Glenn Robert Masson

The paper identifies three GCN2 activators, one of which works independently of GCN1, and describes its unique binding mechanism.

This paper shows that DELE1CTD binds to HRI's N-terminal region, displacing haem and activating HRI through competition for the haem-binding site.

This study identifies FAF2 as a strong activator of the p97-UN complex and uses its mechanism to design de novo proteins that enhance p97 activity.

This study shows RAF inhibitors activate the integrated stress response via direct GCN2 activation, independent of ERK1/2, leading to ATF4 and CHOP expression.

This paper introduces an HDX-MS workflow to estimate dissociation constants for ligand-protein interactions at peptide and amino acid resolution, enabling spatially resolved affinity mapping.

This study shows that a specific PTEN mutation causes macrocephaly, lymphoid overgrowth, and late-onset cancer in mice by impairing nuclear PTEN functions, while maintaining normal PI3K/AKT signaling.

This study shows WEE1 inhibitors work better with mRNA translation defects by activating GCN2, and suggests ways to reduce off-target effects.

This study shows heme binding to HRI causes structural changes that inhibit its autophosphorylation, affecting eIF2 kinase activity.

This paper designs and evaluates Dyr726, a brain-penetrant multi-kinase inhibitor that targets PI3Kα, receptor tyrosine kinases, and WNT signaling, showing efficacy in preclinical cancer models.

This study identifies an ISR-independent role of GCN2 in preventing excessive ribosome biogenesis and mRNA translation, with implications for cancer therapy.

The paper shows ATP-competitive inhibitors paradoxically activate GCN2 through allosteric activation and autophosphorylation, suggesting alternative strategies for GCN2 inhibition.