate-binding modules (CBMs) that bind synthetic and natural polymers, discovering binders for PET, PE, PS, and polysaccharides, and demonstrating their utility in enhancing plastic-degrading enzyme activity.

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.