Christopher S. Fraser

The paper determines the structure of C9orf72 RAN translation initiation complexes and identifies a key RNA-RNA interaction that drives DPR production, suggesting a therapeutic target.

This study shows that the eIF4B RRM regulates stress granule assembly and translational repression during oxidative stress.

This study uses single-molecule assays to show eIF4F binding and mRNA remodeling during translation initiation, revealing ATP-dependent conformational changes and their role in ribosome loading.

This study identifies a ribosomal kinetic checkpoint that governs selective mRNA recruitment through a branched pathway involving productive and arrested states.

This study identifies nanometer-scale RNA-protein clusters (RPCs) formed by eIF4A with cofactors eIF4B and eIF4G, showing their role in enhancing helicase activity through multivalent RNA interactions.

This study determines the structure of Pdcd4 bound to the 40S ribosomal subunit, revealing its binding site and mechanism in translational control.

The paper describes the structure of a human 48S initiation complex, revealing a second eIF4A helicase at the mRNA entry site that unwinds secondary structure downstream of the scanning complex.