Mathieu Edouard Rebeaud

The paper introduces CLAPP, a method to determine paralog interactions by class, showing it can accurately assign interaction partners using weak or noisy scores when class labels are reliable.

This study examines the conservation of the Atc protein system's functional traits across bacteria, showing preserved core interactions despite sequence variability.

The paper analyzes archaeal proteomes to show a correlation between HSP70 family presence and optimal growth temperature, suggesting HSP70s enabled adaptation to mesophilic environments and eukaryotic emergence.

The paper shows that DNAJB6's conserved intrinsically disordered region enables its surveillance of FG-Nup condensates by forming stable assemblies that outcompete FG-Nup interactions.

The paper identifies specific regions in TilS proteins that determine Hsp90 dependence by comparing bacterial orthologs and their interactions with proteases.

This study investigates how Hsp110 enhances Hsp70's disaggregation activity through entropic pulling by increasing effective volume.

This study uses single-molecule nanopore experiments to demonstrate Hsp70 chaperones exert forces equivalent to 46 pN to extract trapped polypeptides, supporting the Entropic Pulling mechanism.

The paper investigates how J-domain proteins in yeast regulate Hsp70 chaperones through intramolecular interactions, showing auto-regulatory effects that reduce ATPase cycles.

The paper uses ANNs to classify J-domain proteins, revealing phylogeny, localization, and domain composition from sequence data, with insights into coevolution with Hsp70 partners.