G. Muruganandam

This study investigates the structural and biochemical effects of CMT-linked GDAP1 mutations, finding reduced thermal stability and disrupted interaction networks that may impair neuronal function.

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 shows that the intrinsically disordered C-terminal domain of VcParD2 restricts its oligomerization to stable 10-mer or 12-mer structures due to entropic pressure.

The paper determines the crystal structure of the human GDAP1 core domain, identifies a fatty acid ligand, and reveals structural insights into disease-related mutations and oligomerization.

The paper determines the crystal structure of mouse CSAD, identifies substrate specificity determinants, and shows open/close motions in solution.

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