Thomas Michiels

This study shows that cardiovirus L protein disrupts nucleocytoplasmic trafficking, leading to PKR inhibition by sequestering PKR in nucleoli and releasing nuclear RNA-binding proteins into the cytosol.

This study identifies conserved phosphorylatable residues in motif G of viral RdRps that inhibit polymerase activity and suggests they as targets for antiviral drugs.

This paper identifies a second SLiM in cardiovirus L proteins that enables RSK kinases to target the nuclear pore complex via RAE1 interaction.

This paper introduces a workflow using AlphaFold and MiniPAE to predict and validate novel Small Linear Motif (SLiM)-mediated protein interactions, demonstrating its effectiveness with RSK kinases.

The paper identifies human proteins that interact with RSK kinases via DDVF-like SLiMs, showing pathogens mimic these motifs to alter RAS-ERK MAPK pathway regulation.