Parker T. Bassett

The paper investigates structural polymorphism in ATTR amyloid fibrils from a fourth patient, extending previous findings of two cardiac polymorphs to other organs.

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 determines cryo-EM structures of brain-derived ATTR fibrils from patients with V30M and V30G variants, revealing distinct folds compared to peripheral tissues.

This study uses cryo-EM to reveal structural polymorphism in ex-vivo ALECT2 amyloid fibrils, identifying three morphologies and acetylation sites.

This study uses cryo-EM to analyze structural variability of apolipoprotein A-I amyloid fibrils across organs and mutations, revealing conformational differences and potential clinical implications.

The paper uses cryo-EM to show that ATTR-T60A amyloid fibrils from multiple organs in patients have a consistent structural conformation.

The paper uses cryo-electron microscopy to characterize amyloid fibrils from the heart and liver of an ATTRv amyloidosis patient with the V122Δ mutation, finding structural polymorphism linked to polyneuropathy.