E. I. Hallin

This study produces and characterizes high-affinity anti-Arc nanobodies, revealing structural dynamics of Arc CTD and its role in oligomerization and capsid formation.

This study identifies conserved interactions in the Arc protein's peptide binding site and characterizes its structural properties and potential functional roles in synaptic processes.

This study compares the structural properties of dArc lobes to mammalian Arc, showing dArc forms oligomers while mammalian Arc is monomeric, suggesting different capsid assembly mechanisms.

This paper identifies a 28-amino-acid region in Arc critical for oligomerization and virus-like capsid formation, showing that exogenous RNA enhances assembly.

This study investigates how neuropathy-related mutations in the cytoplasmic tail of the human myelin protein P0 affect its membrane binding properties and function.

This study determines the structure of monomeric full-length ARC, revealing its compact conformation and interaction sites for postsynaptic proteins and phospholipid membranes.