Gareth J. Morgan

The paper reports cryo-EM structures of cardiac AL amyloid fibrils from IGLV6 light chains, revealing conserved structural motifs and sequence-dependent folding mechanisms.

This study identifies small molecules that stabilize diverse amyloidogenic immunoglobulin light chains by reducing conformational dynamics and proteolysis.

The paper identifies early molecular and functional signatures in cardiac AL amyloidosis patients with abnormal GLS and reduced inflammatory markers despite no significant amyloid fibril deposition.

The paper updates the AL-Base database and identifies enriched immunoglobulin light chain variable genes in AL amyloidosis, showing some genes are highly enriched and others have mutation patterns distinct from other conditions.

This study uses NMR relaxation dispersion to characterize the structural dynamics of an amyloidogenic intermediate of transthyretin, revealing conformational fluctuations that promote amyloid formation.