Ugo Dionne

The paper measures how mutations in residues near an SH3-binding motif affect binding strength in vivo and proposes a model involving interactions outside the canonical binding pocket.

The paper shows that mutations in protein binding domains, combined with regulatory divergence, determine the fate of gene duplicates in a protein interaction network.

The paper quantifies the fitness cost of spurious phosphorylation in yeast by expressing tyrosine kinases and analyzing phosphoproteomes, finding a strong correlation between spurious phosphorylation and decreased growth.

The paper shows that SH3 domain specificity in PPIs is influenced by host protein identity and domain position, not just intrinsic domain properties.